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Conserved domains on  [gi|732683275|gb|AIZ90080|]
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(Fe-S)-binding protein [Escherichia coli str. K-12 substr. MG1655]

Protein Classification

oxidoreductase FeS-binding subunit( domain architecture ID 11486207)

oxidoreductase FeS-binding subunit similar to Escherichia coli protein YgfT

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
PRK12809 PRK12809
putative oxidoreductase Fe-S binding subunit; Reviewed
1-639 0e+00

putative oxidoreductase Fe-S binding subunit; Reviewed


:

Pssm-ID: 183762 [Multi-domain]  Cd Length: 639  Bit Score: 1343.91  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275   1 MNKFIAAEAAECIGCHACEIACAVAHNQENWPLSHSDFRPRIHVVGKGQAANPVACHHCNNAPCVTACPVNALTFQSDSV 80
Cdd:PRK12809   1 MNKFIAAEAAECIGCHACEIACAVAHNQENWPLSHSDFRPRIHVVGKGQAANPVACHHCNNAPCVTACPVNALTFQSDSV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275  81 QLDEQKCIGCKRCAIACPFGVVEMVDTIAQKCDLCNQRSSGTQACIEVCPTQALRLMDDKGLQQIKVARQRKTAAGKASS 160
Cdd:PRK12809  81 QLDEQKCIGCKRCAIACPFGVVEMVDTIAQKCDLCNQRSSGTQACIEVCPTQALRLMDDKGLQQIKVARQRKTAAGKASS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275 161 DAQPSRSAALLPVNSRKGADKISASERKTHFGEIYCGLDPQQATYESDRCVYCAEKANCNWHCPLHNAIPDYIRLVQEGK 240
Cdd:PRK12809 161 DAQPSRSAALLPVNSRKGADKISASERKTHFGEIYCGLDPQQATYESDRCVYCAEKANCNWHCPLHNAIPDYIRLVQEGK 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275 241 IIEAAELCHQTSSLPEICGRVCPQDRLCEGACTLKDHSGAVSIGNLERYITDTALAMGWRPDVSKVVPRSEKVAVIGAGP 320
Cdd:PRK12809 241 IIEAAELCHQTSSLPEICGRVCPQDRLCEGACTLKDHSGAVSIGNLERYITDTALAMGWRPDVSKVVPRSEKVAVIGAGP 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275 321 AGLGCADILARAGVQVDVFDRHPEIGGMLTFGIPPFKLDKTVLSQRREIFTAMGIDFHLNCEIGRDITFSDLTSEYDAVF 400
Cdd:PRK12809 321 AGLGCADILARAGVQVDVFDRHPEIGGMLTFGIPPFKLDKTVLSQRREIFTAMGIDFHLNCEIGRDITFSDLTSEYDAVF 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275 401 IGVGTYGMMRADLPHEDAPGVIQALPFLTAHTRQLMGLPESEEYPLTDVEGKRVVVLGGGDTTMDCLRTSIRLNAASVTC 480
Cdd:PRK12809 401 IGVGTYGMMRADLPHEDAPGVIQALPFLTAHTRQLMGLPESEEYPLTDVEGKRVVVLGGGDTTMDCLRTSIRLNAASVTC 480
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275 481 AYRRDEVSMPGSRKEVVNAREEGVEFQFNVQPQYIACDEDGRLTAVGLIRTAMGEPGPDGRRRPRPVAGSEFELPADVLI 560
Cdd:PRK12809 481 AYRRDEVSMPGSRKEVVNAREEGVEFQFNVQPQYIACDEDGRLTAVGLIRTAMGEPGPDGRRRPRPVAGSEFELPADVLI 560
                        570       580       590       600       610       620       630
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 732683275 561 MAFGFQAHAMPWLQGSGIKLDKWGLIQTGDVGYLPTQTHLKKVFAGGDAVHGADLVVTAMAAGRQAARDMLTLFDTKAS 639
Cdd:PRK12809 561 MAFGFQAHAMPWLQGSGIKLDKWGLIQTGDVGYLPTQTHLKKVFAGGDAVHGADLVVTAMAAGRQAARDMLTLFDTKAS 639
 
Name Accession Description Interval E-value
PRK12809 PRK12809
putative oxidoreductase Fe-S binding subunit; Reviewed
1-639 0e+00

putative oxidoreductase Fe-S binding subunit; Reviewed


Pssm-ID: 183762 [Multi-domain]  Cd Length: 639  Bit Score: 1343.91  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275   1 MNKFIAAEAAECIGCHACEIACAVAHNQENWPLSHSDFRPRIHVVGKGQAANPVACHHCNNAPCVTACPVNALTFQSDSV 80
Cdd:PRK12809   1 MNKFIAAEAAECIGCHACEIACAVAHNQENWPLSHSDFRPRIHVVGKGQAANPVACHHCNNAPCVTACPVNALTFQSDSV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275  81 QLDEQKCIGCKRCAIACPFGVVEMVDTIAQKCDLCNQRSSGTQACIEVCPTQALRLMDDKGLQQIKVARQRKTAAGKASS 160
Cdd:PRK12809  81 QLDEQKCIGCKRCAIACPFGVVEMVDTIAQKCDLCNQRSSGTQACIEVCPTQALRLMDDKGLQQIKVARQRKTAAGKASS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275 161 DAQPSRSAALLPVNSRKGADKISASERKTHFGEIYCGLDPQQATYESDRCVYCAEKANCNWHCPLHNAIPDYIRLVQEGK 240
Cdd:PRK12809 161 DAQPSRSAALLPVNSRKGADKISASERKTHFGEIYCGLDPQQATYESDRCVYCAEKANCNWHCPLHNAIPDYIRLVQEGK 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275 241 IIEAAELCHQTSSLPEICGRVCPQDRLCEGACTLKDHSGAVSIGNLERYITDTALAMGWRPDVSKVVPRSEKVAVIGAGP 320
Cdd:PRK12809 241 IIEAAELCHQTSSLPEICGRVCPQDRLCEGACTLKDHSGAVSIGNLERYITDTALAMGWRPDVSKVVPRSEKVAVIGAGP 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275 321 AGLGCADILARAGVQVDVFDRHPEIGGMLTFGIPPFKLDKTVLSQRREIFTAMGIDFHLNCEIGRDITFSDLTSEYDAVF 400
Cdd:PRK12809 321 AGLGCADILARAGVQVDVFDRHPEIGGMLTFGIPPFKLDKTVLSQRREIFTAMGIDFHLNCEIGRDITFSDLTSEYDAVF 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275 401 IGVGTYGMMRADLPHEDAPGVIQALPFLTAHTRQLMGLPESEEYPLTDVEGKRVVVLGGGDTTMDCLRTSIRLNAASVTC 480
Cdd:PRK12809 401 IGVGTYGMMRADLPHEDAPGVIQALPFLTAHTRQLMGLPESEEYPLTDVEGKRVVVLGGGDTTMDCLRTSIRLNAASVTC 480
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275 481 AYRRDEVSMPGSRKEVVNAREEGVEFQFNVQPQYIACDEDGRLTAVGLIRTAMGEPGPDGRRRPRPVAGSEFELPADVLI 560
Cdd:PRK12809 481 AYRRDEVSMPGSRKEVVNAREEGVEFQFNVQPQYIACDEDGRLTAVGLIRTAMGEPGPDGRRRPRPVAGSEFELPADVLI 560
                        570       580       590       600       610       620       630
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 732683275 561 MAFGFQAHAMPWLQGSGIKLDKWGLIQTGDVGYLPTQTHLKKVFAGGDAVHGADLVVTAMAAGRQAARDMLTLFDTKAS 639
Cdd:PRK12809 561 MAFGFQAHAMPWLQGSGIKLDKWGLIQTGDVGYLPTQTHLKKVFAGGDAVHGADLVVTAMAAGRQAARDMLTLFDTKAS 639
gltD_gamma_fam TIGR01318
glutamate synthase small subunit family protein, proteobacterial; This model represents one of ...
169-636 0e+00

glutamate synthase small subunit family protein, proteobacterial; This model represents one of three built for the NADPH-dependent or NADH-dependent glutamate synthase (EC 1.4.1.13 and 1.4.1.14, respectively) small subunit and homologs. TIGR01317 describes the small subunit (or equivalent region from longer forms) in eukaryotes, Gram-positive bacteria, and some other lineages, both NADH and NADPH-dependent. TIGR01316 describes a protein of similar length, from Archaea and a number of bacterial lineages, that forms glutamate synthase homotetramers without a large subunit. This model describes both glutatate synthase small subunit and closely related paralogs of unknown function from a number of gamma and alpha subdivision Proteobacteria, including E. coli.


Pssm-ID: 273553 [Multi-domain]  Cd Length: 467  Bit Score: 911.11  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275  169 ALLPVNSRKGADKISASERKTHFGEIYCGLDPQQATYESDRCVYCAEkANCNWHCPLHNAIPDYIRLVQEGKIIEAAELC 248
Cdd:TIGR01318   1 FQFIDLPRQDPDKIPVEERKTDFREIYGPFDKGQAQYQADRCLDCGN-PYCEWKCPVHNAIPQWLQLVQEGRIDEAAELS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275  249 HQTSSLPEICGRVCPQDRLCEGACTLKDHSGAVSIGNLERYITDTALAMGWRPDVSKVVPRSEKVAVIGAGPAGLGCADI 328
Cdd:TIGR01318  80 HQTNTLPEICGRVCPQDRLCEGACTLNDEGGAVTIGNLERYITDTALAMGWRPDLSHVQPTGKRVAVIGAGPAGLACADI 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275  329 LARAGVQVDVFDRHPEIGGMLTFGIPPFKLDKTVLSQRREIFTAMGIDFHLNCEIGRDITFSDLTSEYDAVFIGVGTYGM 408
Cdd:TIGR01318 160 LARAGVQVVVFDRHPEIGGLLTFGIPSFKLDKAVLSRRREIFTAMGIEFRLNCEVGRDISLDDLLEDYDAVFLGVGTYRS 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275  409 MRADLPHEDAPGVIQALPFLTAHTRQLMGLPESEEYPLTDVEGKRVVVLGGGDTTMDCLRTSIRLNAASVTCAYRRDEVS 488
Cdd:TIGR01318 240 MRGGLPGEDAPGVLPALPFLIANTRQLMGLPEEPEEPLIDVEGKRVVVLGGGDTAMDCVRTAIRLGATKVTCAYRRDEAN 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275  489 MPGSRKEVVNAREEGVEFQFNVQPQYIACDEDGRLTAVGLIRTAMGEPGPDGRRRPRPVAGSEFELPADVLIMAFGFQAH 568
Cdd:TIGR01318 320 MPGSRREVANAREEGVEFLFNVQPVSIESDEDGQVIGVTVVRTKLGEPDANGRRRPVPVAGSEFVLPADVVIMAFGFSPH 399
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 732683275  569 AMPWLQGSGIKLDKWGLIQTGDVGYLPTQTHLKKVFAGGDAVHGADLVVTAMAAGRQAARDMLTLFDT 636
Cdd:TIGR01318 400 LMPWLAAHGITLDSWGRIITALSSGLTYQTTNPKIFAGGDAVRGADLVVTAVAEGRDAAQGILDWLGV 467
GltD COG0493
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ...
187-630 0e+00

NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport and metabolism, General function prediction only]; NADPH-dependent glutamate synthase beta chain or related oxidoreductase is part of the Pathway/BioSystem: Glutamine biosynthesis


Pssm-ID: 440259 [Multi-domain]  Cd Length: 434  Bit Score: 611.37  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275 187 RKTHFGEIYCGLDPQQATYESDRCVYCAeKANCNWHCPLHNAIPDYIRLVQEGKIIEAAELCHQTSSLPEICGRVCPqdR 266
Cdd:COG0493    1 RIKDFREVYPGLSEEEAIEQAARCLDCG-DPPCQTGCPVGNDIPEWIRLIAEGDYEEALELIHETNPFPEVCGRVCP--A 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275 267 LCEGACTLKDHSGAVSIGNLERYITDTALAMGWRPDVSKVVPRSEKVAVIGAGPAGLGCADILARAGVQVDVFDRHPEIG 346
Cdd:COG0493   78 PCEGACVRGIVDEPVAIGALERFIADKAFEEGWVKPPPPAPRTGKKVAVVGSGPAGLAAAYQLARAGHEVTVFEALDKPG 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275 347 GMLTFGIPPFKLDKTVLSQRREIFTAMGIDFHLNCEIGRDITFSDLTSEYDAVFIGVGTYGMMRADLPHEDAPGVIQALP 426
Cdd:COG0493  158 GLLRYGIPEFRLPKDVLDREIELIEALGVEFRTNVEVGKDITLDELLEEFDAVFLATGAGKPRDLGIPGEDLKGVHSAMD 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275 427 FLTAHTRqlMGLPESeeyplTDVEGKRVVVLGGGDTTMDCLRTSIRLNAASVTCAYRRDEVSMPGSRKEVVNAREEGVEF 506
Cdd:COG0493  238 FLTAVNL--GEAPDT-----ILAVGKRVVVIGGGNTAMDCARTALRLGAESVTIVYRRTREEMPASKEEVEEALEEGVEF 310
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275 507 QFNVQPQYIACDEDGRLTAVGLIRTAMGEPGPDGRRRPRPVAGSEFELPADVLIMAFGFQAHAMPWLQGSGIKLDKWGLI 586
Cdd:COG0493  311 LFLVAPVEIIGDENGRVTGLECVRMELGEPDESGRRRPVPIEGSEFTLPADLVILAIGQTPDPSGLEEELGLELDKRGTI 390
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....
gi 732683275 587 QTGDVGYlptQTHLKKVFAGGDAVHGADLVVTAMAAGRQAARDM 630
Cdd:COG0493  391 VVDEETY---QTSLPGVFAGGDAVRGPSLVVWAIAEGRKAARAI 431
HycB_like cd10554
HycB, HydN and similar proteins; This family includes HycB, the FeS subunit of a ...
4-137 1.03e-60

HycB, HydN and similar proteins; This family includes HycB, the FeS subunit of a membrane-associated formate hydrogenlyase system (FHL-1) in Escherichia coli that breaks down formate, produced during anaerobic fermentation, to H2 and CO2. FHL-1 consists of formate dehydrogenase H (FDH-H) and the hydrogenase 3 complex (Hyd-3). HycB is thought to code for the [4Fe-4S] ferredoxin subunit of hydrogenase 3, which functions as an intermediate electron carrier protein between hydrogenase 3 and formate dehydrogenase. HydN codes for the [4Fe-4S] ferredoxin subunit of FDH-H; a hydN in-frame deletion mutation causes only weak reduction in hydrogenase activity, but loss of more than 60% of FDH-H activity. This pathway is only active at low pH and high formate concentrations, and is thought to provide a detoxification/de-acidification system countering the buildup of formate during fermentation.


Pssm-ID: 319876 [Multi-domain]  Cd Length: 149  Bit Score: 199.02  E-value: 1.03e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275   4 FIAAEAAECIGCHACEIACAVAHNQENWP---LSHSDFRPRIHVVGKGQAANPVACHHCNNAPCVTACPVNALTFQSDSV 80
Cdd:cd10554    1 FVIADPDKCIGCRTCEVACAAAHSGKGIFeagTDGLPFLPRLRVVKTGEVTAPVQCRQCEDAPCANVCPVGAISQEDGVV 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275  81 QLDEQKCIGCKRCAIACPFGVVEMVDT-------------IAQKCDLCNQRSSGTqACIEVCPTQALRLM 137
Cdd:cd10554   81 QVDEERCIGCKLCVLACPFGAIEMAPTtvpgvdwergpraVAVKCDLCAGREGGP-ACVEACPTKALTLV 149
Fer4_20 pfam14691
Dihydroprymidine dehydrogenase domain II, 4Fe-4S cluster; Domain II of the enzyme ...
187-299 1.40e-51

Dihydroprymidine dehydrogenase domain II, 4Fe-4S cluster; Domain II of the enzyme dihydroprymidine dehydrogenase binds FAD. Dihydroprymidine dehydrogenase catalyzes the first and rate-limiting step of pyrimidine degradation by converting pyrimidines to the corresponding 5,6- dihydro compounds. This domain carries two Fe4-S4 clusters.


Pssm-ID: 434132 [Multi-domain]  Cd Length: 113  Bit Score: 173.49  E-value: 1.40e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275  187 RKTHFGEIYCGLDPQQATYESDRCVYCAeKANCNWHCPLHNAIPDYIRLVQEGKIIEAAELCHQTSSLPEICGRVCPQDR 266
Cdd:pfam14691   1 RIKNFEEVALGYTEEEAIAEASRCLQCK-DPPCVKGCPVHIDIPEFIKLIAEGNFEGAARIILETNPLPAICGRVCPQER 79
                          90       100       110
                  ....*....|....*....|....*....|....
gi 732683275  267 LCEGACTL-KDHSGAVSIGNLERYITDTALAMGW 299
Cdd:pfam14691  80 QCEGACVLgKKGFEPVAIGRLERFAADWARENGI 113
ferrodoxin_EFR1 NF038196
EFR1 family ferrodoxin; Members of the family have a C-terminal ferrodoxin domain, with eight ...
86-133 5.25e-06

EFR1 family ferrodoxin; Members of the family have a C-terminal ferrodoxin domain, with eight conserved Cys residues in two CxxCxxCxxxCP motifs, each of which binds a 4Fe-4S cluster. The N-terminal region resembles flavodoxin domains, with some members of the family recognized by Pfam models PF12724 (Flavodoxin_5) or PF00258 (Flavodoxin_1).


Pssm-ID: 468407 [Multi-domain]  Cd Length: 243  Bit Score: 48.32  E-value: 5.25e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 732683275  86 KCIGCKRCAIACPFGVVEMVD---TIAQKCDLCnqrssgtQACIEVCPTQA 133
Cdd:NF038196 186 KCIGCGICAKVCPVNNIEMEDgkpVWGHNCTHC-------LACIHRCPKEA 229
AlaDh_PNT_C smart01002
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the ...
312-344 5.32e-05

Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the NAD-dependent reversible reductive amination of pyruvate into alanine.


Pssm-ID: 214966 [Multi-domain]  Cd Length: 149  Bit Score: 43.65  E-value: 5.32e-05
                           10        20        30
                   ....*....|....*....|....*....|...
gi 732683275   312 KVAVIGAGPAGLGCADILARAGVQVDVFDRHPE 344
Cdd:smart01002  22 KVVVIGAGVVGLGAAATAKGLGAEVTVLDVRPA 54
 
Name Accession Description Interval E-value
PRK12809 PRK12809
putative oxidoreductase Fe-S binding subunit; Reviewed
1-639 0e+00

putative oxidoreductase Fe-S binding subunit; Reviewed


Pssm-ID: 183762 [Multi-domain]  Cd Length: 639  Bit Score: 1343.91  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275   1 MNKFIAAEAAECIGCHACEIACAVAHNQENWPLSHSDFRPRIHVVGKGQAANPVACHHCNNAPCVTACPVNALTFQSDSV 80
Cdd:PRK12809   1 MNKFIAAEAAECIGCHACEIACAVAHNQENWPLSHSDFRPRIHVVGKGQAANPVACHHCNNAPCVTACPVNALTFQSDSV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275  81 QLDEQKCIGCKRCAIACPFGVVEMVDTIAQKCDLCNQRSSGTQACIEVCPTQALRLMDDKGLQQIKVARQRKTAAGKASS 160
Cdd:PRK12809  81 QLDEQKCIGCKRCAIACPFGVVEMVDTIAQKCDLCNQRSSGTQACIEVCPTQALRLMDDKGLQQIKVARQRKTAAGKASS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275 161 DAQPSRSAALLPVNSRKGADKISASERKTHFGEIYCGLDPQQATYESDRCVYCAEKANCNWHCPLHNAIPDYIRLVQEGK 240
Cdd:PRK12809 161 DAQPSRSAALLPVNSRKGADKISASERKTHFGEIYCGLDPQQATYESDRCVYCAEKANCNWHCPLHNAIPDYIRLVQEGK 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275 241 IIEAAELCHQTSSLPEICGRVCPQDRLCEGACTLKDHSGAVSIGNLERYITDTALAMGWRPDVSKVVPRSEKVAVIGAGP 320
Cdd:PRK12809 241 IIEAAELCHQTSSLPEICGRVCPQDRLCEGACTLKDHSGAVSIGNLERYITDTALAMGWRPDVSKVVPRSEKVAVIGAGP 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275 321 AGLGCADILARAGVQVDVFDRHPEIGGMLTFGIPPFKLDKTVLSQRREIFTAMGIDFHLNCEIGRDITFSDLTSEYDAVF 400
Cdd:PRK12809 321 AGLGCADILARAGVQVDVFDRHPEIGGMLTFGIPPFKLDKTVLSQRREIFTAMGIDFHLNCEIGRDITFSDLTSEYDAVF 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275 401 IGVGTYGMMRADLPHEDAPGVIQALPFLTAHTRQLMGLPESEEYPLTDVEGKRVVVLGGGDTTMDCLRTSIRLNAASVTC 480
Cdd:PRK12809 401 IGVGTYGMMRADLPHEDAPGVIQALPFLTAHTRQLMGLPESEEYPLTDVEGKRVVVLGGGDTTMDCLRTSIRLNAASVTC 480
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275 481 AYRRDEVSMPGSRKEVVNAREEGVEFQFNVQPQYIACDEDGRLTAVGLIRTAMGEPGPDGRRRPRPVAGSEFELPADVLI 560
Cdd:PRK12809 481 AYRRDEVSMPGSRKEVVNAREEGVEFQFNVQPQYIACDEDGRLTAVGLIRTAMGEPGPDGRRRPRPVAGSEFELPADVLI 560
                        570       580       590       600       610       620       630
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 732683275 561 MAFGFQAHAMPWLQGSGIKLDKWGLIQTGDVGYLPTQTHLKKVFAGGDAVHGADLVVTAMAAGRQAARDMLTLFDTKAS 639
Cdd:PRK12809 561 MAFGFQAHAMPWLQGSGIKLDKWGLIQTGDVGYLPTQTHLKKVFAGGDAVHGADLVVTAMAAGRQAARDMLTLFDTKAS 639
PRK12769 PRK12769
putative oxidoreductase Fe-S binding subunit; Reviewed
1-631 0e+00

putative oxidoreductase Fe-S binding subunit; Reviewed


Pssm-ID: 183733 [Multi-domain]  Cd Length: 654  Bit Score: 937.63  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275   1 MNKFIAAEAAECIGCHACEIACAVAHNQENWPLSHSDFRPRIHVVGKGQAANPVACHHCNNAPCVTACPVNALTFQSDSV 80
Cdd:PRK12769   1 MNRFIMANSQQCLGCHACEIACVMAHNDEQHVLSQHHFHPRITVIKHQQQRSAVTCHHCEDAPCARSCPNGAISHVDDSI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275  81 QLDEQKCIGCKRCAIACPFGVVEMVDT---------IAQKCDLCNQRSSGtQACIEVCPTQALRLMDDKGLQQIKVARQR 151
Cdd:PRK12769  81 QVNQQKCIGCKSCVVACPFGTMQIVLTpvaagkvkaTAHKCDLCAGRENG-PACVENCPADALQLVTEQALSGMAKSRRL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275 152 KTA----AGKASSDAQPSrSAALLPVNSRKG------ADKISASERKTHFGEIYCGLDPQQATYESDRCVYCAEKANCNW 221
Cdd:PRK12769 160 RTArqehQPWHASTAAQE-MPAMSKVEQMQAtpprgePDKLAIEARKTGFDEIYLPFRADQAQREASRCLKCGEHSICEW 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275 222 HCPLHNAIPDYIRLVQEGKIIEAAELCHQTSSLPEICGRVCPQDRLCEGACTLKDHSGAVSIGNLERYITDTALAMGWRP 301
Cdd:PRK12769 239 TCPLHNHIPQWIELVKAGNIDAAVELSHQTNSLPEITGRVCPQDRLCEGACTLRDEYGAVTIGNIERYISDQALAKGWRP 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275 302 DVSKVVPRSEKVAVIGAGPAGLGCADILARAGVQVDVFDRHPEIGGMLTFGIPPFKLDKTVLSQRREIFTAMGIDFHLNC 381
Cdd:PRK12769 319 DLSQVTKSDKRVAIIGAGPAGLACADVLARNGVAVTVYDRHPEIGGLLTFGIPAFKLDKSLLARRREIFSAMGIEFELNC 398
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275 382 EIGRDITFSDLTSEYDAVFIGVGTYGMMRADLPHEDAPGVIQALPFLTAHTRQLMGLPESEEYPLTDVEGKRVVVLGGGD 461
Cdd:PRK12769 399 EVGKDISLESLLEDYDAVFVGVGTYRSMKAGLPNEDAPGVYDALPFLIANTKQVMGLEELPEEPFINTAGLNVVVLGGGD 478
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275 462 TTMDCLRTSIRLNAASVTCAYRRDEVSMPGSRKEVVNAREEGVEFQFNVQPQYIACDEDGRLTAVGLIRTAMGEPGPDGR 541
Cdd:PRK12769 479 TAMDCVRTALRHGASNVTCAYRRDEANMPGSKKEVKNAREEGANFEFNVQPVALELNEQGHVCGIRFLRTRLGEPDAQGR 558
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275 542 RRPRPVAGSEFELPADVLIMAFGFQAHAMPWLQGSGIKLDKWGLIQTGDVGYLPTQTHLKKVFAGGDAVHGADLVVTAMA 621
Cdd:PRK12769 559 RRPVPIPGSEFVMPADAVIMAFGFNPHGMPWLESHGVTVDKWGRIIADVESQYRYQTSNPKIFAGGDAVRGADLVVTAMA 638
                        650
                 ....*....|
gi 732683275 622 AGRQAARDML 631
Cdd:PRK12769 639 EGRHAAQGII 648
gltD_gamma_fam TIGR01318
glutamate synthase small subunit family protein, proteobacterial; This model represents one of ...
169-636 0e+00

glutamate synthase small subunit family protein, proteobacterial; This model represents one of three built for the NADPH-dependent or NADH-dependent glutamate synthase (EC 1.4.1.13 and 1.4.1.14, respectively) small subunit and homologs. TIGR01317 describes the small subunit (or equivalent region from longer forms) in eukaryotes, Gram-positive bacteria, and some other lineages, both NADH and NADPH-dependent. TIGR01316 describes a protein of similar length, from Archaea and a number of bacterial lineages, that forms glutamate synthase homotetramers without a large subunit. This model describes both glutatate synthase small subunit and closely related paralogs of unknown function from a number of gamma and alpha subdivision Proteobacteria, including E. coli.


Pssm-ID: 273553 [Multi-domain]  Cd Length: 467  Bit Score: 911.11  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275  169 ALLPVNSRKGADKISASERKTHFGEIYCGLDPQQATYESDRCVYCAEkANCNWHCPLHNAIPDYIRLVQEGKIIEAAELC 248
Cdd:TIGR01318   1 FQFIDLPRQDPDKIPVEERKTDFREIYGPFDKGQAQYQADRCLDCGN-PYCEWKCPVHNAIPQWLQLVQEGRIDEAAELS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275  249 HQTSSLPEICGRVCPQDRLCEGACTLKDHSGAVSIGNLERYITDTALAMGWRPDVSKVVPRSEKVAVIGAGPAGLGCADI 328
Cdd:TIGR01318  80 HQTNTLPEICGRVCPQDRLCEGACTLNDEGGAVTIGNLERYITDTALAMGWRPDLSHVQPTGKRVAVIGAGPAGLACADI 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275  329 LARAGVQVDVFDRHPEIGGMLTFGIPPFKLDKTVLSQRREIFTAMGIDFHLNCEIGRDITFSDLTSEYDAVFIGVGTYGM 408
Cdd:TIGR01318 160 LARAGVQVVVFDRHPEIGGLLTFGIPSFKLDKAVLSRRREIFTAMGIEFRLNCEVGRDISLDDLLEDYDAVFLGVGTYRS 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275  409 MRADLPHEDAPGVIQALPFLTAHTRQLMGLPESEEYPLTDVEGKRVVVLGGGDTTMDCLRTSIRLNAASVTCAYRRDEVS 488
Cdd:TIGR01318 240 MRGGLPGEDAPGVLPALPFLIANTRQLMGLPEEPEEPLIDVEGKRVVVLGGGDTAMDCVRTAIRLGATKVTCAYRRDEAN 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275  489 MPGSRKEVVNAREEGVEFQFNVQPQYIACDEDGRLTAVGLIRTAMGEPGPDGRRRPRPVAGSEFELPADVLIMAFGFQAH 568
Cdd:TIGR01318 320 MPGSRREVANAREEGVEFLFNVQPVSIESDEDGQVIGVTVVRTKLGEPDANGRRRPVPVAGSEFVLPADVVIMAFGFSPH 399
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 732683275  569 AMPWLQGSGIKLDKWGLIQTGDVGYLPTQTHLKKVFAGGDAVHGADLVVTAMAAGRQAARDMLTLFDT 636
Cdd:TIGR01318 400 LMPWLAAHGITLDSWGRIITALSSGLTYQTTNPKIFAGGDAVRGADLVVTAVAEGRDAAQGILDWLGV 467
gltD PRK12810
glutamate synthase subunit beta; Reviewed
176-631 0e+00

glutamate synthase subunit beta; Reviewed


Pssm-ID: 237213 [Multi-domain]  Cd Length: 471  Bit Score: 625.27  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275 176 RKGADKISASERKTHFGEIYCGLDPQQATYESDRCVYCAEkANCNWHCPLHNAIPDYIRLVQEGKIIEAAELCHQTSSLP 255
Cdd:PRK12810  12 RVDPKKRPVAERIKDFKEFYEPFSEEQAKIQAARCMDCGI-PFCHWGCPVHNYIPEWNDLVYRGRWEEAAERLHQTNNFP 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275 256 EICGRVCPQDrlCEGACTLKDHSGAVSIGNLERYITDTALAMGW-RPDvSKVVPRSEKVAVIGAGPAGLGCADILARAGV 334
Cdd:PRK12810  91 EFTGRVCPAP--CEGACTLNINFGPVTIKNIERYIIDKAFEEGWvKPD-PPVKRTGKKVAVVGSGPAGLAAADQLARAGH 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275 335 QVDVFDRHPEIGGMLTFGIPPFKLDKTVLSQRREIFTAMGIDFHLNCEIGRDITFSDLTSEYDAVFIGVGTYGMMRADLP 414
Cdd:PRK12810 168 KVTVFERADRIGGLLRYGIPDFKLEKEVIDRRIELMEAEGIEFRTNVEVGKDITAEELLAEYDAVFLGTGAYKPRDLGIP 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275 415 HEDAPGVIQALPFLTAHTRQLMGlpeSEEYPLTDVEGKRVVVLGGGDTTMDCLRTSIRLNAASVTcayRRDEVSMPGSRK 494
Cdd:PRK12810 248 GRDLDGVHFAMDFLIQNTRRVLG---DETEPFISAKGKHVVVIGGGDTGMDCVGTAIRQGAKSVT---QRDIMPMPPSRR 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275 495 -------------EVVNAREEGVEFQFNVQPQYIACdEDGRLTAVGLIRTAMGEPgpdgrrRPRPVAGSEFELPADVLIM 561
Cdd:PRK12810 322 nknnpwpywpmklEVSNAHEEGVEREFNVQTKEFEG-ENGKVTGVKVVRTELGEG------DFEPVEGSEFVLPADLVLL 394
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275 562 AFGFQAHAMPWLQGSGIKLDKWGLIQTGDVGYlptQTHLKKVFAGGDAVHGADLVVTAMAAGRQAARDML 631
Cdd:PRK12810 395 AMGFTGPEAGLLAQFGVELDERGRVAAPDNAY---QTSNPKVFAAGDMRRGQSLVVWAIAEGRQAARAID 461
GltD COG0493
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ...
187-630 0e+00

NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport and metabolism, General function prediction only]; NADPH-dependent glutamate synthase beta chain or related oxidoreductase is part of the Pathway/BioSystem: Glutamine biosynthesis


Pssm-ID: 440259 [Multi-domain]  Cd Length: 434  Bit Score: 611.37  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275 187 RKTHFGEIYCGLDPQQATYESDRCVYCAeKANCNWHCPLHNAIPDYIRLVQEGKIIEAAELCHQTSSLPEICGRVCPqdR 266
Cdd:COG0493    1 RIKDFREVYPGLSEEEAIEQAARCLDCG-DPPCQTGCPVGNDIPEWIRLIAEGDYEEALELIHETNPFPEVCGRVCP--A 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275 267 LCEGACTLKDHSGAVSIGNLERYITDTALAMGWRPDVSKVVPRSEKVAVIGAGPAGLGCADILARAGVQVDVFDRHPEIG 346
Cdd:COG0493   78 PCEGACVRGIVDEPVAIGALERFIADKAFEEGWVKPPPPAPRTGKKVAVVGSGPAGLAAAYQLARAGHEVTVFEALDKPG 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275 347 GMLTFGIPPFKLDKTVLSQRREIFTAMGIDFHLNCEIGRDITFSDLTSEYDAVFIGVGTYGMMRADLPHEDAPGVIQALP 426
Cdd:COG0493  158 GLLRYGIPEFRLPKDVLDREIELIEALGVEFRTNVEVGKDITLDELLEEFDAVFLATGAGKPRDLGIPGEDLKGVHSAMD 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275 427 FLTAHTRqlMGLPESeeyplTDVEGKRVVVLGGGDTTMDCLRTSIRLNAASVTCAYRRDEVSMPGSRKEVVNAREEGVEF 506
Cdd:COG0493  238 FLTAVNL--GEAPDT-----ILAVGKRVVVIGGGNTAMDCARTALRLGAESVTIVYRRTREEMPASKEEVEEALEEGVEF 310
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275 507 QFNVQPQYIACDEDGRLTAVGLIRTAMGEPGPDGRRRPRPVAGSEFELPADVLIMAFGFQAHAMPWLQGSGIKLDKWGLI 586
Cdd:COG0493  311 LFLVAPVEIIGDENGRVTGLECVRMELGEPDESGRRRPVPIEGSEFTLPADLVILAIGQTPDPSGLEEELGLELDKRGTI 390
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....
gi 732683275 587 QTGDVGYlptQTHLKKVFAGGDAVHGADLVVTAMAAGRQAARDM 630
Cdd:COG0493  391 VVDEETY---QTSLPGVFAGGDAVRGPSLVVWAIAEGRKAARAI 431
PRK11749 PRK11749
dihydropyrimidine dehydrogenase subunit A; Provisional
179-630 0e+00

dihydropyrimidine dehydrogenase subunit A; Provisional


Pssm-ID: 236967 [Multi-domain]  Cd Length: 457  Bit Score: 539.38  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275 179 ADKISASERKTHFGEIYCGLDPQQATYESDRCVYCaEKANCNWHCPLHNAIPDYIRLVQEGKIIEAAELCHQTSSLPEIC 258
Cdd:PRK11749  11 MPRQDAEERAQNFDEVAPGYTPEEAIEEASRCLQC-KDAPCVKACPVSIDIPEFIRLIAEGNLKGAAETILETNPLPAVC 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275 259 GRVCPQDRLCEGACTLKDHSGAVSIGNLERYITDTALAMGWRPDVsKVVPRSEKVAVIGAGPAGLGCADILARAGVQVDV 338
Cdd:PRK11749  90 GRVCPQERLCEGACVRGKKGEPVAIGRLERYITDWAMETGWVLFK-RAPKTGKKVAVIGAGPAGLTAAHRLARKGYDVTI 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275 339 FDRHPEIGGMLTFGIPPFKLDKTVLSQRREIFTAMGIDFHLNCEIGRDITFSDLTSEYDAVFIGVGTYG--MMRadLPHE 416
Cdd:PRK11749 169 FEARDKAGGLLRYGIPEFRLPKDIVDREVERLLKLGVEIRTNTEVGRDITLDELRAGYDAVFIGTGAGLprFLG--IPGE 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275 417 DAPGVIQALPFLTAhtrqlmglPESEEYPLTDVEGKRVVVLGGGDTTMDCLRTSIRLNAASVTCAYRRDEVSMPGSRKEV 496
Cdd:PRK11749 247 NLGGVYSAVDFLTR--------VNQAVADYDLPVGKRVVVIGGGNTAMDAARTAKRLGAESVTIVYRRGREEMPASEEEV 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275 497 VNAREEGVEFQFNVQPQYIACDEDGRlTAVGLIRTAMGEPGPDGRRRpRPVAGSEFELPADVLIMAFGFQAHAMPWLQGS 576
Cdd:PRK11749 319 EHAKEEGVEFEWLAAPVEILGDEGRV-TGVEFVRMELGEPDASGRRR-VPIEGSEFTLPADLVIKAIGQTPNPLILSTTP 396
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....
gi 732683275 577 GIKLDKWGLIQTGDVGYlptQTHLKKVFAGGDAVHGADLVVTAMAAGRQAARDM 630
Cdd:PRK11749 397 GLELNRWGTIIADDETG---RTSLPGVFAGGDIVTGAATVVWAVGDGKDAAEAI 447
PRK12831 PRK12831
putative oxidoreductase; Provisional
183-629 2.78e-124

putative oxidoreductase; Provisional


Pssm-ID: 183780 [Multi-domain]  Cd Length: 464  Bit Score: 375.90  E-value: 2.78e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275 183 SASERKTHFGEIYCGLDPQQATYESDRCVYCaEKANCNWHCPLHNAIPDYIRLVQEGKIIEAAELCHQTSSLPEICGRVC 262
Cdd:PRK12831  15 DPEVRATNFEEVCLGYNEEEAVKEASRCLQC-KKPKCVKGCPVSINIPGFISKLKEGDFEEAAKIIAKYNALPAVCGRVC 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275 263 PQDRLCEGACTLKDHSGAVSIGNLERYITDTALAMGWRPDvSKVVPRSEKVAVIGAGPAGLGCADILARAGVQVDVFDRH 342
Cdd:PRK12831  94 PQESQCEGKCVLGIKGEPVAIGKLERFVADWARENGIDLS-ETEEKKGKKVAVIGSGPAGLTCAGDLAKMGYDVTIFEAL 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275 343 PEIGGMLTFGIPPFKLDK-TVLSQRREIFTAMGIDFHLNCEIGRDITFSDLTSE--YDAVFIGVGTYGMMRADLPHEDAP 419
Cdd:PRK12831 173 HEPGGVLVYGIPEFRLPKeTVVKKEIENIKKLGVKIETNVVVGKTVTIDELLEEegFDAVFIGSGAGLPKFMGIPGENLN 252
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275 420 GVIQALPFLTahtRQLMGLPESEEYPLTDVEGKRVVVLGGGDTTMDCLRTSIRLnAASVTCAYRRDEVSMPGSRKEVVNA 499
Cdd:PRK12831 253 GVFSANEFLT---RVNLMKAYKPEYDTPIKVGKKVAVVGGGNVAMDAARTALRL-GAEVHIVYRRSEEELPARVEEVHHA 328
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275 500 REEGVEFQFNVQPQYIACDEDGRLTAVGLIRTAMGEPGPDGRRRPRPVAGSEFELPADVLIMAFGFQAHAMPWLQGSGIK 579
Cdd:PRK12831 329 KEEGVIFDLLTNPVEILGDENGWVKGMKCIKMELGEPDASGRRRPVEIEGSEFVLEVDTVIMSLGTSPNPLISSTTKGLK 408
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....
gi 732683275 580 LDKWGLI----QTGdvgylptQTHLKKVFAGGDAVHGADLVVTAMAAGRQAARD 629
Cdd:PRK12831 409 INKRGCIvadeETG-------LTSKEGVFAGGDAVTGAATVILAMGAGKKAAKA 455
PRK12778 PRK12778
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ...
176-630 1.12e-115

bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;


Pssm-ID: 237200 [Multi-domain]  Cd Length: 752  Bit Score: 362.91  E-value: 1.12e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275 176 RKGADKISASERKT-HFGEIYCGLDPQQATYESDRCVYCAeKANCNWHCPLHNAIPDYIRLVQEGKIIEAAELCHQTSSL 254
Cdd:PRK12778 296 RVPMPELDPEYRAHnRFEEVNLGLTKEQAMTEAKRCLDCK-NPGCVEGCPVGIDIPRFIKNIERGNFLEAAKILKETSAL 374
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275 255 PEICGRVCPQDRLCEGACT-LKDHSGAVSIGNLERYITDTALAMGwRPDVSKVVPRS-EKVAVIGAGPAGLGCADILARA 332
Cdd:PRK12778 375 PAVCGRVCPQEKQCESKCIhGKMGEEAVAIGYLERFVADYERESG-NISVPEVAEKNgKKVAVIGSGPAGLSFAGDLAKR 453
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275 333 GVQVDVFDRHPEIGGMLTFGIPPFKLDKTVLSQRREIFTAMGIDFHLNCEIGRDITFSDLTSE-YDAVFIGVGTyGMMR- 410
Cdd:PRK12778 454 GYDVTVFEALHEIGGVLKYGIPEFRLPKKIVDVEIENLKKLGVKFETDVIVGKTITIEELEEEgFKGIFIASGA-GLPNf 532
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275 411 ADLPHEDAPGVIQALPFLTahTRQLMGlPESEEYPLTDVEGKRVVVLGGGDTTMDCLRTSIRLNAASVTCAYRRDEVSMP 490
Cdd:PRK12778 533 MNIPGENSNGVMSSNEYLT--RVNLMD-AASPDSDTPIKFGKKVAVVGGGNTAMDSARTAKRLGAERVTIVYRRSEEEMP 609
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275 491 GSRKEVVNAREEGVEFQFNVQPQYIACDEDGRLTAVGLIRTAMGEPGPDGRRRPRPVAGSEFELPADVLIMAFGFQAHam 570
Cdd:PRK12778 610 ARLEEVKHAKEEGIEFLTLHNPIEYLADEKGWVKQVVLQKMELGEPDASGRRRPVAIPGSTFTVDVDLVIVSVGVSPN-- 687
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 732683275 571 PWLQGS--GIKLDKWGLIQTGDVgylpTQTHLKKVFAGGDAVHGADLVVTAMAAGRQAARDM 630
Cdd:PRK12778 688 PLVPSSipGLELNRKGTIVVDEE----MQSSIPGIYAGGDIVRGGATVILAMGDGKRAAAAI 745
gltA TIGR01316
glutamate synthase (NADPH), homotetrameric; This protein is homologous to the small subunit of ...
186-628 7.04e-111

glutamate synthase (NADPH), homotetrameric; This protein is homologous to the small subunit of NADPH and NADH forms of glutamate synthase as found in eukaryotes and some bacteria. This protein is found in numerous species having no homolog of the glutamate synthase large subunit. The prototype of the family, from Pyrococcus sp. KOD1, was shown to be active as a homotetramer and to require NADPH. [Amino acid biosynthesis, Glutamate family]


Pssm-ID: 130383 [Multi-domain]  Cd Length: 449  Bit Score: 340.69  E-value: 7.04e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275  186 ERKTHFGEIYCGLDPQQATYESDRCVYC-AEKANCNWHCPLHNAIPDYIRLVQEGKIIEAAELCHQTSSLPEICGRVCPQ 264
Cdd:TIGR01316   4 ERSKLFQEAALGYTEQLALVEAQRCLNCkDATKPCIKGCPVHVPIPEFIAKIQEGDFKGAVDIIKTTSLLPAICGRVCPQ 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275  265 DRLCEGACTL----KDHSGAVSIGNLERYITDTALAMGWRPDVSKVVPRSEKVAVIGAGPAGLGCADILARAGVQVDVFD 340
Cdd:TIGR01316  84 ERQCEGQCTVgkmfKDVGKPVSIGALERFVADWERQHGIETEPEKAPSTHKKVAVIGAGPAGLACASELAKAGHSVTVFE 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275  341 RHPEIGGMLTFGIPPFKLDKTVLSQRREIFTAMGIDFHLNCEIGRDITFSDLTSEYDAVFIGVGTYGMMRADLPHEDAPG 420
Cdd:TIGR01316 164 ALHKPGGVVTYGIPEFRLPKEIVVTEIKTLKKLGVTFRMNFLVGKTATLEELFSQYDAVFIGTGAGLPKLMNIPGEELCG 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275  421 VIQALPFLTAHTrqLMGLPESEEYPLTDVEGKRVVVLGGGDTTMDCLRTSIRLnAASVTCAYRRDEVSMPGSRKEVVNAR 500
Cdd:TIGR01316 244 VYSANDFLTRAN--LMKAYEFPHADTPVYAGKSVVVIGGGNTAVDSARTALRL-GAEVHCLYRRTREDMTARVEEIAHAE 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275  501 EEGVEFQFNVQPQYIACDEDGRLTAVGLIRTAMGEPGPDGRRRPRPVAGSEFELPADVLIMAFGFQAHAMPWlQGSGIKL 580
Cdd:TIGR01316 321 EEGVKFHFLCQPVEIIGDEEGNVRAVKFRKMDCQEQIDSGERRFLPCGDAECKLEADAVIVAIGNGSNPIMA-ETTRLKT 399
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*...
gi 732683275  581 DKWGLIQTGDvgylPTQTHLKKVFAGGDAVHGADLVVTAMAAGRQAAR 628
Cdd:TIGR01316 400 SERGTIVVDE----DQRTSIPGVFAGGDIILGAATVIRAMGQGKRAAK 443
PRK12771 PRK12771
putative glutamate synthase (NADPH) small subunit; Provisional
219-630 9.12e-101

putative glutamate synthase (NADPH) small subunit; Provisional


Pssm-ID: 237198 [Multi-domain]  Cd Length: 564  Bit Score: 318.36  E-value: 9.12e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275 219 CNWHCPLHNAIPDYIRLVQEGKIIEAAELCHQTSSLPEICGRVCPQDrlCEGACTLKDHSGAVSIGNLERYITDTALAMG 298
Cdd:PRK12771  49 CNAACPAGEDIRGWLALVRGGDYEYAWRRLTKDNPFPAVMGRVCYHP--CESGCNRGQVDDAVGINAVERFLGDYAIANG 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275 299 WRPDVSKVvPRSEKVAVIGAGPAGLGCADILARAGVQVDVFDRHPEIGGMLTFGIPPFKLDKTVLSQrrEI--FTAMGID 376
Cdd:PRK12771 127 WKFPAPAP-DTGKRVAVIGGGPAGLSAAYHLRRMGHAVTIFEAGPKLGGMMRYGIPAYRLPREVLDA--EIqrILDLGVE 203
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275 377 FHLNCEIGRDITFSDLTSEYDAVFIGVGTYGMMRADLPHEDAPGVIQALPFLTAHtrqlmglpESEEYPLTdveGKRVVV 456
Cdd:PRK12771 204 VRLGVRVGEDITLEQLEGEFDAVFVAIGAQLGKRLPIPGEDAAGVLDAVDFLRAV--------GEGEPPFL---GKRVVV 272
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275 457 LGGGDTTMDCLRTSIRLNAASVTCAYRRDEVSMPGSRKEVVNAREEGVEFQFNVQPQYIACDEDGRlTAVGLIRTAMGEP 536
Cdd:PRK12771 273 IGGGNTAMDAARTARRLGAEEVTIVYRRTREDMPAHDEEIEEALREGVEINWLRTPVEIEGDENGA-TGLRVITVEKMEL 351
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275 537 GPDGrrRPRPVAGSEFELPADVLIMAFGfQAHAMPWLQGSGIKLDKWGLIQTGDVGYLPTQthlKKVFAGGDAVHGADLV 616
Cdd:PRK12771 352 DEDG--RPSPVTGEEETLEADLVVLAIG-QDIDSAGLESVPGVEVGRGVVQVDPNFMMTGR---PGVFAGGDMVPGPRTV 425
                        410
                 ....*....|....
gi 732683275 617 VTAMAAGRQAARDM 630
Cdd:PRK12771 426 TTAIGHGKKAARNI 439
PRK12775 PRK12775
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin ...
98-632 1.49e-94

putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin domain-containing protein; Provisional


Pssm-ID: 183738 [Multi-domain]  Cd Length: 1006  Bit Score: 313.03  E-value: 1.49e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275   98 PFGVVEMVDTIAQKCD---LCN--QRSSGTQ---ACIEvCPTQALRLMDDKGLqqikVARQR--KTAAGKASSD-AQPSR 166
Cdd:PRK12775  202 PFGVKTMVSLNAIMVDgtgMCGscRVTVGGEvkfACVD-GPDFDGHKVDFKEL----HARQKrfKSQEDRANEDyAHVCN 276
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275  167 SAALLPVNSRKGADKIS-------------ASERKTHFGEIYCGLDPQQATYESDRCVYCAeKANCNWHCPLHNAIPDYI 233
Cdd:PRK12775  277 LEKQLFEEGKRNYKKLKtlvphqtpmperdAVERARNFKEVNLGYSLEDALQEAERCIQCA-KPTCIAGCPVQIDIPVFI 355
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275  234 RLVQEGKIIEAAELCHQTSSLPEICGRVCPQDRLCEGACTLKDHSGAVSIGNLERYITDTALAMGWRP-DVSKVVprsEK 312
Cdd:PRK12775  356 RHVVVRDFDGALEVIYEASIFPSICGRVCPQETQCEAQCIIAKKHESVGIGRLERFVGDNARAKPVKPpRFSKKL---GK 432
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275  313 VAVIGAGPAGLGCADILARAGVQVDVFDRHPEIGGMLTFGIPPFKLDKTVLSQRREIFTAMGIDFHLNCEIGRDITFSDL 392
Cdd:PRK12775  433 VAICGSGPAGLAAAADLVKYGVDVTVYEALHVVGGVLQYGIPSFRLPRDIIDREVQRLVDIGVKIETNKVIGKTFTVPQL 512
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275  393 TSE--YDAVFIGVGTYGMMRADLPHEDAPGVIQALPFLTahTRQLMGlpeSEEYPLTDVE---GKRVVVLGGGDTTMDCL 467
Cdd:PRK12775  513 MNDkgFDAVFLGVGAGAPTFLGIPGEFAGQVYSANEFLT--RVNLMG---GDKFPFLDTPislGKSVVVIGAGNTAMDCL 587
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275  468 RTSIRLNAASVTCAYRRDEVSMPGSRKEVVNAREEGVEFQFNVQPQYIACDEDGRLTAVGLIRTAMGEPGPDGRRRPRPV 547
Cdd:PRK12775  588 RVAKRLGAPTVRCVYRRSEAEAPARIEEIRHAKEEGIDFFFLHSPVEIYVDAEGSVRGMKVEEMELGEPDEKGRRKPMPT 667
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275  548 aGSEFELPADVLIMAFGFQAHAMPWLQGSGIKLDKWGLIQTGDVGYLPTQ-THLKKVFAGGDAVHGADLVVTAMAAGRQA 626
Cdd:PRK12775  668 -GEFKDLECDTVIYALGTKANPIITQSTPGLALNKWGNIAADDGKLESTQsTNLPGVFAGGDIVTGGATVILAMGAGRRA 746

                  ....*.
gi 732683275  627 ARDMLT 632
Cdd:PRK12775  747 ARSIAT 752
GOGAT_sm_gam TIGR01317
glutamate synthases, NADH/NADPH, small subunit; This model represents one of three built for ...
187-628 9.99e-94

glutamate synthases, NADH/NADPH, small subunit; This model represents one of three built for the NADPH-dependent or NADH-dependent glutamate synthase (EC 1.4.1.13 and 1.4.1.14, respectively) small subunit or homologous region. TIGR01316 describes a family in several archaeal and deeply branched bacterial lineages of a homotetrameric form for which there is no large subunit. Another model describes glutamate synthase small subunit from gamma and some alpha subdivision Proteobacteria plus paralogs of unknown function. This model describes the small subunit, or homologous region of longer forms proteins, of eukaryotes, Gram-positive bacteria, cyanobacteria, and some other lineages. All members with known function participate in NADH or NADPH-dependent reactions to interconvert between glutamine plus 2-oxoglutarate and two molecules of glutamate.


Pssm-ID: 162300 [Multi-domain]  Cd Length: 485  Bit Score: 297.51  E-value: 9.99e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275  187 RKTHFGEIYCGLDPQQATYESDRCVYCAEK-ANCNWHCPLHNAIPDYIRLVQEGKIIEAAELCHQTSSLPEICGRVCPQD 265
Cdd:TIGR01317  21 RLKDWKEFTNPFDKESAKYQAARCMDCGTPfCHNDSGCPLNNLIPEFNDLVFRGRWKEALDRLHATNNFPEFTGRVCPAP 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275  266 rlCEGACTLKDHSGAVSIGNLERYITDTALAMGW-RPDVSKVVPrSEKVAVIGAGPAGLGCADILARAGVQVDVFDRHPE 344
Cdd:TIGR01317 101 --CEGACTLGISEDPVGIKSIERIIIDKGFQEGWvQPRPPSKRT-GKKVAVVGSGPAGLAAADQLNRAGHTVTVFEREDR 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275  345 IGGMLTFGIPPFKLDKTVLSQRREIFTAMGIDFHLNCEIGRDITFSDLTSEYDAVFIGVGTYGMMRADLPHEDAPGVIQA 424
Cdd:TIGR01317 178 CGGLLMYGIPNMKLDKAIVDRRIDLLSAEGIDFVTNTEIGVDISADELKEQFDAVVLAGGATKPRDLPIPGRELKGIHYA 257
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275  425 LPFLTAHTRQLMGLPESEEYPLtDVEGKRVVVLGGGDTTMDCLRTSIRLNAASVTcayrRDEV--SMPGSRKE------- 495
Cdd:TIGR01317 258 MEFLPSATKALLGKDFKDIIFI-KAKGKKVVVIGGGDTGADCVGTSLRHGAASVH----QFEImpKPPEARAKdnpwpew 332
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275  496 -----VVNAREEGVEF------QFNVQPQYIACDEDGRLTAVGLIRTAMgEPGPDGRRRPRPVAGSEFELPADVLIMAFG 564
Cdd:TIGR01317 333 prvyrVDYAHEEAAAHygrdprEYSILTKEFIGDDEGKVTALRTVRVEW-KKSQDGKWQFVEIPGSEEVFEADLVLLAMG 411
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 732683275  565 FQAHAMPWLQGSGIKLDKWGLIQTGDVGYlptQTHLKKVFAGGDAVHGADLVVTAMAAGRQAAR 628
Cdd:TIGR01317 412 FVGPEQILLDDFGVKKTRRGNISAGYDDY---STSIPGVFAAGDCRRGQSLIVWAINEGRKAAA 472
PRK12814 PRK12814
putative NADPH-dependent glutamate synthase small subunit; Provisional
219-628 3.34e-83

putative NADPH-dependent glutamate synthase small subunit; Provisional


Pssm-ID: 139246 [Multi-domain]  Cd Length: 652  Bit Score: 274.68  E-value: 3.34e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275 219 CNWHCPLHNAIPDYIRLVQEGKIIEAAELCHQTSSLPEICGRVCPQDrlCEGACTLKDHSGAVSIGNLERYITDTALAMG 298
Cdd:PRK12814 104 CELACPAGCNIPGFIAAIARGDDREAIRIIKETIPLPGILGRICPAP--CEEACRRHGVDEPVSICALKRYAADRDMESA 181
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275 299 WRPdVSKVVPRS-EKVAVIGAGPAGLGCADILARAGVQVDVFDRHPEIGGMLTFGIPPFKLDKTVLSQRREIFTAMGIDF 377
Cdd:PRK12814 182 ERY-IPERAPKSgKKVAIIGAGPAGLTAAYYLLRKGHDVTIFDANEQAGGMMRYGIPRFRLPESVIDADIAPLRAMGAEF 260
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275 378 HLNCEIGRDITFSDLTSEYDAVFIGVGTYGMMRADLPHEDAPGVIQALPFLTAHTRQLMGLPeseeypltdveGKRVVVL 457
Cdd:PRK12814 261 RFNTVFGRDITLEELQKEFDAVLLAVGAQKASKMGIPGEELPGVISGIDFLRNVALGTALHP-----------GKKVVVI 329
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275 458 GGGDTTMDCLRTSIRLNAASVTCAYRRDEVSMPGSRKEVVNAREEGVEFQFNVQPQYIACDEDG-RLTAvglIRTAMGEP 536
Cdd:PRK12814 330 GGGNTAIDAARTALRLGAESVTILYRRTREEMPANRAEIEEALAEGVSLRELAAPVSIERSEGGlELTA---IKMQQGEP 406
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275 537 GPDGRRRPRPVAGSEFELPADVLIMAFGFQAHaMPWLQGSGIKLDKWGLIQTgDVGYLptQTHLKKVFAGGDAVHGADLV 616
Cdd:PRK12814 407 DESGRRRPVPVEGSEFTLQADTVISAIGQQVD-PPIAEAAGIGTSRNGTVKV-DPETL--QTSVAGVFAGGDCVTGADIA 482
                        410
                 ....*....|..
gi 732683275 617 VTAMAAGRQAAR 628
Cdd:PRK12814 483 INAVEQGKRAAH 494
PRK13984 PRK13984
putative oxidoreductase; Provisional
83-628 6.88e-81

putative oxidoreductase; Provisional


Pssm-ID: 172486 [Multi-domain]  Cd Length: 604  Bit Score: 267.40  E-value: 6.88e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275  83 DEQKCIGCKRCAIACPFGVVEMVDT---------IAQKCDLCNQRSSGTQACIEVCPTQALRLM---------------- 137
Cdd:PRK13984  43 DWEKCIGCGTCSKICPTDAITMVEVpdlpqeygkKPQRPVIDYGRCSFCALCVDICTTGSLKMTreyihispdpedfifm 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275 138 -DDKGLQQIKVARQRKTAAGKASSDaqpsrsaaLLPVnSRKGADKISASERKTHFGEIYCGLDPQQATYESDRCVYCAEk 216
Cdd:PRK13984 123 pTEKGINAKEPDNAPLGWVRDENSE--------LLDL-ERVEMEEIPPEERVKSFIEIVKGYSKEQAMQEAARCVECGI- 192
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275 217 anCNWHCPLHNAIPDYIRLVQEGKIIEAAELCHQTSSLPEICGRVCPQDrlCEGACTLKDHSGAVSIGNLERYITDTALA 296
Cdd:PRK13984 193 --CTDTCPAHMDIPQYIKAIYKDDLEEGLRWLYKTNPLSMVCGRVCTHK--CETVCSIGHRGEPIAIRWLKRYIVDNVPV 268
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275 297 MGWRPDVS-KVVPRSEKVAVIGAGPAGLGCADILARAGVQVDVFDRHPEIGGMLTFGIPPFKLDKTVLSQRREIFTAMGI 375
Cdd:PRK13984 269 EKYSEILDdEPEKKNKKVAIVGSGPAGLSAAYFLATMGYEVTVYESLSKPGGVMRYGIPSYRLPDEALDKDIAFIEALGV 348
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275 376 DFHLNCEIGRDITFSDLTSEYDAVFIGVGtYGMMRA-DLPHEDAPGVIQALPFLTAHTRQLMGLPESEEYPltdvegKRV 454
Cdd:PRK13984 349 KIHLNTRVGKDIPLEELREKHDAVFLSTG-FTLGRStRIPGTDHPDVIQALPLLREIRDYLRGEGPKPKIP------RSL 421
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275 455 VVLGGGDTTMDCLRTSIRLNAAS-------VTCaYRRDEVSMPGSRKEVVNAREEGVEFQFNVQPQYIACdEDGRLTAVG 527
Cdd:PRK13984 422 VVIGGGNVAMDIARSMARLQKMEygevnvkVTS-LERTFEEMPADMEEIEEGLEEGVVIYPGWGPMEVVI-ENDKVKGVK 499
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275 528 LIR-TAMGEpgPDGRRRPRPVAGSEFELPADVLIMAFGfQAHAMPWLQGSGIKLDKW--GLIQTGDVGylptQTHLKKVF 604
Cdd:PRK13984 500 FKKcVEVFD--EEGRFNPKFDESDQIIVEADMVVEAIG-QAPDYSYLPEELKSKLEFvrGRILTNEYG----QTSIPWLF 572
                        570       580
                 ....*....|....*....|....
gi 732683275 605 AGGDAVHGADlVVTAMAAGRQAAR 628
Cdd:PRK13984 573 AGGDIVHGPD-IIHGVADGYWAAE 595
PRK12770 PRK12770
putative glutamate synthase subunit beta; Provisional
308-630 1.31e-72

putative glutamate synthase subunit beta; Provisional


Pssm-ID: 237197 [Multi-domain]  Cd Length: 352  Bit Score: 237.97  E-value: 1.31e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275 308 PRSEKVAVIGAGPAGLGCADILARAGVQVDVFDRHPEIGGMLTFGIPPFKL-DKTVLSQRREIFTAmGIDFHLNCEI--- 383
Cdd:PRK12770  16 PTGKKVAIIGAGPAGLAAAGYLACLGYEVHVYDKLPEPGGLMLFGIPEFRIpIERVREGVKELEEA-GVVFHTRTKVccg 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275 384 ------------GRDITFSDLTSEYDAVFIGVGTYGMMRADLPHEDAPGVIQALPFLTA-HTRQLMGLPESEEYPltdVE 450
Cdd:PRK12770  95 eplheeegdefvERIVSLEELVKKYDAVLIATGTWKSRKLGIPGEDLPGVYSALEYLFRiRAAKLGYLPWEKVPP---VE 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275 451 GKRVVVLGGGDTTMDCLRTSIRLNAASVTCAYRRDEVSMPGSRKEVVNAREEGVEFQFNVQPqyIACDEDGRLTAVGLIR 530
Cdd:PRK12770 172 GKKVVVVGAGLTAVDAALEAVLLGAEKVYLAYRRTINEAPAGKYEIERLIARGVEFLELVTP--VRIIGEGRVEGVELAK 249
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275 531 TAMGEPGPDGRRRPRPVAGSEFELPADVLIMAFGFQAHAMPWLQGSGIKLDKWGLIQTGDVGylptQTHLKKVFAGGDAV 610
Cdd:PRK12770 250 MRLGEPDESGRPRPVPIPGSEFVLEADTVVFAIGEIPTPPFAKECLGIELNRKGEIVVDEKH----MTSREGVFAAGDVV 325
                        330       340
                 ....*....|....*....|
gi 732683275 611 HGADLVVTAMAAGRQAARDM 630
Cdd:PRK12770 326 TGPSKIGKAIKSGLRAAQSI 345
PRK12779 PRK12779
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; ...
211-630 7.28e-69

putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; Provisional


Pssm-ID: 183740 [Multi-domain]  Cd Length: 944  Bit Score: 241.27  E-value: 7.28e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275 211 VYCAEKANCNWHCPLHNAIPDYIRLVQEGKIIEAAELCHQTSSLPEICGRVCPQDRLCEGACTLKDHSgaVSIGNLERYI 290
Cdd:PRK12779 202 VLVQGKAEPKGGCPVKIHIPEMLDLLGNGKHREALELIESCNPLPNVTGRVCPQELQCQGVCTHTKRP--IEIGQLEWYL 279
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275 291 --------TDTALAMGWRPD--VSKVVPrseKVAVIGAGPAGLGCADILARAGVQVDVFDRHPEIGGMLTFGIPPFKLDK 360
Cdd:PRK12779 280 pqheklvnPNANERFAGRISpwAAAVKP---PIAVVGSGPSGLINAYLLAVEGFPVTVFEAFHDLGGVLRYGIPEFRLPN 356
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275 361 TVLSQRREIFTAMGIDFHLNCEIGRDITFSDLTSE-YDAVFIGVGTyGMMR-ADLPHEDAPGVIQALPFLTahTRQLM-G 437
Cdd:PRK12779 357 QLIDDVVEKIKLLGGRFVKNFVVGKTATLEDLKAAgFWKIFVGTGA-GLPTfMNVPGEHLLGVMSANEFLT--RVNLMrG 433
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275 438 LPESEEYPLTDVEGKRVVVLGGGDTTMDCLRTSIRLnAASVTCAYRRDEVSMPGSRKEVVNAREEGVEFQFNVQP-QYIA 516
Cdd:PRK12779 434 LDDDYETPLPEVKGKEVFVIGGGNTAMDAARTAKRL-GGNVTIVYRRTKSEMPARVEELHHALEEGINLAVLRAPrEFIG 512
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275 517 CDEDGRLTAVGLIRTAMGEPGPDGRRRPRPVAGSEfELPADVLIMAFGFQAHAMPWLQGSGIKLDKWGLIqtgDVGYLPT 596
Cdd:PRK12779 513 DDHTHFVTHALLDVNELGEPDKSGRRSPKPTGEIE-RVPVDLVIMALGNTANPIMKDAEPGLKTNKWGTI---EVEKGSQ 588
                        410       420       430
                 ....*....|....*....|....*....|....
gi 732683275 597 QTHLKKVFAGGDAVHGADLVVTAMAAGRQAARDM 630
Cdd:PRK12779 589 RTSIKGVYSGGDAARGGSTAIRAAGDGQAAAKEI 622
HycB_like cd10554
HycB, HydN and similar proteins; This family includes HycB, the FeS subunit of a ...
4-137 1.03e-60

HycB, HydN and similar proteins; This family includes HycB, the FeS subunit of a membrane-associated formate hydrogenlyase system (FHL-1) in Escherichia coli that breaks down formate, produced during anaerobic fermentation, to H2 and CO2. FHL-1 consists of formate dehydrogenase H (FDH-H) and the hydrogenase 3 complex (Hyd-3). HycB is thought to code for the [4Fe-4S] ferredoxin subunit of hydrogenase 3, which functions as an intermediate electron carrier protein between hydrogenase 3 and formate dehydrogenase. HydN codes for the [4Fe-4S] ferredoxin subunit of FDH-H; a hydN in-frame deletion mutation causes only weak reduction in hydrogenase activity, but loss of more than 60% of FDH-H activity. This pathway is only active at low pH and high formate concentrations, and is thought to provide a detoxification/de-acidification system countering the buildup of formate during fermentation.


Pssm-ID: 319876 [Multi-domain]  Cd Length: 149  Bit Score: 199.02  E-value: 1.03e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275   4 FIAAEAAECIGCHACEIACAVAHNQENWP---LSHSDFRPRIHVVGKGQAANPVACHHCNNAPCVTACPVNALTFQSDSV 80
Cdd:cd10554    1 FVIADPDKCIGCRTCEVACAAAHSGKGIFeagTDGLPFLPRLRVVKTGEVTAPVQCRQCEDAPCANVCPVGAISQEDGVV 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275  81 QLDEQKCIGCKRCAIACPFGVVEMVDT-------------IAQKCDLCNQRSSGTqACIEVCPTQALRLM 137
Cdd:cd10554   81 QVDEERCIGCKLCVLACPFGAIEMAPTtvpgvdwergpraVAVKCDLCAGREGGP-ACVEACPTKALTLV 149
HycB COG1142
Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion];
1-139 5.90e-57

Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion];


Pssm-ID: 440757 [Multi-domain]  Cd Length: 138  Bit Score: 188.71  E-value: 5.90e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275   1 MNKFIAAEAAECIGCHACEIACAVAHNQENWPLshsdFRPRIHVVGKGQAANPVACHHCNNAPCVTACPVNALTFQSDSV 80
Cdd:COG1142    1 MNKFIIADPEKCIGCRTCEAACAVAHEGEEGEP----FLPRIRVVRKAGVSAPVQCRHCEDAPCAEVCPVGAITRDDGAV 76
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 732683275  81 QLDEQKCIGCKRCAIACPFGVVEMVD----TIAQKCDLCNQRSSGtQACIEVCPTQALRLMDD 139
Cdd:COG1142   77 VVDEEKCIGCGLCVLACPFGAITMVGeksrAVAVKCDLCGGREGG-PACVEACPTGALRLVDV 138
Fer4_20 pfam14691
Dihydroprymidine dehydrogenase domain II, 4Fe-4S cluster; Domain II of the enzyme ...
187-299 1.40e-51

Dihydroprymidine dehydrogenase domain II, 4Fe-4S cluster; Domain II of the enzyme dihydroprymidine dehydrogenase binds FAD. Dihydroprymidine dehydrogenase catalyzes the first and rate-limiting step of pyrimidine degradation by converting pyrimidines to the corresponding 5,6- dihydro compounds. This domain carries two Fe4-S4 clusters.


Pssm-ID: 434132 [Multi-domain]  Cd Length: 113  Bit Score: 173.49  E-value: 1.40e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275  187 RKTHFGEIYCGLDPQQATYESDRCVYCAeKANCNWHCPLHNAIPDYIRLVQEGKIIEAAELCHQTSSLPEICGRVCPQDR 266
Cdd:pfam14691   1 RIKNFEEVALGYTEEEAIAEASRCLQCK-DPPCVKGCPVHIDIPEFIKLIAEGNFEGAARIILETNPLPAICGRVCPQER 79
                          90       100       110
                  ....*....|....*....|....*....|....
gi 732683275  267 LCEGACTL-KDHSGAVSIGNLERYITDTALAMGW 299
Cdd:pfam14691  80 QCEGACVLgKKGFEPVAIGRLERFAADWARENGI 113
PRK10330 PRK10330
electron transport protein HydN;
1-160 4.84e-41

electron transport protein HydN;


Pssm-ID: 182382 [Multi-domain]  Cd Length: 181  Bit Score: 147.34  E-value: 4.84e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275   1 MNKFIAAEAAECIGCHACEIACAVAH--NQENWPLSHSDFRPRIHVVGKGQAANPVACHHCNNAPCVTACPVNALTFQSD 78
Cdd:PRK10330   1 MNRFIIADASKCIGCRTCEVACVVSHqeNQDCASLTPETFLPRIHVIKGVNVSTATVCRQCEDAPCANVCPNGAISRDKG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275  79 SVQLDEQKCIGCKRCAIACPFGVVEMV-----------------DTIAQKCDLCNQRSSGTqACIEVCPTQALRLMDDKG 141
Cdd:PRK10330  81 FVHVMQERCIGCKTCVVACPYGAMEVVvrpvirnsgaglnvraeKAEANKCDLCNHREDGP-ACMAACPTHALICVDRNK 159
                        170
                 ....*....|....*....
gi 732683275 142 LQQIKVARQRKTAAGKASS 160
Cdd:PRK10330 160 LEQLSAEKRRRAALDSTAS 178
HybA COG0437
Fe-S-cluster-containing dehydrogenase component (DMSO reductase) [Energy production and ...
12-138 5.62e-37

Fe-S-cluster-containing dehydrogenase component (DMSO reductase) [Energy production and conversion];


Pssm-ID: 440206 [Multi-domain]  Cd Length: 184  Bit Score: 136.23  E-value: 5.62e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275  12 CIGCHACEIACAVAHNqenwpLSHSDFRPRIHVVGKGQAAN------PVACHHCNNAPCVTACPVNALTFQSD-SVQLDE 84
Cdd:COG0437   15 CIGCRACVVACKEENN-----LPVGVTWRRVRRYEEGEFPNvewlfvPVLCNHCDDPPCVKVCPTGATYKREDgIVLVDY 89
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 732683275  85 QKCIGCKRCAIACPFGVVEMVDT--IAQKCDLCNQRSSGTQ--ACIEVCPTQALRLMD 138
Cdd:COG0437   90 DKCIGCRYCVAACPYGAPRFNPEtgVVEKCTFCADRLDEGLlpACVEACPTGALVFGD 147
DMSOR_beta_like cd10550
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
5-136 1.93e-36

uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.


Pssm-ID: 319872 [Multi-domain]  Cd Length: 130  Bit Score: 132.70  E-value: 1.93e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275   5 IAAEAAECIGCHACEIACAVAHNQENWPlSHSdfrpRIHVVGKGQAA--NPVACHHCNNAPCVTACPVNALTFQSDS--V 80
Cdd:cd10550    1 LVVDPEKCTGCRTCELACSLKHEGVFNP-SLS----RIRVVRFEPEGldVPVVCRQCEDAPCVEACPVGAISRDEETgaV 75
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 732683275  81 QLDEQKCIGCKRCAIACPFGVVEM--VDTIAQKCDLCNqrssGTQACIEVCPTQALRL 136
Cdd:cd10550   76 VVDEDKCIGCGMCVEACPFGAIRVdpETGKAIKCDLCG----GDPACVKVCPTGALEF 129
DMSOR_beta_like cd16374
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
12-146 3.42e-36

uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.


Pssm-ID: 319896 [Multi-domain]  Cd Length: 139  Bit Score: 132.40  E-value: 3.42e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275  12 CIGCHACEIACAVAHNQenwplshsdfRPRIHV-VGKGQAANPVACHHCNNAPCVTACPVNALTFQSDS-VQLDEQKCIG 89
Cdd:cd16374    8 CIGCRACEIACAREHSG----------KPRISVeVVEDLASVPVRCRHCEDAPCMEVCPTGAIYRDEDGaVLVDPDKCIG 77
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 732683275  90 CKRCAIACPFGVVEMV--DTIAQKCDLC-NQRSSGTQ-ACIEVCPTQALRLMDDKGLQQIK 146
Cdd:cd16374   78 CGMCAMACPFGVPRFDpsLKVAVKCDLCiDRRREGKLpACVEACPTGALKFGDIEELLKEK 138
CooF_like cd10563
CooF, iron-sulfur subunit of carbon monoxide dehydrogenase; This family includes CooF, the ...
12-134 7.47e-36

CooF, iron-sulfur subunit of carbon monoxide dehydrogenase; This family includes CooF, the iron-sulfur subunit of carbon monoxide dehydrogenase (CODH), found in anaerobic bacteria and archaea. Carbon monoxide dehydrogenase is a key enzyme for carbon monoxide (CO) metabolism, where CooF is the proposed mediator of electron transfer between CODH and the CO-induced hydrogenase, catalyzing the reaction that uses CO as a single carbon and energy source, and producing only H2 and CO2. The ion-sulfur subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons in the protein complex during reaction.


Pssm-ID: 319885 [Multi-domain]  Cd Length: 140  Bit Score: 131.61  E-value: 7.47e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275  12 CIGCHACEIACAVAHNQENWPLSHSDF----RPRIHVVGKGQAANPVACHHCNNAPCVTACPVNALTF--QSDSVQLDEQ 85
Cdd:cd10563    9 CLGCKLCEVACAVAHSKSKDLIKAKLEkerpRPRIRVEESGGRSFPLQCRHCDEPPCVKACMSGAMHKdpETGIVIHDEE 88
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 732683275  86 KCIGCKRCAIACPFGVV--EMVDTIAQKCDLCNQRssGTQACIEVCPTQAL 134
Cdd:cd10563   89 KCVGCWMCVMVCPYGAIrpDKERKVALKCDLCPDR--ETPACVEACPTGAL 137
DMSOR_beta-like cd04410
Beta subunit of the DMSO Reductase (DMSOR) family; This family consists of the small beta ...
12-136 9.18e-34

Beta subunit of the DMSO Reductase (DMSOR) family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.


Pssm-ID: 319870 [Multi-domain]  Cd Length: 136  Bit Score: 125.58  E-value: 9.18e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275  12 CIGCHACEIACAVAHNQENWPlshsdFRPRIHVV---GKGQAANPVACHHCNNAPCVTACPVNALTFQSD-SVQLDEQKC 87
Cdd:cd04410    8 CIGCGTCEVACKQEHGLRPGP-----DWSRIKVIeggGLERAFLPVSCMHCEDPPCVKACPTGAIYKDEDgIVLIDEDKC 82
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 732683275  88 IGCKRCAIACPFGVVEMVDT--IAQKCDLCNQRSSGTQ--ACIEVCPTQALRL 136
Cdd:cd04410   83 IGCGSCVEACPYGAIVFDPEpgKAVKCDLCGDRLDEGLepACVKACPTGALTF 135
PsrB cd10551
polysulfide reductase beta (PsrB) subunit; This family includes the beta subunit of bacterial ...
12-134 5.91e-33

polysulfide reductase beta (PsrB) subunit; This family includes the beta subunit of bacterial polysulfide reductase (PsrABC), an integral membrane-bound enzyme responsible for quinone-coupled reduction of polysulfides, a process important in extreme environments such as deep-sea vents and hot springs. Polysulfide reductase contains three subunits: a catalytic subunit PsrA, an electron transfer PsrB subunit and the hydrophobic transmembrane PsrC subunit. PsrB belongs to the DMSO reductase superfamily that contains [4Fe-4S] clusters which transfer the electrons from the A subunit to the hydrophobic integral membrane C subunit via the B subunit. In Shewanella oneidensis, which has highly diverse anaerobic respiratory pathways, PsrABC is responsible for H2S generation as well as its regulation via respiration of sulfur species. PsrB transfers electrons from PsrC (serving as quinol oxidase) to the catalytic subunit PsrA for reduction of corresponding electron acceptors. It has been shown that T. thermophilus polysulfide reductase could be a key energy-conserving enzyme of the respiratory chain, using polysulfide as the terminal electron acceptor and pumping protons across the membrane.


Pssm-ID: 319873 [Multi-domain]  Cd Length: 185  Bit Score: 124.95  E-value: 5.91e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275  12 CIGCHACEIACAVAHNQenwPLSHsdFRPRIHVVGKGQAAN------PVACHHCNNAPCVTACPVNAlTFQSDS--VQLD 83
Cdd:cd10551    8 CIGCGACVVACKAENNV---PPGV--FRNRVLEYEVGEYPNvkrtflPVLCNHCENPPCVKVCPTGA-TYKREDgiVLVD 81
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 732683275  84 EQKCIGCKRCAIACPFGVVEMVDT--------------IAQKCDLCNQR-SSGTQ-ACIEVCPTQAL 134
Cdd:cd10551   82 YDKCIGCRYCMAACPYGARYFNPEephefgevpvrpkgVVEKCTFCYHRlDEGLLpACVEACPTGAR 148
DMSOR_beta_like cd16371
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
12-134 6.53e-31

uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.


Pssm-ID: 319893 [Multi-domain]  Cd Length: 140  Bit Score: 117.66  E-value: 6.53e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275  12 CIGCHACEIACAVAHNQEnwplSHSDFRpRIHVVGKGQAAN------PVACHHCNNAPCVTACPVNALTFQSD-SVQLDE 84
Cdd:cd16371    9 CIGCKACEIACKDKNDLP----PGVNWR-RVYEYEGGEFPEvfayflSMSCNHCENPACVKVCPTGAITKREDgIVVVDQ 83
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 732683275  85 QKCIGCKRCAIACPFGVVEM--VDTIAQKCDLCNQRSSGTQ--ACIEVCPTQAL 134
Cdd:cd16371   84 DKCIGCGYCVWACPYGAPQYnpETGKMDKCDMCVDRLDEGEkpACVAACPTRAL 137
HybA_like cd10561
the FeS subunit of hydrogenase 2; This subfamily includes the beta-subunit of hydrogenase 2 ...
12-154 3.93e-26

the FeS subunit of hydrogenase 2; This subfamily includes the beta-subunit of hydrogenase 2 (Hyd-2), an enzyme that catalyzes the reversible oxidation of H2 to protons and electrons. Hyd-2 is membrane-associated and forms an unusual heterotetrameric [NiFe]-hydrogenase in that it lacks the typical cytochrome b membrane anchor subunit that transfers electrons to the quinone pool. The electron transfer subunit of Hyd-2 (HybA) which is predicted to contain four iron-sulfur clusters, is essential for electron transfer from Hyd-2 to menaquinone/demethylmenaquinone (MQ/DMQ) to couple hydrogen oxidation to fumarate reduction.


Pssm-ID: 319883 [Multi-domain]  Cd Length: 196  Bit Score: 106.14  E-value: 3.93e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275  12 CIGCHACEIACAVAHNQENWPLSHSD--FRPR-----------IHVVGKGQAAN---PVACHHCNNAPCVTACPVNALTF 75
Cdd:cd10561    9 CIGCRACEVACKEWNGLPAEDTAFGPgwDNPRdlsaktytvikRYEVETGGKGFvfvKRQCMHCLDPACVSACPVGALRK 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275  76 QSD-SVQLDEQKCIGCKRCAIACPFGVVEM----VDTIAQKCDLCNQR-SSGTQ-ACIEVCPTQALRLMDDKGLqqIKVA 148
Cdd:cd10561   89 TPEgPVTYDEDKCIGCRYCMVACPFNIPKYewdsANPKIRKCTMCYDRlKEGKQpACVEACPTGALLFGKREEL--LAEA 166

                 ....*.
gi 732683275 149 RQRKTA 154
Cdd:cd10561  167 KRRIAA 172
DMSOR_beta_like cd16369
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
12-144 4.50e-26

uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.


Pssm-ID: 319891 [Multi-domain]  Cd Length: 172  Bit Score: 105.16  E-value: 4.50e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275  12 CIGCHACEIACAVAHNQENWPLSHSDFRPRIHVVgkgqAANPVACHHCNNAPCVTACPVNALTFQSDSVQL--DEQKCIG 89
Cdd:cd16369   11 CIGCRACVAACRECGTHRGKSMIHVDYIDRGEST----QTAPTVCMHCEDPTCAEVCPADAIKVTEDGVVQsaLKPRCIG 86
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 732683275  90 CKRCAIACPFGVVEMVDTIAQ--KCDLCNQRSSGTQA--CIEVCPTQALRLMDDKGLQQ 144
Cdd:cd16369   87 CSNCVNACPFGVPKYDEERNLmmKCDMCYDRTSVGKApmCASVCPSGALFYGTREEIQA 145
DMSOR_beta_like cd16367
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
12-138 4.45e-24

uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.


Pssm-ID: 319889 [Multi-domain]  Cd Length: 138  Bit Score: 98.15  E-value: 4.45e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275  12 CIGCHACEIACAVAHnqenwplshsDFRPRIHVVGkGQAAN---PVACHHCNNAPCVTACPVNALTFQSDSVQLDEQKCI 88
Cdd:cd16367   21 CIRCDNCEKACADTH----------DGHSRLDRNG-LRFGNllvPTACRHCVDPVCMIGCPTGAIHRDDGGEVVISDACC 89
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 732683275  89 GCKRCAIACPFGVVEMVdtIAQKCDLCNQRssGTQACIEVCPTQALRLMD 138
Cdd:cd16367   90 GCGNCASACPYGAIQMV--RAVKCDLCAGY--AGPACVSACPTGAAIRVN 135
TrxB COG0492
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
312-629 7.75e-24

Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440258 [Multi-domain]  Cd Length: 305  Bit Score: 102.51  E-value: 7.75e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275 312 KVAVIGAGPAGLGCADILARAGVQVDVFDRhPEIGGMLT------------FGIPPFKLDKTVLSQRR----EIFTAM-- 373
Cdd:COG0492    2 DVVIIGAGPAGLTAAIYAARAGLKTLVIEG-GEPGGQLAttkeienypgfpEGISGPELAERLREQAErfgaEILLEEvt 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275 374 GID-----FHLNCEIGRDITFsdltseyDAVFIGVGTyGMMRADLPHEDAP--------GVIQALPFltahtrqlmglpe 440
Cdd:COG0492   81 SVDkddgpFRVTTDDGTEYEA-------KAVIIATGA-GPRKLGLPGEEEFegrgvsycATCDGFFF------------- 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275 441 seeypltdvEGKRVVVLGGGDTTMDclrTSIRLN--AASVTCAYRRDEVSmpGSRKEVVNARE-EGVEFQFNVQPQYIac 517
Cdd:COG0492  140 ---------RGKDVVVVGGGDSALE---EALYLTkfASKVTLIHRRDELR--ASKILVERLRAnPKIEVLWNTEVTEI-- 203
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275 518 DEDGRLTAVGLIRTAMGEpgpdgrrrprpvagsEFELPADVLIMAFGFQAHAmPWLQGSGIKLDKWGLIQTGDVgylpTQ 597
Cdd:COG0492  204 EGDGRVEGVTLKNVKTGE---------------EKELEVDGVFVAIGLKPNT-ELLKGLGLELDEDGYIVVDED----ME 263
                        330       340       350
                 ....*....|....*....|....*....|...
gi 732683275 598 THLKKVFAGGDAVHGA-DLVVTAMAAGRQAARD 629
Cdd:COG0492  264 TSVPGVFAAGDVRDYKyRQAATAAGEGAIAALS 296
FDH_b_like cd10562
uncharacterized subfamily of beta subunit of formate dehydrogenase; This subfamily includes ...
10-134 2.05e-21

uncharacterized subfamily of beta subunit of formate dehydrogenase; This subfamily includes the beta-subunit of formate dehydrogenases that are as yet uncharacterized. Members of the DMSO reductase family include formate dehydrogenase N and O (FDH-N, FDH-O) and tungsten-containing formate dehydrogenase (W-FDH) and other similar proteins. FDH-N, a major component of nitrate respiration of Escherichia coli, is involved in the major anaerobic respiratory pathway in the presence of nitrate, catalyzing the oxidation of formate to carbon dioxide at the expense of nitrate reduction to nitrite. It forms a heterotrimer; the alpha-subunit (FDH-G) is the catalytic site of formate oxidation and membrane-associated, incorporating a selenocysteine (SeCys) residue and a [4Fe/4S] cluster in addition to two bis-MGD cofactors, the beta subunit (FDH-H) contains four [4Fe/4S] clusters which transfer the electrons from the alpha subunit to the gamma-subunit (FDH-I), a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. W-FDH contains a tungsten instead of molybdenum at the catalytic center. This enzyme seems to be exclusively found in organisms such as hyperthermophilic archaea that live in extreme environments. It is a heterodimer of a large and a small subunit; the large subunit harbors the W site and one [4Fe-4S] center and the small subunit, containing three [4Fe-4S] clusters, functions to transfer electrons.


Pssm-ID: 319884 [Multi-domain]  Cd Length: 161  Bit Score: 91.21  E-value: 2.05e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275  10 AECIGCHACEIAC-----------AVAHNQENWPLSHSDFRPRIHVVGKGQAANPV-------ACHHCNNAPCVTACPVN 71
Cdd:cd10562    6 SKCTACRGCQVACkqwnqlpaektPFTGSYQNPPDLTPNTWTLIRFYEHEEDNGGIrwlfrkrQCMHCTDAACVKVCPTG 85
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 732683275  72 ALTFQSD-SVQLDEQKCIGCKRCAIACPFGVVEMVDTI--AQKCDLCNQR-SSGTQ-ACIEVCPTQAL 134
Cdd:cd10562   86 ALYKTENgAVVVDEDKCIGCGYCVAACPFDVPRYDETTnkITKCTLCFDRiENGMQpACVKTCPTGAL 153
FDH-O_like cd10560
beta subunit of formate dehydrogenase O (FDH-O) and similar proteins; This subfamily includes ...
12-163 4.08e-21

beta subunit of formate dehydrogenase O (FDH-O) and similar proteins; This subfamily includes beta subunit of formate dehydrogenase family O (FDH-O), which is highly homologous to formate dehydrogenase N (FDH-N), a member of the DMSO reductase family. In E. coli three formate dehydrogenases are synthesized that are capable of oxidizing formate; Fdh-H, couples formate disproportionation to hydrogen and CO2, and is part of the cytoplasmically oriented formate hydrogenlyase complex, while FDH-N and FDH-O indicate their respective induction after growth with nitrate and oxygen. Little is known about FDH-O, although it shows formate oxidase activity during aerobic growth and is also synthesized during nitrate respiration, similar to FDH-N.


Pssm-ID: 319882 [Multi-domain]  Cd Length: 225  Bit Score: 92.45  E-value: 4.08e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275  12 CIGCHACEIACA------------VAHNQENWP-LSHSDFRpriHV--VGKGQAANPV-------------ACHHCNNAP 63
Cdd:cd10560    9 CIGCKACEVACKqwnqlpadgydfSGMSYDNTGdLSASTWR---HVkfIERPTEDGPAneggdlqwlfmsdVCKHCTDAG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275  64 CVTACPVNALTF-QSDSVQLDEQKCIGCKRCAIACPFGVVEM--VDTIAQKCDLCNQRSSGTQ--ACIEVCPTQALRLMD 138
Cdd:cd10560   86 CLEACPTGAIFRtEFGTVYIQPDICNGCGYCVAACPFGVIDRneETGRAHKCTLCYDRLKDGLepACAKACPTGSIQFGP 165
                        170       180
                 ....*....|....*....|....*.
gi 732683275 139 DKGLQQIkvARQR-KTAAGKASSDAQ 163
Cdd:cd10560  166 LEELRER--ARARvEQLHEQGVVEAY 189
FDH_beta_like cd16366
beta FeS subunits of formate dehydrogenase N (FDH-N) and similar proteins; This family ...
12-134 8.37e-21

beta FeS subunits of formate dehydrogenase N (FDH-N) and similar proteins; This family contains beta FeS subunits of several dehydrogenases in the DMSO reductase superfamily, including formate dehydrogenase N (FDH-N), tungsten-containing formate dehydrogenase (W-FDH) and other similar proteins. FDH-N is a major component of nitrate respiration of Escherichia coli; it catalyzes the oxidation of formate to carbon dioxide, donating the electrons to a second substrate to a cytochrome. W-FDH contains a tungsten instead of molybdenum at the catalytic center and seems to be exclusively found in organisms such as hyperthermophilic archaea that live in extreme environments. It catalyzes the oxidation of formate to carbon dioxide, donating the electrons to a second substrate.


Pssm-ID: 319888 [Multi-domain]  Cd Length: 156  Bit Score: 89.38  E-value: 8.37e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275  12 CIGCHACEIACAVAHNQ-----ENW--------PLSHSDFRPRIHVVGKGQAA-----NPVACHHCNNAPCVTACPVNAL 73
Cdd:cd16366    8 CTGCRACQVACKQWNGLpaektEFTgsyqnppdLTAHTWTLVRFYEVEKPGGDlswlfRKDQCMHCTDAGCLAACPTGAI 87
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 732683275  74 tFQSDS--VQLDEQKCIGCKRCAIACPFGVVEM--VDTIAQKCDLCNQRSSGTQ--ACIEVCPTQAL 134
Cdd:cd16366   88 -IRTETgtVVVDPETCIGCGYCVNACPFDIPRFdeETGRVAKCTLCYDRISNGLqpACVKTCPTGAL 153
FDH-N cd10558
The beta FeS subunit of formate dehydrogenase-N (FDH-N); This subfamily contains beta FeS ...
8-151 2.29e-20

The beta FeS subunit of formate dehydrogenase-N (FDH-N); This subfamily contains beta FeS subunit of formate dehydrogenase-N (FDH-N), a member of the DMSO reductase family. FDH-N is involved in the major anaerobic respiratory pathway in the presence of nitrate, catalyzing the oxidation of formate to carbon dioxide at the expense of nitrate reduction to nitrite. Thus, FDH-N is a major component of nitrate respiration of Escherichia coli. This integral membrane enzyme forms a heterotrimer; the alpha-subunit (FDH-G) is the catalytic site of formate oxidation and membrane-associated, incorporating a selenocysteine (SeCys) residue and a [4Fe/4S] cluster in addition to two bis-MGD cofactors, the beta subunit (FDH-H) contains four [4Fe/4S] clusters which transfer the electrons from the alpha subunit to the gamma-subunit (FDH-I), a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups.


Pssm-ID: 319880 [Multi-domain]  Cd Length: 208  Bit Score: 89.75  E-value: 2.29e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275   8 EAAECIGCHACEIACavahnqENWplshSDFRPRI-HVVGKGQaaNPV----------------------------ACHH 58
Cdd:cd10558    5 DVSKCIGCKACQVAC------KEW----NDLRAEVgHNVGTYQ--NPAdlspetwtlmkfrevedngklewlirkdGCMH 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275  59 CNNAPCVTACP-VNAL-TFQSDSVQLDEQKCIGCKRCAIACPFGV--VEMVDTIAQKCDLCNQRSSGTQ--ACIEVCPTQ 132
Cdd:cd10558   73 CADPGCLKACPsPGAIvQYANGIVDFQSDKCIGCGYCIKGCPFDIprISKDDNKMYKCTLCSDRVSVGLepACVKTCPTG 152
                        170
                 ....*....|....*....
gi 732683275 133 ALRLmDDKGlQQIKVARQR 151
Cdd:cd10558  153 ALHF-GTKE-DMLALAEKR 169
TH_beta_N cd10552
N-terminal FeS domain of pyrogallol-phloroglucinol transhydroxylase (TH), beta subunit; This ...
10-138 5.32e-20

N-terminal FeS domain of pyrogallol-phloroglucinol transhydroxylase (TH), beta subunit; This family includes the beta subunit of pyrogallol-phloroglucinol transhydroxylase (TH), a cytoplasmic molybdenum (Mo) enzyme from anaerobic microorganisms like Pelobacter acidigallici and Desulfitobacterium hafniense which catalyzes the conversion of pyrogallol to phloroglucinol, an important building block of plant polymers. TH belongs to the DMSO reductase (DMSOR) family; it is a heterodimer consisting of a large alpha catalytic subunit and a small beta FeS subunit. The beta subunit has two domains with the N-terminal domain containing three [4Fe-4S] centers and a seven-stranded, mainly antiparallel beta-barrel domain. In the anaerobic bacterium Pelobacter acidigallici, gallic acid, pyrogallol, phloroglucinol, or phloroglucinol carboxylic acid are fermented to three molecules of acetate (plus CO2), and TH is the key enzyme in the fermentation pathway, which converts pyrogallol to phloroglucinol in the absence of O2.


Pssm-ID: 319874 [Multi-domain]  Cd Length: 186  Bit Score: 88.15  E-value: 5.32e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275  10 AECIGCHACEIACAVAHNQENWP---LSHSD---FRPRIHVVGKGQAAN------PVACHHCNNAPCVTACPVNALTFQS 77
Cdd:cd10552    6 AKCNGCYNCFLACKDEHVGNDWPgyaAPQPRhghFWMRILRRERGQYPKvdvaylPVPCNHCDNAPCIKAAKDGAVYKRD 85
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 732683275  78 DS-VQLDEQKCIGCKRCAIACPFGVVEMVDT--IAQKCDLCNQ---RSSGTQACIEVCPTQALRLMD 138
Cdd:cd10552   86 DGiVIIDPEKAKGQKQLVDACPYGAIYWNEElqVPQKCTFCAHlldDGWKEPRCVQACPTGALRFGK 152
PhsB_like cd10553
uncharacterized beta subfamily of DMSO Reductase similar to Desulfonauticus sp PhsB; This ...
12-136 5.48e-20

uncharacterized beta subfamily of DMSO Reductase similar to Desulfonauticus sp PhsB; This family includes beta FeS subunits of anaerobic DMSO reductase (DMSOR) superfamily that have yet to be characterized. DMSOR consists of a large, periplasmic molybdenum-containing alpha subunit as well as a small beta FeS subunit, and may also have a small gamma subunit. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and the tungsten-containing formate dehydrogenase (FDH-T). Examples of heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.


Pssm-ID: 319875 [Multi-domain]  Cd Length: 146  Bit Score: 86.65  E-value: 5.48e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275  12 CIGCHACEIACAVAHNQENWPL--SHSDFRPRIhVVGKGQAANP-VACHHCNNAPCVTACPVNALTFQSDS--VQLDEQK 86
Cdd:cd10553   12 CIGCLACEVHCKVKNNLPVGPRlcRIFAVGPKM-VGGKPRLKFVyMSCFHCENPWCVKACPTGAMQKREKDgiVYVDQEL 90
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 732683275  87 CIGCKRCAIACPFGVV---EMVDTIAqKCDLCNQR-SSGTQ-ACIEVCPTQALRL 136
Cdd:cd10553   91 CIGCKACIEACPWGIPqwnPATGKVV-KCDYCMDRiDQGLKpACVTGCTTHALSF 144
PRK10882 PRK10882
hydrogenase 2 operon protein HybA;
12-133 7.84e-20

hydrogenase 2 operon protein HybA;


Pssm-ID: 236786 [Multi-domain]  Cd Length: 328  Bit Score: 90.88  E-value: 7.84e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275  12 CIGCHACEIACA-VAHNQEN------W--PLSHSDF-RPRIHV------VGKGQAANPVA-----CHHCNNAPCVTACPV 70
Cdd:PRK10882  47 CVGCQACVTKCQeINFPERNpqgeqtWdnPDKLSPYtNNIIKVwksgtgVNKDQEENGYAyikkqCMHCVDPNCVSVCPV 126
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 732683275  71 NALTFQSDS--VQLDEQKCIGCKRCAIACPFGV--VEMVDTIAQ--KCDLCNQRS------SGTQACIEVCPTQA 133
Cdd:PRK10882 127 SALTKDPKTgiVHYDKDVCTGCRYCMVACPFNVpkYDYNNPFGAihKCELCNQKGverldkGGLPGCVEVCPTGA 201
DMSOR_beta_like cd16372
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
3-138 9.93e-20

uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.


Pssm-ID: 319894 [Multi-domain]  Cd Length: 125  Bit Score: 85.47  E-value: 9.93e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275   3 KFIAAEAAECIGCHACEIACAVAHNQENWPLshsdfRPRIHVVGKGQAANPVACHHCNNapCVTACPVNALTF-QSDSVQ 81
Cdd:cd16372    1 KLLVTDPEKCIGCLQCEEACSKTFFKEEDRE-----KSCIRITETEGGYAINVCNQCGE--CIDVCPTGAITRdANGVVM 73
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 732683275  82 LDEQKCIGCKRCAIACPFGVVEMVDTIAQ--KCDLCNqrssgtqACIEVCPTQALRLMD 138
Cdd:cd16372   74 INKKLCVGCLMCVGFCPEGAMFKHEDYPEpfKCIACG-------ICVKACPTGALELVE 125
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
312-623 1.47e-18

Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.


Pssm-ID: 400379 [Multi-domain]  Cd Length: 301  Bit Score: 86.60  E-value: 1.47e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275  312 KVAVIGAGPAGLGCADILARAGVQVDVFDR---HPEIGGMLTFGI-------PPFKLDKTVLSQRREIFTAM--GIDFHL 379
Cdd:pfam07992   2 DVVVIGGGPAGLAAALTLAQLGGKVTLIEDegtCPYGGCVLSKALlgaaeapEIASLWADLYKRKEEVVKKLnnGIEVLL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275  380 NCEI------GRDITFSDLTS------EYDAVFIGVGTygmmRADLPheDAPGVIQALPFLTAHtrqlmglPESEEYPLT 447
Cdd:pfam07992  82 GTEVvsidpgAKKVVLEELVDgdgetiTYDRLVIATGA----RPRLP--PIPGVELNVGFLVRT-------LDSAEALRL 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275  448 DVEGKRVVVLGGGDTTMDCLRTSIRLnAASVTCAYRRDEVsMPGSRKEVVNA-----REEGVEFQFNVQPQYIACDEDGR 522
Cdd:pfam07992 149 KLLPKRVVVVGGGYIGVELAAALAKL-GKEVTLIEALDRL-LRAFDEEISAAlekalEKNGVEVRLGTSVKEIIGDGDGV 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275  523 LTAVGlirtamgepgpDGRrrprpvagsefELPADVLIMAFGFQAhAMPWLQGSGIKLDKWGLIQTGDvgYLptQTHLKK 602
Cdd:pfam07992 227 EVILK-----------DGT-----------EIDADLVVVAIGRRP-NTELLEAAGLELDERGGIVVDE--YL--RTSVPG 279
                         330       340
                  ....*....|....*....|..
gi 732683275  603 VFAGGD-AVHGADLVVTAMAAG 623
Cdd:pfam07992 280 IYAAGDcRVGGPELAQNAVAQG 301
PLN02852 PLN02852
ferredoxin-NADP+ reductase
304-468 8.80e-18

ferredoxin-NADP+ reductase


Pssm-ID: 215457  Cd Length: 491  Bit Score: 86.67  E-value: 8.80e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275 304 SKVVPRSEKVAVIGAGPAGLGCADILARA--GVQVDVFDRHPEIGGMLTFGIPPFKLD-KTVLSQRREIFTAMGIDFHLN 380
Cdd:PLN02852  20 SSSTSEPLHVCVVGSGPAGFYTADKLLKAhdGARVDIIERLPTPFGLVRSGVAPDHPEtKNVTNQFSRVATDDRVSFFGN 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275 381 CEIGRDITFSDLTSEYDAVFIGVGTYGMMRADLPHEDAPGVIQALPFLTAHTrqlmGLPESEEYPLTDVEGKRVVVLGGG 460
Cdd:PLN02852 100 VTLGRDVSLSELRDLYHVVVLAYGAESDRRLGIPGEDLPGVLSAREFVWWYN----GHPDCVHLPPDLKSSDTAVVLGQG 175

                 ....*...
gi 732683275 461 DTTMDCLR 468
Cdd:PLN02852 176 NVALDCAR 183
PRK09898 PRK09898
ferredoxin-like protein;
7-138 1.23e-17

ferredoxin-like protein;


Pssm-ID: 182135 [Multi-domain]  Cd Length: 208  Bit Score: 81.81  E-value: 1.23e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275   7 AEAAECIGCHACEIACAVAHNQENWPLSHsdfRPRIHV----------VGKGQAAN----PVACHHCNNAPCVTACPVNA 72
Cdd:PRK09898  63 TQRARCTGCHRCEISCTNFNDGSVGTFFS---RIKIHRnyffgdngvgSGGGLYGDlnytADTCRQCKEPQCMNVCPIGA 139
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275  73 LTFQSD--SVQLDEQKCIGCKRCAIACPFGV--VEMVDTIAQKCDLCNqrssgtqACIEVCPTQALRLMD 138
Cdd:PRK09898 140 ITWQQKegCITVDHKRCIGCSACTTACPWMMatVNTESKKSSKCVLCG-------ECANACPTGALKIIE 202
PRK14993 PRK14993
tetrathionate reductase subunit TtrB;
12-147 1.39e-16

tetrathionate reductase subunit TtrB;


Pssm-ID: 184955 [Multi-domain]  Cd Length: 244  Bit Score: 79.53  E-value: 1.39e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275  12 CIGCHACEIACAVaHNQenwpLSHSDFRPRI---HVVGKGQAAN-----PVACHHCNNAPCVTACPVNAlTFQSDS--VQ 81
Cdd:PRK14993  53 CIGCQSCTVSCTI-ENQ----TPQGAFRTTVnqyQVQREGSQEVtnvllPRLCNHCDNPPCVPVCPVQA-TFQREDgiVV 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275  82 LDEQKCIGCKRCAIACPFGV--VEMVDTIAQKCDLCNQRSSG--TQACIEVC------------PTQALRLMDDKGLQQI 145
Cdd:PRK14993 127 VDNKRCVGCAYCVQACPYDArfINHETQTADKCTFCVHRLEAglLPACVESCvggariigdikdPHSRIATMLHQHRDAI 206

                 ..
gi 732683275 146 KV 147
Cdd:PRK14993 207 KV 208
DMSOR_beta_like cd16370
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
12-136 3.90e-15

uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.


Pssm-ID: 319892 [Multi-domain]  Cd Length: 131  Bit Score: 72.31  E-value: 3.90e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275  12 CIGCHACEIACAVAHNQenwplSHSDFRPRIHVVGKG---QAANPVACHHCNNAPCVTACPVNALTFQSD-SVQLDEQKC 87
Cdd:cd16370   11 CIGCYSCMLACSRRVHK-----SASLSKSAIRVRTRGgleGGFTVVVCRACEDPPCAEACPTGALEPRKGgGVVLDKEKC 85
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 732683275  88 IGCKRCAIACPFGVVEMvDTIAQKCDLCNQrssgTQACIEVCPTQALRL 136
Cdd:cd16370   86 IGCGNCVKACIVGAIFW-DEETNKPIICIH----CGYCARYCPHDVLAM 129
Fer4_11 pfam13247
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
56-138 1.46e-13

4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich. Domain contains two 4Fe4S clusters.


Pssm-ID: 404184 [Multi-domain]  Cd Length: 99  Bit Score: 66.89  E-value: 1.46e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275   56 CHHCNNAPCVTACPVNALTFQSDS--VQLDEQKCIGCKRCAIACPFGVVEMVDT--IAQKCDLCNQRSSGTQ--ACIEVC 129
Cdd:pfam13247  10 CRHCLNPPCKASCPVGAIYKDEETgaVLLDEKTCRGWRECVSACPYNIPRYNDEtgKAEKCDMCYDRVEAGLlpACVQTC 89

                  ....*....
gi 732683275  130 PTQALRLMD 138
Cdd:pfam13247  90 PTGAMNFGD 98
CzcO COG2072
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ...
313-606 8.77e-13

Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ion transport and metabolism];


Pssm-ID: 441675 [Multi-domain]  Cd Length: 414  Bit Score: 70.66  E-value: 8.77e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275 313 VAVIGAGPAGLGCADILARAGVQVDVFDRHPEIGG---------------MLTFGIP--PFKLDKTVLSQRREIF----- 370
Cdd:COG2072    9 VVVIGAGQAGLAAAYHLRRAGIDFVVLEKADDVGGtwrdnrypglrldtpSHLYSLPffPNWSDDPDFPTGDEILaylea 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275 371 TA----MGIDFHLNCEIgRDITFSDLTS------------EYDAVFIGVGTYGmmRADLPH----EDAPGVIqalpFLTA 430
Cdd:COG2072   89 YAdkfgLRRPIRFGTEV-TSARWDEADGrwtvttddgetlTARFVVVATGPLS--RPKIPDipglEDFAGEQ----LHSA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275 431 HtrqlmgLPESEEYPltdveGKRVVVLGGGDTTMDCLrTSIRLNAASVTCAYRRDEVSMPgsRKEVVNAREEGVEFQFNV 510
Cdd:COG2072  162 D------WRNPVDLA-----GKRVLVVGTGASAVQIA-PELARVAAHVTVFQRTPPWVLP--RPNYDPERGRPANYLGLE 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275 511 QPqYIACDEDGRLTAVGLIRTAMGEPgPDGRRRP-------RPVAGSEF------------------------------E 553
Cdd:COG2072  228 AP-PALNRRDARAWLRRLLRAQVKDP-ELGLLTPdyppgckRPLLSTDYyealrrgnvelvtggieritedgvvfadgtE 305
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 732683275 554 LPADVLIMAFGFQAhAMPWLQGSGIkldkwgliqTGDVGYLPTQTHLKKVFAG 606
Cdd:COG2072  306 HEVDVIVWATGFRA-DLPWLAPLDV---------RGRDGRSGPRAYLGVVVPG 348
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
52-140 2.87e-12

Uncharacterized polyferredoxin-like protein; This family contains uncharacterized polyferredoxin protein similar to Methanobacterium thermoautotrophicum MvhB. The mvhB is a gene of the methylviologen-reducing hydrogenase operon. It is predicted to contain 12 [4Fe-4S] clusters, and was therefore suggested to be a polyferredoxin. As a subfamily of the beta subunit of the DMSO Reductase (DMSOR) family, it is predicted to function as electron carrier in the reducing reaction.


Pssm-ID: 319871 [Multi-domain]  Cd Length: 128  Bit Score: 63.96  E-value: 2.87e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275  52 NPVACHHCNNapCVTACPVNALTFQSD-----SVQLDEQKCIGCKRCAIACPFGVVEMVDTIAQ-------------KCD 113
Cdd:cd10549    4 DPEKCIGCGI--CVKACPTDAIELGPNgaiarGPEIDEDKCVFCGACVEVCPTGAIELTPEGKEyvpkekeaeideeKCI 81
                         90       100
                 ....*....|....*....|....*..
gi 732683275 114 LCnqrssgtQACIEVCPTQALRLMDDK 140
Cdd:cd10549   82 GC-------GLCVKVCPVDAITLEDEL 101
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
12-136 9.00e-12

Uncharacterized polyferredoxin-like protein; This family contains uncharacterized polyferredoxin protein similar to Methanobacterium thermoautotrophicum MvhB. The mvhB is a gene of the methylviologen-reducing hydrogenase operon. It is predicted to contain 12 [4Fe-4S] clusters, and was therefore suggested to be a polyferredoxin. As a subfamily of the beta subunit of the DMSO Reductase (DMSOR) family, it is predicted to function as electron carrier in the reducing reaction.


Pssm-ID: 319871 [Multi-domain]  Cd Length: 128  Bit Score: 62.80  E-value: 9.00e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275  12 CIGCHACEIACAVahnqenwplshsdfrPRIHVVGKGQAA-----NPVACHHCNNapCVTACPVNALTFQSD-------- 78
Cdd:cd10549    8 CIGCGICVKACPT---------------DAIELGPNGAIArgpeiDEDKCVFCGA--CVEVCPTGAIELTPEgkeyvpke 70
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 732683275  79 -SVQLDEQKCIGCKRCAIACPFGVVEMVDTIA-----QKCDLCNqrssgtqACIEVCPTQALRL 136
Cdd:cd10549   71 kEAEIDEEKCIGCGLCVKVCPVDAITLEDELEividkEKCIGCG-------ICAEVCPVNAIKL 127
Nar1 COG4624
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];
12-100 2.85e-11

Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];


Pssm-ID: 443663 [Multi-domain]  Cd Length: 450  Bit Score: 65.82  E-value: 2.85e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275  12 CIGCHACEIACAVAHNQENwplshSDFRPRIHVVGKGQAANPVACHHCNnaPCVTACPVNALTFQSDSVQLDEQKCIGCK 91
Cdd:COG4624   54 CCLCCCCCCRCCVAISCIQ-----VRGIIIIDKRGPSIIRDKEKCKNCY--PCVRACPVKAIKVDDGKAEIDEEKCISCG 126

                 ....*....
gi 732683275  92 RCAIACPFG 100
Cdd:COG4624  127 QCVAVCPFG 135
NarH_like cd16365
beta FeS subunits DMSOR NarH-like family; This subfamily contains beta FeS subunits of several ...
11-154 7.51e-11

beta FeS subunits DMSOR NarH-like family; This subfamily contains beta FeS subunits of several DMSO reductase superfamily, including nitrate reductase A, ethylbenzene dehydrogenase and selenate reductase. DMSO Reductase (DMSOR) family members have a large, periplasmic molybdenum-containing alpha subunit as well as a small beta FeS subunit, and may also have a small gamma subunit. . The beta subunits of DMSOR contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system. Nitrate reductase A contains three subunits (the catalytic subunit NarG, the catalytic subunit NarH with four [Fe-S] clusters, and integral membrane subunit NarI) and often forms a respiratory chain with the formate dehydrogenase via the lipid soluble quinol pool. Ethylbenzene dehydrogenase oxidizes the hydrocarbon ethylbenzene to (S)-1-phenylethanol. Selenate reductase catalyzes reduction of selenate to selenite in bacterial species that can obtain energy by respiring anaerobically with selenate as the terminal electron acceptor.


Pssm-ID: 319887 [Multi-domain]  Cd Length: 201  Bit Score: 61.83  E-value: 7.51e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275  11 ECIGCHACEIACAVA------------HNQENWPLSHSDFRPRIHVVGKGQAAN-----PVACHHCNNAPCVTACPVNAL 73
Cdd:cd16365   11 KCIGCQTCTVACKNAwtyrkgqeymwwNNVETKPGGGYPQDWEVKTIDNGGNTRfffylQRLCNHCTNPACLAACPRGAI 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275  74 TFQSDS--VQLDEQKCIGCKRCAIACPFGVVEM--VDTIAQKCDLCNQRSSGTQ--ACIEVCPTQ--ALRLMDDKGLQQI 145
Cdd:cd16365   91 YKREEDgiVLIDQKRCRGYRKCVEQCPYKKIYFngLSRVSEKCIACYPRIEGGDptRCMSACVGRirLQGFLDDNPKSPV 170
                        170
                 ....*....|
gi 732683275 146 -KVARQRKTA 154
Cdd:cd16365  171 tKLIRHWKVA 180
COG1233 COG1233
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ...
309-379 8.78e-11

Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440846 [Multi-domain]  Cd Length: 491  Bit Score: 64.49  E-value: 8.78e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 732683275 309 RSEKVAVIGAGPAGLGCADILARAGVQVDVFDRHPEIGGML-TFGIPPFKLD--KTVLSQR---REIFTAMGIDFHL 379
Cdd:COG1233    2 MMYDVVVIGAGIGGLAAAALLARAGYRVTVLEKNDTPGGRArTFERPGFRFDvgPSVLTMPgvlERLFRELGLEDYL 78
COG2768 COG2768
Uncharacterized Fe-S cluster protein [Function unknown];
56-104 4.17e-10

Uncharacterized Fe-S cluster protein [Function unknown];


Pssm-ID: 442050 [Multi-domain]  Cd Length: 74  Bit Score: 56.28  E-value: 4.17e-10
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 732683275  56 CHHCNNapCVTACPVNALTFQSDSVQLDEQKCIGCKRCAIACPFGVVEM 104
Cdd:COG2768   13 CIGCGA--CVKVCPVGAISIEDGKAVIDPEKCIGCGACIEVCPVGAIKI 59
Ndh COG1252
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
312-626 6.18e-10

NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];


Pssm-ID: 440864 [Multi-domain]  Cd Length: 386  Bit Score: 61.30  E-value: 6.18e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275 312 KVAVIGAGPAGLGCADILAR---AGVQVDVFDRH------PEIGGMLTFGIPPfklDKTVLSQRReIFTAMGIDFHL--- 379
Cdd:COG1252    3 RIVIVGGGFAGLEAARRLRKklgGDAEVTLIDPNpyhlfqPLLPEVAAGTLSP---DDIAIPLRE-LLRRAGVRFIQgev 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275 380 ----------NCEIGRDItfsdltsEYDAVFIGVGtygmmrADLPHEDAPGVIQ-ALPF------LTAHtRQLMGLPESE 442
Cdd:COG1252   79 tgidpeartvTLADGRTL-------SYDYLVIATG------SVTNFFGIPGLAEhALPLktledaLALR-ERLLAAFERA 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275 443 EypltDVEGKRVVVLGGGDT------TMD------CLRTSIRLNAASVTCAYRRDEVsMPGSRKEVVNA-----REEGVE 505
Cdd:COG1252  145 E----RRRLLTIVVVGGGPTgvelagELAellrklLRYPGIDPDKVRITLVEAGPRI-LPGLGEKLSEAaekelEKRGVE 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275 506 FQFNVQPQyiACDEDGrltavglIRTAMGEpgpdgrrrprpvagsefELPADVLIMAFGFQAHamPWLQGSGIKLDKWGL 585
Cdd:COG1252  220 VHTGTRVT--EVDADG-------VTLEDGE-----------------EIPADTVIWAAGVKAP--PLLADLGLPTDRRGR 271
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 732683275 586 IQTGDvgYLPTQTHlKKVFAGGDAVHGADLVV-----TAMAAGRQA 626
Cdd:COG1252  272 VLVDP--TLQVPGH-PNVFAIGDCAAVPDPDGkpvpkTAQAAVQQA 314
EBDH_beta cd10555
beta subunit of ethylbenzene-dehydrogenase (EBDH); This subfamily includes ethylbenzene ...
30-130 7.23e-10

beta subunit of ethylbenzene-dehydrogenase (EBDH); This subfamily includes ethylbenzene dehydrogenase (EBDH, EC 1.17.99.2), a member of the DMSO reductase family. EBDH oxidizes the hydrocarbon ethylbenzene to (S)-1-phenylethanol. It is a heterotrimer, with the alpha subunit containing the catalytic center with a molybdenum held by two molybdopterin-guanine dinucleotides, the beta subunit containing four iron-sulfur clusters (the electron transfer subunit) and the gamma subunit containing a methionine and a lysine as axial heme ligands. During catalysis, electrons produced by substrate oxidation are transferred to a heme in the gamma subunit and then presumably to a separate cytochrome involved in nitrate respiration.


Pssm-ID: 319877 [Multi-domain]  Cd Length: 316  Bit Score: 60.78  E-value: 7.23e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275  30 NWPLSHSDFRPRIhvvgkgqaanpvaCHHCNNAPCVTACPVNALT-FQSDSVQL-DEQKCIGCKRCAIACPFGVV--EMV 105
Cdd:cd10555  120 EYPNSYYFYLPRI-------------CNHCTNPACLAACPRKAIYkREEDGIVLvDQDRCRGYRYCVEACPYKKIyfNPV 186
                         90       100
                 ....*....|....*....|....*..
gi 732683275 106 DTIAQKCDLCNQR--SSGTQACIEVCP 130
Cdd:cd10555  187 EQKSEKCIFCYPRieKGVAPACARQCV 213
PRK07233 PRK07233
hypothetical protein; Provisional
312-360 1.10e-09

hypothetical protein; Provisional


Pssm-ID: 235977 [Multi-domain]  Cd Length: 434  Bit Score: 61.06  E-value: 1.10e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 732683275 312 KVAVIGAGPAGLGCADILARAGVQVDVFDRHPEIGGML-TFGIPPFKLDK 360
Cdd:PRK07233   1 KIAIVGGGIAGLAAAYRLAKRGHEVTVFEADDQLGGLAaSFEFGGLPIER 50
FadH2 COG0446
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ...
334-631 3.22e-09

NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase [Lipid transport and metabolism];


Pssm-ID: 440215 [Multi-domain]  Cd Length: 322  Bit Score: 58.67  E-value: 3.22e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275 334 VQVDVFDRHPEI-----GGMLTFGIPPFKLDKTVLSQRREiFTAMGIDFHLNCE---IGRD---ITFSDLTSE-YDAVFI 401
Cdd:COG0446    6 AEITVIEKGPHHsyqpcGLPYYVGGGIKDPEDLLVRTPES-FERKGIDVRTGTEvtaIDPEaktVTLRDGETLsYDKLVL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275 402 GVGTYgMMRADLPHEDAPGViqalpfLTAHTRQLMglPESEEYpLTDVEGKRVVVLGGGDTTMDcLRTSIRLNAASVTCA 481
Cdd:COG0446   85 ATGAR-PRPPPIPGLDLPGV------FTLRTLDDA--DALREA-LKEFKGKRAVVIGGGPIGLE-LAEALRKRGLKVTLV 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275 482 YRRDEVsMPGSRKEVVNA-----REEGVEFQFNVQPQYIacDEDGRLTavglIRTAmgepgpDGRrrprpvagsefELPA 556
Cdd:COG0446  154 ERAPRL-LGVLDPEMAALleeelREHGVELRLGETVVAI--DGDDKVA----VTLT------DGE-----------EIPA 209
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275 557 DVLIMAFGFQAHAmPWLQGSGIKLDKWGLIQTGDvgYLptQTHLKKVFAGGDAV----------HGADLVVTAMAAGRQA 626
Cdd:COG0446  210 DLVVVAPGVRPNT-ELAKDAGLALGERGWIKVDE--TL--QTSDPDVYAAGDCAevphpvtgktVYIPLASAANKQGRVA 284

                 ....*
gi 732683275 627 ARDML 631
Cdd:COG0446  285 AENIL 289
Lpd COG1249
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ...
313-631 3.43e-09

Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase [Energy production and conversion]; Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase is part of the Pathway/BioSystem: Glycine cleavagePyruvate oxidation


Pssm-ID: 440861 [Multi-domain]  Cd Length: 456  Bit Score: 59.33  E-value: 3.43e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275 313 VAVIGAGPAGLGCADILARAGVQVDVFDRHPeIGG-------------------------MLTFGI--PPFKLD-KTVLS 364
Cdd:COG1249    6 LVVIGAGPGGYVAAIRAAQLGLKVALVEKGR-LGGtclnvgcipskallhaaevahearhAAEFGIsaGAPSVDwAALMA 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275 365 QRREI-----------FTAMGIDF-----------HLNCEIGRDITFsdltseyDAVFIGVGTygmmRADLPheDAPGvI 422
Cdd:COG1249   85 RKDKVvdrlrggveelLKKNGVDVirgrarfvdphTVEVTGGETLTA-------DHIVIATGS----RPRVP--PIPG-L 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275 423 QALPFLTahTRQLMGLpesEEYPltdvegKRVVVLGGGdttmdclrtSIRLNAAS--------VTCAYRRDEVsMPGSRK 494
Cdd:COG1249  151 DEVRVLT--SDEALEL---EELP------KSLVVIGGG---------YIGLEFAQifarlgseVTLVERGDRL-LPGEDP 209
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275 495 EVVNA-----REEGVEFQFNVQPQYIACDEDG-RLTAVGlirtamgepgpdgrrrprpvAGSEFELPADVLIMAFGFQAH 568
Cdd:COG1249  210 EISEAlekalEKEGIDILTGAKVTSVEKTGDGvTVTLED--------------------GGGEEAVEADKVLVATGRRPN 269
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 732683275 569 ampwlqGSGIKLDKWGlIQTGDVGYLPT----QTHLKKVFAGGDAVHGADLVVTAMAAGRQAARDML 631
Cdd:COG1249  270 ------TDGLGLEAAG-VELDERGGIKVdeylRTSVPGIYAIGDVTGGPQLAHVASAEGRVAAENIL 329
COG1149 COG1149
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ...
80-136 5.63e-09

MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function prediction only];


Pssm-ID: 440763 [Multi-domain]  Cd Length: 68  Bit Score: 52.81  E-value: 5.63e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 732683275  80 VQLDEQKCIGCKRCAIACPFGVVEMVDTIA-----QKCDLCNqrssgtqACIEVCPTQALRL 136
Cdd:COG1149    6 PVIDEEKCIGCGLCVEVCPEGAIKLDDGGApvvdpDLCTGCG-------ACVGVCPTGAITL 60
DMSOR_beta_like cd16368
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
46-135 6.68e-09

uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.


Pssm-ID: 319890 [Multi-domain]  Cd Length: 200  Bit Score: 56.28  E-value: 6.68e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275  46 GKGQAAN-PVACHHCNNAPCVTACPVNALTFQ-SDSVQLDEQKCIGCKRCAIACPFGV------VEMVDTIAQ------- 110
Cdd:cd16368   80 GGEKEVFiPRRCMHCDNPPCAKLCPFGAARKTpEGAVYIDDDLCFGGAKCRDVCPWHIpqrqagVGIYLHLAPeyagggv 159
                         90       100
                 ....*....|....*....|....*....
gi 732683275 111 --KCDLCNQRSSGTQ--ACIEVCPTQALR 135
Cdd:cd16368  160 myKCDLCKDLLAQGKppACIEACPKGAQY 188
Pyr_redox pfam00070
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
312-383 7.29e-09

Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.


Pssm-ID: 425450 [Multi-domain]  Cd Length: 80  Bit Score: 52.98  E-value: 7.29e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 732683275  312 KVAVIGAGPAGLGCADILARAGVQVDVFDRHPEIGGMltfgippfkLDKTVLSQRREIFTAMGIDFHLNCEI 383
Cdd:pfam00070   1 RVVVVGGGYIGLELAGALARLGSKVTVVERRDRLLPG---------FDPEIAKILQEKLEKNGIEFLLNTTV 63
FeFe_hydrog_B1 TIGR04105
[FeFe] hydrogenase, group B1/B3; See for descriptions of different groups.
2-108 8.35e-09

[FeFe] hydrogenase, group B1/B3; See for descriptions of different groups.


Pssm-ID: 274983 [Multi-domain]  Cd Length: 462  Bit Score: 58.37  E-value: 8.35e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275    2 NKFIAAEAaeCIGC--HACEIACavahnqenwplshsdfrPR--IHVVGKGQAANP---VACHHCNNA-----------P 63
Cdd:TIGR04105 105 NRYTVTDA--CRGClaHPCIEVC-----------------PKgaISMVNGRAYIDQekcIECGKCKKAcpynaiveierP 165
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 732683275   64 CVTACPVNALTF-QSDSVQLDEQKCIGCKRCAIACPFGVV----EMVDTI 108
Cdd:TIGR04105 166 CEKACPVGAISSdEDGRAVIDYDKCISCGACMVACPFGAIsdksQIVQVI 215
DsrA COG2221
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ...
55-103 8.58e-09

Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion transport and metabolism];


Pssm-ID: 441823 [Multi-domain]  Cd Length: 69  Bit Score: 52.36  E-value: 8.58e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 732683275  55 ACHHCNNapCVTACPVNALTFQSDSVQLDEQKCIGCKRCAIACPFGVVE 103
Cdd:COG2221   16 KCIGCGL--CVAVCPTGAISLDDGKLVIDEEKCIGCGACIRVCPTGAIK 62
Lpd COG1249
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ...
287-404 1.04e-08

Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase [Energy production and conversion]; Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase is part of the Pathway/BioSystem: Glycine cleavagePyruvate oxidation


Pssm-ID: 440861 [Multi-domain]  Cd Length: 456  Bit Score: 57.79  E-value: 1.04e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275 287 ERYIT-DTALAMgwrpdvsKVVPRSekVAVIGAGPAGLGCADILARAGVQVDVFDRHPEIGGmltfgippfKLDKTVLSQ 365
Cdd:COG1249  153 VRVLTsDEALEL-------EELPKS--LVVIGGGYIGLEFAQIFARLGSEVTLVERGDRLLP---------GEDPEISEA 214
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 732683275 366 RREIFTAMGIDFHLNCEIGR--------DITFSD----LTSEYDAVFIGVG 404
Cdd:COG1249  215 LEKALEKEGIDILTGAKVTSvektgdgvTVTLEDgggeEAVEADKVLVATG 265
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
12-105 1.10e-08

Uncharacterized polyferredoxin-like protein; This family contains uncharacterized polyferredoxin protein similar to Methanobacterium thermoautotrophicum MvhB. The mvhB is a gene of the methylviologen-reducing hydrogenase operon. It is predicted to contain 12 [4Fe-4S] clusters, and was therefore suggested to be a polyferredoxin. As a subfamily of the beta subunit of the DMSO Reductase (DMSOR) family, it is predicted to function as electron carrier in the reducing reaction.


Pssm-ID: 319871 [Multi-domain]  Cd Length: 128  Bit Score: 53.94  E-value: 1.10e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275  12 CIGCHACEIACAVAhnqenwPLSHSDFRPRIHVVGKGQAANPVACHHCNNapCVTACPVNALTFQSD-SVQLDEQKCIGC 90
Cdd:cd10549   42 CVFCGACVEVCPTG------AIELTPEGKEYVPKEKEAEIDEEKCIGCGL--CVKVCPVDAITLEDElEIVIDKEKCIGC 113
                         90
                 ....*....|....*
gi 732683275  91 KRCAIACPFGVVEMV 105
Cdd:cd10549  114 GICAEVCPVNAIKLV 128
NAD_binding_8 pfam13450
NAD(P)-binding Rossmann-like domain;
315-359 1.34e-08

NAD(P)-binding Rossmann-like domain;


Pssm-ID: 433218 [Multi-domain]  Cd Length: 67  Bit Score: 51.76  E-value: 1.34e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 732683275  315 VIGAGPAGLGCADILARAGVQVDVFDRHPEIGG-MLTFGIPPFKLD 359
Cdd:pfam13450   1 IVGAGLAGLVAAALLAKRGFRVLVLEKRDRLGGnAYSYRVPGYVFD 46
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
286-404 1.75e-08

Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.


Pssm-ID: 400379 [Multi-domain]  Cd Length: 301  Bit Score: 56.17  E-value: 1.75e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275  286 LERYITDT-ALAMGWRPdvskvvprsEKVAVIGAGPAGLGCADILARAGVQVDVFDRHPEIGGMltfgippfkLDKTVLS 364
Cdd:pfam07992 136 LVRTLDSAeALRLKLLP---------KRVVVVGGGYIGVELAAALAKLGKEVTLIEALDRLLRA---------FDEEISA 197
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 732683275  365 QRREIFTAMGIDFHLNCE----IGRDITFSDLTSE-----YDAVFIGVG 404
Cdd:pfam07992 198 ALEKALEKNGVEVRLGTSvkeiIGDGDGVEVILKDgteidADLVVVAIG 246
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
82-146 1.94e-08

Uncharacterized polyferredoxin-like protein; This family contains uncharacterized polyferredoxin protein similar to Methanobacterium thermoautotrophicum MvhB. The mvhB is a gene of the methylviologen-reducing hydrogenase operon. It is predicted to contain 12 [4Fe-4S] clusters, and was therefore suggested to be a polyferredoxin. As a subfamily of the beta subunit of the DMSO Reductase (DMSOR) family, it is predicted to function as electron carrier in the reducing reaction.


Pssm-ID: 319871 [Multi-domain]  Cd Length: 128  Bit Score: 53.17  E-value: 1.94e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 732683275  82 LDEQKCIGCKRCAIACPFGVVEMVDTIAQ---------KCDLCnqrssgtQACIEVCPTQALRLMDDKGLQQIK 146
Cdd:cd10549    3 YDPEKCIGCGICVKACPTDAIELGPNGAIargpeidedKCVFC-------GACVEVCPTGAIELTPEGKEYVPK 69
COG3380 COG3380
Predicted NAD/FAD-dependent oxidoreductase [General function prediction only];
312-347 2.89e-08

Predicted NAD/FAD-dependent oxidoreductase [General function prediction only];


Pssm-ID: 442607 [Multi-domain]  Cd Length: 331  Bit Score: 56.04  E-value: 2.89e-08
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 732683275 312 KVAVIGAGPAGLGCADILARAGVQVDVFDRHPEIGG 347
Cdd:COG3380    5 DIAIIGAGIAGLAAARALQDAGHEVTVFEKSRGVGG 40
NapF COG1145
Ferredoxin [Energy production and conversion];
1-110 5.21e-08

Ferredoxin [Energy production and conversion];


Pssm-ID: 440760 [Multi-domain]  Cd Length: 238  Bit Score: 54.34  E-value: 5.21e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275   1 MNKFIAAEAAECIGCHACEIACAVAHNQENWPLSHSDFRPRIHVVGKGQAANPVACHHCNNapCVTACPVNALTFQSDSV 80
Cdd:COG1145  129 GEVLLVIAAALAEAGLAILGAAAPVDALAISGGKKIEEELKIAIKKAKAVIDAEKCIGCGL--CVKVCPTGAIRLKDGKP 206
                         90       100       110
                 ....*....|....*....|....*....|..
gi 732683275  81 QL--DEQKCIGCKRCAIACPFGVVEMVDTIAQ 110
Cdd:COG1145  207 QIvvDPDKCIGCGACVKVCPVGAISLEPKEIE 238
W-FDH cd10559
tungsten-containing formate dehydrogenase, small subunit; This subfamily contains beta subunit ...
10-163 5.51e-08

tungsten-containing formate dehydrogenase, small subunit; This subfamily contains beta subunit of Tungsten-containing formate dehydrogenase (W-FDH), a member of the DMSO reductase family. W-FDH contains a tungsten instead of molybdenum at the catalytic center. This enzyme seems to be exclusively found in organisms such as hyperthermophilic archaea that live in extreme environments. It is a heterodimer of a large and a small subunit; the large subunit harbors the W site and one [4Fe-4S] center and the small subunit, containing three [4Fe-4S] clusters, functions to transfer electrons.


Pssm-ID: 319881 [Multi-domain]  Cd Length: 200  Bit Score: 53.59  E-value: 5.51e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275  10 AECIGCHACEIACAVAH----NQENWPLSHS---DFRP---RIHVVGKGQAAN--------PVACHHCNNAPCVTACPVn 71
Cdd:cd10559    7 TRCTACRGCQVACKQWNqlpaEQTKNTGSHQnppDLSAntyKLVRFNEVRNENgkpdwlffPDQCRHCVTPPCKDAADM- 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275  72 altfQSDSVQLDEQKciGC--------KRCAI----ACPFGVVEMVDTIAQ--KCDLCNQR-SSGTQ-ACIEVCPTQALR 135
Cdd:cd10559   86 ----VPGAVIQDEAT--GAvvftektaELDFDdvlsACPYNIPRKNEATGRivKCDMCIDRvSNGLQpACVKACPTGAMN 159
                        170       180
                 ....*....|....*....|....*...
gi 732683275 136 LMDDKGLqqIKVARQRKTAAGKASSDAQ 163
Cdd:cd10559  160 FGDRDEM--LAMASKRLEELKKRYPKAN 185
PRK07118 PRK07118
Fe-S cluster domain-containing protein;
64-155 6.50e-08

Fe-S cluster domain-containing protein;


Pssm-ID: 235941 [Multi-domain]  Cd Length: 280  Bit Score: 54.55  E-value: 6.50e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275  64 CVTACPVNALTFQSDSVQL-------DEQK---------CIGCKRCAIACPFGVVEMVDTIA----QKCDLCNqrssgtq 123
Cdd:PRK07118 176 CVKACPRNVIELIPKSARVfvacnskDKGKavkkvcevgCIGCGKCVKACPAGAITMENNLAvidqEKCTSCG------- 248
                         90       100       110
                 ....*....|....*....|....*....|..
gi 732683275 124 ACIEVCPTQALRLMDDKGLQQIKVARQRKTAA 155
Cdd:PRK07118 249 KCVEKCPTKAIRILNKPPKVKEPKKAAAEAAA 280
NirB COG1251
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
310-631 6.60e-08

NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];


Pssm-ID: 440863 [Multi-domain]  Cd Length: 402  Bit Score: 55.15  E-value: 6.60e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275 310 SEKVAVIGAGPAGLGCADILARAGVQVDV----------FDRHP---EIGGMLTFgippfklDKTVLSQRrEIFTAMGID 376
Cdd:COG1251    1 KMRIVIIGAGMAGVRAAEELRKLDPDGEItvigaephppYNRPPlskVLAGETDE-------EDLLLRPA-DFYEENGID 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275 377 FHLNCEI------GRDITFSDLTS-EYDAVFIGVGTYGMmRADLPHEDAPGViqalpfLTAHTrqlmglpeseeypLTDV 449
Cdd:COG1251   73 LRLGTRVtaidraARTVTLADGETlPYDKLVLATGSRPR-VPPIPGADLPGV------FTLRT-------------LDDA 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275 450 E--------GKRVVVLGGGdttmdcLrtsIRLNAASvTCAYRRDEVSM--PGSR-------KEVVNA-----REEGVEFQ 507
Cdd:COG1251  133 DalraalapGKRVVVIGGG------L---IGLEAAA-ALRKRGLEVTVveRAPRllprqldEEAGALlqrllEALGVEVR 202
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275 508 FNVQPQYIacDEDGRLTAVGLirtamgepgPDGRrrprpvagsefELPADVLIMAFGfqahAMP---WLQGSGIKLDKwG 584
Cdd:COG1251  203 LGTGVTEI--EGDDRVTGVRL---------ADGE-----------ELPADLVVVAIG----VRPnteLARAAGLAVDR-G 255
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 732683275 585 lIQTGDvgYLptQTHLKKVFAGGDAVHGAD---------LVVTAMAAGRQAARDML 631
Cdd:COG1251  256 -IVVDD--YL--RTSDPDIYAAGDCAEHPGpvygrrvleLVAPAYEQARVAAANLA 306
HemY COG1232
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ...
312-349 6.88e-08

Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen oxidase HemY/PPOX is part of the Pathway/BioSystem: Heme biosynthesis


Pssm-ID: 440845 [Multi-domain]  Cd Length: 443  Bit Score: 55.22  E-value: 6.88e-08
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 732683275 312 KVAVIGAGPAGLGCADILARAGVQVDVFDRHPEIGGML 349
Cdd:COG1232    3 RVAVIGGGIAGLTAAYRLAKAGHEVTVLEASDRVGGLI 40
IorA COG4231
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and ...
64-106 8.00e-08

TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and conversion];


Pssm-ID: 443375 [Multi-domain]  Cd Length: 76  Bit Score: 49.66  E-value: 8.00e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 732683275  64 CVTACPVNALTFQSDSVQLDEQKCIGCKRCAIACPFGVVEMVD 106
Cdd:COG4231   30 CVKVCPADAIEEGDGKAVIDPDLCIGCGSCVQVCPVDAIKLEK 72
SER_beta cd10556
Beta subunit of selenate reductase; This subfamily includes beta FeS subunit of selenate ...
53-137 8.16e-08

Beta subunit of selenate reductase; This subfamily includes beta FeS subunit of selenate reductase (SER), a member of the DMSO reductase family. SER catalyzes the reduction of selenate to selenite in bacterial species that can obtain energy by respiring anaerobically with selenate as the terminal electron acceptor. The enzyme comprises three subunits SerABC, forming a heterotrimer, with the catalytic component (alpha-subunit), iron-sulfur protein (beta-subunit) and monomeric b-type heme-containing gamma subunit. Beta subunit contains coordinating one [3Fe-4S] cluster and three [4Fe-4S] clusters and functions as electron carrier.


Pssm-ID: 319878 [Multi-domain]  Cd Length: 287  Bit Score: 54.00  E-value: 8.16e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275  53 PVACHHCNNAPCVTACPVNALTFQSDS--VQLDEQKCIGCKRCAIACPF--GVVEMVDTIAQKCDLCNQRSSGTQA--CI 126
Cdd:cd10556  138 PRICNHCTYPACLAACPRKAIYKREEDgiVLIDQERCRGYRECVEACPYkkPMYNPTTRVSEKCIGCYPRIEEGDQtqCV 217
                         90
                 ....*....|.
gi 732683275 127 EVCPTQaLRLM 137
Cdd:cd10556  218 SACIGK-IRLQ 227
COG2768 COG2768
Uncharacterized Fe-S cluster protein [Function unknown];
83-136 9.59e-08

Uncharacterized Fe-S cluster protein [Function unknown];


Pssm-ID: 442050 [Multi-domain]  Cd Length: 74  Bit Score: 49.34  E-value: 9.59e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 732683275  83 DEQKCIGCKRCAIACPFGVVEMVDTIAQ----KCDLCnqrssgtQACIEVCPTQALRL 136
Cdd:COG2768    9 DEEKCIGCGACVKVCPVGAISIEDGKAVidpeKCIGC-------GACIEVCPVGAIKI 59
Nar1 COG4624
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];
56-139 1.02e-07

Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];


Pssm-ID: 443663 [Multi-domain]  Cd Length: 450  Bit Score: 54.65  E-value: 1.02e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275  56 CHHCNNAPCVTACPVNALTFQSDSVQLDEQKCIGCKRCAIACPFGVVEMVDTIAQ----KCDLCNQrssgtqaCIEVCPT 131
Cdd:COG4624   62 CRCCVAISCIQVRGIIIIDKRGPSIIRDKEKCKNCYPCVRACPVKAIKVDDGKAEideeKCISCGQ-------CVAVCPF 134

                 ....*...
gi 732683275 132 QALRLMDD 139
Cdd:COG4624  135 GAITEKSD 142
COG1149 COG1149
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ...
52-106 1.24e-07

MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function prediction only];


Pssm-ID: 440763 [Multi-domain]  Cd Length: 68  Bit Score: 48.96  E-value: 1.24e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 732683275  52 NPVACHHCNNapCVTACPVNALTFQ-SDSVQLDEQKCIGCKRCAIACPFGVVEMVD 106
Cdd:COG1149    9 DEEKCIGCGL--CVEVCPEGAIKLDdGGAPVVDPDLCTGCGACVGVCPTGAITLEE 62
NuoI COG1143
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ...
56-104 1.26e-07

Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy production and conversion]; Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) is part of the Pathway/BioSystem: NADH dehydrogenase


Pssm-ID: 440758 [Multi-domain]  Cd Length: 66  Bit Score: 48.97  E-value: 1.26e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 732683275  56 CHHCNNapCVTACPVNALTFQSD----SVQLDEQKCIGCKRCAIACPFGVVEM 104
Cdd:COG1143    4 CIGCGL--CVRVCPVDAITIEDGepgkVYVIDPDKCIGCGLCVEVCPTGAISM 54
NapF COG1145
Ferredoxin [Energy production and conversion];
83-140 1.44e-07

Ferredoxin [Energy production and conversion];


Pssm-ID: 440760 [Multi-domain]  Cd Length: 238  Bit Score: 52.80  E-value: 1.44e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 732683275  83 DEQKCIGCKRCAIACPFGVVEMVDTIAQ------KCDLCnqrssgtQACIEVCPTQALRLMDDK 140
Cdd:COG1145  180 DAEKCIGCGLCVKVCPTGAIRLKDGKPQivvdpdKCIGC-------GACVKVCPVGAISLEPKE 236
PRK07208 PRK07208
hypothetical protein; Provisional
308-348 1.52e-07

hypothetical protein; Provisional


Pssm-ID: 235967 [Multi-domain]  Cd Length: 479  Bit Score: 54.12  E-value: 1.52e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 732683275 308 PRSEKVAVIGAGPAGLGCADILARAGVQVDVFDRHPEIGGM 348
Cdd:PRK07208   2 TNKKSVVIIGAGPAGLTAAYELLKRGYPVTVLEADPVVGGI 42
Fer4_7 pfam12838
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
56-101 2.08e-07

4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich. Domain contains two 4Fe4S clusters.


Pssm-ID: 463724 [Multi-domain]  Cd Length: 51  Bit Score: 47.91  E-value: 2.08e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 732683275   56 CHHCNNapCVTACPVNALTFQS-------DSVQLDEQKCIGCKRCAIACPFGV 101
Cdd:pfam12838   1 CIGCGA--CVAACPVGAITLDEvgekkgtKTVVIDPERCVGCGACVAVCPTGA 51
PRK07118 PRK07118
Fe-S cluster domain-containing protein;
64-139 3.18e-07

Fe-S cluster domain-containing protein;


Pssm-ID: 235941 [Multi-domain]  Cd Length: 280  Bit Score: 52.24  E-value: 3.18e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275  64 CVTACPVNALTFQSDSVQLDEQKCIGCKRCAIACPFGVVEMVDTIAQKCDLCNQRSSGTQA-------------CIEVCP 130
Cdd:PRK07118 147 CVAACPFDAIHIENGLPVVDEDKCTGCGACVKACPRNVIELIPKSARVFVACNSKDKGKAVkkvcevgcigcgkCVKACP 226

                 ....*....
gi 732683275 131 TQALRLMDD 139
Cdd:PRK07118 227 AGAITMENN 235
PorD COG1144
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta ...
56-106 3.52e-07

Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta subunit [Energy production and conversion]; Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta subunit is part of the Pathway/BioSystem: Pyruvate oxidation


Pssm-ID: 440759 [Multi-domain]  Cd Length: 84  Bit Score: 48.12  E-value: 3.52e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 732683275  56 CHHCNNapCVTACPVNALTFQSDS-VQLDEQKCIGCKRCAIACPFGVVEMVD 106
Cdd:COG1144   32 CIGCGL--CWIVCPDGAIRVDDGKyYGIDYDYCKGCGICAEVCPVKAIEMVP 81
NuoI COG1143
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ...
84-136 4.04e-07

Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy production and conversion]; Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) is part of the Pathway/BioSystem: NADH dehydrogenase


Pssm-ID: 440758 [Multi-domain]  Cd Length: 66  Bit Score: 47.43  E-value: 4.04e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 732683275  84 EQKCIGCKRCAIACPFGVVEMVDTIAQ--------KCDLCnqrssgtQACIEVCPTQALRL 136
Cdd:COG1143    1 EDKCIGCGLCVRVCPVDAITIEDGEPGkvyvidpdKCIGC-------GLCVEVCPTGAISM 54
NapH COG0348
Polyferredoxin NapH [Energy production and conversion];
64-136 4.31e-07

Polyferredoxin NapH [Energy production and conversion];


Pssm-ID: 440117 [Multi-domain]  Cd Length: 263  Bit Score: 51.60  E-value: 4.31e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275  64 CVTACPVNAltFQS-----DSVQL--DEQKCIGCKRCAIACPFGVVEMVDTIAQ-KCDLCnqrssgtQACIEVCPTQALR 135
Cdd:COG0348  184 CRYLCPYGA--FQGllsdlSTLRVryDRGDCIDCGLCVKVCPMGIDIRKGEINQsECINC-------GRCIDACPKDAIR 254

                 .
gi 732683275 136 L 136
Cdd:COG0348  255 F 255
PTZ00188 PTZ00188
adrenodoxin reductase; Provisional
312-404 4.92e-07

adrenodoxin reductase; Provisional


Pssm-ID: 240308  Cd Length: 506  Bit Score: 52.58  E-value: 4.92e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275 312 KVAVIGAGPAGLGCAD-ILARAGVQVDVFDRHPEIGGMLTFGIPPFKLD-KTVLSQRREIFTAMGIDFHLNCEIGRDITF 389
Cdd:PTZ00188  41 KVGIIGAGPSALYCCKhLLKHERVKVDIFEKLPNPYGLIRYGVAPDHIHvKNTYKTFDPVFLSPNYRFFGNVHVGVDLKM 120
                         90
                 ....*....|....*
gi 732683275 390 SDLTSEYDAVFIGVG 404
Cdd:PTZ00188 121 EELRNHYNCVIFCCG 135
PorD COG1144
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta ...
82-140 5.40e-07

Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta subunit [Energy production and conversion]; Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta subunit is part of the Pathway/BioSystem: Pyruvate oxidation


Pssm-ID: 440759 [Multi-domain]  Cd Length: 84  Bit Score: 47.74  E-value: 5.40e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 732683275  82 LDEQKCIGCKRCAIACPFGVVEMVDT-----IAQKCDLCNqrssgtqACIEVCPTQALRLMDDK 140
Cdd:COG1144   27 VDEDKCIGCGLCWIVCPDGAIRVDDGkyygiDYDYCKGCG-------ICAEVCPVKAIEMVPEE 83
FadH2 COG0446
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ...
311-404 5.41e-07

NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase [Lipid transport and metabolism];


Pssm-ID: 440215 [Multi-domain]  Cd Length: 322  Bit Score: 51.74  E-value: 5.41e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275 311 EKVAVIGAGPAGLGCADILARAGVQVDVFDRHPEIGGmltfgippfKLDKTVLSQRREIFTAMGIDFHLNCEI----GRD 386
Cdd:COG0446  125 KRAVVIGGGPIGLELAEALRKRGLKVTLVERAPRLLG---------VLDPEMAALLEEELREHGVELRLGETVvaidGDD 195
                         90       100
                 ....*....|....*....|..
gi 732683275 387 ---ITFSDLTS-EYDAVFIGVG 404
Cdd:COG0446  196 kvaVTLTDGEEiPADLVVVAPG 217
DsrA COG2221
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ...
80-135 6.96e-07

Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion transport and metabolism];


Pssm-ID: 441823 [Multi-domain]  Cd Length: 69  Bit Score: 46.97  E-value: 6.96e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275  80 VQLDEQKCIGCKRCAIACPFGVVEMVD----TIAQKCDLCnqrssgtQACIEVCPTQALR 135
Cdd:COG2221   10 PKIDEEKCIGCGLCVAVCPTGAISLDDgklvIDEEKCIGC-------GACIRVCPTGAIK 62
PRK08348 PRK08348
NADH-plastoquinone oxidoreductase subunit; Provisional
83-139 8.72e-07

NADH-plastoquinone oxidoreductase subunit; Provisional


Pssm-ID: 181399 [Multi-domain]  Cd Length: 120  Bit Score: 48.29  E-value: 8.72e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 732683275  83 DEQKCIGCKRCAIACPFGVVEMVDTIAQ------KCDLCNQrssgtqaCIEVCPTQALRLMDD 139
Cdd:PRK08348  40 DVDKCVGCRMCVTVCPAGVFVYLPEIRKvalwtgRCVFCGQ-------CVDVCPTGALQMSDD 95
YhiN COG2081
Predicted flavoprotein YhiN [General function prediction only];
314-346 9.59e-07

Predicted flavoprotein YhiN [General function prediction only];


Pssm-ID: 441684 [Multi-domain]  Cd Length: 402  Bit Score: 51.59  E-value: 9.59e-07
                         10        20        30
                 ....*....|....*....|....*....|...
gi 732683275 314 AVIGAGPAGLGCADILARAGVQVDVFDRHPEIG 346
Cdd:COG2081    1 IVIGAGAAGLMAAITAAERGARVLLLEKNPKVG 33
PreA COG1146
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and ...
80-144 9.59e-07

NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and metabolism];


Pssm-ID: 440761 [Multi-domain]  Cd Length: 67  Bit Score: 46.63  E-value: 9.59e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 732683275  80 VQLDEQKCIGCKRCAIACPFGVVEMVDTIAQ-------KCDLCnqrssgtQACIEVCPTQALRLMDDKGLQQ 144
Cdd:COG1146    3 PVIDTDKCIGCGACVEVCPVDVLELDEEGKKalvinpeECIGC-------GACELVCPVGAITVEDDEPEEQ 67
IorA COG4231
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and ...
83-141 1.12e-06

TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and conversion];


Pssm-ID: 443375 [Multi-domain]  Cd Length: 76  Bit Score: 46.57  E-value: 1.12e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 732683275  83 DEQKCIGCKRCAIACPFGVVEMVDTIAQ----KCDLCNqrssgtqACIEVCPTQALRLMDDKG 141
Cdd:COG4231   20 DEDKCTGCGACVKVCPADAIEEGDGKAVidpdLCIGCG-------SCVQVCPVDAIKLEKRVP 75
NapF_like cd10564
NapF, iron-sulfur subunit of periplasmic nitrate reductase; This family contains NapF protein, ...
8-104 1.18e-06

NapF, iron-sulfur subunit of periplasmic nitrate reductase; This family contains NapF protein, the iron-sulfur subunit of periplasmic nitrate reductase. The periplasmic nitrate reductase NapABC of Escherichia coli likely functions during anaerobic growth in low-nitrate environments; napF operon expression is activated by cyclic AMP receptor protein (Crp). NapF is a subfamily of the beta subunit of DMSO reductase (DMSOR) family. DMSOR family members have a large, periplasmic molybdenum-containing alpha subunit as well as a small beta FeS subunit, and may also have a small gamma subunit. The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.


Pssm-ID: 319886 [Multi-domain]  Cd Length: 139  Bit Score: 48.39  E-value: 1.18e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275   8 EAAECIGCHACEIACA----VAHNQENWPLshsdfrpRIHVVGKGQAANPVACHhcnnaPCVTACPVNALTFQ-----SD 78
Cdd:cd10564   43 SRGECTFCGACAEACPegalDPAREAPWPL-------RAEIGDSCLALQGVECR-----SCQDACPTQAIRFRprlggIA 110
                         90       100
                 ....*....|....*....|....*.
gi 732683275  79 SVQLDEQKCIGCKRCAIACPFGVVEM 104
Cdd:cd10564  111 LPELDADACTGCGACVSVCPVGAITL 136
COG3349 COG3349
Uncharacterized protein, contains NAD-binding domain and a Fe-S cluster [General function ...
312-347 1.41e-06

Uncharacterized protein, contains NAD-binding domain and a Fe-S cluster [General function prediction only];


Pssm-ID: 442577 [Multi-domain]  Cd Length: 445  Bit Score: 51.01  E-value: 1.41e-06
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 732683275 312 KVAVIGAGPAGLGCADILARAGVQVDVFDRHPEIGG 347
Cdd:COG3349    5 RVVVVGGGLAGLAAAVELAEAGFRVTLLEARPRLGG 40
HI0933_like pfam03486
HI0933-like protein;
312-346 3.13e-06

HI0933-like protein;


Pssm-ID: 427330 [Multi-domain]  Cd Length: 406  Bit Score: 49.89  E-value: 3.13e-06
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 732683275  312 KVAVIGAGPAGLGCADILARAGVQVDVFDRHPEIG 346
Cdd:pfam03486   2 DVIVIGGGAAGLMAAISAAKRGRRVLLIEKGKKLG 36
YobN COG1231
Monoamine oxidase [Amino acid transport and metabolism];
308-347 4.25e-06

Monoamine oxidase [Amino acid transport and metabolism];


Pssm-ID: 440844 [Multi-domain]  Cd Length: 440  Bit Score: 49.53  E-value: 4.25e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 732683275 308 PRSEKVAVIGAGPAGLGCADILARAGVQVDVFDRHPEIGG 347
Cdd:COG1231    5 ARGKDVVIVGAGLAGLAAARELRKAGLDVTVLEARDRVGG 44
HdrA COG1148
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
81-148 4.58e-06

Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];


Pssm-ID: 440762 [Multi-domain]  Cd Length: 563  Bit Score: 49.86  E-value: 4.58e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 732683275  81 QLDEQKCIGCKRCAIACPFGVVEMV-DTIAQ----KCDLCnqrssGTqaCIEVCPTQALRLM---DDKGLQQIKVA 148
Cdd:COG1148  492 EVDPEKCTGCGRCVEVCPYGAISIDeKGVAEvnpaLCKGC-----GT--CAAACPSGAISLKgftDDQILAQIDAL 560
ferrodoxin_EFR1 NF038196
EFR1 family ferrodoxin; Members of the family have a C-terminal ferrodoxin domain, with eight ...
86-133 5.25e-06

EFR1 family ferrodoxin; Members of the family have a C-terminal ferrodoxin domain, with eight conserved Cys residues in two CxxCxxCxxxCP motifs, each of which binds a 4Fe-4S cluster. The N-terminal region resembles flavodoxin domains, with some members of the family recognized by Pfam models PF12724 (Flavodoxin_5) or PF00258 (Flavodoxin_1).


Pssm-ID: 468407 [Multi-domain]  Cd Length: 243  Bit Score: 48.32  E-value: 5.25e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 732683275  86 KCIGCKRCAIACPFGVVEMVD---TIAQKCDLCnqrssgtQACIEVCPTQA 133
Cdd:NF038196 186 KCIGCGICAKVCPVNNIEMEDgkpVWGHNCTHC-------LACIHRCPKEA 229
NarH_beta-like cd10557
beta subunit of nitrate reductase A (NarH) and similar proteins; This subfamily includes ...
53-129 5.37e-06

beta subunit of nitrate reductase A (NarH) and similar proteins; This subfamily includes nitrate reductase A, a member of the DMSO reductase family. The respiratory nitrate reductase complex (NarGHI) from E. coli is a heterotrimer, with the catalytic subunit (NarG) with a molybdo-bis (molybdopterin guanine dinucleotide) cofactor and an [Fe-S] cluster, the electron transfer subunit (NarH) with four [Fe-S] clusters, and the integral membrane subunit (NarI) with two b-type hemes. Nitrate reductase A often forms a respiratory chain with the formate dehydrogenase via the lipid soluble quinol pool. Electron transfer from formate to nitrate is coupled to proton translocation across the cytoplasmic membrane generating proton motive force by a redox loop mechanism. Demethylmenaquinol (DMKH2) has been shown to be a good substrate for NarGHI in nitrate respiration in E. coli.


Pssm-ID: 319879 [Multi-domain]  Cd Length: 363  Bit Score: 48.90  E-value: 5.37e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275  53 PVACHHCNNAPCVTACPVNALTFQSDS--VQLDEQKCIGCKRCAIACPFGVV--EMVDTIAQKCDLCNQRSSGTQ--ACI 126
Cdd:cd10557  176 PRICNHCLNPACVAACPSGAIYKREEDgiVLIDQDRCRGWRMCVSACPYKKVyyNWKTGKSEKCIFCYPRLEAGQptVCS 255

                 ...
gi 732683275 127 EVC 129
Cdd:cd10557  256 ETC 258
UbiH COG0654
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ...
312-375 5.91e-06

2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme transport and metabolism, Energy production and conversion]; 2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases is part of the Pathway/BioSystem: Ubiquinone biosynthesis


Pssm-ID: 440419 [Multi-domain]  Cd Length: 326  Bit Score: 48.78  E-value: 5.91e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 732683275 312 KVAVIGAGPAGLGCADILARAGVQVDVFDRHPEIGGmLTFGIppfkldktVLSQR-REIFTAMGI 375
Cdd:COG0654    5 DVLIVGGGPAGLALALALARAGIRVTVVERAPPPRP-DGRGI--------ALSPRsLELLRRLGL 60
PreA COG1146
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and ...
52-106 1.02e-05

NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and metabolism];


Pssm-ID: 440761 [Multi-domain]  Cd Length: 67  Bit Score: 43.54  E-value: 1.02e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 732683275  52 NPVACHHCNnaPCVTACPVNALTFQSD---SVQLDEQKCIGCKRCAIACPFGVVEMVD 106
Cdd:COG1146    6 DTDKCIGCG--ACVEVCPVDVLELDEEgkkALVINPEECIGCGACELVCPVGAITVED 61
PRK12387 PRK12387
formate hydrogenlyase complex iron-sulfur subunit; Provisional
85-139 1.39e-05

formate hydrogenlyase complex iron-sulfur subunit; Provisional


Pssm-ID: 183492 [Multi-domain]  Cd Length: 180  Bit Score: 46.18  E-value: 1.39e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 732683275  85 QKCIGCKRCAIACPFGVVEMVDTIAQK----------CDLCNQrssgtqaCIEVCPTQALRLMDD 139
Cdd:PRK12387  38 QQCIGCAACVNACPSNALTVETDLATGelawefnlgrCIFCGR-------CEEVCPTAAIKLSQE 95
PRK05249 PRK05249
Si-specific NAD(P)(+) transhydrogenase;
315-631 1.55e-05

Si-specific NAD(P)(+) transhydrogenase;


Pssm-ID: 235373 [Multi-domain]  Cd Length: 461  Bit Score: 47.84  E-value: 1.55e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275 315 VIGAGPAGLGCADILARAGVQVDVFDRHPEIGGMLTF-G-IPPFKLDKTVLS----QRREIFTAMGIDfhlnceigRDIT 388
Cdd:PRK05249  10 VIGSGPAGEGAAMQAAKLGKRVAVIERYRNVGGGCTHtGtIPSKALREAVLRligfNQNPLYSSYRVK--------LRIT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275 389 FSDLtseydavfigvgtygMMRAD--LPHEDApgVIQAL-------------PFLTAHTRQLMGlPESEEYPLT------ 447
Cdd:PRK05249  82 FADL---------------LARADhvINKQVE--VRRGQyernrvdliqgraRFVDPHTVEVEC-PDGEVETLTadkivi 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275 448 ------------DVEGKRV----------------VVLGGGdtTMDCLRTSI-RLNAASVTCAYRRDEVsMPGSRKEVVN 498
Cdd:PRK05249 144 atgsrpyrppdvDFDHPRIydsdsilsldhlprslIIYGAG--VIGCEYASIfAALGVKVTLINTRDRL-LSFLDDEISD 220
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275 499 A-----REEGVEFQFNVQPQYIACDEDGRLTAVGlirtamgepgpDGRRrprpvagsefeLPADVLIMAFGFQA-----H 568
Cdd:PRK05249 221 AlsyhlRDSGVTIRHNEEVEKVEGGDDGVIVHLK-----------SGKK-----------IKADCLLYANGRTGntdglN 278
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 732683275 569 ampwLQGSGIKLDKWGLIQTGDVGylptQTHLKKVFAGGDAVHGADLVVTAMAAGRQAARDML 631
Cdd:PRK05249 279 ----LENAGLEADSRGQLKVNENY----QTAVPHIYAVGDVIGFPSLASASMDQGRIAAQHAV 333
PRK12387 PRK12387
formate hydrogenlyase complex iron-sulfur subunit; Provisional
52-129 1.56e-05

formate hydrogenlyase complex iron-sulfur subunit; Provisional


Pssm-ID: 183492 [Multi-domain]  Cd Length: 180  Bit Score: 45.79  E-value: 1.56e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275  52 NPVACHHCnnAPCVTACPVNALTFQSDSV------QLDEQKCIGCKRCAIACPFGVVEMVD----TIAQKCDLCnQRSSG 121
Cdd:PRK12387  36 NPQQCIGC--AACVNACPSNALTVETDLAtgelawEFNLGRCIFCGRCEEVCPTAAIKLSQefelAVWKKEDLL-QQSEF 112

                 ....*...
gi 732683275 122 TQACIEVC 129
Cdd:PRK12387 113 ALCNCRVC 120
DAO pfam01266
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ...
312-379 1.79e-05

FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: Glycerol-3-phosphate dehydrogenase EC:1.1.99.5, Sarcosine oxidase beta subunit EC:1.5.3.1, D-alanine oxidase EC:1.4.99.1, D-aspartate oxidase EC:1.4.3.1.


Pssm-ID: 426168 [Multi-domain]  Cd Length: 339  Bit Score: 47.39  E-value: 1.79e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275  312 KVAVIGAGPAGLGCADILARAGVQVDVFDRHPEIG--------GMLTFGIPPFKLDKTV------LSQRREIFTAMGIDF 377
Cdd:pfam01266   1 DVVVIGGGIVGLSTAYELARRGLSVTLLERGDDPGsgasgrnaGLIHPGLRYLEPSELArlaleaLDLWEELEEELGIDC 80

                  ..
gi 732683275  378 HL 379
Cdd:pfam01266  81 GF 82
COG2509 COG2509
FAD-dependent dehydrogenase [General function prediction only];
305-341 2.21e-05

FAD-dependent dehydrogenase [General function prediction only];


Pssm-ID: 441999 [Multi-domain]  Cd Length: 466  Bit Score: 47.41  E-value: 2.21e-05
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 732683275 305 KVVPRSEKVAVIGAGPAGLGCADILARAGVQVDVFDR 341
Cdd:COG2509   25 GIPSLKYDVVIVGAGPAGLFAALELAEAGLKPLVLER 61
DMSOR_beta_like cd16373
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
85-149 3.12e-05

uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.


Pssm-ID: 319895 [Multi-domain]  Cd Length: 154  Bit Score: 44.55  E-value: 3.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275  85 QKCIGCKRCAIACPFGVVEMVDT--------------IAQKCDLCNQrssgtqACIEVCPTQALRLMDDKGLQ-QIKVAR 149
Cdd:cd16373   14 ALCIRCGLCVEACPTGVIQPAGLedgleggrtpyldpREGPCDLCCD------ACVEVCPTGALRPLDLEEQKvKMGVAV 87
HdrA COG1148
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
300-627 3.89e-05

Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];


Pssm-ID: 440762 [Multi-domain]  Cd Length: 563  Bit Score: 46.78  E-value: 3.89e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275 300 RPDVSKVVPRSEKVAVIGAGPAGLGCADILARAGVQVDVFDRHPEIGGMLTfgippfKLDKT----------VLSQRREI 369
Cdd:COG1148  130 EPLEPIKVPVNKRALVIGGGIAGMTAALELAEQGYEVYLVEKEPELGGRAA------QLHKTfpgldcpqciLEPLIAEV 203
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275 370 FTAMGIDFHLNCEI-------GR-DITFS-----DLTSEYDAVFIGVGtYGMMRADLPHEDA----PGVIQALpfltaht 432
Cdd:COG1148  204 EANPNITVYTGAEVeevsgyvGNfTVTIKkgpreEIEIEVGAIVLATG-FKPYDPTKLGEYGygkyPNVITNL------- 275
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275 433 rQLMGL--PESEEYPLTDVEGKRVVVL---GGGDTTMD-------CLRTSIRlNA---------ASVTCAYRrdEVSMPG 491
Cdd:COG1148  276 -ELERLlaAGKILRPSDGKEPKSVAFIqcvGSRDEENGlpycsrvCCMYALK-QAlylkeknpdADVYIFYR--DIRTYG 351
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275 492 SRKEVVN-AREEGVEFqfnvqpqyiacdedgrltavglIRTAMGEPGPDGRRRPR-----PVAGSEFELPADVLIMAFGF 565
Cdd:COG1148  352 KYEEFYRrAREDGVRF----------------------IRGRVAEIEEDEGGKLVvtvedTLLGEPVEIEADLVVLATGM 409
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 732683275 566 QAH-AMPWLQGS-GIKLDKWGLIQTGDVGYLPTQTHLKKVFAGGdAVHGADLVVTAMAAGRQAA 627
Cdd:COG1148  410 VPSeDNEELAKLlKLPLDQDGFFLEAHPKLRPVETATDGIFLAG-AAHGPKDIPESIAQATAAA 472
PRK12771 PRK12771
putative glutamate synthase (NADPH) small subunit; Provisional
182-224 5.11e-05

putative glutamate synthase (NADPH) small subunit; Provisional


Pssm-ID: 237198 [Multi-domain]  Cd Length: 564  Bit Score: 46.41  E-value: 5.11e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 732683275 182 ISASERKTHFGEIYCGLDPQQATYESDRCV---YCAEKANCNWHCP 224
Cdd:PRK12771 478 LDADERVGDFDEVLGGLTEEEARQEAARCLscgNCFECDNCYGACP 523
PRK09126 PRK09126
FAD-dependent hydroxylase;
313-344 5.27e-05

FAD-dependent hydroxylase;


Pssm-ID: 236385 [Multi-domain]  Cd Length: 392  Bit Score: 46.09  E-value: 5.27e-05
                         10        20        30
                 ....*....|....*....|....*....|..
gi 732683275 313 VAVIGAGPAGLGCADILARAGVQVDVFDRHPE 344
Cdd:PRK09126   6 IVVVGAGPAGLSFARSLAGSGLKVTLIERQPL 37
AlaDh_PNT_C smart01002
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the ...
312-344 5.32e-05

Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the NAD-dependent reversible reductive amination of pyruvate into alanine.


Pssm-ID: 214966 [Multi-domain]  Cd Length: 149  Bit Score: 43.65  E-value: 5.32e-05
                           10        20        30
                   ....*....|....*....|....*....|...
gi 732683275   312 KVAVIGAGPAGLGCADILARAGVQVDVFDRHPE 344
Cdd:smart01002  22 KVVVIGAGVVGLGAAATAKGLGAEVTVLDVRPA 54
PRK06292 PRK06292
dihydrolipoamide dehydrogenase; Validated
313-629 7.12e-05

dihydrolipoamide dehydrogenase; Validated


Pssm-ID: 235774 [Multi-domain]  Cd Length: 460  Bit Score: 45.55  E-value: 7.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275 313 VAVIGAGPAGLGCADILARAGVQVDVFDRHP------------------------EIGGMLTFGI--PPFKLD-KTVLSQ 365
Cdd:PRK06292   6 VIVIGAGPAGYVAARRAAKLGKKVALIEKGPlggtclnvgcipskaliaaaeafhEAKHAEEFGIhaDGPKIDfKKVMAR 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275 366 RREI---FTAM---------GIDF-----------HLncEIG-RDITFsdltseyDAVFIGVGtygmmrADLPheDAPGV 421
Cdd:PRK06292  86 VRRErdrFVGGvveglekkpKIDKikgtarfvdpnTV--EVNgERIEA-------KNIVIATG------SRVP--PIPGV 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275 422 IQAL--PFLTahTRQLMGLpesEEYPltdvegKRVVVLGGGdttmdclrtSIRLNAASvtcAYRR--DEVSMPGSRKEVV 497
Cdd:PRK06292 149 WLILgdRLLT--SDDAFEL---DKLP------KSLAVIGGG---------VIGLELGQ---ALSRlgVKVTVFERGDRIL 205
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275 498 NAREEGVEFQFN-VQPQYIACDEDGRLTAVglirtamgEPGPDGRRRPRPVAGSEFELPADVLIMAFGFQahamPWLQG- 575
Cdd:PRK06292 206 PLEDPEVSKQAQkILSKEFKIKLGAKVTSV--------EKSGDEKVEELEKGGKTETIEADYVLVATGRR----PNTDGl 273
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 732683275 576 ----SGIKLDKWGLIQTGDVgylpTQTHLKKVFAGGDAVHGADLVVTA----MAAGRQAARD 629
Cdd:PRK06292 274 glenTGIELDERGRPVVDEH----TQTSVPGIYAAGDVNGKPPLLHEAadegRIAAENAAGD 331
PRK06292 PRK06292
dihydrolipoamide dehydrogenase; Validated
288-383 7.12e-05

dihydrolipoamide dehydrogenase; Validated


Pssm-ID: 235774 [Multi-domain]  Cd Length: 460  Bit Score: 45.55  E-value: 7.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275 288 RYIT-DTALAMgwrpdvsKVVPRSekVAVIGAGPAGLGCADILARAGVQVDVFDRHPEIGGMltfgippfkLDKTVLSQR 366
Cdd:PRK06292 155 RLLTsDDAFEL-------DKLPKS--LAVIGGGVIGLELGQALSRLGVKVTVFERGDRILPL---------EDPEVSKQA 216
                         90
                 ....*....|....*..
gi 732683275 367 REIFTAMgIDFHLNCEI 383
Cdd:PRK06292 217 QKILSKE-FKIKLGAKV 232
RnfB COG2878
Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit [Energy production and ...
83-137 7.65e-05

Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit [Energy production and conversion]; Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit is part of the Pathway/BioSystem: Na+-translocating Fd:NADH oxidoreductase


Pssm-ID: 442125 [Multi-domain]  Cd Length: 254  Bit Score: 44.60  E-value: 7.65e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275  83 DEQKCIGCKRCAIACPFGVVEMVDT-----IAQKCDLCNqrssgtqACIEVCPTQALRLM 137
Cdd:COG2878  135 CEYGCIGCGDCIKACPFDAIVGAAKgmhtvDEDKCTGCG-------LCVEACPVDCIEMV 187
PLN02172 PLN02172
flavin-containing monooxygenase FMO GS-OX
310-361 8.31e-05

flavin-containing monooxygenase FMO GS-OX


Pssm-ID: 215116 [Multi-domain]  Cd Length: 461  Bit Score: 45.62  E-value: 8.31e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 732683275 310 SEKVAVIGAGPAGLGCADILARAGVQVDVFDRHPEIGGMLTFGiP-----PFKLDKT 361
Cdd:PLN02172  10 SQHVAVIGAGAAGLVAARELRREGHTVVVFEREKQVGGLWVYT-PksesdPLSLDPT 65
FAD_binding_3 pfam01494
FAD binding domain; This domain is involved in FAD binding in a number of enzymes.
312-344 9.33e-05

FAD binding domain; This domain is involved in FAD binding in a number of enzymes.


Pssm-ID: 396193 [Multi-domain]  Cd Length: 348  Bit Score: 45.01  E-value: 9.33e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 732683275  312 KVAVIGAGPAGLGCADILARAGVQVDVFDRHPE 344
Cdd:pfam01494   3 DVLIVGGGPAGLMLALLLARAGVRVVLVERHAT 35
Fer4_7 pfam12838
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
87-133 9.89e-05

4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich. Domain contains two 4Fe4S clusters.


Pssm-ID: 463724 [Multi-domain]  Cd Length: 51  Bit Score: 40.20  E-value: 9.89e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 732683275   87 CIGCKRCAIACPFGVVEM--------VDTIAQKCDLCNqrssGTQACIEVCPTQA 133
Cdd:pfam12838   1 CIGCGACVAACPVGAITLdevgekkgTKTVVIDPERCV----GCGACVAVCPTGA 51
FAD_oxidored pfam12831
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases ...
313-352 1.04e-04

FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases and related proteins.


Pssm-ID: 432816 [Multi-domain]  Cd Length: 420  Bit Score: 44.91  E-value: 1.04e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 732683275  313 VAVIGAGPAGLGCADILARAGVQVDVFDRHPEIGGMLTFG 352
Cdd:pfam12831   2 VVVVGGGPAGVAAAIAAARAGAKVLLVERRGFLGGMLTSG 41
PRK06370 PRK06370
FAD-containing oxidoreductase;
288-383 1.20e-04

FAD-containing oxidoreductase;


Pssm-ID: 235787 [Multi-domain]  Cd Length: 463  Bit Score: 44.81  E-value: 1.20e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275 288 RYIT-DTALAMGWRPdvskvvprsEKVAVIGAGPAGLGCADILARAGVQVDVFDRHPEIggmltfgIPpfKLDKTVLSQR 366
Cdd:PRK06370 157 GYLTnETIFSLDELP---------EHLVIIGGGYIGLEFAQMFRRFGSEVTVIERGPRL-------LP--REDEDVAAAV 218
                         90
                 ....*....|....*..
gi 732683275 367 REIFTAMGIDFHLNCEI 383
Cdd:PRK06370 219 REILEREGIDVRLNAEC 235
DMSOR_beta_like cd16373
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
12-131 1.33e-04

uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.


Pssm-ID: 319895 [Multi-domain]  Cd Length: 154  Bit Score: 42.63  E-value: 1.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275  12 CIGCHACEIAC-----AVAHNQENWPLShsdFRPRIHVVGKgqaanpvACHHCNNApCVTACPVNALTFQSDSVQ----- 81
Cdd:cd16373   16 CIRCGLCVEACptgviQPAGLEDGLEGG---RTPYLDPREG-------PCDLCCDA-CVEVCPTGALRPLDLEEQkvkmg 84
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 732683275  82 ---LDEQKCI------GCKRCAIACPFGVVEMVDT--------IAQKCDLCnqrssGtqACIEVCPT 131
Cdd:cd16373   85 vavIDKDRCLawqggtDCGVCVEACPTEAIAIVLEddvlrpvvDEDKCVGC-----G--LCEYVCPV 144
TIGR00275 TIGR00275
flavoprotein, HI0933 family; The model when searched with a partial length search brings in ...
314-346 1.37e-04

flavoprotein, HI0933 family; The model when searched with a partial length search brings in proteins with a dinucleotide-binding motif (Rossman fold) over the initial 40 residues of the model, including oxidoreductases and dehydrogenases. Partially characterized members include an FAD-binding protein from Bacillus cereus and flavoprotein HI0933 from Haemophilus influenzae. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 272992 [Multi-domain]  Cd Length: 400  Bit Score: 44.51  E-value: 1.37e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 732683275  314 AVIGAGPAGLGCADILARAGVQVDVFDRHPEIG 346
Cdd:TIGR00275   1 IIIGGGAAGLMAAITAARAGLSVLLLEKNKKIG 33
PRK13795 PRK13795
hypothetical protein; Provisional
64-98 1.38e-04

hypothetical protein; Provisional


Pssm-ID: 237510 [Multi-domain]  Cd Length: 636  Bit Score: 44.99  E-value: 1.38e-04
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 732683275  64 CVTACPVNALTFQS--DSVQLDEQKCIGCKRCAIACP 98
Cdd:PRK13795 589 CVGACPTGAIRIEEgkRKISVDEEKCIHCGKCTEVCP 625
Fer4_9 pfam13187
4Fe-4S dicluster domain;
86-134 1.46e-04

4Fe-4S dicluster domain;


Pssm-ID: 463801 [Multi-domain]  Cd Length: 50  Bit Score: 39.84  E-value: 1.46e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 732683275   86 KCIGCKRCAIACPFGVVEM--------VDTIAQKCDLCnqrssgtQACIEVCPTQAL 134
Cdd:pfam13187   1 KCTGCGACVAACPAGAIVPdlvgqtirGDIAGLACIGC-------GACVDACPRGAI 50
DadA COG0665
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
312-379 1.75e-04

Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];


Pssm-ID: 440429 [Multi-domain]  Cd Length: 364  Bit Score: 44.13  E-value: 1.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275 312 KVAVIGAGPAGLGCADILARAGVQVDVFDRHpEIG--------GMLTFGIPPFKLDKTV-LSQR-----REIFTAMGIDF 377
Cdd:COG0665    4 DVVVIGGGIAGLSTAYHLARRGLDVTVLERG-RPGsgasgrnaGQLRPGLAALADRALVrLAREaldlwRELAAELGIDC 82

                 ..
gi 732683275 378 HL 379
Cdd:COG0665   83 DF 84
mhpA PRK06183
bifunctional 3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic acid hydroxylase;
313-345 1.77e-04

bifunctional 3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic acid hydroxylase;


Pssm-ID: 235727 [Multi-domain]  Cd Length: 500  Bit Score: 44.51  E-value: 1.77e-04
                         10        20        30
                 ....*....|....*....|....*....|...
gi 732683275 313 VAVIGAGPAGLGCADILARAGVQVDVFDRHPEI 345
Cdd:PRK06183  13 VVIVGAGPVGLTLANLLGQYGVRVLVLERWPTL 45
NapF_like cd10564
NapF, iron-sulfur subunit of periplasmic nitrate reductase; This family contains NapF protein, ...
55-135 1.91e-04

NapF, iron-sulfur subunit of periplasmic nitrate reductase; This family contains NapF protein, the iron-sulfur subunit of periplasmic nitrate reductase. The periplasmic nitrate reductase NapABC of Escherichia coli likely functions during anaerobic growth in low-nitrate environments; napF operon expression is activated by cyclic AMP receptor protein (Crp). NapF is a subfamily of the beta subunit of DMSO reductase (DMSOR) family. DMSOR family members have a large, periplasmic molybdenum-containing alpha subunit as well as a small beta FeS subunit, and may also have a small gamma subunit. The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.


Pssm-ID: 319886 [Multi-domain]  Cd Length: 139  Bit Score: 41.85  E-value: 1.91e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275  55 ACHHCNnaPCVTACPVNALTFQSD---SVQLDEQKCIGCKRCAIACPFGV--------VEMVDTIAQKCDlcNQRSSGTQ 123
Cdd:cd10564   14 LCTRCG--DCVEACPEGIIVRGDGgfpELDFSRGECTFCGACAEACPEGAldpareapWPLRAEIGDSCL--ALQGVECR 89
                         90
                 ....*....|..
gi 732683275 124 ACIEVCPTQALR 135
Cdd:cd10564   90 SCQDACPTQAIR 101
FixX COG2440
Ferredoxin-like protein FixX [Energy production and conversion];
35-103 2.54e-04

Ferredoxin-like protein FixX [Energy production and conversion];


Pssm-ID: 441981 [Multi-domain]  Cd Length: 87  Bit Score: 40.19  E-value: 2.54e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 732683275  35 HSDFRPRIHVvgkgqaANPVACH-HCNNAPCVTACPVNALTFQSD-SVQLDEQKCIGCKRCAIACPFGVVE 103
Cdd:COG2440    8 VDEDQPHIKV------KDPDICIaRCLAKPCTRYCPAGVYEIVGDgRLQINYENCLECGTCRIKCPTQNIT 72
flavo_MJ0208 TIGR02700
archaeoflavoprotein, MJ0208 family; This model describes one of two paralogous families of ...
56-102 2.54e-04

archaeoflavoprotein, MJ0208 family; This model describes one of two paralogous families of archaealflavoprotein. The other, described by TIGR02699 and typified by the partially characterized AF1518 of Archaeoglobus fulgidus, is a homodimeric FMN-containing flavoprotein that accepts electrons from ferredoxin and can transfer them to various oxidoreductases. The function of this protein family is unknown. [Unknown function, General]


Pssm-ID: 131747 [Multi-domain]  Cd Length: 234  Bit Score: 42.94  E-value: 2.54e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 732683275   56 CHHCNNapCVTACPVNALTFQSDSVQLDEQKCIGCKRCAIACPFGVV 102
Cdd:TIGR02700 150 CKGCGI--CVDACPRSAIDMVDGKAFIRLLKCVGCGKCKEACPYNAI 194
RnfB COG2878
Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit [Energy production and ...
64-105 2.71e-04

Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit [Energy production and conversion]; Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit is part of the Pathway/BioSystem: Na+-translocating Fd:NADH oxidoreductase


Pssm-ID: 442125 [Multi-domain]  Cd Length: 254  Bit Score: 43.06  E-value: 2.71e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 732683275  64 CVTACPVNALTFQSDSV-QLDEQKCIGCKRCAIACPFGVVEMV 105
Cdd:COG2878  145 CIKACPFDAIVGAAKGMhTVDEDKCTGCGLCVEACPVDCIEMV 187
Ppro0129 COG2907
Predicted flavin-containing amine oxidase [General function prediction only];
309-347 2.71e-04

Predicted flavin-containing amine oxidase [General function prediction only];


Pssm-ID: 442151 [Multi-domain]  Cd Length: 423  Bit Score: 43.95  E-value: 2.71e-04
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 732683275 309 RSEKVAVIGAGPAGLGCADILARAgVQVDVFDRHPEIGG 347
Cdd:COG2907    2 ARMRIAVIGSGISGLTAAWLLSRR-HDVTLFEANDRLGG 39
PRK08222 PRK08222
hydrogenase 4 subunit H; Validated
81-139 2.87e-04

hydrogenase 4 subunit H; Validated


Pssm-ID: 181301 [Multi-domain]  Cd Length: 181  Bit Score: 42.05  E-value: 2.87e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 732683275  81 QLDEQKCIGCKRCAIACPFGVVEMVDTIAQ----------KCDLCNQrssgtqaCIEVCPTQALRLMDD 139
Cdd:PRK08222  34 DLMPSQCIACGACTCACPANALTIQTDDQQnsrtwqlylgRCIYCGR-------CEEVCPTRAIQLTNN 95
mnmC PRK01747
bifunctional tRNA (5-methylaminomethyl-2-thiouridine)(34)-methyltransferase MnmD/FAD-dependent ...
308-346 2.89e-04

bifunctional tRNA (5-methylaminomethyl-2-thiouridine)(34)-methyltransferase MnmD/FAD-dependent 5-carboxymethylaminomethyl-2-thiouridine(34) oxidoreductase MnmC;


Pssm-ID: 234978 [Multi-domain]  Cd Length: 662  Bit Score: 44.07  E-value: 2.89e-04
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 732683275 308 PRSEKVAVIGAGPAGLGCADILARAGVQVDVFDRHPEIG 346
Cdd:PRK01747 258 PKARDAAIIGGGIAGAALALALARRGWQVTLYEADEAPA 296
rnfB TIGR01944
electron transport complex, RnfABCDGE type, B subunit; The six subunit complex RnfABCDGE in ...
82-136 3.26e-04

electron transport complex, RnfABCDGE type, B subunit; The six subunit complex RnfABCDGE in Rhodobacter capsulatus encodes an apparent NADH oxidoreductase responsible for electron transport to nitrogenase, necessary for nitrogen fixation. A closely related complex in E. coli, RsxABCDGE (Reducer of SoxR), reduces the 2Fe-2S-containing superoxide sensor SoxR, active as a transcription factor when oxidized. This family of putative NADH oxidoreductase complexes exists in many of the same species as the related NQR, a Na(+)-translocating NADH-quinone reductase, but is distinct. This model describes the B subunit. [Energy metabolism, Electron transport]


Pssm-ID: 273887 [Multi-domain]  Cd Length: 165  Bit Score: 41.71  E-value: 3.26e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 732683275   82 LDEQKCIGCKRCAIACP----FGVVEMVDTIAQkcDLCnqrsSGTQACIEVCPTQALRL 136
Cdd:TIGR01944 110 IDEDNCIGCTKCIQACPvdaiVGAAKAMHTVIA--DEC----TGCDLCVEPCPTDCIEM 162
PRK06116 PRK06116
glutathione reductase; Validated
452-637 3.51e-04

glutathione reductase; Validated


Pssm-ID: 235701 [Multi-domain]  Cd Length: 450  Bit Score: 43.61  E-value: 3.51e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275 452 KRVVVLGGGdttmdclrtSIR------LNA--ASVTCAYRRDEVSM---PGSRKEVVNARE-EGVEFQFNVQPQYIACDE 519
Cdd:PRK06116 168 KRVAVVGAG---------YIAvefagvLNGlgSETHLFVRGDAPLRgfdPDIRETLVEEMEkKGIRLHTNAVPKAVEKNA 238
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275 520 DGRLTavglIRTAMGEpgpdgrrrprpvagsefELPADVLIMAFGfqahAMPWLQG-----SGIKLDKWGLIQTGDVgyl 594
Cdd:PRK06116 239 DGSLT----LTLEDGE-----------------TLTVDCLIWAIG----REPNTDGlglenAGVKLNEKGYIIVDEY--- 290
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 732683275 595 pTQTHLKKVFAGGDAVHGADLVVTAMAAGRQAARdmlTLFDTK 637
Cdd:PRK06116 291 -QNTNVPGIYAVGDVTGRVELTPVAIAAGRRLSE---RLFNNK 329
PLN00093 PLN00093
geranylgeranyl diphosphate reductase; Provisional
301-362 3.69e-04

geranylgeranyl diphosphate reductase; Provisional


Pssm-ID: 177713 [Multi-domain]  Cd Length: 450  Bit Score: 43.59  E-value: 3.69e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 732683275 301 PDVSKVVPRSEKVAVIGAGPAGLGCADILARAGVQVDVFDRHPE----IGG-----ML-TFGIPPFKLDKTV 362
Cdd:PLN00093  30 AASKKLSGRKLRVAVIGGGPAGACAAETLAKGGIETFLIERKLDnakpCGGaiplcMVgEFDLPLDIIDRKV 101
PRK10194 PRK10194
ferredoxin-type protein NapF;
11-102 3.74e-04

ferredoxin-type protein NapF;


Pssm-ID: 182296 [Multi-domain]  Cd Length: 163  Bit Score: 41.55  E-value: 3.74e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275  11 ECIGCHACEIACavahnqenwplSHSDFRPR-------IHVVGKG-QAANPVACHHCNNApcvtaCPVNALTFQSD---- 78
Cdd:PRK10194  67 ECSFCYACAQAC-----------PESLFSPRhtrawdlQFTIGDAcLAYQSVECRRCQDS-----CEPMAIIFRPTlsgi 130
                         90       100
                 ....*....|....*....|....*
gi 732683275  79 -SVQLDEQKCIGCKRCAIACPFGVV 102
Cdd:PRK10194 131 yQPQLNSQLCNGCGACAASCPVSAI 155
DMSOR_beta-like cd04410
Beta subunit of the DMSO Reductase (DMSOR) family; This family consists of the small beta ...
82-134 3.74e-04

Beta subunit of the DMSO Reductase (DMSOR) family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.


Pssm-ID: 319870 [Multi-domain]  Cd Length: 136  Bit Score: 40.84  E-value: 3.74e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275  82 LDEQKCIGCKRCAIACPF-----------------GVVEMVDTIAQKCDLCNQRssgtqACIEVCPTQAL 134
Cdd:cd04410    3 VDLDRCIGCGTCEVACKQehglrpgpdwsrikvieGGGLERAFLPVSCMHCEDP-----PCVKACPTGAI 67
DMSOR_beta_like cd16371
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
12-75 4.73e-04

uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.


Pssm-ID: 319893 [Multi-domain]  Cd Length: 140  Bit Score: 40.62  E-value: 4.73e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 732683275  12 CIGCHACEIACavahnqenwPLSHSDFRPRIHVVGKgqaanpvaCHHCNN------AP-CVTACPVNALTF 75
Cdd:cd16371   86 CIGCGYCVWAC---------PYGAPQYNPETGKMDK--------CDMCVDrldegeKPaCVAACPTRALDF 139
PRK06185 PRK06185
FAD-dependent oxidoreductase;
313-343 4.76e-04

FAD-dependent oxidoreductase;


Pssm-ID: 235729 [Multi-domain]  Cd Length: 407  Bit Score: 42.92  E-value: 4.76e-04
                         10        20        30
                 ....*....|....*....|....*....|.
gi 732683275 313 VAVIGAGPAGLGCADILARAGVQVDVFDRHP 343
Cdd:PRK06185   9 CCIVGGGPAGMMLGLLLARAGVDVTVLEKHA 39
PRK07118 PRK07118
Fe-S cluster domain-containing protein;
12-111 5.14e-04

Fe-S cluster domain-containing protein;


Pssm-ID: 235941 [Multi-domain]  Cd Length: 280  Bit Score: 42.23  E-value: 5.14e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275  12 CIGCHACEIACavahnqenwPLSHSDFRP---RIHVV----GKGQAAN---PVACHHCnnAPCVTACPVNALTFQSDSVQ 81
Cdd:PRK07118 170 CTGCGACVKAC---------PRNVIELIPksaRVFVAcnskDKGKAVKkvcEVGCIGC--GKCVKACPAGAITMENNLAV 238
                         90       100       110
                 ....*....|....*....|....*....|
gi 732683275  82 LDEQKCIGCKRCAIACPFGVVEMVDTIAQK 111
Cdd:PRK07118 239 IDQEKCTSCGKCVEKCPTKAIRILNKPPKV 268
Fer4_10 pfam13237
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ...
80-130 5.26e-04

4Fe-4S dicluster domain; This family includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. The structure of the domain is an alpha-antiparallel beta sandwich.


Pssm-ID: 404174 [Multi-domain]  Cd Length: 56  Bit Score: 38.39  E-value: 5.26e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 732683275   80 VQLDEQKCIGCKRCAIACPFG-----------VVEMVDTIAQKCDLCNqrssgtqACIEVCP 130
Cdd:pfam13237   2 VVIDPDKCIGCGRCTAACPAGltrvgaiverlEGEAVRIGVWKCIGCG-------ACVEACP 56
Pyr_redox_3 pfam13738
Pyridine nucleotide-disulphide oxidoreductase;
320-586 6.29e-04

Pyridine nucleotide-disulphide oxidoreductase;


Pssm-ID: 404603 [Multi-domain]  Cd Length: 296  Bit Score: 42.21  E-value: 6.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275  320 PAGLGCADILARAGVQ----------VDVFDRHPEIGGMLT-------FGI-----------PPFKLDKTVLSQR----- 366
Cdd:pfam13738   1 PAGIGCAIALKKAGLEdylilekgniGNSFYRYPTHMTFFSpsftsngFGIpdlnaispgtsPAFTFNREHPSGNeyaey 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275  367 -REIFTAMGIDFHLNCEIgRDITFSDL-----TS--EYDA--VFIGVGTYgmmraDLPHedapgviqalpfltahtrqLM 436
Cdd:pfam13738  81 lRRVADHFELPINLFEEV-TSVKKEDDgfvvtTSkgTYQAryVIIATGEF-----DFPN-------------------KL 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275  437 GLPE-----SEEYPLTDVEGKRVVVLGGGDTTMDclrTSIRLNA--ASVTCAYRRDEVSMPGSR-------------KEV 496
Cdd:pfam13738 136 GVPElpkhySYVKDFHPYAGQKVVVIGGYNSAVD---AALELVRkgARVTVLYRGSEWEDRDSDpsyslspdtlnrlEEL 212
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275  497 VNAREEGVEFQFNVQpqyiacdEDGRLTAVGLIRTamgepgPDGRrrprpvagsEFELPADVlIMAFGFQAHAMPwLQGS 576
Cdd:pfam13738 213 VKNGKIKAHFNAEVK-------EITEVDVSYKVHT------EDGR---------KVTSNDDP-ILATGYHPDLSF-LKKG 268
                         330
                  ....*....|
gi 732683275  577 GIKLDKWGLI 586
Cdd:pfam13738 269 LFELDEDGRP 278
Ala_dh_like cd01620
Alanine dehydrogenase and related dehydrogenases; Alanine dehydrogenase/Transhydrogenase, such ...
301-373 6.89e-04

Alanine dehydrogenase and related dehydrogenases; Alanine dehydrogenase/Transhydrogenase, such as the hexameric L-alanine dehydrogenase of Phormidium lapideum, contain 2 Rossmann fold-like domains linked by an alpha helical region. Related proteins include Saccharopine Dehydrogenase (SDH), bifunctional lysine ketoglutarate reductase /saccharopine dehydrogenase enzyme, N(5)-(carboxyethyl)ornithine synthase, and Rubrum transdehydrogenase. Alanine dehydrogenase (L-AlaDH) catalyzes the NAD-dependent conversion of pyrucate to L-alanine via reductive amination. Transhydrogenases found in bacterial and inner mitochondrial membranes link NAD(P)(H)-dependent redox reactions to proton translocation. The energy of the proton electrochemical gradient (delta-p), generated by the respiratory electron transport chain, is consumed by transhydrogenase in NAD(P)+ reduction. Transhydrogenase is likely involved in the regulation of the citric acid cycle. Rubrum transhydrogenase has 3 components, dI, dII, and dIII. dII spans the membrane while dI and dIII protrude on the cytoplasmic/matirx side. DI contains 2 domains with Rossmann folds, linked by a long alpha helix, and contains a NAD binding site. Two dI polypeptides (represented in this sub-family) spontaneously form a heterotrimer with one dIII in the absence of dII. In the heterotrimer, both dI chains may bind NAD, but only one is well-ordered. dIII also binds a well-ordered NADP, but in a different orientation than classical Rossmann domains.


Pssm-ID: 240621 [Multi-domain]  Cd Length: 317  Bit Score: 42.01  E-value: 6.89e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 732683275 301 PDVSKVVPRSE--KVAVIGAGPAGLGCADILARAGVQVDVFDRHPEiggmLTFGIPPFKLDKTVLSQRREIFTAM 373
Cdd:cd01620  151 GGRMGGAGGVPpaKVLIIGAGVVGLGAAKIAKKLGANVLVYDIKEE----KLKGVETLGGSRLRYSQKEELEKEL 221
PRK06753 PRK06753
hypothetical protein; Provisional
312-345 7.17e-04

hypothetical protein; Provisional


Pssm-ID: 168661 [Multi-domain]  Cd Length: 373  Bit Score: 42.37  E-value: 7.17e-04
                         10        20        30
                 ....*....|....*....|....*....|....
gi 732683275 312 KVAVIGAGPAGLGCADILARAGVQVDVFDRHPEI 345
Cdd:PRK06753   2 KIAIIGAGIGGLTAAALLQEQGHEVKVFEKNESV 35
PRK08222 PRK08222
hydrogenase 4 subunit H; Validated
52-114 7.44e-04

hydrogenase 4 subunit H; Validated


Pssm-ID: 181301 [Multi-domain]  Cd Length: 181  Bit Score: 40.89  E-value: 7.44e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 732683275  52 NPVACHHCnnAPCVTACPVNALTFQSD------SVQLDEQKCIGCKRCAIACPFGVVEMVD----TIAQKCDL 114
Cdd:PRK08222  36 MPSQCIAC--GACTCACPANALTIQTDdqqnsrTWQLYLGRCIYCGRCEEVCPTRAIQLTNnfelTVTNKADL 106
Thi4 pfam01946
Thi4 family; This family includes Swiss:P32318 a putative thiamine biosynthetic enzyme.
313-347 7.74e-04

Thi4 family; This family includes Swiss:P32318 a putative thiamine biosynthetic enzyme.


Pssm-ID: 460393  Cd Length: 232  Bit Score: 41.69  E-value: 7.74e-04
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 732683275  313 VAVIGAGPAGLGCADILARA-GVQVDVFDRHPEIGG 347
Cdd:pfam01946  20 VVIVGAGSSGLTAAYYLAKNrGLKVAIIERSVSPGG 55
3HCDH_N pfam02737
3-hydroxyacyl-CoA dehydrogenase, NAD binding domain; This family also includes lambda ...
312-345 8.05e-04

3-hydroxyacyl-CoA dehydrogenase, NAD binding domain; This family also includes lambda crystallin.


Pssm-ID: 397037 [Multi-domain]  Cd Length: 180  Bit Score: 40.98  E-value: 8.05e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 732683275  312 KVAVIGAGPAGLGCADILARAGVQVDVFDRHPEI 345
Cdd:pfam02737   1 KVAVIGAGTMGAGIAQVFALAGLEVVLVDISEEA 34
NuoI TIGR01971
NADH-quinone oxidoreductase, chain I; This model represents the I subunit (one of 14: A->N) of ...
84-136 9.75e-04

NADH-quinone oxidoreductase, chain I; This model represents the I subunit (one of 14: A->N) of the NADH-quinone oxidoreductase complex I which generally couples NADH and ubiquinone oxidation/reduction in bacteria and mammalian mitochondria, but may act on NADPH and/or plastoquinone in cyanobacteria and plant chloroplasts. This model excludes "I" subunits from the closely related F420H2 dehydrogenase and formate hydrogenlyase complexes. [Energy metabolism, Electron transport]


Pssm-ID: 273902 [Multi-domain]  Cd Length: 122  Bit Score: 39.32  E-value: 9.75e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 732683275   84 EQKCIGCKRCAIACPFGVVEMVDtiaQKCDLCNQRSSGTQA----------CIEVCPTQALRL 136
Cdd:TIGR01971  42 EEKCIGCTLCAAVCPADAIRVVP---AEGEDGKRRLKFYEInfgrcifcglCEEACPTDAIVL 101
Fer4_21 pfam14697
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
83-131 9.94e-04

4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich. Domain contains two 4Fe4S clusters.


Pssm-ID: 434137 [Multi-domain]  Cd Length: 59  Bit Score: 37.65  E-value: 9.94e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 732683275   83 DEQKCIGCKRCAIACPFGVVE--------MVDTIAQKCDLCNqrssgtqACIEVCPT 131
Cdd:pfam14697   4 DEDTCIGCGKCYIACPDTSHQaivgdgkrHHTVIEDECTGCN-------LCVSVCPV 53
Pyr_redox pfam00070
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
453-524 1.20e-03

Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.


Pssm-ID: 425450 [Multi-domain]  Cd Length: 80  Bit Score: 37.95  E-value: 1.20e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 732683275  453 RVVVLGGGDTTMDCLRTSIRLnAASVTCAYRRDEVsMPGSRKEVVNA-----REEGVEFQFNVQPQYIACDEDGRLT 524
Cdd:pfam00070   1 RVVVVGGGYIGLELAGALARL-GSKVTVVERRDRL-LPGFDPEIAKIlqeklEKNGIEFLLNTTVEAIEGNGDGVVV 75
PRK06273 PRK06273
ferredoxin; Provisional
83-107 1.26e-03

ferredoxin; Provisional


Pssm-ID: 235764 [Multi-domain]  Cd Length: 165  Bit Score: 40.08  E-value: 1.26e-03
                         10        20
                 ....*....|....*....|....*
gi 732683275  83 DEQKCIGCKRCAIACPFGVVEMVDT 107
Cdd:PRK06273  47 FEELCIGCGGCANVCPTKAIEMIPV 71
PLN02487 PLN02487
zeta-carotene desaturase
312-347 1.29e-03

zeta-carotene desaturase


Pssm-ID: 215268 [Multi-domain]  Cd Length: 569  Bit Score: 41.71  E-value: 1.29e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 732683275 312 KVAVIGAGPAGLGCADILARAGVQVDVFDRHPEIGG 347
Cdd:PLN02487  77 KVAIIGAGLAGMSTAVELLDQGHEVDIYESRPFIGG 112
carotene-cycl TIGR01790
lycopene cyclase family protein; This family includes lycopene beta and epsilion cyclases ...
313-353 1.34e-03

lycopene cyclase family protein; This family includes lycopene beta and epsilion cyclases (which form beta and delta carotene, respectively) from bacteria and plants as well as the plant capsanthin/capsorubin and neoxanthin cyclases which appear to have evolved from the plant lycopene cyclases. The plant lycopene epsilon cyclases also transform neurosporene to alpha zeacarotene.


Pssm-ID: 130850 [Multi-domain]  Cd Length: 388  Bit Score: 41.65  E-value: 1.34e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 732683275  313 VAVIGAGPAGLGCADILARAGVQVDVFDRHPEIGGMLTFGI 353
Cdd:TIGR01790   2 LAVIGGGPAGLAIALELARPGLRVQLIEPHPPIPGNHTYGV 42
YdhS COG4529
Uncharacterized NAD(P)/FAD-binding protein YdhS [General function prediction only];
308-348 1.40e-03

Uncharacterized NAD(P)/FAD-binding protein YdhS [General function prediction only];


Pssm-ID: 443597 [Multi-domain]  Cd Length: 466  Bit Score: 41.48  E-value: 1.40e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 732683275 308 PRSEKVAVIGAGPAGLGCADILAR---AGVQVDVFDRHPEIG-GM 348
Cdd:COG4529    3 GARKRIAIIGGGASGTALAIHLLRrapEPLRITLFEPRPELGrGV 47
NapF_like cd10564
NapF, iron-sulfur subunit of periplasmic nitrate reductase; This family contains NapF protein, ...
10-136 1.48e-03

NapF, iron-sulfur subunit of periplasmic nitrate reductase; This family contains NapF protein, the iron-sulfur subunit of periplasmic nitrate reductase. The periplasmic nitrate reductase NapABC of Escherichia coli likely functions during anaerobic growth in low-nitrate environments; napF operon expression is activated by cyclic AMP receptor protein (Crp). NapF is a subfamily of the beta subunit of DMSO reductase (DMSOR) family. DMSOR family members have a large, periplasmic molybdenum-containing alpha subunit as well as a small beta FeS subunit, and may also have a small gamma subunit. The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.


Pssm-ID: 319886 [Multi-domain]  Cd Length: 139  Bit Score: 39.15  E-value: 1.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275  10 AECIGCHACEIACavahnqenwplshsdfrPRiHVVGKGQAANPV------ACHHCnnAPCVTACPVNALTFQSDS---- 79
Cdd:cd10564   13 DLCTRCGDCVEAC-----------------PE-GIIVRGDGGFPEldfsrgECTFC--GACAEACPEGALDPAREApwpl 72
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 732683275  80 -VQLDEqKC-----IGCKRCAIACPFGVVEMVDTIAQKC------DLCNqrssGTQACIEVCPTQALRL 136
Cdd:cd10564   73 rAEIGD-SClalqgVECRSCQDACPTQAIRFRPRLGGIAlpeldaDACT----GCGACVSVCPVGAITL 136
DMSOR_beta_like cd16374
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
80-135 1.63e-03

uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.


Pssm-ID: 319896 [Multi-domain]  Cd Length: 139  Bit Score: 39.18  E-value: 1.63e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 732683275  80 VQLDEQKCIGCKRCAIACPF----------GVVEMVDTIAQKCDLCNqrssgTQACIEVCPTQALR 135
Cdd:cd16374    1 VYVDPERCIGCRACEIACARehsgkprisvEVVEDLASVPVRCRHCE-----DAPCMEVCPTGAIY 61
Fer4_7 pfam12838
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
12-72 1.67e-03

4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich. Domain contains two 4Fe4S clusters.


Pssm-ID: 463724 [Multi-domain]  Cd Length: 51  Bit Score: 36.74  E-value: 1.67e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 732683275   12 CIGCHACEIACAVAhnqenwplsHSDFRPRIHVVGKGQAA-NPVACHHCNNapCVTACPVNA 72
Cdd:pfam12838   1 CIGCGACVAACPVG---------AITLDEVGEKKGTKTVViDPERCVGCGA--CVAVCPTGA 51
PRK12409 PRK12409
D-amino acid dehydrogenase small subunit; Provisional
312-342 1.92e-03

D-amino acid dehydrogenase small subunit; Provisional


Pssm-ID: 237093 [Multi-domain]  Cd Length: 410  Bit Score: 41.16  E-value: 1.92e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 732683275 312 KVAVIGAGPAGLGCADILARAGVQVDVFDRH 342
Cdd:PRK12409   3 HIAVIGAGITGVTTAYALAQRGYQVTVFDRH 33
Zn_ADH7 cd08261
Alcohol dehydrogenases of the MDR family; This group contains members identified as related to ...
311-344 1.93e-03

Alcohol dehydrogenases of the MDR family; This group contains members identified as related to zinc-dependent alcohol dehydrogenase and other members of the MDR family. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group includes various activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176222 [Multi-domain]  Cd Length: 337  Bit Score: 41.02  E-value: 1.93e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 732683275 311 EKVAVIGAGPAGLGCADILARAGVQVDVFDRHPE 344
Cdd:cd08261  161 DTVLVVGAGPIGLGVIQVAKARGARVIVVDIDDE 194
Fer4 pfam00037
4Fe-4S binding domain; Superfamily includes proteins containing domains which bind to ...
80-103 2.06e-03

4Fe-4S binding domain; Superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich.


Pssm-ID: 459642 [Multi-domain]  Cd Length: 24  Bit Score: 35.69  E-value: 2.06e-03
                          10        20
                  ....*....|....*....|....
gi 732683275   80 VQLDEQKCIGCKRCAIACPFGVVE 103
Cdd:pfam00037   1 VVIDEEKCIGCGACVEVCPVGAIT 24
Tdh COG1063
Threonine dehydrogenase or related Zn-dependent dehydrogenase [Amino acid transport and ...
311-380 2.27e-03

Threonine dehydrogenase or related Zn-dependent dehydrogenase [Amino acid transport and metabolism, General function prediction only]; Threonine dehydrogenase or related Zn-dependent dehydrogenase is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway


Pssm-ID: 440683 [Multi-domain]  Cd Length: 341  Bit Score: 40.51  E-value: 2.27e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 732683275 311 EKVAVIGAGPAGLGCADILARAGV-QVDVFDRHPEiggmltfgippfkldktvlsqRREIFTAMGIDFHLN 380
Cdd:COG1063  163 DTVLVIGAGPIGLLAALAARLAGAaRVIVVDRNPE---------------------RLELARELGADAVVN 212
napG PRK09476
quinol dehydrogenase periplasmic component; Provisional
2-99 2.79e-03

quinol dehydrogenase periplasmic component; Provisional


Pssm-ID: 236534 [Multi-domain]  Cd Length: 254  Bit Score: 39.99  E-value: 2.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275   2 NKFIAAeaaeCIGCHACEIACAVAHNQENWPLSHSD-----FRPRihvvgkgqaanPVACHHCNNAPCVTACPVNALTFQ 76
Cdd:PRK09476  55 NDFLSA----CIRCGLCVQACPYDTLKLATLASGLSagtpyFVAR-----------DIPCEMCEDIPCVKACPSGALDRE 119
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 732683275  77 SD---------SVQLDEQKCIG-----CKRCAIACPF 99
Cdd:PRK09476 120 LVdiddarmglAVLVDQENCLNfqglrCDVCYRVCPL 156
PRK08132 PRK08132
FAD-dependent oxidoreductase; Provisional
300-346 2.91e-03

FAD-dependent oxidoreductase; Provisional


Pssm-ID: 236158 [Multi-domain]  Cd Length: 547  Bit Score: 40.62  E-value: 2.91e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 732683275 300 RPDVSKVVPRSEKVAVIGAGPAGLGCADILARAGVQVDVFDRHPEIG 346
Cdd:PRK08132  13 HADQDADDPARHPVVVVGAGPVGLALAIDLAQQGVPVVLLDDDDTLS 59
FadB COG1250
3-hydroxyacyl-CoA dehydrogenase [Lipid transport and metabolism]; 3-hydroxyacyl-CoA ...
311-344 2.93e-03

3-hydroxyacyl-CoA dehydrogenase [Lipid transport and metabolism]; 3-hydroxyacyl-CoA dehydrogenase is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440862 [Multi-domain]  Cd Length: 281  Bit Score: 40.09  E-value: 2.93e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 732683275 311 EKVAVIGAGPAGLGCADILARAGVQVDVFDRHPE 344
Cdd:COG1250    3 KKVAVIGAGTMGAGIAAVFANAGYEVVLLDISPE 36
GG-red-SF TIGR02032
geranylgeranyl reductase family; This model represents a subfamily which includes ...
313-346 3.73e-03

geranylgeranyl reductase family; This model represents a subfamily which includes geranylgeranyl reductases involved in chlorophyll and bacteriochlorophyll biosynthesis as well as other related enzymes which may also act on geranylgeranyl groups or related substrates. [Biosynthesis of cofactors, prosthetic groups, and carriers, Chlorophyll and bacteriochlorphyll]


Pssm-ID: 273936 [Multi-domain]  Cd Length: 295  Bit Score: 39.61  E-value: 3.73e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 732683275  313 VAVIGAGPAGLGCADILARAGVQVDVFDRHPEIG 346
Cdd:TIGR02032   3 VVVVGAGPAGASAAYRLADKGLRVLLLEKKSFPR 36
PRK07251 PRK07251
FAD-containing oxidoreductase;
311-404 4.19e-03

FAD-containing oxidoreductase;


Pssm-ID: 180907 [Multi-domain]  Cd Length: 438  Bit Score: 40.12  E-value: 4.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275 311 EKVAVIGAGPAGLGCADILARAGVQVDVFDRHPEIGGmltfgippfKLDKTVLSQRREIFTAMGIDFHLNC---EIGRD- 386
Cdd:PRK07251 158 ERLGIIGGGNIGLEFAGLYNKLGSKVTVLDAASTILP---------REEPSVAALAKQYMEEDGITFLLNAhttEVKNDg 228
                         90       100
                 ....*....|....*....|..
gi 732683275 387 ----ITFSDLTSEYDAVFIGVG 404
Cdd:PRK07251 229 dqvlVVTEDETYRFDALLYATG 250
PRK12771 PRK12771
putative glutamate synthase (NADPH) small subunit; Provisional
56-105 4.30e-03

putative glutamate synthase (NADPH) small subunit; Provisional


Pssm-ID: 237198 [Multi-domain]  Cd Length: 564  Bit Score: 40.24  E-value: 4.30e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 732683275  56 CHHCNNapCVTACPVNALTF--QSDSVQLDEQKCIGCKRCAIACPFGVVEMV 105
Cdd:PRK12771 512 CFECDN--CYGACPQDAIIKlgPGRRYHFDYDKCTGCHICADVCPCGAIEMG 561
Fer4_6 pfam12837
4Fe-4S binding domain; This superfamily includes proteins containing domains which bind to ...
83-101 4.94e-03

4Fe-4S binding domain; This superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich.


Pssm-ID: 432822 [Multi-domain]  Cd Length: 24  Bit Score: 34.90  E-value: 4.94e-03
                          10
                  ....*....|....*....
gi 732683275   83 DEQKCIGCKRCAIACPFGV 101
Cdd:pfam12837   5 DPDKCIGCGRCVVVCPYGA 23
PLN02976 PLN02976
amine oxidase
312-347 5.15e-03

amine oxidase


Pssm-ID: 215527 [Multi-domain]  Cd Length: 1713  Bit Score: 40.24  E-value: 5.15e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 732683275  312 KVAVIGAGPAGLGCADILARAGVQVDVFDRHPEIGG 347
Cdd:PLN02976  695 KIIVVGAGPAGLTAARHLQRQGFSVTVLEARSRIGG 730
Nar1 COG4624
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];
2-82 5.17e-03

Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];


Pssm-ID: 443663 [Multi-domain]  Cd Length: 450  Bit Score: 39.62  E-value: 5.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275   2 NKFIAAEAAECIGCHACEIACAVAhnqenwplshsdfrpRIHVVGKGQAANPVACHHCNNapCVTACPVNALTFQSDSVQ 81
Cdd:COG4624   83 GPSIIRDKEKCKNCYPCVRACPVK---------------AIKVDDGKAEIDEEKCISCGQ--CVAVCPFGAITEKSDIEK 145

                 .
gi 732683275  82 L 82
Cdd:COG4624  146 V 146
MDR cd05188
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
293-344 5.27e-03

Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; The medium chain reductase/dehydrogenases (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH) , quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines. Other MDR members have only a catalytic zinc, and some contain no coordinated zinc.


Pssm-ID: 176178 [Multi-domain]  Cd Length: 271  Bit Score: 39.23  E-value: 5.27e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 732683275 293 TALAMGWRP-DVSKVVPRSEKVAVIGAGPAGLGCADILARAGVQVDVFDRHPE 344
Cdd:cd05188  117 EPLATAYHAlRRAGVLKPGDTVLVLGAGGVGLLAAQLAKAAGARVIVTDRSDE 169
PRK08243 PRK08243
4-hydroxybenzoate 3-monooxygenase; Validated
312-341 6.19e-03

4-hydroxybenzoate 3-monooxygenase; Validated


Pssm-ID: 236198 [Multi-domain]  Cd Length: 392  Bit Score: 39.40  E-value: 6.19e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 732683275 312 KVAVIGAGPAGLGCADILARAGVQVDVFDR 341
Cdd:PRK08243   4 QVAIIGAGPAGLLLGQLLHLAGIDSVVLER 33
Malic_M smart00919
Malic enzyme, NAD binding domain; Malic enzymes (malate oxidoreductases) catalyse the ...
312-342 6.34e-03

Malic enzyme, NAD binding domain; Malic enzymes (malate oxidoreductases) catalyse the oxidative decarboxylation of malate to form pyruvate.


Pssm-ID: 214912  Cd Length: 231  Bit Score: 38.55  E-value: 6.34e-03
                           10        20        30
                   ....*....|....*....|....*....|....
gi 732683275   312 KVAVIGAGPAGLGCADILARAGVQVD---VFDRH 342
Cdd:smart00919  27 RIVVNGAGAAGIGIAKLLVAAGVKRKniwLVDSK 60
RnfB COG2878
Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit [Energy production and ...
9-135 6.37e-03

Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit [Energy production and conversion]; Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit is part of the Pathway/BioSystem: Na+-translocating Fd:NADH oxidoreductase


Pssm-ID: 442125 [Multi-domain]  Cd Length: 254  Bit Score: 38.82  E-value: 6.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275   9 AAECIGCHACEIACAV-----AHNQenwplshsdfrprIHVVgkgqaaNPVACHHCNNapCVTACPVNALTFQSDSVQL- 82
Cdd:COG2878  136 EYGCIGCGDCIKACPFdaivgAAKG-------------MHTV------DEDKCTGCGL--CVEACPVDCIEMVPVSPTVv 194
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 732683275  83 --------DEQKCIGCKR-CAIACPFGVVEMVDTIAQKCDLCNQRssGTQACIEVCPTQALR 135
Cdd:COG2878  195 vsswdkgkAVRKVVGCIGlCCKKCCPAAAITVNNLAAIIDYKKCT--CCGCCEKCCPTAIIA 254
PRK05113 PRK05113
electron transport complex protein RnfB; Provisional
83-132 6.44e-03

electron transport complex protein RnfB; Provisional


Pssm-ID: 235347 [Multi-domain]  Cd Length: 191  Bit Score: 38.39  E-value: 6.44e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 732683275  83 DEQKCIGCKRCAIACPfgvvemVDTI--AQKC------DLCnqrsSGTQACIEVCPTQ 132
Cdd:PRK05113 112 DEDNCIGCTKCIQACP------VDAIvgATKAmhtvisDLC----TGCDLCVAPCPTD 159
MurD COG0771
UDP-N-acetylmuramoylalanine-D-glutamate ligase [Cell wall/membrane/envelope biogenesis]; ...
312-344 6.63e-03

UDP-N-acetylmuramoylalanine-D-glutamate ligase [Cell wall/membrane/envelope biogenesis]; UDP-N-acetylmuramoylalanine-D-glutamate ligase is part of the Pathway/BioSystem: Mureine biosynthesis


Pssm-ID: 440534 [Multi-domain]  Cd Length: 445  Bit Score: 39.29  E-value: 6.63e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 732683275 312 KVAVIGAGPAGLGCADILARAGVQVDVFDRHPE 344
Cdd:COG0771    6 KVLVLGLGKSGLAAARLLAKLGAEVTVSDDRPA 38
FixC COG0644
Dehydrogenase (flavoprotein) [Energy production and conversion];
318-346 7.12e-03

Dehydrogenase (flavoprotein) [Energy production and conversion];


Pssm-ID: 440409 [Multi-domain]  Cd Length: 281  Bit Score: 38.80  E-value: 7.12e-03
                         10        20
                 ....*....|....*....|....*....
gi 732683275 318 AGPAGLGCADILARAGVQVDVFDRHPEIG 346
Cdd:COG0644    1 AGPAGSAAARRLARAGLSVLLLEKGSFPG 29
Fer4_10 pfam13237
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ...
52-98 8.07e-03

4Fe-4S dicluster domain; This family includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. The structure of the domain is an alpha-antiparallel beta sandwich.


Pssm-ID: 404174 [Multi-domain]  Cd Length: 56  Bit Score: 34.92  E-value: 8.07e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 732683275   52 NPVACHHCNNapCVTACPVN-------ALTFQSDSVQLDEQKCIGCKRCAIACP 98
Cdd:pfam13237   5 DPDKCIGCGR--CTAACPAGltrvgaiVERLEGEAVRIGVWKCIGCGACVEACP 56
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
41-105 8.50e-03

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 39.02  E-value: 8.50e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 732683275  41 RIHVVGKgQAANPVACHHcnnaPCVTACPVN-----ALTF--QSDSVQLDEQKCIGCKRCAIACPFGVVEMV 105
Cdd:PRK13409   3 RIAVVDY-DRCQPKKCNY----ECIKYCPVVrtgeeTIEIdeDDGKPVISEELCIGCGICVKKCPFDAISIV 69
2-desacetyl-2-hydroxyethyl_bacteriochlorophyllide_ cd08255
2-desacetyl-2-hydroxyethyl bacteriochlorophyllide and other MDR family members; This subgroup ...
311-401 9.94e-03

2-desacetyl-2-hydroxyethyl bacteriochlorophyllide and other MDR family members; This subgroup of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family has members identified as 2-desacetyl-2-hydroxyethyl bacteriochlorophyllide A dehydrogenase and alcohol dehydrogenases. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability.


Pssm-ID: 176217 [Multi-domain]  Cd Length: 277  Bit Score: 38.41  E-value: 9.94e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683275 311 EKVAVIGAGPAGLGCADILARAG-VQVDVFDRHPEiggmltfgippfkldktvlsqRREIFTAMGIDFhlncEIGRDITF 389
Cdd:cd08255   99 ERVAVVGLGLVGLLAAQLAKAAGaREVVGVDPDAA---------------------RRELAEALGPAD----PVAADTAD 153
                         90
                 ....*....|..
gi 732683275 390 SDLTSEYDAVFI 401
Cdd:cd08255  154 EIGGRGADVVIE 165
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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