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Conserved domains on  [gi|489194187|ref|WP_003103513|]
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MULTISPECIES: NADPH-dependent 2,4-dienoyl-CoA reductase [Pseudomonas]

Protein Classification

NADPH-dependent 2,4-dienoyl-CoA reductase( domain architecture ID 11554248)

2,4-dienoyl-CoA reductase catalyzes the NADPH-dependent reduction of 2,4 dienoyl-CoA to 3-trans-enoyl-CoA

CATH:  3.20.20.70|3.50.50.60
EC:  1.3.1.34
Gene Ontology:  GO:0008670|GO:0051539|GO:0071949|GO:0046872|GO:0010181|GO:0033543

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DCR_FMN cd02930
2,4-dienoyl-CoA reductase (DCR) FMN-binding domain. DCR in E. coli is an iron-sulfur ...
 10-362 0e+00

2,4-dienoyl-CoA reductase (DCR) FMN-binding domain. DCR in E. coli is an iron-sulfur flavoenzyme which contains FMN, FAD, and a 4Fe-4S cluster. It is also a monomer, unlike that of its eukaryotic counterparts which form homotetramers and lack the flavin and iron-sulfur cofactors. Metabolism of unsaturated fatty acids requires auxiliary enzymes in addition to those used in b-oxidation. After a given number of cycles through the b-oxidation pathway, those unsaturated fatty acyl-CoAs with double bonds at even-numbered carbon positions contain 2-trans, 4-cis double bonds that can not be modified by enoyl-CoA hydratase. DCR utilizes NADPH to remove the C4-C5 double bond. DCR can catalyze the reduction of both natural fatty acids with cis double bonds, as well as substrates containing trans double bonds. The reaction is initiated by hybrid transfer from NADPH to FAD, which in turn transfers electrons, one at a time, to FMN via the 4Fe-4S cluster. The fully reduced FMN provides a hydrid ion to the C5 atom of substrate, and Tyr and His are proposed to form a catalytic dyad that protonates the C4 atom of the substrate and completes the reaction.


:

Pssm-ID: 239240 [Multi-domain]  Cd Length: 353  Bit Score: 671.69  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187  10 LLAPLDLGFTTLRNRTLMGSMHTGLEEKPQGFERMAAYFAERARGGVGLMVTGGIGPNEEGGVYSGAAKLSTPEEAEKHR 89
Cdd:cd02930    1 LLSPLDLGFTTLRNRVLMGSMHTGLEELDDGIDRLAAFYAERARGGVGLIVTGGFAPNEAGKLGPGGPVLNSPRQAAGHR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187  90 IVTQAVHEAGGKICMQILHAGRYAYSPKQVAPSAIQAPINPFKPKELDEEGIEKQIADFVNCASLAQVAGYDGVEIMGSE 169
Cdd:cd02930   81 LITDAVHAEGGKIALQILHAGRYAYHPLCVAPSAIRAPINPFTPRELSEEEIEQTIEDFARCAALAREAGYDGVEIMGSE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187 170 GYFINQFLVQHTNQRTDRWGGSYENRMRLPVEIVRRVREAVGPNFIIIYRLSMLDLVEGGSSWDEIVLLAKAVEKAGATL 249
Cdd:cd02930  161 GYLINQFLAPRTNKRTDEWGGSFENRMRFPVEIVRAVRAAVGEDFIIIYRLSMLDLVEGGSTWEEVVALAKALEAAGADI 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187 250 INTGIGWHEARIPTIATKVPRAAFTKVTAKLRGEVGIPLITTNRINTPEVAEKVLAEGDADMVSMARPFLADPDFVNKAA 329
Cdd:cd02930  241 LNTGIGWHEARVPTIATSVPRGAFAWATAKLKRAVDIPVIASNRINTPEVAERLLADGDADMVSMARPFLADPDFVAKAA 320

                        330       340       350
                 ....*....|....*....|....*....|...
gi 489194187 330 AGHAERINTCIGCNQACLDHTFGGKLTSCLVNP 362
Cdd:cd02930  321 AGRADEINTCIACNQACLDHIFTGQRASCLVNP 353
FadH2 super family cl43146
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ...
 403-636 1.00e-11

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


The actual alignment was detected with superfamily member COG0446:

Pssm-ID: 440215 [Multi-domain]  Cd Length: 322  Bit Score: 66.76  E-value: 1.00e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187 403 RVSLFDAAGEIGGQ-FNVAKRVPGKEEFHETLRYF-RNKLESTGVELHLNRRV-DVDD-----LVAGG----YDEIVLAT 470
Cdd:COG0446    7 EITVIEKGPHHSYQpCGLPYYVGGGIKDPEDLLVRtPESFERKGIDVRTGTEVtAIDPeaktvTLRDGetlsYDKLVLAT 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187 471 GIVPRTPAIPGIEHPKV-----ISYLDAILE--RKPVGGKVAVIGAGGIGFDVSEFithagpstslereafWKEWGIDTR 543
Cdd:COG0446   87 GARPRPPPIPGLDLPGVftlrtLDDADALREalKEFKGKRAVVIGGGPIGLELAEA---------------LRKRGLKVT 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187 544 LearggiagvkaeVHPAARqvfLLQRKKSKVGDGLGKttgWIHRAGLKNKQVQMVNAVEylgiDDAGLHIRVAEGEpqVL 623
Cdd:COG0446  152 L------------VERAPR---LLGVLDPEMAALLEE---ELREHGVELRLGETVVAID----GDDKVAVTLTDGE--EI 207

                        250
                 ....*....|...
gi 489194187 624 PVDTVIVCAGQDP 636
Cdd:COG0446  208 PADLVVVAPGVRP 220
GlxA super family cl34854
Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH ...
 609-668 9.30e-03

Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH domain [Transcription];


The actual alignment was detected with superfamily member COG4977:

Pssm-ID: 444002 [Multi-domain]  Cd Length: 318  Bit Score: 38.60  E-value: 9.30e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489194187 609 AGLHIRVAEGEPQVLPVDTVIVCAGQDPLRELQDGLL-----AAGQSVHLIG---GADVAAE---LDAKRA 668
Cdd:COG4977   51 SGLTVAPDHGLADLAAADTLIVPGGLDPAAAADPALLawlrrAAARGARLASictGAFLLAAaglLDGRRA 121
 
Name Accession Description Interval E-value
DCR_FMN cd02930
2,4-dienoyl-CoA reductase (DCR) FMN-binding domain. DCR in E. coli is an iron-sulfur ...
 10-362 0e+00

2,4-dienoyl-CoA reductase (DCR) FMN-binding domain. DCR in E. coli is an iron-sulfur flavoenzyme which contains FMN, FAD, and a 4Fe-4S cluster. It is also a monomer, unlike that of its eukaryotic counterparts which form homotetramers and lack the flavin and iron-sulfur cofactors. Metabolism of unsaturated fatty acids requires auxiliary enzymes in addition to those used in b-oxidation. After a given number of cycles through the b-oxidation pathway, those unsaturated fatty acyl-CoAs with double bonds at even-numbered carbon positions contain 2-trans, 4-cis double bonds that can not be modified by enoyl-CoA hydratase. DCR utilizes NADPH to remove the C4-C5 double bond. DCR can catalyze the reduction of both natural fatty acids with cis double bonds, as well as substrates containing trans double bonds. The reaction is initiated by hybrid transfer from NADPH to FAD, which in turn transfers electrons, one at a time, to FMN via the 4Fe-4S cluster. The fully reduced FMN provides a hydrid ion to the C5 atom of substrate, and Tyr and His are proposed to form a catalytic dyad that protonates the C4 atom of the substrate and completes the reaction.


Pssm-ID: 239240 [Multi-domain]  Cd Length: 353  Bit Score: 671.69  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187  10 LLAPLDLGFTTLRNRTLMGSMHTGLEEKPQGFERMAAYFAERARGGVGLMVTGGIGPNEEGGVYSGAAKLSTPEEAEKHR 89
Cdd:cd02930    1 LLSPLDLGFTTLRNRVLMGSMHTGLEELDDGIDRLAAFYAERARGGVGLIVTGGFAPNEAGKLGPGGPVLNSPRQAAGHR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187  90 IVTQAVHEAGGKICMQILHAGRYAYSPKQVAPSAIQAPINPFKPKELDEEGIEKQIADFVNCASLAQVAGYDGVEIMGSE 169
Cdd:cd02930   81 LITDAVHAEGGKIALQILHAGRYAYHPLCVAPSAIRAPINPFTPRELSEEEIEQTIEDFARCAALAREAGYDGVEIMGSE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187 170 GYFINQFLVQHTNQRTDRWGGSYENRMRLPVEIVRRVREAVGPNFIIIYRLSMLDLVEGGSSWDEIVLLAKAVEKAGATL 249
Cdd:cd02930  161 GYLINQFLAPRTNKRTDEWGGSFENRMRFPVEIVRAVRAAVGEDFIIIYRLSMLDLVEGGSTWEEVVALAKALEAAGADI 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187 250 INTGIGWHEARIPTIATKVPRAAFTKVTAKLRGEVGIPLITTNRINTPEVAEKVLAEGDADMVSMARPFLADPDFVNKAA 329
Cdd:cd02930  241 LNTGIGWHEARVPTIATSVPRGAFAWATAKLKRAVDIPVIASNRINTPEVAERLLADGDADMVSMARPFLADPDFVAKAA 320

                        330       340       350
                 ....*....|....*....|....*....|...
gi 489194187 330 AGHAERINTCIGCNQACLDHTFGGKLTSCLVNP 362
Cdd:cd02930  321 AGRADEINTCIACNQACLDHIFTGQRASCLVNP 353
FadH COG1902
2,4-dienoyl-CoA reductase or related NADH-dependent reductase, Old Yellow Enzyme (OYE) family ...
 6-366 1.60e-170

2,4-dienoyl-CoA reductase or related NADH-dependent reductase, Old Yellow Enzyme (OYE) family [Energy production and conversion];


Pssm-ID: 441506 [Multi-domain]  Cd Length: 365  Bit Score: 491.61  E-value: 1.60e-170
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187   6 PYPHLLAPLDLGFTTLRNRTLMGSMHTGLEEkPQGF--ERMAAYFAERARGGVGLMVTGGIGPNEEGGVYSGAAKLSTPE 83
Cdd:COG1902    3 KMPKLFSPLTLGGLTLKNRIVMAPMTRGRAD-EDGVptDLHAAYYAQRARGGAGLIITEATAVSPEGRGYPGQPGIWDDE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187  84 EAEKHRIVTQAVHEAGGKICMQILHAGRYAYSPKQ-----VAPSAIQAPINPFKPKELDEEGIEKQIADFVNCASLAQVA 158
Cdd:COG1902   82 QIAGLRRVTDAVHAAGGKIFIQLWHAGRKAHPDLPggwppVAPSAIPAPGGPPTPRALTTEEIERIIEDFAAAARRAKEA 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187 159 GYDGVEIMGSEGYFINQFLVQHTNQRTDRWGGSYENRMRLPVEIVRRVREAVGPNFIIIYRLSMLDLVEGGSSWDEIVLL 238
Cdd:COG1902  162 GFDGVEIHGAHGYLLDQFLSPLTNQRTDEYGGSLENRARFLLEVVEAVRAAVGPDFPVGVRLSPTDFVEGGLTLEESVEL 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187 239 AKAVEKAGATLINTGIGWHEARiPTIATKVPRAAFTKVTAKLRGEVGIPLITTNRINTPEVAEKVLAEGDADMVSMARPF 318
Cdd:COG1902  242 AKALEEAGVDYLHVSSGGYEPD-AMIPTIVPEGYQLPFAARIRKAVGIPVIAVGGITTPEQAEAALASGDADLVALGRPL 320

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 489194187 319 LADPDFVNKAAAGHAERINTCIGCNQaCLDHTFGGklTSCLVNPRACH 366
Cdd:COG1902  321 LADPDLPNKAAAGRGDEIRPCIGCNQ-CLPTFYGG--ASCYVDPRLGR 365
Oxidored_FMN pfam00724
NADH:flavin oxidoreductase / NADH oxidase family;
10-331 1.17e-97

NADH:flavin oxidoreductase / NADH oxidase family;


Pssm-ID: 395587 [Multi-domain]  Cd Length: 341  Bit Score: 303.99  E-value: 1.17e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187   10 LLAPLDLGFTTLRNRTLMGSMhTGLEEKPQGF---ERMAAYFAERARGGVGLMVTGGIGPNEEGGVYSGAAKLSTPEEAE 86
Cdd:pfam00724   2 LFEPIKIGNTTLKNRIVMAPM-TRLRSLDDGTkatGLLAEYYSQRSRGPGTLIITEGAFVNPQSGGFDNGPRIWDDEQIE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187   87 KHRIVTQAVHEAGGKICMQILHAGRYA---YSPKQVAPSAIQAPINPFKP-------KELDEEGIEKQIADFVNCASLAQ 156
Cdd:pfam00724  81 GWRKLTEAVHKNGSKAGVQLWHLGREApmeYRPDLEVDGPSDPFALGAQEfeiasprYEMSKEEIKQHIQDFVDAAKRAR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187  157 VAGYDGVEIMGSEGYFINQFLVQHTNQRTDRWGGSYENRMRLPVEIVRRVREAVGPNFIIIYRLSMLDLVEGGSSWDEIv 236
Cdd:pfam00724 161 EAGFDGVEIHGANGYLINQFLSPGTNQRTDEYGGSLENRARFPLEVVDAVKEAVGQERIVGYRLSPFDVVGPGLDFAET- 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187  237 llAKAVEKAGATLINTGIGWHEARIpTIATKVPRAAFTKVT------AKLRGEVGIPLITTNRINTPEVAEKVLAEGDAD 310
Cdd:pfam00724 240 --AQFIYLLAELGVRLPDGWHLAYI-HAIEPRPRGAGPVRTrqqhntLFVKGVWKGPLITVGRIDDPSVAAEIVSKGRAD 316

                         330       340
                  ....*....|....*....|.
gi 489194187  311 MVSMARPFLADPDFVNKAAAG 331
Cdd:pfam00724 317 LVAMGRPFLADPDLPFKAKKG 337
PRK08255 PRK08255
bifunctional salicylyl-CoA 5-hydroxylase/oxidoreductase;
2-330 8.27e-45

bifunctional salicylyl-CoA 5-hydroxylase/oxidoreductase;


Pssm-ID: 236203 [Multi-domain]  Cd Length: 765  Bit Score: 171.28  E-value: 8.27e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187   2 TAAVPYPHLLAPLDLGFTTLRNRTLMGSM-----HTGLeekPQGFERMaaYFAERARGGVGLMVTGGIGPNEEGGVYSGA 76
Cdd:PRK08255 391 PVARPPPPMFTPFRLRGLTLKNRVVVSPMamysaVDGV---PGDFHLV--HLGARALGGAGLVMTEMTCVSPEGRITPGC 465

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187  77 AKLSTPEEAEKHRIVTQAVH-EAGGKICMQILHAGRYAySPKQ----------------VAPSAIQAPINPFKPKELDEE 139
Cdd:PRK08255 466 PGLYNDEQEAAWKRIVDFVHaNSDAKIGIQLGHSGRKG-STRLgwegidepleegnwplISASPLPYLPGSQVPREMTRA 544

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187 140 GIEKQIADFVNCASLAQVAGYDGVEIMGSEGYFINQFLVQHTNQRTDRWGGSYENRMRLPVEIVRRVREAVGPNFIIIYR 219
Cdd:PRK08255 545 DMDRVRDDFVAAARRAAEAGFDWLELHCAHGYLLSSFISPLTNQRTDEYGGSLENRLRYPLEVFRAVRAVWPAEKPMSVR 624

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187 220 LSMLDLVEGGSSWDEIVLLAKAVEKAGATLIN--TGIGWHEARiPTIAtkvpRAAFTKVTAKLRGEVGIPLITTNRINTP 297
Cdd:PRK08255 625 ISAHDWVEGGNTPDDAVEIARAFKAAGADLIDvsSGQVSKDEK-PVYG----RMYQTPFADRIRNEAGIATIAVGAISEA 699

                        330       340       350
                 ....*....|....*....|....*....|...
gi 489194187 298 EVAEKVLAEGDADMVSMARPFLADPDFVNKAAA 330
Cdd:PRK08255 700 DHVNSIIAAGRADLCALARPHLADPAWTLHEAA 732
FadH2 COG0446
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ...
 403-636 1.00e-11

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: 66.76  E-value: 1.00e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187 403 RVSLFDAAGEIGGQ-FNVAKRVPGKEEFHETLRYF-RNKLESTGVELHLNRRV-DVDD-----LVAGG----YDEIVLAT 470
Cdd:COG0446    7 EITVIEKGPHHSYQpCGLPYYVGGGIKDPEDLLVRtPESFERKGIDVRTGTEVtAIDPeaktvTLRDGetlsYDKLVLAT 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187 471 GIVPRTPAIPGIEHPKV-----ISYLDAILE--RKPVGGKVAVIGAGGIGFDVSEFithagpstslereafWKEWGIDTR 543
Cdd:COG0446   87 GARPRPPPIPGLDLPGVftlrtLDDADALREalKEFKGKRAVVIGGGPIGLELAEA---------------LRKRGLKVT 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187 544 LearggiagvkaeVHPAARqvfLLQRKKSKVGDGLGKttgWIHRAGLKNKQVQMVNAVEylgiDDAGLHIRVAEGEpqVL 623
Cdd:COG0446  152 L------------VERAPR---LLGVLDPEMAALLEE---ELREHGVELRLGETVVAID----GDDKVAVTLTDGE--EI 207

                        250
                 ....*....|...
gi 489194187 624 PVDTVIVCAGQDP 636
Cdd:COG0446  208 PADLVVVAPGVRP 220
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 399-644 1.21e-11

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: 66.19  E-value: 1.21e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187  399 ERGHRVSLFDAAGEI-GGQFNVAKRVPGKEEFHETLRYFRN---------KLESTGVELHLN----------RRVDVDDL 458
Cdd:pfam07992  21 QLGGKVTLIEDEGTCpYGGCVLSKALLGAAEAPEIASLWADlykrkeevvKKLNNGIEVLLGtevvsidpgaKKVVLEEL 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187  459 VAGG-----YDEIVLATGIVPRTPAIPGIEHP--KVISYLDA--ILERKPVGGKVAVIGAGGIGFDVSEFITHAGpstsl 529
Cdd:pfam07992 101 VDGDgetitYDRLVIATGARPRLPPIPGVELNvgFLVRTLDSaeALRLKLLPKRVVVVGGGYIGVELAAALAKLG----- 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187  530 ereafwkewgidtrlearggiagvkAEVHPAARQVFLLQRKKSKVGDglgkttgWIHRAgLKNKQVQMVNAVEYLGIDDA 609
Cdd:pfam07992 176 -------------------------KEVTLIEALDRLLRAFDEEISA-------ALEKA-LEKNGVEVRLGTSVKEIIGD 222

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 489194187  610 GLHIRVAEGEPQVLPVDTVIVCAGQDPLREL--QDGL 644
Cdd:pfam07992 223 GDGVEVILKDGTEIDADLVVVAIGRRPNTELleAAGL 259
PRK12771 PRK12771
putative glutamate synthase (NADPH) small subunit; Provisional
 379-516 1.55e-08

putative glutamate synthase (NADPH) small subunit; Provisional


Pssm-ID: 237198 [Multi-domain]  Cd Length: 564  Bit Score: 57.58  E-value: 1.55e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187 379 KKIAVVGAGPAGLAAATVAAERGHRVSLFDAAGEIGG--QFNV-AKRVPgkeefHETLRYFRNKLESTGVELHLNRRVDV 455
Cdd:PRK12771 138 KRVAVIGGGPAGLSAAYHLRRMGHAVTIFEAGPKLGGmmRYGIpAYRLP-----REVLDAEIQRILDLGVEVRLGVRVGE 212

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187 456 D---DLVAGGYDEIVLATGI-VPRTPAIPGIEHPKV---ISYLDAI--LERKPVGGKVAVIGAGGIGFDV 516
Cdd:PRK12771 213 DitlEQLEGEFDAVFVAIGAqLGKRLPIPGEDAAGVldaVDFLRAVgeGEPPFLGKRVVVIGGGNTAMDA 282
nitri_red_nirB TIGR02374
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ...
 441-648 3.70e-05

nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen metabolism]


Pssm-ID: 162827 [Multi-domain]  Cd Length: 785  Bit Score: 47.13  E-value: 3.70e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187  441 ESTGVELHLNRRV---DVDDLV----AG---GYDEIVLATGIVPRTPAIPGIEHPKVISY-----LDAILERKPVGGKVA 505
Cdd:TIGR02374  65 EKHGITLYTGETViqiDTDQKQvitdAGrtlSYDKLILATGSYPFILPIPGADKKGVYVFrtiedLDAIMAMAQRFKKAA 144

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187  506 VIGAGGIGfdvsefithagpstslereafwkewgidtrLEARGGIAGVKAEVHPAARQVFLLQRKkskvgdgLGKTTGWI 585
Cdd:TIGR02374 145 VIGGGLLG------------------------------LEAAVGLQNLGMDVSVIHHAPGLMAKQ-------LDQTAGRL 187

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489194187  586 HRAGLKNKQVQMV---NAVEYLGiDDAGLHIRVAEGEpqVLPVDTVIVCAGQDPLREL--QDGLLAAG 648
Cdd:TIGR02374 188 LQRELEQKGLTFLlekDTVEIVG-ATKADRIRFKDGS--SLEADLIVMAAGIRPNDELavSAGIKVNR 252
GlxA COG4977
Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH ...
 609-668 9.30e-03

Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH domain [Transcription];


Pssm-ID: 444002 [Multi-domain]  Cd Length: 318  Bit Score: 38.60  E-value: 9.30e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489194187 609 AGLHIRVAEGEPQVLPVDTVIVCAGQDPLRELQDGLL-----AAGQSVHLIG---GADVAAE---LDAKRA 668
Cdd:COG4977   51 SGLTVAPDHGLADLAAADTLIVPGGLDPAAAADPALLawlrrAAARGARLASictGAFLLAAaglLDGRRA 121
 
Name Accession Description Interval E-value
DCR_FMN cd02930
2,4-dienoyl-CoA reductase (DCR) FMN-binding domain. DCR in E. coli is an iron-sulfur ...
 10-362 0e+00

2,4-dienoyl-CoA reductase (DCR) FMN-binding domain. DCR in E. coli is an iron-sulfur flavoenzyme which contains FMN, FAD, and a 4Fe-4S cluster. It is also a monomer, unlike that of its eukaryotic counterparts which form homotetramers and lack the flavin and iron-sulfur cofactors. Metabolism of unsaturated fatty acids requires auxiliary enzymes in addition to those used in b-oxidation. After a given number of cycles through the b-oxidation pathway, those unsaturated fatty acyl-CoAs with double bonds at even-numbered carbon positions contain 2-trans, 4-cis double bonds that can not be modified by enoyl-CoA hydratase. DCR utilizes NADPH to remove the C4-C5 double bond. DCR can catalyze the reduction of both natural fatty acids with cis double bonds, as well as substrates containing trans double bonds. The reaction is initiated by hybrid transfer from NADPH to FAD, which in turn transfers electrons, one at a time, to FMN via the 4Fe-4S cluster. The fully reduced FMN provides a hydrid ion to the C5 atom of substrate, and Tyr and His are proposed to form a catalytic dyad that protonates the C4 atom of the substrate and completes the reaction.


Pssm-ID: 239240 [Multi-domain]  Cd Length: 353  Bit Score: 671.69  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187  10 LLAPLDLGFTTLRNRTLMGSMHTGLEEKPQGFERMAAYFAERARGGVGLMVTGGIGPNEEGGVYSGAAKLSTPEEAEKHR 89
Cdd:cd02930    1 LLSPLDLGFTTLRNRVLMGSMHTGLEELDDGIDRLAAFYAERARGGVGLIVTGGFAPNEAGKLGPGGPVLNSPRQAAGHR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187  90 IVTQAVHEAGGKICMQILHAGRYAYSPKQVAPSAIQAPINPFKPKELDEEGIEKQIADFVNCASLAQVAGYDGVEIMGSE 169
Cdd:cd02930   81 LITDAVHAEGGKIALQILHAGRYAYHPLCVAPSAIRAPINPFTPRELSEEEIEQTIEDFARCAALAREAGYDGVEIMGSE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187 170 GYFINQFLVQHTNQRTDRWGGSYENRMRLPVEIVRRVREAVGPNFIIIYRLSMLDLVEGGSSWDEIVLLAKAVEKAGATL 249
Cdd:cd02930  161 GYLINQFLAPRTNKRTDEWGGSFENRMRFPVEIVRAVRAAVGEDFIIIYRLSMLDLVEGGSTWEEVVALAKALEAAGADI 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187 250 INTGIGWHEARIPTIATKVPRAAFTKVTAKLRGEVGIPLITTNRINTPEVAEKVLAEGDADMVSMARPFLADPDFVNKAA 329
Cdd:cd02930  241 LNTGIGWHEARVPTIATSVPRGAFAWATAKLKRAVDIPVIASNRINTPEVAERLLADGDADMVSMARPFLADPDFVAKAA 320

                        330       340       350
                 ....*....|....*....|....*....|...
gi 489194187 330 AGHAERINTCIGCNQACLDHTFGGKLTSCLVNP 362
Cdd:cd02930  321 AGRADEINTCIACNQACLDHIFTGQRASCLVNP 353
FadH COG1902
2,4-dienoyl-CoA reductase or related NADH-dependent reductase, Old Yellow Enzyme (OYE) family ...
 6-366 1.60e-170

2,4-dienoyl-CoA reductase or related NADH-dependent reductase, Old Yellow Enzyme (OYE) family [Energy production and conversion];


Pssm-ID: 441506 [Multi-domain]  Cd Length: 365  Bit Score: 491.61  E-value: 1.60e-170
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187   6 PYPHLLAPLDLGFTTLRNRTLMGSMHTGLEEkPQGF--ERMAAYFAERARGGVGLMVTGGIGPNEEGGVYSGAAKLSTPE 83
Cdd:COG1902    3 KMPKLFSPLTLGGLTLKNRIVMAPMTRGRAD-EDGVptDLHAAYYAQRARGGAGLIITEATAVSPEGRGYPGQPGIWDDE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187  84 EAEKHRIVTQAVHEAGGKICMQILHAGRYAYSPKQ-----VAPSAIQAPINPFKPKELDEEGIEKQIADFVNCASLAQVA 158
Cdd:COG1902   82 QIAGLRRVTDAVHAAGGKIFIQLWHAGRKAHPDLPggwppVAPSAIPAPGGPPTPRALTTEEIERIIEDFAAAARRAKEA 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187 159 GYDGVEIMGSEGYFINQFLVQHTNQRTDRWGGSYENRMRLPVEIVRRVREAVGPNFIIIYRLSMLDLVEGGSSWDEIVLL 238
Cdd:COG1902  162 GFDGVEIHGAHGYLLDQFLSPLTNQRTDEYGGSLENRARFLLEVVEAVRAAVGPDFPVGVRLSPTDFVEGGLTLEESVEL 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187 239 AKAVEKAGATLINTGIGWHEARiPTIATKVPRAAFTKVTAKLRGEVGIPLITTNRINTPEVAEKVLAEGDADMVSMARPF 318
Cdd:COG1902  242 AKALEEAGVDYLHVSSGGYEPD-AMIPTIVPEGYQLPFAARIRKAVGIPVIAVGGITTPEQAEAALASGDADLVALGRPL 320

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 489194187 319 LADPDFVNKAAAGHAERINTCIGCNQaCLDHTFGGklTSCLVNPRACH 366
Cdd:COG1902  321 LADPDLPNKAAAGRGDEIRPCIGCNQ-CLPTFYGG--ASCYVDPRLGR 365
OYE_like_FMN_family cd02803
Old yellow enzyme (OYE)-like FMN binding domain. OYE was the first flavin-dependent enzyme ...
 11-331 8.50e-120

Old yellow enzyme (OYE)-like FMN binding domain. OYE was the first flavin-dependent enzyme identified, however its true physiological role remains elusive to this day. Each monomer of OYE contains FMN as a non-covalently bound cofactor, uses NADPH as a reducing agent with oxygens, quinones, and alpha,beta-unsaturated aldehydes and ketones, and can act as electron acceptors in the catalytic reaction. Members of OYE family include trimethylamine dehydrogenase, 2,4-dienoyl-CoA reductase, enoate reductase, pentaerythriol tetranitrate reductase, xenobiotic reductase, and morphinone reductase.


Pssm-ID: 239201 [Multi-domain]  Cd Length: 327  Bit Score: 360.35  E-value: 8.50e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187  11 LAPLDLGFTTLRNRTLMGSMHTGLEEkPQGF--ERMAAYFAERARGGVGLMVTGGIGPNEEGGVYSGAAKLSTPEEAEKH 88
Cdd:cd02803    1 FSPIKIGGLTLKNRIVMAPMTENMAT-EDGTptDELIEYYEERAKGGVGLIITEAAYVDPEGKGYPGQLGIYDDEQIPGL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187  89 RIVTQAVHEAGGKICMQILHAGRYAYSP----KQVAPSAIQAPINPFKPKELDEEGIEKQIADFVNCASLAQVAGYDGVE 164
Cdd:cd02803   80 RKLTEAVHAHGAKIFAQLAHAGRQAQPNltggPPPAPSAIPSPGGGEPPREMTKEEIEQIIEDFAAAARRAKEAGFDGVE 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187 165 IMGSEGYFINQFLVQHTNQRTDRWGGSYENRMRLPVEIVRRVREAVGPNFIIIYRLSMLDLVEGGSSWDEIVLLAKAVEK 244
Cdd:cd02803  160 IHGAHGYLLSQFLSPYTNKRTDEYGGSLENRARFLLEIVAAVREAVGPDFPVGVRLSADDFVPGGLTLEEAIEIAKALEE 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187 245 AGATLINTGIGWHEARIPTIA-TKVPRAAFTKVTAKLRGEVGIPLITTNRINTPEVAEKVLAEGDADMVSMARPFLADPD 323
Cdd:cd02803  240 AGVDALHVSGGSYESPPPIIPpPYVPEGYFLELAEKIKKAVKIPVIAVGGIRDPEVAEEILAEGKADLVALGRALLADPD 319


                 ....*...
gi 489194187 324 FVNKAAAG 331
Cdd:cd02803  320 LPNKAREG 327
Oxidored_FMN pfam00724
NADH:flavin oxidoreductase / NADH oxidase family;
10-331 1.17e-97

NADH:flavin oxidoreductase / NADH oxidase family;


Pssm-ID: 395587 [Multi-domain]  Cd Length: 341  Bit Score: 303.99  E-value: 1.17e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187   10 LLAPLDLGFTTLRNRTLMGSMhTGLEEKPQGF---ERMAAYFAERARGGVGLMVTGGIGPNEEGGVYSGAAKLSTPEEAE 86
Cdd:pfam00724   2 LFEPIKIGNTTLKNRIVMAPM-TRLRSLDDGTkatGLLAEYYSQRSRGPGTLIITEGAFVNPQSGGFDNGPRIWDDEQIE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187   87 KHRIVTQAVHEAGGKICMQILHAGRYA---YSPKQVAPSAIQAPINPFKP-------KELDEEGIEKQIADFVNCASLAQ 156
Cdd:pfam00724  81 GWRKLTEAVHKNGSKAGVQLWHLGREApmeYRPDLEVDGPSDPFALGAQEfeiasprYEMSKEEIKQHIQDFVDAAKRAR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187  157 VAGYDGVEIMGSEGYFINQFLVQHTNQRTDRWGGSYENRMRLPVEIVRRVREAVGPNFIIIYRLSMLDLVEGGSSWDEIv 236
Cdd:pfam00724 161 EAGFDGVEIHGANGYLINQFLSPGTNQRTDEYGGSLENRARFPLEVVDAVKEAVGQERIVGYRLSPFDVVGPGLDFAET- 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187  237 llAKAVEKAGATLINTGIGWHEARIpTIATKVPRAAFTKVT------AKLRGEVGIPLITTNRINTPEVAEKVLAEGDAD 310
Cdd:pfam00724 240 --AQFIYLLAELGVRLPDGWHLAYI-HAIEPRPRGAGPVRTrqqhntLFVKGVWKGPLITVGRIDDPSVAAEIVSKGRAD 316

                         330       340
                  ....*....|....*....|.
gi 489194187  311 MVSMARPFLADPDFVNKAAAG 331
Cdd:pfam00724 317 LVAMGRPFLADPDLPFKAKKG 337
OYE_like_3_FMN cd04734
Old yellow enzyme (OYE)-related FMN binding domain, group 3. Each monomer of OYE contains FMN ...
 10-343 4.56e-85

Old yellow enzyme (OYE)-related FMN binding domain, group 3. Each monomer of OYE contains FMN as a non-covalently bound cofactor, uses NADPH as a reducing agent with oxygens, quinones, and alpha,beta-unsaturated aldehydes and ketones, and can act as electron acceptors in the catalytic reaction. Other members of OYE family include trimethylamine dehydrogenase, 2,4-dienoyl-CoA reductase, enoate reductase, pentaerythriol tetranitrate reductase, xenobiotic reductase, and morphinone reductase. One member of this subgroup, the Sinorhizobium meliloti stachydrine utilization protein stcD, has been idenified as a putative N-methylproline demethylase.


Pssm-ID: 240085 [Multi-domain]  Cd Length: 343  Bit Score: 271.02  E-value: 4.56e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187  10 LLAPLDLGFTTLRNRTLMGSMHTGLEEKPQGFERMAAYFAERARGGVGLMVTGGIGPNEEGGVYSGAAKLSTPEEAEKHR 89
Cdd:cd04734    1 LLSPLQLGHLTLRNRIVSTAHATNYAEDGLPSERYIAYHEERARGGAGLIITEGSSVHPSDSPAFGNLNASDDEIIPGFR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187  90 IVTQAVHEAGGKICMQILHAGR---YAYS-PKQVAPSAIQAPINPFKPKELDEEGIEKQIADFVNCASLAQVAGYDGVEI 165
Cdd:cd04734   81 RLAEAVHAHGAVIMIQLTHLGRrgdGDGSwLPPLAPSAVPEPRHRAVPKAMEEEDIEEIIAAFADAARRCQAGGLDGVEL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187 166 MGSEGYFINQFLVQHTNQRTDRWGGSYENRMRLPVEIVRRVREAVGPNFIIIYRLSMLDLVEGGSSWDEIVLLAKAVEKA 245
Cdd:cd04734  161 QAAHGHLIDQFLSPLTNRRTDEYGGSLENRMRFLLEVLAAVRAAVGPDFIVGIRISGDEDTEGGLSPDEALEIAARLAAE 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187 246 GAT-LINTGIG------WHEARIPTIAtkVPRAAFTKVTAKLRGEVGIPLITTNRINTPEVAEKVLAEGDADMVSMARPF 318
Cdd:cd04734  241 GLIdYVNVSAGsyytllGLAHVVPSMG--MPPGPFLPLAARIKQAVDLPVFHAGRIRDPAEAEQALAAGHADMVGMTRAH 318

                        330       340
                 ....*....|....*....|....*
gi 489194187 319 LADPDFVNKAAAGHAERINTCIGCN 343
Cdd:cd04734  319 IADPHLVAKAREGREDDIRPCIGCN 343
OYE_YqiM_FMN cd02932
Old yellow enzyme (OYE) YqjM-like FMN binding domain. YqjM is involved in the oxidative stress ...
 10-330 1.97e-74

Old yellow enzyme (OYE) YqjM-like FMN binding domain. YqjM is involved in the oxidative stress response of Bacillus subtilis. Like the other OYE members, each monomer of YqjM contains FMN as a non-covalently bound cofactor and uses NADPH as a reducing agent. The YqjM enzyme exists as a homotetramer that is assembled as a dimer of catalytically dependent dimers, while other OYE members exist only as monomers or dimers. Moreover, the protein displays a shared active site architecture where an arginine finger at the COOH terminus of one monomer extends into the active site of the adjacent monomer and is directly involved in substrate recognition. Another remarkable difference in the binding of the ligand in YqjM is represented by the contribution of the NH2-terminal tyrosine instead of a COOH-terminal tyrosine in OYE and its homologs.


Pssm-ID: 239242 [Multi-domain]  Cd Length: 336  Bit Score: 242.78  E-value: 1.97e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187  10 LLAPLDLGFTTLRNRTLMGSM-----HTGLeekPQGFERMaaYFAERARGGVGLMVTGGIGPNEEGGVYSGAAKLSTPEE 84
Cdd:cd02932    1 LFTPLTLRGVTLKNRIVVSPMcqysaEDGV---ATDWHLV--HYGSRALGGAGLVIVEATAVSPEGRITPGDLGLWNDEQ 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187  85 AEKHRIVTQAVHEAGGKICMQILHAGRYA--YSPKQ---------------VAPSAIQAPINPFKPKELDEEGIEKQIAD 147
Cdd:cd02932   76 IEALKRIVDFIHSQGAKIGIQLAHAGRKAstAPPWEgggpllppggggwqvVAPSAIPFDEGWPTPRELTREEIAEVVDA 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187 148 FVNCASLAQVAGYDGVEIMGSEGYFINQFLVQHTNQRTDRWGGSYENRMRLPVEIVRRVREAVGPNFIIIYRLSMLDLVE 227
Cdd:cd02932  156 FVAAARRAVEAGFDVIEIHAAHGYLLHQFLSPLSNKRTDEYGGSLENRMRFLLEVVDAVRAVWPEDKPLFVRISATDWVE 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187 228 GGSSWDEIVLLAKAVEKAGATLINTGIG--WHEARIPT-IATKVPRAaftkvtAKLRGEVGIPLITTNRINTPEVAEKVL 304
Cdd:cd02932  236 GGWDLEDSVELAKALKELGVDLIDVSSGgnSPAQKIPVgPGYQVPFA------ERIRQEAGIPVIAVGLITDPEQAEAIL 309

                        330       340
                 ....*....|....*....|....*.
gi 489194187 305 AEGDADMVSMARPFLADPDFVNKAAA 330
Cdd:cd02932  310 ESGRADLVALGRELLRNPYWPLHAAA 335
OYE_like_FMN cd02933
Old yellow enzyme (OYE)-like FMN binding domain. OYE was the first flavin-dependent enzyme ...
 9-331 6.96e-66

Old yellow enzyme (OYE)-like FMN binding domain. OYE was the first flavin-dependent enzyme identified, however its true physiological role remains elusive to this day. Each monomer of OYE contains FMN as a non-covalently bound cofactor, uses NADPH as a reducing agent with oxygens, quinones, and alpha,beta-unsaturated aldehydes and ketones, and can act as electron acceptors in the catalytic reaction. Members of OYE family include 12-oxophytodienoate reductase, pentaerythritol tetranitrate reductase, morphinone reductase, and related enzymes.


Pssm-ID: 239243 [Multi-domain]  Cd Length: 338  Bit Score: 220.42  E-value: 6.96e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187   9 HLLAPLDLGFTTLRNRTLMGSM---HTGLEEKPQgfERMAAYFAERArgGVGLMVTGGIGPNEEGGVYSGAAKLSTPEEA 85
Cdd:cd02933    1 KLFSPLKLGNLTLKNRIVMAPLtrsRADPDGVPT--DLMAEYYAQRA--SAGLIITEATQISPQGQGYPNTPGIYTDEQV 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187  86 EKHRIVTQAVHEAGGKICMQILHAGRYAYSPKQ------VAPSAIQAPINPFK---------PKELDEEGIEKQIADFVN 150
Cdd:cd02933   77 EGWKKVTDAVHAKGGKIFLQLWHVGRVSHPSLLpggappVAPSAIAAEGKVFTpagkvpyptPRALTTEEIPGIVADFRQ 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187 151 CASLAQVAGYDGVEIMGSEGYFINQFLVQHTNQRTDRWGGSYENRMRLPVEIVRRVREAVGPNFIIIyRLSMLDLVEGGS 230
Cdd:cd02933  157 AARNAIEAGFDGVEIHGANGYLIDQFLRDGSNKRTDEYGGSIENRARFLLEVVDAVAEAIGADRVGI-RLSPFGTFNDMG 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187 231 SWDEIVL---LAKAVEKAG-ATLintgigwH--EARIPTIATKVPRAAFTKVTAKLRGevgiPLITTNRInTPEVAEKVL 304
Cdd:cd02933  236 DSDPEATfsyLAKELNKRGlAYL-------HlvEPRVAGNPEDQPPDFLDFLRKAFKG----PLIAAGGY-DAESAEAAL 303

                        330       340
                 ....*....|....*....|....*..
gi 489194187 305 AEGDADMVSMARPFLADPDFVNKAAAG 331
Cdd:cd02933  304 ADGKADLVAFGRPFIANPDLVERLKNG 330
ER_like_FMN cd02931
Enoate reductase (ER)-like FMN-binding domain. Enoate reductase catalyzes the NADH-dependent ...
 10-362 5.99e-62

Enoate reductase (ER)-like FMN-binding domain. Enoate reductase catalyzes the NADH-dependent reduction of carbon-carbon double bonds of several molecules, including nonactivated 2-enoates, alpha,beta-unsaturated aldehydes, cyclic ketones, and methylketones. ERs are similar to 2,4-dienoyl-CoA reductase from E. coli and to the old yellow enzyme from Saccharomyces cerevisiae.


Pssm-ID: 239241 [Multi-domain]  Cd Length: 382  Bit Score: 211.21  E-value: 5.99e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187  10 LLAPLDLGFTTLRNRTLMGSMHT-GLEEKPQGF-ERMAAYFAERARGGVGLMVTGGIGPNEEGGVYsGAAKLSTPEEAEK 87
Cdd:cd02931    1 LFEPIKIGKVEIKNRFAMAPMGPlGLADNDGAFnQRGIDYYVERAKGGTGLIITGVTMVDNEIEQF-PMPSLPCPTYNPT 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187  88 H-----RIVTQAVHEAGGKICMQILHA-GRYA---YSP--KQVAPSAIQAPINPFKP-KELDEEGIEKQIADFVNCASLA 155
Cdd:cd02931   80 AfirtaKEMTERVHAYGTKIFLQLTAGfGRVCipgFLGedKPVAPSPIPNRWLPEITcRELTTEEVETFVGKFGESAVIA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187 156 QVAGYDGVEIMG-SEGYFINQFLVQHTNQRTDRWGGSYENRMRLPVEIVRRVREAVGPNFIIIYRLS----MLDL----- 225
Cdd:cd02931  160 KEAGFDGVEIHAvHEGYLLDQFTISLFNKRTDKYGGSLENRLRFAIEIVEEIKARCGEDFPVSLRYSvksyIKDLrqgal 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187 226 -----VEGGSSWDEIVLLAKAVEKAGATLINTGIG----WHEARIPTIATKvprAAFTKVTAKLRGEVGIPLITTNRINT 296
Cdd:cd02931  240 pgeefQEKGRDLEEGLKAAKILEEAGYDALDVDAGsydaWYWNHPPMYQKK---GMYLPYCKALKEVVDVPVIMAGRMED 316

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489194187 297 PEVAEKVLAEGDADMVSMARPFLADPDFVNKAAAGHAERINTCIGCNQACLDHTFGGKLTSCLVNP 362
Cdd:cd02931  317 PELASEAINEGIADMISLGRPLLADPDVVNKIRRGRFKNIRPCISCHDGCLGRMALGGNLSCAVNP 382
OYE_like_2_FMN cd04733
Old yellow enzyme (OYE)-related FMN binding domain, group 2. Each monomer of OYE contains FMN ...
 10-331 5.87e-60

Old yellow enzyme (OYE)-related FMN binding domain, group 2. Each monomer of OYE contains FMN as a non-covalently bound cofactor, uses NADPH as a reducing agent with oxygens, quinones, and alpha,beta-unsaturated aldehydes and ketones, and can act as electron acceptors in the catalytic reaction. Other members of OYE family include trimethylamine dehydrogenase, 2,4-dienoyl-CoA reductase, enoate reductase, pentaerythriol tetranitrate reductase, xenobiotic reductase, and morphinone reductase.


Pssm-ID: 240084 [Multi-domain]  Cd Length: 338  Bit Score: 204.74  E-value: 5.87e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187  10 LLAPLDLGF-TTLRNRTLMGSMHTGLEEKPQ--GFERMAAYfaER-ARGGVGLMVTGGI-----GPNEEGGVYSGAakLS 80
Cdd:cd04733    1 LGQPLTLPNgATLPNRLAKAAMSERLADGRGlpTPELIRLY--RRwAEGGIGLIITGNVmvdprHLEEPGIIGNVV--LE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187  81 TPEEAEKHRIVTQAVHEAGGKICMQILHAGRYAY---SPKQVAPSAIQAPINPF----KPKELDEEGIEKQIADFVNCAS 153
Cdd:cd04733   77 SGEDLEAFREWAAAAKANGALIWAQLNHPGRQSPaglNQNPVAPSVALDPGGLGklfgKPRAMTEEEIEDVIDRFAHAAR 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187 154 LAQVAGYDGVEIMGSEGYFINQFLVQHTNQRTDRWGGSYENRMRLPVEIVRRVREAVGPNFIIIYRLSMLDLVEGGSSWD 233
Cdd:cd04733  157 LAQEAGFDGVQIHAAHGYLLSQFLSPLTNKRTDEYGGSLENRARLLLEIYDAIRAAVGPGFPVGIKLNSADFQRGGFTEE 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187 234 EIVLLAKAVEKAGATLINTGIGWHEAriPTIATKVP-----RAA-FTKVTAKLRGEVGIPLITTNRINTPEVAEKVLAEG 307
Cdd:cd04733  237 DALEVVEALEEAGVDLVELSGGTYES--PAMAGAKKestiaREAyFLEFAEKIRKVTKTPLMVTGGFRTRAAMEQALASG 314

                        330       340
                 ....*....|....*....|....
gi 489194187 308 DADMVSMARPFLADPDFVNKAAAG 331
Cdd:cd04733  315 AVDGIGLARPLALEPDLPNKLLAG 338
OYE_like_4_FMN cd04735
Old yellow enzyme (OYE)-related FMN binding domain, group 4. Each monomer of OYE contains FMN ...
 20-340 9.64e-59

Old yellow enzyme (OYE)-related FMN binding domain, group 4. Each monomer of OYE contains FMN as a non-covalently bound cofactor, uses NADPH as a reducing agent with oxygens, quinones, and alpha,beta-unsaturated aldehydes and ketones, and can act as electron acceptors in the catalytic reaction. Other members of OYE family include trimethylamine dehydrogenase, 2,4-dienoyl-CoA reductase, enoate reductase, pentaerythriol tetranitrate reductase, xenobiotic reductase, and morphinone reductase.


Pssm-ID: 240086 [Multi-domain]  Cd Length: 353  Bit Score: 201.67  E-value: 9.64e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187  20 TLRNRTLMGSMHTGLEEkPQGF--ERMAAYFAERArGGVGLMVTGGIGPNEEGGVYSGAAKLSTPEEAEKHRIVTQAVHE 97
Cdd:cd04735   12 TLKNRFVMAPMTTYSSN-PDGTitDDELAYYQRRA-GGVGMVITGATYVSPSGIGFEGGFSADDDSDIPGLRKLAQAIKS 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187  98 AGGKICMQILHAGRYAYS-----PKQVAPSAIQAPiNPFK--PKELDEEGIEKQIADFVNCASLAQVAGYDGVEIMGSEG 170
Cdd:cd04735   90 KGAKAILQIFHAGRMANPalvpgGDVVSPSAIAAF-RPGAhtPRELTHEEIEDIIDAFGEATRRAIEAGFDGVEIHGANG 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187 171 YFINQFLVQHTNQRTDRWGGSYENRMRLPVEIVRRVREAVG----PNFIIIYRLSMLDLVEGGSSWDEIVLLAKAVEKAG 246
Cdd:cd04735  169 YLIQQFFSPHSNRRTDEWGGSLENRMRFPLAVVKAVQEVIDkhadKDFILGYRFSPEEPEEPGIRMEDTLALVDKLADKG 248

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187 247 ATLINTGIGWHEARIPTIATKVPRAAfTKVTAKLRGEvgIPLITTNRINTPEVAEKVLAEGdADMVSMARPFLADPDFVN 326
Cdd:cd04735  249 LDYLHISLWDFDRKSRRGRDDNQTIM-ELVKERIAGR--LPLIAVGSINTPDDALEALETG-ADLVAIGRGLLVDPDWVE 324

                        330
                 ....*....|....
gi 489194187 327 KAAAGHAERINTCI 340
Cdd:cd04735  325 KIKEGREDEINLEI 338
OYE_like_5_FMN cd04747
Old yellow enzyme (OYE)-related FMN binding domain, group 5. Each monomer of OYE contains FMN ...
 10-331 1.48e-48

Old yellow enzyme (OYE)-related FMN binding domain, group 5. Each monomer of OYE contains FMN as a non-covalently bound cofactor, uses NADPH as a reducing agent with oxygens, quinones, and alpha,beta-unsaturated aldehydes and ketones, and can act as electron acceptors in the catalytic reaction. Other members of OYE family include trimethylamine dehydrogenase, 2,4-dienoyl-CoA reductase, enoate reductase, pentaerythriol tetranitrate reductase, xenobiotic reductase, and morphinone reductase.


Pssm-ID: 240095 [Multi-domain]  Cd Length: 361  Bit Score: 174.43  E-value: 1.48e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187  10 LLAPLDLGFTTLRNRTLMGSMhtGLEEKPQGF--ERMAAYFAERARGGVGLMVTGGIGPNEEGGVYSGAAKLSTPEEA-E 86
Cdd:cd04747    1 LFTPFTLKGLTLPNRIVMAPM--TRSFSPGGVpgQDVAAYYRRRAAGGVGLIITEGTAVDHPAASGDPNVPRFHGEDAlA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187  87 KHRIVTQAVHEAGGKICMQILHAG--RYAYSP-----KQVAPSAIQAPINPFKPkELDEEGIEKQIADFVNCASLAQVAG 159
Cdd:cd04747   79 GWKKVVDEVHAAGGKIAPQLWHVGamRKLGTPpfpdvPPLSPSGLVGPGKPVGR-EMTEADIDDVIAAFARAAADARRLG 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187 160 YDGVEIMGSEGYFINQFLVQHTNQRTDRWGGSYENRMRLPVEIVRRVREAVGPNFIIIYRLSMLDLVEGGS----SWDEI 235
Cdd:cd04747  158 FDGIELHGAHGYLIDQFFWAGTNRRADGYGGSLAARSRFAAEVVKAIRAAVGPDFPIILRFSQWKQQDYTArladTPDEL 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187 236 -VLLAKAVEkAGATLIN----------------TGIGWheAR----IPTIAT------KVPRAAFtkvtaklrgeVGIPL 288
Cdd:cd04747  238 eALLAPLVD-AGVDIFHcstrrfwepefegselNLAGW--TKkltgLPTITVgsvgldGDFIGAF----------AGDEG 304

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 489194187 289 ITTNRIntpEVAEKVLAEGDADMVSMARPFLADPDFVNKAAAG 331
Cdd:cd04747  305 ASPASL---DRLLERLERGEFDLVAVGRALLSDPAWVAKVREG 344
PRK08255 PRK08255
bifunctional salicylyl-CoA 5-hydroxylase/oxidoreductase;
2-330 8.27e-45

bifunctional salicylyl-CoA 5-hydroxylase/oxidoreductase;


Pssm-ID: 236203 [Multi-domain]  Cd Length: 765  Bit Score: 171.28  E-value: 8.27e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187   2 TAAVPYPHLLAPLDLGFTTLRNRTLMGSM-----HTGLeekPQGFERMaaYFAERARGGVGLMVTGGIGPNEEGGVYSGA 76
Cdd:PRK08255 391 PVARPPPPMFTPFRLRGLTLKNRVVVSPMamysaVDGV---PGDFHLV--HLGARALGGAGLVMTEMTCVSPEGRITPGC 465

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187  77 AKLSTPEEAEKHRIVTQAVH-EAGGKICMQILHAGRYAySPKQ----------------VAPSAIQAPINPFKPKELDEE 139
Cdd:PRK08255 466 PGLYNDEQEAAWKRIVDFVHaNSDAKIGIQLGHSGRKG-STRLgwegidepleegnwplISASPLPYLPGSQVPREMTRA 544

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187 140 GIEKQIADFVNCASLAQVAGYDGVEIMGSEGYFINQFLVQHTNQRTDRWGGSYENRMRLPVEIVRRVREAVGPNFIIIYR 219
Cdd:PRK08255 545 DMDRVRDDFVAAARRAAEAGFDWLELHCAHGYLLSSFISPLTNQRTDEYGGSLENRLRYPLEVFRAVRAVWPAEKPMSVR 624

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187 220 LSMLDLVEGGSSWDEIVLLAKAVEKAGATLIN--TGIGWHEARiPTIAtkvpRAAFTKVTAKLRGEVGIPLITTNRINTP 297
Cdd:PRK08255 625 ISAHDWVEGGNTPDDAVEIARAFKAAGADLIDvsSGQVSKDEK-PVYG----RMYQTPFADRIRNEAGIATIAVGAISEA 699

                        330       340       350
                 ....*....|....*....|....*....|...
gi 489194187 298 EVAEKVLAEGDADMVSMARPFLADPDFVNKAAA 330
Cdd:PRK08255 700 DHVNSIIAAGRADLCALARPHLADPAWTLHEAA 732
PRK13523 PRK13523
NADPH dehydrogenase NamA; Provisional
 10-329 1.25e-43

NADPH dehydrogenase NamA; Provisional


Pssm-ID: 184110 [Multi-domain]  Cd Length: 337  Bit Score: 159.86  E-value: 1.25e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187  10 LLAPLDLGFTTLRNRTLMGSMHTGLEEKPQGFER---MAAYFAeRARGGVGLMVTGGIGPNEEGGVYSGAAKLSTPEEAE 86
Cdd:PRK13523   3 LFSPYTIKDVTLKNRIVMSPMCMYSSENKDGKVTnfhLIHYGT-RAAGQVGLVIVEATAVLPEGRISDKDLGIWDDEHIE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187  87 KHRIVTQAVHEAGGKICMQILHAGRYAYSPKQ-VAPSAIQAPINPFKPKELDEEGIEKQIADFVNCASLAQVAGYDGVEI 165
Cdd:PRK13523  82 GLHKLVTFIHDHGAKAAIQLAHAGRKAELEGDiVAPSAIPFDEKSKTPVEMTKEQIKETVLAFKQAAVRAKEAGFDVIEI 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187 166 MGSEGYFINQFLVQHTNQRTDRWGGSYENRMRLPVEIVRRVREA-VGPNFIiiyRLSMLDLVEGGSSWDEIVLLAKAVEK 244
Cdd:PRK13523 162 HGAHGYLINEFLSPLSNKRTDEYGGSPENRYRFLREIIDAVKEVwDGPLFV---RISASDYHPGGLTVQDYVQYAKWMKE 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187 245 AGATLINTGIG-WHEARIPTI-ATKVPRAaftkvtAKLRGEVGIPLITTNRINTPEVAEKVLAEGDADMVSMARPFLADP 322
Cdd:PRK13523 239 QGVDLIDVSSGaVVPARIDVYpGYQVPFA------EHIREHANIATGAVGLITSGAQAEEILQNNRADLIFIGRELLRNP 312


                 ....*..
gi 489194187 323 DFVNKAA 329
Cdd:PRK13523 313 YFPRIAA 319
TMADH_HD_FMN cd02929
Trimethylamine dehydrogenase (TMADH) and histamine dehydrogenase (HD) FMN-binding domain. ...
 6-367 1.91e-38

Trimethylamine dehydrogenase (TMADH) and histamine dehydrogenase (HD) FMN-binding domain. TMADH is an iron-sulfur flavoprotein that catalyzes the oxidative demethylation of trimethylamine to form dimethylamine and formaldehyde. The protein forms a symetrical dimer with each subunit containing one 4Fe-4S cluster and one FMN cofactor. It contains a unique flavin, in the form of a 6-S-cysteinyl FMN which is bent by ~25 degrees along the N5-N10 axis of the flavin isoalloxazine ring. This modification of the conformation of the flavin is thought to facilitate catalysis.The closely related histamine dehydrogenase catalyzes oxidative deamination of histamine.


Pssm-ID: 239239 [Multi-domain]  Cd Length: 370  Bit Score: 146.35  E-value: 1.91e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187   6 PYPHLLAPLDLGFTTLRNR-------TLMGSMHTGLeekpqgferMAAYFAERARGGVGLMVTG--GIGPNEEGGVYSgA 76
Cdd:cd02929    4 RHDILFEPIKIGPVTARNRfyqvphcNGMGYRKPSA---------QAAMRGIKAEGGWGVVNTEqcSIHPSSDDTPRI-S 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187  77 AKLSTPEEAEKHRIVTQAVHEAGGKICMQILHAGRYA--YSPKQV--APSAIQ---APINPFKPKELDEEGIEKQIADFV 149
Cdd:cd02929   74 ARLWDDGDIRNLAAMTDAVHKHGALAGIELWHGGAHApnRESRETplGPSQLPsefPTGGPVQAREMDKDDIKRVRRWYV 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187 150 NCASLAQVAGYDGVEIMGSEGYFINQFLVQHTNQRTDRWGGSYENRMRLPVEIVRRVREAVGPNFIIIYRLSMLDLV--E 227
Cdd:cd02929  154 DAALRARDAGFDIVYVYAAHGYLPLQFLLPRYNKRTDEYGGSLENRARFWRETLEDTKDAVGDDCAVATRFSVDELIgpG 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187 228 GGSSWDEIVllaKAVEKAGATL----INTG--IGWHE-ARIPTIATKVPRAAFTK-VTAKlrgevgiPLITTNRINTPEV 299
Cdd:cd02929  234 GIESEGEGV---EFVEMLDELPdlwdVNVGdwANDGEdSRFYPEGHQEPYIKFVKqVTSK-------PVVGVGRFTSPDK 303

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489194187 300 AEKVLAEGDADMVSMARPFLADPDFVNKAAAGHAERINTCIGCNqACLDHTFGGKLTSCLVNPRACHE 367
Cdd:cd02929  304 MVEVVKSGILDLIGAARPSIADPFLPKKIREGRIDDIRECIGCN-ICISGDEGGVPMRCTQNPTAGEE 370
PRK10605 PRK10605
N-ethylmaleimide reductase; Provisional
 10-327 3.47e-38

N-ethylmaleimide reductase; Provisional


Pssm-ID: 182584 [Multi-domain]  Cd Length: 362  Bit Score: 145.25  E-value: 3.47e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187  10 LLAPLDLGFTTLRNRTLM-----------GSMHTGLeekpqgferMAAYFAERArgGVGLMVTGG--IGPNEEGgvYSGA 76
Cdd:PRK10605   3 LFSPLKVGAITAPNRVFMapltrlrsiepGDIPTPL---------MAEYYRQRA--SAGLIISEAtqISAQAKG--YAGA 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187  77 AKLSTPEEAEKHRIVTQAVHEAGGKICMQILHAGRYAYSPKQ------VAPSAIQAP--------------INPFKPKEL 136
Cdd:PRK10605  70 PGLHSPEQIAAWKKITAGVHAEGGHIAVQLWHTGRISHASLQpggqapVAPSAINAGtrtslrdengqairVETSTPRAL 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187 137 DEEGIEKQIADFVNCASLAQVAGYDGVEIMGSEGYFINQFLVQHTNQRTDRWGGSYENRMRLPVEIVRRVREAVGPNFII 216
Cdd:PRK10605 150 ELEEIPGIVNDFRQAIANAREAGFDLVELHSAHGYLLHQFLSPSSNQRTDQYGGSVENRARLVLEVVDAGIAEWGADRIG 229

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187 217 IyRLSML---DLVEGGSSWDEIVL-LAKAVEKagatlinTGIGWHEARIPTIATKVP-RAAFTKvtaKLRGEVGIPLITT 291
Cdd:PRK10605 230 I-RISPLgtfNNVDNGPNEEADALyLIEQLGK-------RGIAYLHMSEPDWAGGEPySDAFRE---KVRARFHGVIIGA 298

                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 489194187 292 NRInTPEVAEKVLAEGDADMVSMARPFLADPDFVNK 327
Cdd:PRK10605 299 GAY-TAEKAETLIGKGLIDAVAFGRDYIANPDLVAR 333
PLN02411 PLN02411
12-oxophytodienoate reductase
 8-325 8.96e-31

12-oxophytodienoate reductase


Pssm-ID: 178033 [Multi-domain]  Cd Length: 391  Bit Score: 124.97  E-value: 8.96e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187   8 PHLLAPLDLGFTTLRNRTLMGSMHT--GLEEKPQgfERMAAYFAERARGGvGLMVTGG--IGPNEEG-----GVYSGaak 78
Cdd:PLN02411  10 ETLFSPYKMGRFDLSHRVVLAPMTRcrALNGIPN--AALAEYYAQRSTPG-GFLISEGtlISPTAPGfphvpGIYSD--- 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187  79 lstpEEAEKHRIVTQAVHEAGGKICMQILHAGR---YAYSPKQVAP-SAIQAPIN---------------PfKPKELDEE 139
Cdd:PLN02411  84 ----EQVEAWKKVVDAVHAKGSIIFCQLWHVGRashQVYQPGGAAPiSSTNKPISerwrilmpdgsygkyP-KPRALETS 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187 140 GIEKQIADFVNCASLAQVAGYDGVEIMGSEGYFINQFLVQHTNQRTDRWGGSYENRMRLPVEIVRRVREAVGPNFIIIYR 219
Cdd:PLN02411 159 EIPEVVEHYRQAALNAIRAGFDGIEIHGAHGYLIDQFLKDGINDRTDEYGGSIENRCRFLMQVVQAVVSAIGADRVGVRV 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187 220 LSMLDLVEGGSSwDEIVLLAKAVEKAGATLINTGigwheARIPTIATKVPRAAFTKVTAKLR---GEVGIPLITTNRIN- 295
Cdd:PLN02411 239 SPAIDHLDATDS-DPLNLGLAVVERLNKLQLQNG-----SKLAYLHVTQPRYTAYGQTESGRhgsEEEEAQLMRTLRRAy 312

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 489194187 296 ----------TPEVAEKVLAEGDADMVSMARPFLADPDFV 325
Cdd:PLN02411 313 qgtfmcsggfTRELGMQAVQQGDADLVSYGRLFISNPDLV 352
FadH2 COG0446
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ...
 403-636 1.00e-11

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: 66.76  E-value: 1.00e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187 403 RVSLFDAAGEIGGQ-FNVAKRVPGKEEFHETLRYF-RNKLESTGVELHLNRRV-DVDD-----LVAGG----YDEIVLAT 470
Cdd:COG0446    7 EITVIEKGPHHSYQpCGLPYYVGGGIKDPEDLLVRtPESFERKGIDVRTGTEVtAIDPeaktvTLRDGetlsYDKLVLAT 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187 471 GIVPRTPAIPGIEHPKV-----ISYLDAILE--RKPVGGKVAVIGAGGIGFDVSEFithagpstslereafWKEWGIDTR 543
Cdd:COG0446   87 GARPRPPPIPGLDLPGVftlrtLDDADALREalKEFKGKRAVVIGGGPIGLELAEA---------------LRKRGLKVT 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187 544 LearggiagvkaeVHPAARqvfLLQRKKSKVGDGLGKttgWIHRAGLKNKQVQMVNAVEylgiDDAGLHIRVAEGEpqVL 623
Cdd:COG0446  152 L------------VERAPR---LLGVLDPEMAALLEE---ELREHGVELRLGETVVAID----GDDKVAVTLTDGE--EI 207

                        250
                 ....*....|...
gi 489194187 624 PVDTVIVCAGQDP 636
Cdd:COG0446  208 PADLVVVAPGVRP 220
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 399-644 1.21e-11

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: 66.19  E-value: 1.21e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187  399 ERGHRVSLFDAAGEI-GGQFNVAKRVPGKEEFHETLRYFRN---------KLESTGVELHLN----------RRVDVDDL 458
Cdd:pfam07992  21 QLGGKVTLIEDEGTCpYGGCVLSKALLGAAEAPEIASLWADlykrkeevvKKLNNGIEVLLGtevvsidpgaKKVVLEEL 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187  459 VAGG-----YDEIVLATGIVPRTPAIPGIEHP--KVISYLDA--ILERKPVGGKVAVIGAGGIGFDVSEFITHAGpstsl 529
Cdd:pfam07992 101 VDGDgetitYDRLVIATGARPRLPPIPGVELNvgFLVRTLDSaeALRLKLLPKRVVVVGGGYIGVELAAALAKLG----- 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187  530 ereafwkewgidtrlearggiagvkAEVHPAARQVFLLQRKKSKVGDglgkttgWIHRAgLKNKQVQMVNAVEYLGIDDA 609
Cdd:pfam07992 176 -------------------------KEVTLIEALDRLLRAFDEEISA-------ALEKA-LEKNGVEVRLGTSVKEIIGD 222

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 489194187  610 GLHIRVAEGEPQVLPVDTVIVCAGQDPLREL--QDGL 644
Cdd:pfam07992 223 GDGVEVILKDGTEIDADLVVVAIGRRPNTELleAAGL 259
NirB COG1251
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
425-633 1.78e-10

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


Pssm-ID: 440863 [Multi-domain]  Cd Length: 402  Bit Score: 63.24  E-value: 1.78e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187 425 GKEEFHETLRYFRNKLESTGVELHLNRRV---DVDD---LVAGG----YDEIVLATGIVPRTPAIPGIEHPKVISY---- 490
Cdd:COG1251   51 GETDEEDLLLRPADFYEENGIDLRLGTRVtaiDRAArtvTLADGetlpYDKLVLATGSRPRVPPIPGADLPGVFTLrtld 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187 491 -LDAILERKPVGGKVAVIGAGGIGfdvsefithagpstslereafwkewgidtrLEARGGIAGVKAEV---HPAARqvfL 566
Cdd:COG1251  131 dADALRAALAPGKRVVVIGGGLIG------------------------------LEAAAALRKRGLEVtvvERAPR---L 177

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187 567 LQRKkskvgdgLGKTTGWIHRAGLKNKQVQM---VNAVEYLGiDDAGLHIRVAEGEpqVLPVDTVIVCAG 633
Cdd:COG1251  178 LPRQ-------LDEEAGALLQRLLEALGVEVrlgTGVTEIEG-DDRVTGVRLADGE--ELPADLVVVAIG 237
TIM_phosphate_binding cd04722
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ...
 145-316 6.54e-09

TIM barrel proteins share a structurally conserved phosphate binding motif and in general share an eight beta/alpha closed barrel structure. Specific for this family is the conserved phosphate binding site at the edges of strands 7 and 8. The phosphate comes either from the substrate, as in the case of inosine monophosphate dehydrogenase (IMPDH), or from ribulose-5-phosphate 3-epimerase (RPE) or from cofactors, like FMN.


Pssm-ID: 240073 [Multi-domain]  Cd Length: 200  Bit Score: 56.44  E-value: 6.54e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187 145 IADFVNCASLAQVAGYDGVEIMGSEGYfinqflvqhtnqrtdrwggsyenRMRLPVEIVRRVREAVgPNFIIIYRLSMLD 224
Cdd:cd04722   70 AAAVDIAAAAARAAGADGVEIHGAVGY-----------------------LAREDLELIRELREAV-PDVKVVVKLSPTG 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187 225 lveggsswdeiVLLAKAVEKAGATLINTGIGWHEARIPTIATKVPRaaftkVTAKLRGEVGIPLITTNRINTPEVAEKVL 304
Cdd:cd04722  126 -----------ELAAAAAEEAGVDEVGLGNGGGGGGGRDAVPIADL-----LLILAKRGSKVPVIAGGGINDPEDAAEAL 189

                        170
                 ....*....|..
gi 489194187 305 AEGdADMVSMAR 316
Cdd:cd04722  190 ALG-ADGVIVGS 200
PRK12771 PRK12771
putative glutamate synthase (NADPH) small subunit; Provisional
 379-516 1.55e-08

putative glutamate synthase (NADPH) small subunit; Provisional


Pssm-ID: 237198 [Multi-domain]  Cd Length: 564  Bit Score: 57.58  E-value: 1.55e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187 379 KKIAVVGAGPAGLAAATVAAERGHRVSLFDAAGEIGG--QFNV-AKRVPgkeefHETLRYFRNKLESTGVELHLNRRVDV 455
Cdd:PRK12771 138 KRVAVIGGGPAGLSAAYHLRRMGHAVTIFEAGPKLGGmmRYGIpAYRLP-----REVLDAEIQRILDLGVEVRLGVRVGE 212

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187 456 D---DLVAGGYDEIVLATGI-VPRTPAIPGIEHPKV---ISYLDAI--LERKPVGGKVAVIGAGGIGFDV 516
Cdd:PRK12771 213 DitlEQLEGEFDAVFVAIGAqLGKRLPIPGEDAAGVldaVDFLRAVgeGEPPFLGKRVVVIGGGNTAMDA 282
PRK11749 PRK11749
dihydropyrimidine dehydrogenase subunit A; Provisional
 377-510 4.43e-08

dihydropyrimidine dehydrogenase subunit A; Provisional


Pssm-ID: 236967 [Multi-domain]  Cd Length: 457  Bit Score: 55.96  E-value: 4.43e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187 377 RPKKIAVVGAGPAGLAAATVAAERGHRVSLFDAAGEIGG-------QFNVAKRVPGKEEfhetlryfrNKLESTGVELHL 449
Cdd:PRK11749 139 TGKKVAVIGAGPAGLTAAHRLARKGYDVTIFEARDKAGGllrygipEFRLPKDIVDREV---------ERLLKLGVEIRT 209

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489194187 450 NRRV----DVDDLVAgGYDEIVLATGI-VPRTPAIPGIEHPKV---ISYLDAI-----LERKPVGGKVAVIGAG 510
Cdd:PRK11749 210 NTEVgrdiTLDELRA-GYDAVFIGTGAgLPRFLGIPGENLGGVysaVDFLTRVnqavaDYDLPVGKRVVVIGGG 282
GltD COG0493
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ...
 379-636 7.73e-08

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: 55.14  E-value: 7.73e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187 379 KKIAVVGAGpaglaaatvaaeRGHRVSLFDAAGEIGGqfnvakrvpgkeefheTLRY----FR----------NKLESTG 444
Cdd:COG0493  122 KKVAVVGSGpaglaaayqlarAGHEVTVFEALDKPGG----------------LLRYgipeFRlpkdvldreiELIEALG 185

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187 445 VELHLNRRV----DVDDLVAgGYDEIVLATGI-VPRTPAIPGIEHPKVIS---YL------DAILERKPVGGKVAVIGAG 510
Cdd:COG0493  186 VEFRTNVEVgkdiTLDELLE-EFDAVFLATGAgKPRDLGIPGEDLKGVHSamdFLtavnlgEAPDTILAVGKRVVVIGGG 264

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187 511 GIGFDVsefithAGpsTSLereafwkewgidtRLEA-------RGGIAGVKA---EVHPA----ARQVFLLQRKKSkVGD 576
Cdd:COG0493  265 NTAMDC------AR--TAL-------------RLGAesvtivyRRTREEMPAskeEVEEAleegVEFLFLVAPVEI-IGD 322

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489194187 577 GLGKTTGwihraglknkqVQMVNaVEYLGIDDAG-LHIRVAEGEPQVLPVDTVIVCAGQDP 636
Cdd:COG0493  323 ENGRVTG-----------LECVR-MELGEPDESGrRRPVPIEGSEFTLPADLVILAIGQTP 371
PRK13984 PRK13984
putative oxidoreductase; Provisional
 370-517 3.36e-07

putative oxidoreductase; Provisional


Pssm-ID: 172486 [Multi-domain]  Cd Length: 604  Bit Score: 53.62  E-value: 3.36e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187 370 LNYIPTTRPKKIAVVGAGPAGLAAATVAAERGHRVSLFDAAGEIGGQFNVAkrVPGKEEFHETLRYFRNKLESTGVELHL 449
Cdd:PRK13984 275 LDDEPEKKNKKVAIVGSGPAGLSAAYFLATMGYEVTVYESLSKPGGVMRYG--IPSYRLPDEALDKDIAFIEALGVKIHL 352

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187 450 NRRVDVD---DLVAGGYDEIVLATGI-VPRTPAIPGIEHPKVISYLDAILE----------RKPVGGKVAVIGAGGIGFD 515
Cdd:PRK13984 353 NTRVGKDiplEELREKHDAVFLSTGFtLGRSTRIPGTDHPDVIQALPLLREirdylrgegpKPKIPRSLVVIGGGNVAMD 432


                 ..
gi 489194187 516 VS 517
Cdd:PRK13984 433 IA 434
Lpd COG1249
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ...
 466-513 1.47e-05

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: 48.16  E-value: 1.47e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 489194187 466 IVLATGIVPRTPAIPGIEHPKVISYlDAILERKPVGGKVAVIGAGGIG 513
Cdd:COG1249  134 IVIATGSRPRVPPIPGLDEVRVLTS-DEALELEELPKSLVVIGGGYIG 180
PRK12831 PRK12831
putative oxidoreductase; Provisional
 379-636 3.13e-05

putative oxidoreductase; Provisional


Pssm-ID: 183780 [Multi-domain]  Cd Length: 464  Bit Score: 46.93  E-value: 3.13e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187 379 KKIAVVGAGPAGLAAATVAAERGHRVSLFDAAGEIGG-------QFNVAKRVPGKEEFhetlryfrNKLESTGVELHLN- 450
Cdd:PRK12831 141 KKVAVIGSGPAGLTCAGDLAKMGYDVTIFEALHEPGGvlvygipEFRLPKETVVKKEI--------ENIKKLGVKIETNv 212

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187 451 ---RRVDVDDLVA-GGYDEIVLATGI-VPRTPAIPGIEHPKVIS---YLDAI-LER--KP-------VGGKVAVIGAGGI 512
Cdd:PRK12831 213 vvgKTVTIDELLEeEGFDAVFIGSGAgLPKFMGIPGENLNGVFSaneFLTRVnLMKayKPeydtpikVGKKVAVVGGGNV 292

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187 513 GFDVSefithagpstsleREAFwkEWGIDTRLEARGGIAGVKA---EVHPAARQ--VF-LLQRKKSKVGDGLGKTTGWih 586
Cdd:PRK12831 293 AMDAA-------------RTAL--RLGAEVHIVYRRSEEELPArveEVHHAKEEgvIFdLLTNPVEILGDENGWVKGM-- 355

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 489194187 587 raglknKQVQMvnaveYLGIDDAG--LHIRVAEGEPQVLPVDTVIVCAGQDP 636
Cdd:PRK12831 356 ------KCIKM-----ELGEPDASgrRRPVEIEGSEFVLEVDTVIMSLGTSP 396
nitri_red_nirB TIGR02374
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ...
 441-648 3.70e-05

nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen metabolism]


Pssm-ID: 162827 [Multi-domain]  Cd Length: 785  Bit Score: 47.13  E-value: 3.70e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187  441 ESTGVELHLNRRV---DVDDLV----AG---GYDEIVLATGIVPRTPAIPGIEHPKVISY-----LDAILERKPVGGKVA 505
Cdd:TIGR02374  65 EKHGITLYTGETViqiDTDQKQvitdAGrtlSYDKLILATGSYPFILPIPGADKKGVYVFrtiedLDAIMAMAQRFKKAA 144

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187  506 VIGAGGIGfdvsefithagpstslereafwkewgidtrLEARGGIAGVKAEVHPAARQVFLLQRKkskvgdgLGKTTGWI 585
Cdd:TIGR02374 145 VIGGGLLG------------------------------LEAAVGLQNLGMDVSVIHHAPGLMAKQ-------LDQTAGRL 187

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489194187  586 HRAGLKNKQVQMV---NAVEYLGiDDAGLHIRVAEGEpqVLPVDTVIVCAGQDPLREL--QDGLLAAG 648
Cdd:TIGR02374 188 LQRELEQKGLTFLlekDTVEIVG-ATKADRIRFKDGS--SLEADLIVMAAGIRPNDELavSAGIKVNR 252
PRK12770 PRK12770
putative glutamate synthase subunit beta; Provisional
 374-518 6.77e-05

putative glutamate synthase subunit beta; Provisional


Pssm-ID: 237197 [Multi-domain]  Cd Length: 352  Bit Score: 45.75  E-value: 6.77e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187 374 PTTRPKKIAVVGAGPAGLAAATVAAERGHRVSLFDAAGEIGGQ--FNVAK-RVPgKEEFHETLRyfrnKLESTGVELHLN 450
Cdd:PRK12770  14 PPPTGKKVAIIGAGPAGLAAAGYLACLGYEVHVYDKLPEPGGLmlFGIPEfRIP-IERVREGVK----ELEEAGVVFHTR 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187 451 -------------------RRVDVDDLVaGGYDEIVLATGI-VPRTPAIPGIEHPKVISYLDAIL------------ERK 498
Cdd:PRK12770  89 tkvccgeplheeegdefveRIVSLEELV-KKYDAVLIATGTwKSRKLGIPGEDLPGVYSALEYLFriraaklgylpwEKV 167

                        170       180
                 ....*....|....*....|..
gi 489194187 499 P--VGGKVAVIGAGGIGFDVSE 518
Cdd:PRK12770 168 PpvEGKKVVVVGAGLTAVDAAL 189
PRK12778 PRK12778
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ...
 367-515 1.63e-04

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


Pssm-ID: 237200 [Multi-domain]  Cd Length: 752  Bit Score: 45.12  E-value: 1.63e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187 367 ETELNYIPTTRPK---KIAVVGAGPAGLAAATVAAERGHRVSLFDAAGEIGGqfnVAK------RVPGKEEFHETlryfr 437
Cdd:PRK12778 417 ESGNISVPEVAEKngkKVAVIGSGPAGLSFAGDLAKRGYDVTVFEALHEIGG---VLKygipefRLPKKIVDVEI----- 488

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187 438 NKLESTGVELHLN----RRVDVDDLVAGGYDEIVLATGI-VPRTPAIPGIEHPKVIS---YL------DAILE--RKPV- 500
Cdd:PRK12778 489 ENLKKLGVKFETDvivgKTITIEELEEEGFKGIFIASGAgLPNFMNIPGENSNGVMSsneYLtrvnlmDAASPdsDTPIk 568

                        170
                 ....*....|....*.
gi 489194187 501 -GGKVAVIGAGGIGFD 515
Cdd:PRK12778 569 fGKKVAVVGGGNTAMD 584
PRK06292 PRK06292
dihydrolipoamide dehydrogenase; Validated
 450-513 8.49e-04

dihydrolipoamide dehydrogenase; Validated


Pssm-ID: 235774 [Multi-domain]  Cd Length: 460  Bit Score: 42.47  E-value: 8.49e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489194187 450 NRRVDVDD--LVAggyDEIVLATGivPRTPAIPGIEHP--KVISYLDAILERKPVGGKVAVIGAGGIG 513
Cdd:PRK06292 119 PNTVEVNGerIEA---KNIVIATG--SRVPPIPGVWLIlgDRLLTSDDAFELDKLPKSLAVIGGGVIG 181
PRK06116 PRK06116
glutathione reductase; Validated
 436-513 1.10e-03

glutathione reductase; Validated


Pssm-ID: 235701 [Multi-domain]  Cd Length: 450  Bit Score: 42.07  E-value: 1.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187 436 FRNKLESTGVELHLNRRVDVDD---LVAGGY---DEIVLATGIVPRTPAIPGIEHpkVIS-----YLDAILERkpvggkV 504
Cdd:PRK06116  99 YRNGLENNGVDLIEGFARFVDAhtvEVNGERytaDHILIATGGRPSIPDIPGAEY--GITsdgffALEELPKR------V 170


                 ....*....
gi 489194187 505 AVIGAGGIG 513
Cdd:PRK06116 171 AVVGAGYIA 179
PRK12814 PRK12814
putative NADPH-dependent glutamate synthase small subunit; Provisional
 322-515 1.61e-03

putative NADPH-dependent glutamate synthase small subunit; Provisional


Pssm-ID: 139246 [Multi-domain]  Cd Length: 652  Bit Score: 41.64  E-value: 1.61e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187 322 PDFVNKAAAGH---AERI------------NTCIG-CNQACLDHTFGGKLTSC-LVNPRACHETELN--YIPTTRP---K 379
Cdd:PRK12814 115 PGFIAAIARGDdreAIRIiketiplpgilgRICPApCEEACRRHGVDEPVSICaLKRYAADRDMESAerYIPERAPksgK 194

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187 380 KIAVVGAGPAGLAAATVAAERGHRVSLFDAAGEIGGQfnvakrvpgkeefhetLRY----FR----------NKLESTGV 445
Cdd:PRK12814 195 KVAIIGAGPAGLTAAYYLLRKGHDVTIFDANEQAGGM----------------MRYgiprFRlpesvidadiAPLRAMGA 258

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489194187 446 ELHLNRRVDVDDLVAG---GYDEIVLATGI-VPRTPAIPGIEHPKVISYLD-----AILERKPVGGKVAVIGAGGIGFD 515
Cdd:PRK12814 259 EFRFNTVFGRDITLEElqkEFDAVLLAVGAqKASKMGIPGEELPGVISGIDflrnvALGTALHPGKKVVVIGGGNTAID 337
CzcO COG2072
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ...
 399-633 2.16e-03

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: 41.00  E-value: 2.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187 399 ERGHRVSLFDAAGEIGG-------------------QF------NVAKRVPGKEEFHETLRYFRNKLestGVELHLNRRV 453
Cdd:COG2072   27 RAGIDFVVLEKADDVGGtwrdnrypglrldtpshlySLpffpnwSDDPDFPTGDEILAYLEAYADKF---GLRRPIRFGT 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187 454 DVDDL------------VAGG----YDEIVLATGI--VPRTPAIPGIEHPKVIS-----YldaileRKPV---GGKVAVI 507
Cdd:COG2072  104 EVTSArwdeadgrwtvtTDDGetltARFVVVATGPlsRPKIPDIPGLEDFAGEQlhsadW------RNPVdlaGKRVLVV 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187 508 GAGGIGFDVSEFITHAG---------PSTSLEREAFWKEWGidtRLEARGGIAGVKAEVHPAARQvFLLQRKKSKVGD-G 577
Cdd:COG2072  178 GTGASAVQIAPELARVAahvtvfqrtPPWVLPRPNYDPERG---RPANYLGLEAPPALNRRDARA-WLRRLLRAQVKDpE 253

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489194187 578 LGKTTGWIH------------RAGLKNKQVQMVN-AVEylGIDDAGlhIRVAEGEpqVLPVDTVIVCAG 633
Cdd:COG2072  254 LGLLTPDYPpgckrpllstdyYEALRRGNVELVTgGIE--RITEDG--VVFADGT--EHEVDVIVWATG 316
MerA TIGR02053
mercury(II) reductase; This model represents the mercuric reductase found in the mer operon ...
 425-518 3.61e-03

mercury(II) reductase; This model represents the mercuric reductase found in the mer operon for the detoxification of mercury compounds. MerA is a FAD-containing flavoprotein which reduces Hg(II) to Hg(0) utilizing NADPH. [Cellular processes, Detoxification]


Pssm-ID: 273944 [Multi-domain]  Cd Length: 463  Bit Score: 40.48  E-value: 3.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187  425 GKEEFHETLRyfRNK----LESTGVELHLNR-------RVDVDDLVA-GGYDEIVLATGIVPRTPAIPGIehpKVISYLD 492
Cdd:TIGR02053  81 GKREVVEELR--HEKyedvLSSYGVDYLRGRarfkdpkTVKVDLGREvRGAKRFLIATGARPAIPPIPGL---KEAGYLT 155

                          90       100
                  ....*....|....*....|....*...
gi 489194187  493 A--ILERKPVGGKVAVIGAGGIGFDVSE 518
Cdd:TIGR02053 156 SeeALALDRIPESLAVIGGGAIGVELAQ 183
MR_like cd03316
Mandelate racemase (MR)-like subfamily of the enolase superfamily. Enzymes of this subgroup ...
 187-312 3.82e-03

Mandelate racemase (MR)-like subfamily of the enolase superfamily. Enzymes of this subgroup share three conserved carboxylate ligands for the essential divalent metal ion (usually Mg2+), two aspartates and a glutamate, and conserved catalytic residues, a Lys-X-Lys motif and a conserved histidine-aspartate dyad. Members of the MR subgroup are mandelate racemase, D-glucarate/L-idarate dehydratase (GlucD), D-altronate/D-mannonate dehydratase , D-galactonate dehydratase (GalD) , D-gluconate dehydratase (GlcD), and L-rhamnonate dehydratase (RhamD).


Pssm-ID: 239432 [Multi-domain]  Cd Length: 357  Bit Score: 39.90  E-value: 3.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187 187 RWGGSYENR--MRLPVEIVRRVREAVGPNFIIiyrlsmldLVEGGSSWD--EIVLLAKAVEKAgatlintGIGWHEARIP 262
Cdd:cd03316  161 KVGGPDSGGedLREDLARVRAVREAVGPDVDL--------MVDANGRWDlaEAIRLARALEEY-------DLFWFEEPVP 225

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 489194187 263 tiatkvprAAFTKVTAKLRGEVGIPLITTNRINTPEVAEKVLAEGDADMV 312
Cdd:cd03316  226 --------PDDLEGLARLRQATSVPIAAGENLYTRWEFRDLLEAGAVDII 267
PRK06416 PRK06416
dihydrolipoamide dehydrogenase; Reviewed
 466-519 4.69e-03

dihydrolipoamide dehydrogenase; Reviewed


Pssm-ID: 235798 [Multi-domain]  Cd Length: 462  Bit Score: 40.13  E-value: 4.69e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 489194187 466 IVLATGIVPRTpaIPGIE-HPKVISYLDAILERKPVGGKVAVIGAGGIGfdvSEF 519
Cdd:PRK06416 138 IILATGSRPRE--LPGIEiDGRVIWTSDEALNLDEVPKSLVVIGGGYIG---VEF 187
RspA COG4948
L-alanine-DL-glutamate epimerase or related enzyme of enolase superfamily [Cell wall/membrane ...
 200-343 7.29e-03

L-alanine-DL-glutamate epimerase or related enzyme of enolase superfamily [Cell wall/membrane/envelope biogenesis, General function prediction only]; L-alanine-DL-glutamate epimerase or related enzyme of enolase superfamily is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway


Pssm-ID: 443975 [Multi-domain]  Cd Length: 359  Bit Score: 39.03  E-value: 7.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187 200 VEIVRRVREAVGPNFIIiyrlsmldLVEGGSSWD--EIVLLAKAVEKAgatlintGIGWHEAriPTiatkvpRAAFTKVT 277
Cdd:COG4948  169 VERVRAVREAVGPDARL--------RVDANGAWTleEAIRLLRALEDL-------GLEWIEQ--PL------PAEDLEGL 225

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489194187 278 AKLRGEVGIPLITTNRINTPEVAEKVLAEGDADMVsmarpfLADPDFVN-----KAAAGHAER--INTCIGCN 343
Cdd:COG4948  226 AELRRATPVPIAADESLTSRADFRRLIEAGAVDIV------NIKLSKVGglteaLRIAALAEAhgVPVMPHCM 292
gltD PRK12810
glutamate synthase subunit beta; Reviewed
 379-515 8.04e-03

glutamate synthase subunit beta; Reviewed


Pssm-ID: 237213 [Multi-domain]  Cd Length: 471  Bit Score: 39.38  E-value: 8.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187 379 KKIAVVGAGPAGLAAATVAAERGHRVSLFDAAGEIGG-------QFNVAKRVPGKEefhetlryfRNKLESTGVELHLN- 450
Cdd:PRK12810 144 KKVAVVGSGPAGLAAADQLARAGHKVTVFERADRIGGllrygipDFKLEKEVIDRR---------IELMEAEGIEFRTNv 214

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187 451 ---RRVDVDDLVAgGYDEIVLATGI-VPRTPAIPGIEHPKV---ISYL-------------DAILerkPVGGKVAVIGAG 510
Cdd:PRK12810 215 evgKDITAEELLA-EYDAVFLGTGAyKPRDLGIPGRDLDGVhfaMDFLiqntrrvlgdetePFIS---AKGKHVVVIGGG 290


                 ....*
gi 489194187 511 GIGFD 515
Cdd:PRK12810 291 DTGMD 295
Ndh COG1252
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
440-514 8.68e-03

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


Pssm-ID: 440864 [Multi-domain]  Cd Length: 386  Bit Score: 38.96  E-value: 8.68e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489194187 440 LESTGVELHL---------NRRVDVDDLVAGGYDEIVLATGIVPRTPAIPGIE---------------HPKVISYLDAIL 495
Cdd:COG1252   66 LRRAGVRFIQgevtgidpeARTVTLADGRTLSYDYLVIATGSVTNFFGIPGLAehalplktledalalRERLLAAFERAE 145

                         90
                 ....*....|....*....
gi 489194187 496 ERKPvgGKVAVIGAGGIGF 514
Cdd:COG1252  146 RRRL--LTIVVVGGGPTGV 162
GlxA COG4977
Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH ...
 609-668 9.30e-03

Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH domain [Transcription];


Pssm-ID: 444002 [Multi-domain]  Cd Length: 318  Bit Score: 38.60  E-value: 9.30e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489194187 609 AGLHIRVAEGEPQVLPVDTVIVCAGQDPLRELQDGLL-----AAGQSVHLIG---GADVAAE---LDAKRA 668
Cdd:COG4977   51 SGLTVAPDHGLADLAAADTLIVPGGLDPAAAADPALLawlrrAAARGARLASictGAFLLAAaglLDGRRA 121
 
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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