|
Name |
Accession |
Description |
Interval |
E-value |
| gltD_gamma_fam |
TIGR01318 |
glutamate synthase small subunit family protein, proteobacterial; This model represents one of ... |
6-470 |
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: 827.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497534204 6 YQFIDVNRVDPAKKPIKIRKIEFVEIYEPFTKQQAKAQADRCLDCGNPYCEWKCPVHNYIPQWLKLANEGRIIEAAELSH 85
Cdd:TIGR01318 1 FQFIDLPRQDPDKIPVEERKTDFREIYGPFDKGQAQYQADRCLDCGNPYCEWKCPVHNAIPQWLQLVQEGRIDEAAELSH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497534204 86 QTNSLPEVCGRVCPQDRLCEGSCTLNDDFGAVTIGNIEKYINDKAFEMGWKPDMSHVEWTDKKVAIIGAGPAGLAAADIL 165
Cdd:TIGR01318 81 QTNTLPEICGRVCPQDRLCEGACTLNDEGGAVTIGNLERYITDTALAMGWRPDLSHVQPTGKRVAVIGAGPAGLACADIL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497534204 166 VRNGVKAVVFDRYPEIGGLLTFGIPSFKLEKGIMENRRRIFSGMGVEFKMNTEVGKDVQLQQLVDDYDAVFLGVGTYKNM 245
Cdd:TIGR01318 161 ARAGVQVVVFDRHPEIGGLLTFGIPSFKLDKAVLSRRREIFTAMGIEFRLNCEVGRDISLDDLLEDYDAVFLGVGTYRSM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497534204 246 RAGLDNEEAPGVYDALPFLVSNTYKVMELD-NPT-PFIDMKGKKVVVLGGGDTAMDCVRTSIRQHAANVVCAYRRDEANM 323
Cdd:TIGR01318 241 RGGLPGEDAPGVLPALPFLIANTRQLMGLPeEPEePLIDVEGKRVVVLGGGDTAMDCVRTAIRLGATKVTCAYRRDEANM 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497534204 324 PGSRREVKNAKEEGVKFMFNLQPLALETDSSGHVTGVKVVKTALGEPDEAGRRRPEPVEGSEHVLEADAVIMAFGFQPHA 403
Cdd:TIGR01318 321 PGSRREVANAREEGVEFLFNVQPVSIESDEDGQVIGVTVVRTKLGEPDANGRRRPVPVAGSEFVLPADVVIMAFGFSPHL 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 497534204 404 MEWLEPFGVELDQWGRIKAPGKQEFQYQTTNSKIFAGGDAVRGSDLVVTAIDEGRKAAEGILDYLEV 470
Cdd:TIGR01318 401 MPWLAAHGITLDSWGRIITALSSGLTYQTTNPKIFAGGDAVRGADLVVTAVAEGRDAAQGILDWLGV 467
|
|
| PRK12769 |
PRK12769 |
putative oxidoreductase Fe-S binding subunit; Reviewed |
13-470 |
0e+00 |
|
putative oxidoreductase Fe-S binding subunit; Reviewed
Pssm-ID: 183733 [Multi-domain] Cd Length: 654 Bit Score: 794.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497534204 13 RVDPAKKPIKIRKIEFVEIYEPFTKQQAKAQADRCLDCGN-PYCEWKCPVHNYIPQWLKLANEGRIIEAAELSHQTNSLP 91
Cdd:PRK12769 193 RGEPDKLAIEARKTGFDEIYLPFRADQAQREASRCLKCGEhSICEWTCPLHNHIPQWIELVKAGNIDAAVELSHQTNSLP 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497534204 92 EVCGRVCPQDRLCEGSCTLNDDFGAVTIGNIEKYINDKAFEMGWKPDMSHVEWTDKKVAIIGAGPAGLAAADILVRNGVK 171
Cdd:PRK12769 273 EITGRVCPQDRLCEGACTLRDEYGAVTIGNIERYISDQALAKGWRPDLSQVTKSDKRVAIIGAGPAGLACADVLARNGVA 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497534204 172 AVVFDRYPEIGGLLTFGIPSFKLEKGIMENRRRIFSGMGVEFKMNTEVGKDVQLQQLVDDYDAVFLGVGTYKNMRAGLDN 251
Cdd:PRK12769 353 VTVYDRHPEIGGLLTFGIPAFKLDKSLLARRREIFSAMGIEFELNCEVGKDISLESLLEDYDAVFVGVGTYRSMKAGLPN 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497534204 252 EEAPGVYDALPFLVSNTYKVMEL-DNPT-PFIDMKGKKVVVLGGGDTAMDCVRTSIRQHAANVVCAYRRDEANMPGSRRE 329
Cdd:PRK12769 433 EDAPGVYDALPFLIANTKQVMGLeELPEePFINTAGLNVVVLGGGDTAMDCVRTALRHGASNVTCAYRRDEANMPGSKKE 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497534204 330 VKNAKEEGVKFMFNLQPLALETDSSGHVTGVKVVKTALGEPDEAGRRRPEPVEGSEHVLEADAVIMAFGFQPHAMEWLEP 409
Cdd:PRK12769 513 VKNAREEGANFEFNVQPVALELNEQGHVCGIRFLRTRLGEPDAQGRRRPVPIPGSEFVMPADAVIMAFGFNPHGMPWLES 592
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 497534204 410 FGVELDQWGRIKAPGKQEFQYQTTNSKIFAGGDAVRGSDLVVTAIDEGRKAAEGILDYLEV 470
Cdd:PRK12769 593 HGVTVDKWGRIIADVESQYRYQTSNPKIFAGGDAVRGADLVVTAMAEGRHAAQGIIDWLGV 653
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
24-467 |
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: 622.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497534204 24 RKIEFVEIYEPFTKQQAKAQADRCLDCGNPYCEWKCPVHNYIPQWLKLANEGRIIEAAELSHQTNSLPEVCGRVCPqdRL 103
Cdd:COG0493 1 RIKDFREVYPGLSEEEAIEQAARCLDCGDPPCQTGCPVGNDIPEWIRLIAEGDYEEALELIHETNPFPEVCGRVCP--AP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497534204 104 CEGSCTLNDDFGAVTIGNIEKYINDKAFEMGWKPDMSHVEWTDKKVAIIGAgpaglaaaDILVRNGVKAVVFDRYPEIGG 183
Cdd:COG0493 79 CEGACVRGIVDEPVAIGALERFIADKAFEEGWVKPPPPAPRTGKKVAVVGSgpaglaaaYQLARAGHEVTVFEALDKPGG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497534204 184 LLTFGIPSFKLEKGIMENRRRIFSGMGVEFKMNTEVGKDVQLQQLVDDYDAVFLGVGTYKNMRAGLDNEEAPGVYDALPF 263
Cdd:COG0493 159 LLRYGIPEFRLPKDVLDREIELIEALGVEFRTNVEVGKDITLDELLEEFDAVFLATGAGKPRDLGIPGEDLKGVHSAMDF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497534204 264 LVSNTykvmeLDNPTPFIDMKGKKVVVLGGGDTAMDCVRTSIRQHAANVVCAYRRDEANMPGSRREVKNAKEEGVKFMFN 343
Cdd:COG0493 239 LTAVN-----LGEAPDTILAVGKRVVVIGGGNTAMDCARTALRLGAESVTIVYRRTREEMPASKEEVEEALEEGVEFLFL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497534204 344 LQPLALETDSSGHVTGVKVVKTALGEPDEAGRRRPEPVEGSEHVLEADAVIMAFGFQPHAMEWLEPFGVELDQWGRIKAP 423
Cdd:COG0493 314 VAPVEIIGDENGRVTGLECVRMELGEPDESGRRRPVPIEGSEFTLPADLVILAIGQTPDPSGLEEELGLELDKRGTIVVD 393
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 497534204 424 gkqEFQYQTTNSKIFAGGDAVRGSDLVVTAIDEGRKAAEGILDY 467
Cdd:COG0493 394 ---EETYQTSLPGVFAGGDAVRGPSLVVWAIAEGRKAARAIDRY 434
|
|
| Fer4_20 |
pfam14691 |
Dihydroprymidine dehydrogenase domain II, 4Fe-4S cluster; Domain II of the enzyme ... |
24-135 |
3.66e-62 |
|
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: 197.76 E-value: 3.66e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497534204 24 RKIEFVEIYEPFTKQQAKAQADRCLDCGNPYCEWKCPVHNYIPQWLKLANEGRIIEAAELSHQTNSLPEVCGRVCPQDRL 103
Cdd:pfam14691 1 RIKNFEEVALGYTEEEAIAEASRCLQCKDPPCVKGCPVHIDIPEFIKLIAEGNFEGAARIILETNPLPAICGRVCPQERQ 80
|
90 100 110
....*....|....*....|....*....|...
gi 497534204 104 CEGSCTLN-DDFGAVTIGNIEKYINDKAFEMGW 135
Cdd:pfam14691 81 CEGACVLGkKGFEPVAIGRLERFAADWARENGI 113
|
|
| ACS_1 |
cd01916 |
Acetyl-CoA synthase (ACS), also known as acetyl-CoA decarbonylase, is found in acetogenic and ... |
21-100 |
6.85e-04 |
|
Acetyl-CoA synthase (ACS), also known as acetyl-CoA decarbonylase, is found in acetogenic and methanogenic organisms and is responsible for the synthesis and breakdown of acetyl-CoA. ACS forms a heterotetramer with carbon monoxide dehydrogenase (CODH) consisting of two ACS and two CODH subunits. CODH reduces carbon dioxide to carbon monoxide and ACS then synthesizes acetyl-CoA from carbon monoxide, CoA, and a methyl group donated by another protein (CoFeSP). ACS has three structural domains, an N-terminal rossman fold domain with a helical region at its N-terminus which interacts with CODH, and two alpha + beta fold domains. A Ni-Fe-S center referred to as the A-cluster is located in the C-terminal domain. A large cavity exists between the three domains which may bind CoA.
Pssm-ID: 238897 [Multi-domain] Cd Length: 731 Bit Score: 42.01 E-value: 6.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497534204 21 IKIRKIEFVEIYEPfTKQQAKAQADRCLDCGNpyCEWKCPVHNYIPQWLKLANEGRIIEAAELSHQTNSlpevCGR---V 97
Cdd:cd01916 342 MAVKPKRKGEKKLP-TDEEFQELAAKCTDCGW--CTRACPNSLRIKEAMEAAKEGDFSGLADLFDQCVG----CGRceqE 414
|
...
gi 497534204 98 CPQ 100
Cdd:cd01916 415 CPK 417
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| gltD_gamma_fam |
TIGR01318 |
glutamate synthase small subunit family protein, proteobacterial; This model represents one of ... |
6-470 |
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: 827.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497534204 6 YQFIDVNRVDPAKKPIKIRKIEFVEIYEPFTKQQAKAQADRCLDCGNPYCEWKCPVHNYIPQWLKLANEGRIIEAAELSH 85
Cdd:TIGR01318 1 FQFIDLPRQDPDKIPVEERKTDFREIYGPFDKGQAQYQADRCLDCGNPYCEWKCPVHNAIPQWLQLVQEGRIDEAAELSH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497534204 86 QTNSLPEVCGRVCPQDRLCEGSCTLNDDFGAVTIGNIEKYINDKAFEMGWKPDMSHVEWTDKKVAIIGAGPAGLAAADIL 165
Cdd:TIGR01318 81 QTNTLPEICGRVCPQDRLCEGACTLNDEGGAVTIGNLERYITDTALAMGWRPDLSHVQPTGKRVAVIGAGPAGLACADIL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497534204 166 VRNGVKAVVFDRYPEIGGLLTFGIPSFKLEKGIMENRRRIFSGMGVEFKMNTEVGKDVQLQQLVDDYDAVFLGVGTYKNM 245
Cdd:TIGR01318 161 ARAGVQVVVFDRHPEIGGLLTFGIPSFKLDKAVLSRRREIFTAMGIEFRLNCEVGRDISLDDLLEDYDAVFLGVGTYRSM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497534204 246 RAGLDNEEAPGVYDALPFLVSNTYKVMELD-NPT-PFIDMKGKKVVVLGGGDTAMDCVRTSIRQHAANVVCAYRRDEANM 323
Cdd:TIGR01318 241 RGGLPGEDAPGVLPALPFLIANTRQLMGLPeEPEePLIDVEGKRVVVLGGGDTAMDCVRTAIRLGATKVTCAYRRDEANM 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497534204 324 PGSRREVKNAKEEGVKFMFNLQPLALETDSSGHVTGVKVVKTALGEPDEAGRRRPEPVEGSEHVLEADAVIMAFGFQPHA 403
Cdd:TIGR01318 321 PGSRREVANAREEGVEFLFNVQPVSIESDEDGQVIGVTVVRTKLGEPDANGRRRPVPVAGSEFVLPADVVIMAFGFSPHL 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 497534204 404 MEWLEPFGVELDQWGRIKAPGKQEFQYQTTNSKIFAGGDAVRGSDLVVTAIDEGRKAAEGILDYLEV 470
Cdd:TIGR01318 401 MPWLAAHGITLDSWGRIITALSSGLTYQTTNPKIFAGGDAVRGADLVVTAVAEGRDAAQGILDWLGV 467
|
|
| PRK12769 |
PRK12769 |
putative oxidoreductase Fe-S binding subunit; Reviewed |
13-470 |
0e+00 |
|
putative oxidoreductase Fe-S binding subunit; Reviewed
Pssm-ID: 183733 [Multi-domain] Cd Length: 654 Bit Score: 794.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497534204 13 RVDPAKKPIKIRKIEFVEIYEPFTKQQAKAQADRCLDCGN-PYCEWKCPVHNYIPQWLKLANEGRIIEAAELSHQTNSLP 91
Cdd:PRK12769 193 RGEPDKLAIEARKTGFDEIYLPFRADQAQREASRCLKCGEhSICEWTCPLHNHIPQWIELVKAGNIDAAVELSHQTNSLP 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497534204 92 EVCGRVCPQDRLCEGSCTLNDDFGAVTIGNIEKYINDKAFEMGWKPDMSHVEWTDKKVAIIGAGPAGLAAADILVRNGVK 171
Cdd:PRK12769 273 EITGRVCPQDRLCEGACTLRDEYGAVTIGNIERYISDQALAKGWRPDLSQVTKSDKRVAIIGAGPAGLACADVLARNGVA 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497534204 172 AVVFDRYPEIGGLLTFGIPSFKLEKGIMENRRRIFSGMGVEFKMNTEVGKDVQLQQLVDDYDAVFLGVGTYKNMRAGLDN 251
Cdd:PRK12769 353 VTVYDRHPEIGGLLTFGIPAFKLDKSLLARRREIFSAMGIEFELNCEVGKDISLESLLEDYDAVFVGVGTYRSMKAGLPN 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497534204 252 EEAPGVYDALPFLVSNTYKVMEL-DNPT-PFIDMKGKKVVVLGGGDTAMDCVRTSIRQHAANVVCAYRRDEANMPGSRRE 329
Cdd:PRK12769 433 EDAPGVYDALPFLIANTKQVMGLeELPEePFINTAGLNVVVLGGGDTAMDCVRTALRHGASNVTCAYRRDEANMPGSKKE 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497534204 330 VKNAKEEGVKFMFNLQPLALETDSSGHVTGVKVVKTALGEPDEAGRRRPEPVEGSEHVLEADAVIMAFGFQPHAMEWLEP 409
Cdd:PRK12769 513 VKNAREEGANFEFNVQPVALELNEQGHVCGIRFLRTRLGEPDAQGRRRPVPIPGSEFVMPADAVIMAFGFNPHGMPWLES 592
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 497534204 410 FGVELDQWGRIKAPGKQEFQYQTTNSKIFAGGDAVRGSDLVVTAIDEGRKAAEGILDYLEV 470
Cdd:PRK12769 593 HGVTVDKWGRIIADVESQYRYQTSNPKIFAGGDAVRGADLVVTAMAEGRHAAQGIIDWLGV 653
|
|
| gltD |
PRK12810 |
glutamate synthase subunit beta; Reviewed |
2-470 |
0e+00 |
|
glutamate synthase subunit beta; Reviewed
Pssm-ID: 237213 [Multi-domain] Cd Length: 471 Bit Score: 756.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497534204 2 SQNVYQFIDVNRVDPAKKPIKIRKIEFVEIYEPFTKQQAKAQADRCLDCGNPYCEWKCPVHNYIPQWLKLANEGRIIEAA 81
Cdd:PRK12810 1 MGKPTGFLEYDRVDPKKRPVAERIKDFKEFYEPFSEEQAKIQAARCMDCGIPFCHWGCPVHNYIPEWNDLVYRGRWEEAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497534204 82 ELSHQTNSLPEVCGRVCPQDrlCEGSCTLNDDFGAVTIGNIEKYINDKAFEMGW-KPDmSHVEWTDKKVAIIGAGPAGLA 160
Cdd:PRK12810 81 ERLHQTNNFPEFTGRVCPAP--CEGACTLNINFGPVTIKNIERYIIDKAFEEGWvKPD-PPVKRTGKKVAVVGSGPAGLA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497534204 161 AADILVRNGVKAVVFDRYPEIGGLLTFGIPSFKLEKGIMENRRRIFSGMGVEFKMNTEVGKDVQLQQLVDDYDAVFLGVG 240
Cdd:PRK12810 158 AADQLARAGHKVTVFERADRIGGLLRYGIPDFKLEKEVIDRRIELMEAEGIEFRTNVEVGKDITAEELLAEYDAVFLGTG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497534204 241 TYKNMRAGLDNEEAPGVYDALPFLVSNTYKVMElDNPTPFIDMKGKKVVVLGGGDTAMDCVRTSIRQHAANVVcayRRDE 320
Cdd:PRK12810 238 AYKPRDLGIPGRDLDGVHFAMDFLIQNTRRVLG-DETEPFISAKGKHVVVIGGGDTGMDCVGTAIRQGAKSVT---QRDI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497534204 321 ANMPGSRR-------------EVKNAKEEGVKFMFNLQPLALETDsSGHVTGVKVVKTALGEPDeagrrrPEPVEGSEHV 387
Cdd:PRK12810 314 MPMPPSRRnknnpwpywpmklEVSNAHEEGVEREFNVQTKEFEGE-NGKVTGVKVVRTELGEGD------FEPVEGSEFV 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497534204 388 LEADAVIMAFGFQPHAMEWLEPFGVELDQWGRIKAPgkqEFQYQTTNSKIFAGGDAVRGSDLVVTAIDEGRKAAEGILDY 467
Cdd:PRK12810 387 LPADLVLLAMGFTGPEAGLLAQFGVELDERGRVAAP---DNAYQTSNPKVFAAGDMRRGQSLVVWAIAEGRQAARAIDAY 463
|
...
gi 497534204 468 LEV 470
Cdd:PRK12810 464 LMG 466
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
24-467 |
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: 622.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497534204 24 RKIEFVEIYEPFTKQQAKAQADRCLDCGNPYCEWKCPVHNYIPQWLKLANEGRIIEAAELSHQTNSLPEVCGRVCPqdRL 103
Cdd:COG0493 1 RIKDFREVYPGLSEEEAIEQAARCLDCGDPPCQTGCPVGNDIPEWIRLIAEGDYEEALELIHETNPFPEVCGRVCP--AP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497534204 104 CEGSCTLNDDFGAVTIGNIEKYINDKAFEMGWKPDMSHVEWTDKKVAIIGAgpaglaaaDILVRNGVKAVVFDRYPEIGG 183
Cdd:COG0493 79 CEGACVRGIVDEPVAIGALERFIADKAFEEGWVKPPPPAPRTGKKVAVVGSgpaglaaaYQLARAGHEVTVFEALDKPGG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497534204 184 LLTFGIPSFKLEKGIMENRRRIFSGMGVEFKMNTEVGKDVQLQQLVDDYDAVFLGVGTYKNMRAGLDNEEAPGVYDALPF 263
Cdd:COG0493 159 LLRYGIPEFRLPKDVLDREIELIEALGVEFRTNVEVGKDITLDELLEEFDAVFLATGAGKPRDLGIPGEDLKGVHSAMDF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497534204 264 LVSNTykvmeLDNPTPFIDMKGKKVVVLGGGDTAMDCVRTSIRQHAANVVCAYRRDEANMPGSRREVKNAKEEGVKFMFN 343
Cdd:COG0493 239 LTAVN-----LGEAPDTILAVGKRVVVIGGGNTAMDCARTALRLGAESVTIVYRRTREEMPASKEEVEEALEEGVEFLFL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497534204 344 LQPLALETDSSGHVTGVKVVKTALGEPDEAGRRRPEPVEGSEHVLEADAVIMAFGFQPHAMEWLEPFGVELDQWGRIKAP 423
Cdd:COG0493 314 VAPVEIIGDENGRVTGLECVRMELGEPDESGRRRPVPIEGSEFTLPADLVILAIGQTPDPSGLEEELGLELDKRGTIVVD 393
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 497534204 424 gkqEFQYQTTNSKIFAGGDAVRGSDLVVTAIDEGRKAAEGILDY 467
Cdd:COG0493 394 ---EETYQTSLPGVFAGGDAVRGPSLVVWAIAEGRKAARAIDRY 434
|
|
| PRK12809 |
PRK12809 |
putative oxidoreductase Fe-S binding subunit; Reviewed |
9-465 |
0e+00 |
|
putative oxidoreductase Fe-S binding subunit; Reviewed
Pssm-ID: 183762 [Multi-domain] Cd Length: 639 Bit Score: 602.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497534204 9 IDVN-RVDPAKKPIKIRKIEFVEIYEPFTKQQAKAQADRCLDCGN-PYCEWKCPVHNYIPQWLKLANEGRIIEAAELSHQ 86
Cdd:PRK12809 171 LPVNsRKGADKISASERKTHFGEIYCGLDPQQATYESDRCVYCAEkANCNWHCPLHNAIPDYIRLVQEGKIIEAAELCHQ 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497534204 87 TNSLPEVCGRVCPQDRLCEGSCTLNDDFGAVTIGNIEKYINDKAFEMGWKPDMSHVEWTDKKVAIIGAGPAGLAAADILV 166
Cdd:PRK12809 251 TSSLPEICGRVCPQDRLCEGACTLKDHSGAVSIGNLERYITDTALAMGWRPDVSKVVPRSEKVAVIGAGPAGLGCADILA 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497534204 167 RNGVKAVVFDRYPEIGGLLTFGIPSFKLEKGIMENRRRIFSGMGVEFKMNTEVGKDVQLQQLVDDYDAVFLGVGTYKNMR 246
Cdd:PRK12809 331 RAGVQVDVFDRHPEIGGMLTFGIPPFKLDKTVLSQRREIFTAMGIDFHLNCEIGRDITFSDLTSEYDAVFIGVGTYGMMR 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497534204 247 AGLDNEEAPGVYDALPFLVSNTYKVMELDNPT--PFIDMKGKKVVVLGGGDTAMDCVRTSIRQHAANVVCAYRRDEANMP 324
Cdd:PRK12809 411 ADLPHEDAPGVIQALPFLTAHTRQLMGLPESEeyPLTDVEGKRVVVLGGGDTTMDCLRTSIRLNAASVTCAYRRDEVSMP 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497534204 325 GSRREVKNAKEEGVKFMFNLQPLALETDSSGHVTGVKVVKTALGEPDEAGRRRPEPVEGSEHVLEADAVIMAFGFQPHAM 404
Cdd:PRK12809 491 GSRKEVVNAREEGVEFQFNVQPQYIACDEDGRLTAVGLIRTAMGEPGPDGRRRPRPVAGSEFELPADVLIMAFGFQAHAM 570
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 497534204 405 EWLEPFGVELDQWGRIKAPGKQEFQYQTTNSKIFAGGDAVRGSDLVVTAIDEGRKAAEGIL 465
Cdd:PRK12809 571 PWLQGSGIKLDKWGLIQTGDVGYLPTQTHLKKVFAGGDAVHGADLVVTAMAAGRQAARDML 631
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
7-469 |
0e+00 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 528.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497534204 7 QFIDVNRVDPAKKPIKIRKIEFVEIYEPFTKQQAKAQADRCLDCGNPYCEWKCPVHNYIPQWLKLANEGRIIEAAELSHQ 86
Cdd:PRK11749 2 KFLTTPRIPMPRQDAEERAQNFDEVAPGYTPEEAIEEASRCLQCKDAPCVKACPVSIDIPEFIRLIAEGNLKGAAETILE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497534204 87 TNSLPEVCGRVCPQDRLCEGSCTLNDDFGAVTIGNIEKYINDKAFEMGWKPDMSHVEwTDKKVAIIGAGPAGLAAADILV 166
Cdd:PRK11749 82 TNPLPAVCGRVCPQERLCEGACVRGKKGEPVAIGRLERYITDWAMETGWVLFKRAPK-TGKKVAVIGAGPAGLTAAHRLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497534204 167 RNGVKAVVFDRYPEIGGLLTFGIPSFKLEKGIMENR-RRIFSgMGVEFKMNTEVGKDVQLQQLVDDYDAVFLGVGTYKNM 245
Cdd:PRK11749 161 RKGYDVTIFEARDKAGGLLRYGIPEFRLPKDIVDREvERLLK-LGVEIRTNTEVGRDITLDELRAGYDAVFIGTGAGLPR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497534204 246 RAGLDNEEAPGVYDALPFLVSNtyKVMELDNPTPfidmKGKKVVVLGGGDTAMDCVRTSIRQHAANVVCAYRRDEANMPG 325
Cdd:PRK11749 240 FLGIPGENLGGVYSAVDFLTRV--NQAVADYDLP----VGKRVVVIGGGNTAMDAARTAKRLGAESVTIVYRRGREEMPA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497534204 326 SRREVKNAKEEGVKFMFNLQPLALeTDSSGHVTGVKVVKTALGEPDEAGRRRpEPVEGSEHVLEADAVIMAFGFQPHAME 405
Cdd:PRK11749 314 SEEEVEHAKEEGVEFEWLAAPVEI-LGDEGRVTGVEFVRMELGEPDASGRRR-VPIEGSEFTLPADLVIKAIGQTPNPLI 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 497534204 406 WLEPFGVELDQWGRIKAPgkqEFQYQTTNSKIFAGGDAVRGSDLVVTAIDEGRKAAEGILDYLE 469
Cdd:PRK11749 392 LSTTPGLELNRWGTIIAD---DETGRTSLPGVFAGGDIVTGAATVVWAVGDGKDAAEAIHEYLE 452
|
|
| PRK12831 |
PRK12831 |
putative oxidoreductase; Provisional |
13-469 |
7.50e-121 |
|
putative oxidoreductase; Provisional
Pssm-ID: 183780 [Multi-domain] Cd Length: 464 Bit Score: 360.87 E-value: 7.50e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497534204 13 RVDPAKKPIKIRKIEFVEIYEPFTKQQAKAQADRCLDCGNPYCEWKCPVHNYIPQWLKLANEGRIIEAAELSHQTNSLPE 92
Cdd:PRK12831 8 RVPVREQDPEVRATNFEEVCLGYNEEEAVKEASRCLQCKKPKCVKGCPVSINIPGFISKLKEGDFEEAAKIIAKYNALPA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497534204 93 VCGRVCPQDRLCEGSCTLNDDFGAVTIGNIEKYINDKAFEMGWKPdMSHVEWTDKKVAIIGAGPAGLAAADILVRNGVKA 172
Cdd:PRK12831 88 VCGRVCPQESQCEGKCVLGIKGEPVAIGKLERFVADWARENGIDL-SETEEKKGKKVAVIGSGPAGLTCAGDLAKMGYDV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497534204 173 VVFDRYPEIGGLLTFGIPSFKLEK-GIMENRRRIFSGMGVEFKMNTEVGKDVQLQQLVDD--YDAVFLGVGTYKNMRAGL 249
Cdd:PRK12831 167 TIFEALHEPGGVLVYGIPEFRLPKeTVVKKEIENIKKLGVKIETNVVVGKTVTIDELLEEegFDAVFIGSGAGLPKFMGI 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497534204 250 DNEEAPGVYDALPFLV-SNTYKVMELDNPTPFIdmKGKKVVVLGGGDTAMDCVRTSIRQhAANVVCAYRRDEANMPGSRR 328
Cdd:PRK12831 247 PGENLNGVFSANEFLTrVNLMKAYKPEYDTPIK--VGKKVAVVGGGNVAMDAARTALRL-GAEVHIVYRRSEEELPARVE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497534204 329 EVKNAKEEGVKFMFNLQPLALETDSSGHVTGVKVVKTALGEPDEAGRRRPEPVEGSEHVLEADAVIMAFGFQPHAMEWLE 408
Cdd:PRK12831 324 EVHHAKEEGVIFDLLTNPVEILGDENGWVKGMKCIKMELGEPDASGRRRPVEIEGSEFVLEVDTVIMSLGTSPNPLISST 403
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 497534204 409 PFGVELDQWGRIKApgkQEFQYQTTNSKIFAGGDAVRGSDLVVTAIDEGRKAAEGILDYLE 469
Cdd:PRK12831 404 TKGLKINKRGCIVA---DEETGLTSKEGVFAGGDAVTGAATVILAMGAGKKAAKAIDEYLS 461
|
|
| PRK12778 |
PRK12778 |
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ... |
9-468 |
3.15e-108 |
|
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;
Pssm-ID: 237200 [Multi-domain] Cd Length: 752 Bit Score: 337.48 E-value: 3.15e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497534204 9 IDVNRVDPAKKPIKIRKI-EFVEIYEPFTKQQAKAQADRCLDCGNPYCEWKCPVHNYIPQWLKLANEGRIIEAAELSHQT 87
Cdd:PRK12778 292 TAIERVPMPELDPEYRAHnRFEEVNLGLTKEQAMTEAKRCLDCKNPGCVEGCPVGIDIPRFIKNIERGNFLEAAKILKET 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497534204 88 NSLPEVCGRVCPQDRLCEGSCTL---NDDfgAVTIGNIEKYINDKAFEMGwKPDMSHV-EWTDKKVAIIGAGPAGLAAAD 163
Cdd:PRK12778 372 SALPAVCGRVCPQEKQCESKCIHgkmGEE--AVAIGYLERFVADYERESG-NISVPEVaEKNGKKVAVIGSGPAGLSFAG 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497534204 164 ILVRNGVKAVVFDRYPEIGGLLTFGIPSFKLEKGIMENRRRIFSGMGVEFKMNTEVGKDVQLQQL-VDDYDAVFLGVGty 242
Cdd:PRK12778 449 DLAKRGYDVTVFEALHEIGGVLKYGIPEFRLPKKIVDVEIENLKKLGVKFETDVIVGKTITIEELeEEGFKGIFIASG-- 526
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497534204 243 knmrAGLDN------EEAPGVYDALPFLV-SNTYKVMELDNPTPFIdmKGKKVVVLGGGDTAMDCVRTSIRQHAANVVCA 315
Cdd:PRK12778 527 ----AGLPNfmnipgENSNGVMSSNEYLTrVNLMDAASPDSDTPIK--FGKKVAVVGGGNTAMDSARTAKRLGAERVTIV 600
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497534204 316 YRRDEANMPGSRREVKNAKEEGVKFMFNLQPLALETDSSGHVTGVKVVKTALGEPDEAGRRRPEPVEGSEHVLEADAVIM 395
Cdd:PRK12778 601 YRRSEEEMPARLEEVKHAKEEGIEFLTLHNPIEYLADEKGWVKQVVLQKMELGEPDASGRRRPVAIPGSTFTVDVDLVIV 680
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 497534204 396 AFGFQPHAMEWLEPFGVELDQWGRIKAPGKQefqyQTTNSKIFAGGDAVRGSDLVVTAIDEGRKAAEGILDYL 468
Cdd:PRK12778 681 SVGVSPNPLVPSSIPGLELNRKGTIVVDEEM----QSSIPGIYAGGDIVRGGATVILAMGDGKRAAAAIDEYL 749
|
|
| GOGAT_sm_gam |
TIGR01317 |
glutamate synthases, NADH/NADPH, small subunit; This model represents one of three built for ... |
8-468 |
4.13e-105 |
|
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: 321.39 E-value: 4.13e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497534204 8 FIDVNRVDPAKKPIKIRKIEFVEIYEPFTKQQAKAQADRCLDCGNPYC--EWKCPVHNYIPQWLKLANEGRIIEAAELSH 85
Cdd:TIGR01317 5 FLEYKRRKPTERDPRTRLKDWKEFTNPFDKESAKYQAARCMDCGTPFChnDSGCPLNNLIPEFNDLVFRGRWKEALDRLH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497534204 86 QTNSLPEVCGRVCPQDrlCEGSCTLNDDFGAVTIGNIEKYINDKAFEMGW-KPDMSHVEwTDKKVAIIGAGPAGLAAADI 164
Cdd:TIGR01317 85 ATNNFPEFTGRVCPAP--CEGACTLGISEDPVGIKSIERIIIDKGFQEGWvQPRPPSKR-TGKKVAVVGSGPAGLAAADQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497534204 165 LVRNGVKAVVFDRYPEIGGLLTFGIPSFKLEKGIMENRRRIFSGMGVEFKMNTEVGKDVQLQQLVDDYDAVFLGVGTYKN 244
Cdd:TIGR01317 162 LNRAGHTVTVFEREDRCGGLLMYGIPNMKLDKAIVDRRIDLLSAEGIDFVTNTEIGVDISADELKEQFDAVVLAGGATKP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497534204 245 MRAGLDNEEAPGVYDALPFLVSNTyKVMELDNPT--PFIDMKGKKVVVLGGGDTAMDCVRTSIRQHAANVV-------CA 315
Cdd:TIGR01317 242 RDLPIPGRELKGIHYAMEFLPSAT-KALLGKDFKdiIFIKAKGKKVVVIGGGDTGADCVGTSLRHGAASVHqfeimpkPP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497534204 316 YRRDEANM----PGSRReVKNAKEEGVKFM------FNLQPLALETDSSGHVTGVKVVKTALgEPDEAGRRRPEPVEGSE 385
Cdd:TIGR01317 321 EARAKDNPwpewPRVYR-VDYAHEEAAAHYgrdpreYSILTKEFIGDDEGKVTALRTVRVEW-KKSQDGKWQFVEIPGSE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497534204 386 HVLEADAVIMAFGFQPHAMEWLEPFGVELDQWGRIKAPGKqefQYQTTNSKIFAGGDAVRGSDLVVTAIDEGRKAAEGIL 465
Cdd:TIGR01317 399 EVFEADLVLLAMGFVGPEQILLDDFGVKKTRRGNISAGYD---DYSTSIPGVFAAGDCRRGQSLIVWAINEGRKAAAAVD 475
|
...
gi 497534204 466 DYL 468
Cdd:TIGR01317 476 RYL 478
|
|
| gltA |
TIGR01316 |
glutamate synthase (NADPH), homotetrameric; This protein is homologous to the small subunit of ... |
20-468 |
2.70e-104 |
|
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: 317.97 E-value: 2.70e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497534204 20 PIKIRKIEFVEIYEPFTKQQAKAQADRCLDCGNPY--CEWKCPVHNYIPQWLKLANEGRIIEAAELSHQTNSLPEVCGRV 97
Cdd:TIGR01316 1 PPEERSKLFQEAALGYTEQLALVEAQRCLNCKDATkpCIKGCPVHVPIPEFIAKIQEGDFKGAVDIIKTTSLLPAICGRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497534204 98 CPQDRLCEGSCTLNDDFG----AVTIGNIEKYINDKAFEMGWKPDMSHVEWTDKKVAIIGAGPAGLAAADILVRNGVKAV 173
Cdd:TIGR01316 81 CPQERQCEGQCTVGKMFKdvgkPVSIGALERFVADWERQHGIETEPEKAPSTHKKVAVIGAGPAGLACASELAKAGHSVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497534204 174 VFDRYPEIGGLLTFGIPSFKLEKGIMENRRRIFSGMGVEFKMNTEVGKDVQLQQLVDDYDAVFLGVGTYKNMRAGLDNEE 253
Cdd:TIGR01316 161 VFEALHKPGGVVTYGIPEFRLPKEIVVTEIKTLKKLGVTFRMNFLVGKTATLEELFSQYDAVFIGTGAGLPKLMNIPGEE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497534204 254 APGVYDALPFLV-SNTYKVMEL---DNPTPFidmkGKKVVVLGGGDTAMDCVRTSIRQhAANVVCAYRRDEANMPGSRRE 329
Cdd:TIGR01316 241 LCGVYSANDFLTrANLMKAYEFphaDTPVYA----GKSVVVIGGGNTAVDSARTALRL-GAEVHCLYRRTREDMTARVEE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497534204 330 VKNAKEEGVKFMFNLQPLALETDSSGHVTGVKVVKTALGEPDEAGRRRPEPVEGSEHVLEADAVIMAFGFQPHAMEWlEP 409
Cdd:TIGR01316 316 IAHAEEEGVKFHFLCQPVEIIGDEEGNVRAVKFRKMDCQEQIDSGERRFLPCGDAECKLEADAVIVAIGNGSNPIMA-ET 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 497534204 410 FGVELDQWGRIKAPGKQEfqyqTTNSKIFAGGDAVRGSDLVVTAIDEGRKAAEGILDYL 468
Cdd:TIGR01316 395 TRLKTSERGTIVVDEDQR----TSIPGVFAGGDIILGAATVIRAMGQGKRAAKSINEYL 449
|
|
| PRK12771 |
PRK12771 |
putative glutamate synthase (NADPH) small subunit; Provisional |
53-468 |
2.43e-96 |
|
putative glutamate synthase (NADPH) small subunit; Provisional
Pssm-ID: 237198 [Multi-domain] Cd Length: 564 Bit Score: 301.02 E-value: 2.43e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497534204 53 PYCEWKCPVHNYIPQWLKLANEGRIIEAAELSHQTNSLPEVCGRVCPQDrlCEGSC--TLNDDfgAVTIGNIEKYINDKA 130
Cdd:PRK12771 47 PPCNAACPAGEDIRGWLALVRGGDYEYAWRRLTKDNPFPAVMGRVCYHP--CESGCnrGQVDD--AVGINAVERFLGDYA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497534204 131 FEMGWKPDMSHVEwTDKKVAIIGAGPAGLAAADILVRNGVKAVVFDRYPEIGGLLTFGIPSFKLEKGIMENR-RRIFSgM 209
Cdd:PRK12771 123 IANGWKFPAPAPD-TGKRVAVIGGGPAGLSAAYHLRRMGHAVTIFEAGPKLGGMMRYGIPAYRLPREVLDAEiQRILD-L 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497534204 210 GVEFKMNTEVGKDVQLQQLVDDYDAVFLGVGTYKNMRAGLDNEEAPGVYDALPFLvsntyKVMELDNPtpfiDMKGKKVV 289
Cdd:PRK12771 201 GVEVRLGVRVGEDITLEQLEGEFDAVFVAIGAQLGKRLPIPGEDAAGVLDAVDFL-----RAVGEGEP----PFLGKRVV 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497534204 290 VLGGGDTAMDCVRTSIRQHAANVVCAYRRDEANMPGSRREVKNAKEEGVKFMFNLQPLALETDSSGhVTGVKVVKTALGE 369
Cdd:PRK12771 272 VIGGGNTAMDAARTARRLGAEEVTIVYRRTREDMPAHDEEIEEALREGVEINWLRTPVEIEGDENG-ATGLRVITVEKME 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497534204 370 PDEAGrrRPEPVEGSEHVLEADAVIMAFGfQPHAMEWLEPFGVELDQWGRIKApgkQEFQYQTTNSKIFAGGDAVRGSDL 449
Cdd:PRK12771 351 LDEDG--RPSPVTGEEETLEADLVVLAIG-QDIDSAGLESVPGVEVGRGVVQV---DPNFMMTGRPGVFAGGDMVPGPRT 424
|
410
....*....|....*....
gi 497534204 450 VVTAIDEGRKAAEGILDYL 468
Cdd:PRK12771 425 VTTAIGHGKKAARNIDAFL 443
|
|
| PRK12775 |
PRK12775 |
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin ... |
24-468 |
1.43e-90 |
|
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin domain-containing protein; Provisional
Pssm-ID: 183738 [Multi-domain] Cd Length: 1006 Bit Score: 296.47 E-value: 1.43e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497534204 24 RKIEFVEIYEPFTKQQAKAQADRCLDCGNPYCEWKCPVHNYIPQWLKLANEGRIIEAAELSHQTNSLPEVCGRVCPQDRL 103
Cdd:PRK12775 310 RARNFKEVNLGYSLEDALQEAERCIQCAKPTCIAGCPVQIDIPVFIRHVVVRDFDGALEVIYEASIFPSICGRVCPQETQ 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497534204 104 CEGSCTLNDDFGAVTIGNIEKYINDKAFEMGWKP-DMSHvewTDKKVAIIGAGPAGLAAADILVRNGVKAVVFDRYPEIG 182
Cdd:PRK12775 390 CEAQCIIAKKHESVGIGRLERFVGDNARAKPVKPpRFSK---KLGKVAICGSGPAGLAAAADLVKYGVDVTVYEALHVVG 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497534204 183 GLLTFGIPSFKLEKGIMENRRRIFSGMGVEFKMNTEVGKDVQLQQLVDD--YDAVFLGVGTYKNMRAGLDNEEAPGVYDA 260
Cdd:PRK12775 467 GVLQYGIPSFRLPRDIIDREVQRLVDIGVKIETNKVIGKTFTVPQLMNDkgFDAVFLGVGAGAPTFLGIPGEFAGQVYSA 546
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497534204 261 LPFLvsnTYKVMELDNPTPFIDMK---GKKVVVLGGGDTAMDCVRTSIRQHAANVVCAYRRDEANMPGSRREVKNAKEEG 337
Cdd:PRK12775 547 NEFL---TRVNLMGGDKFPFLDTPislGKSVVVIGAGNTAMDCLRVAKRLGAPTVRCVYRRSEAEAPARIEEIRHAKEEG 623
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497534204 338 VKFMFNLQPLALETDSSGHVTGVKVVKTALGEPDEAGRRRPEPVeGSEHVLEADAVIMAFGFQPHAMEWLEPFGVELDQW 417
Cdd:PRK12775 624 IDFFFLHSPVEIYVDAEGSVRGMKVEEMELGEPDEKGRRKPMPT-GEFKDLECDTVIYALGTKANPIITQSTPGLALNKW 702
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 497534204 418 GRIKAPGKQEFQYQTTN-SKIFAGGDAVRGSDLVVTAIDEGRKAAEGILDYL 468
Cdd:PRK12775 703 GNIAADDGKLESTQSTNlPGVFAGGDIVTGGATVILAMGAGRRAARSIATYL 754
|
|
| PRK12814 |
PRK12814 |
putative NADPH-dependent glutamate synthase small subunit; Provisional |
44-468 |
3.21e-81 |
|
putative NADPH-dependent glutamate synthase small subunit; Provisional
Pssm-ID: 139246 [Multi-domain] Cd Length: 652 Bit Score: 264.28 E-value: 3.21e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497534204 44 ADRCLDCGNPyCEWKCPVHNYIPQWLKLANEGRIIEAAELSHQTNSLPEVCGRVCPQDrlCEGSCTLN--DDfgAVTIGN 121
Cdd:PRK12814 94 EQHCGDCLGP-CELACPAGCNIPGFIAAIARGDDREAIRIIKETIPLPGILGRICPAP--CEEACRRHgvDE--PVSICA 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497534204 122 IEKYINDKAFEMG--WKPDMShvEWTDKKVAIIGAGPAGLAAADILVRNGVKAVVFDRYPEIGGLLTFGIPSFKLEKGIM 199
Cdd:PRK12814 169 LKRYAADRDMESAerYIPERA--PKSGKKVAIIGAGPAGLTAAYYLLRKGHDVTIFDANEQAGGMMRYGIPRFRLPESVI 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497534204 200 ENRRRIFSGMGVEFKMNTEVGKDVQLQQLVDDYDAVFLGVGTYKNMRAGLDNEEAPGVYDALPFLvsntYKVMELDNPTP 279
Cdd:PRK12814 247 DADIAPLRAMGAEFRFNTVFGRDITLEELQKEFDAVLLAVGAQKASKMGIPGEELPGVISGIDFL----RNVALGTALHP 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497534204 280 fidmkGKKVVVLGGGDTAMDCVRTSIRQHAANVVCAYRRDEANMPGSRREVKNAKEEGVKFMFNLQPLALETDSSGHVtg 359
Cdd:PRK12814 323 -----GKKVVVIGGGNTAIDAARTALRLGAESVTILYRRTREEMPANRAEIEEALAEGVSLRELAAPVSIERSEGGLE-- 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497534204 360 VKVVKTALGEPDEAGRRRPEPVEGSEHVLEADAVIMAFGfQPHAMEWLEPFGVELDQWGRIKAPGKqefQYQTTNSKIFA 439
Cdd:PRK12814 396 LTAIKMQQGEPDESGRRRPVPVEGSEFTLQADTVISAIG-QQVDPPIAEAAGIGTSRNGTVKVDPE---TLQTSVAGVFA 471
|
410 420
....*....|....*....|....*....
gi 497534204 440 GGDAVRGSDLVVTAIDEGRKAAEGILDYL 468
Cdd:PRK12814 472 GGDCVTGADIAINAVEQGKRAAHAIDLFL 500
|
|
| PRK12770 |
PRK12770 |
putative glutamate synthase subunit beta; Provisional |
145-469 |
1.35e-70 |
|
putative glutamate synthase subunit beta; Provisional
Pssm-ID: 237197 [Multi-domain] Cd Length: 352 Bit Score: 227.95 E-value: 1.35e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497534204 145 TDKKVAIIGAGPAGLAAADILVRNGVKAVVFDRYPEIGGLLTFGIPSFKLEK-GIMENRRRIfSGMGVEFKMNTEV---- 219
Cdd:PRK12770 17 TGKKVAIIGAGPAGLAAAGYLACLGYEVHVYDKLPEPGGLMLFGIPEFRIPIeRVREGVKEL-EEAGVVFHTRTKVccge 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497534204 220 -----------GKDVQLQQLVDDYDAVFLGVGTYKNMRAGLDNEEAPGVYDALPFLVS-NTYKVMELDNPTPFiDMKGKK 287
Cdd:PRK12770 96 plheeegdefvERIVSLEELVKKYDAVLIATGTWKSRKLGIPGEDLPGVYSALEYLFRiRAAKLGYLPWEKVP-PVEGKK 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497534204 288 VVVLGGGDTAMDCVRTSIRQHAANVVCAYRRDEANMPGSRREVKNAKEEGVKFMFNLQPLALETDssGHVTGVKVVKTAL 367
Cdd:PRK12770 175 VVVVGAGLTAVDAALEAVLLGAEKVYLAYRRTINEAPAGKYEIERLIARGVEFLELVTPVRIIGE--GRVEGVELAKMRL 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497534204 368 GEPDEAGRRRPEPVEGSEHVLEADAVIMAFGFQPHAMEWLEPFGVELDQWGRIKAPGKqefqYQTTNSKIFAGGDAVRGS 447
Cdd:PRK12770 253 GEPDESGRPRPVPIPGSEFVLEADTVVFAIGEIPTPPFAKECLGIELNRKGEIVVDEK----HMTSREGVFAAGDVVTGP 328
|
330 340
....*....|....*....|..
gi 497534204 448 DLVVTAIDEGRKAAEGILDYLE 469
Cdd:PRK12770 329 SKIGKAIKSGLRAAQSIHEWLD 350
|
|
| PRK13984 |
PRK13984 |
putative oxidoreductase; Provisional |
7-468 |
1.80e-68 |
|
putative oxidoreductase; Provisional
Pssm-ID: 172486 [Multi-domain] Cd Length: 604 Bit Score: 229.27 E-value: 1.80e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497534204 7 QFIDVNRVDPAKKPIKIRKIEFVEIYEPFTKQQAKAQADRCLDCGnpYCEWKCPVHNYIPQWLKLANEGRIIEAAELSHQ 86
Cdd:PRK13984 147 ELLDLERVEMEEIPPEERVKSFIEIVKGYSKEQAMQEAARCVECG--ICTDTCPAHMDIPQYIKAIYKDDLEEGLRWLYK 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497534204 87 TNSLPEVCGRVCPQDrlCEGSCTLNDDFGAVTIGNIEKYINDKAFEMGWKPDMS-HVEWTDKKVAIIGAGPAGLAAADIL 165
Cdd:PRK13984 225 TNPLSMVCGRVCTHK--CETVCSIGHRGEPIAIRWLKRYIVDNVPVEKYSEILDdEPEKKNKKVAIVGSGPAGLSAAYFL 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497534204 166 VRNGVKAVVFDRYPEIGGLLTFGIPSFKLEKGIMENRRRIFSGMGVEFKMNTEVGKDVQLQQLVDDYDAVFLGVGTYKNM 245
Cdd:PRK13984 303 ATMGYEVTVYESLSKPGGVMRYGIPSYRLPDEALDKDIAFIEALGVKIHLNTRVGKDIPLEELREKHDAVFLSTGFTLGR 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497534204 246 RAGLDNEEAPGVYDALPFLVSNTyKVMELDNPTPFIDmkgKKVVVLGGGDTAMDCVRTSIRQH-----AANV-VCAYRRD 319
Cdd:PRK13984 383 STRIPGTDHPDVIQALPLLREIR-DYLRGEGPKPKIP---RSLVVIGGGNVAMDIARSMARLQkmeygEVNVkVTSLERT 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497534204 320 EANMPGSRREVKNAKEEGVKFMFNLQPLALETDsSGHVTGVKVVKtALGEPDEAGRRRPEPVEGSEHVLEADAVIMAFGF 399
Cdd:PRK13984 459 FEEMPADMEEIEEGLEEGVVIYPGWGPMEVVIE-NDKVKGVKFKK-CVEVFDEEGRFNPKFDESDQIIVEADMVVEAIGQ 536
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 497534204 400 QPHAMEWLEPFGVELdQW--GRIKAPGKQefqyQTTNSKIFAGGDAVRGSDlVVTAIDEGRKAAEGILDYL 468
Cdd:PRK13984 537 APDYSYLPEELKSKL-EFvrGRILTNEYG----QTSIPWLFAGGDIVHGPD-IIHGVADGYWAAEGIDMYL 601
|
|
| Fer4_20 |
pfam14691 |
Dihydroprymidine dehydrogenase domain II, 4Fe-4S cluster; Domain II of the enzyme ... |
24-135 |
3.66e-62 |
|
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: 197.76 E-value: 3.66e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497534204 24 RKIEFVEIYEPFTKQQAKAQADRCLDCGNPYCEWKCPVHNYIPQWLKLANEGRIIEAAELSHQTNSLPEVCGRVCPQDRL 103
Cdd:pfam14691 1 RIKNFEEVALGYTEEEAIAEASRCLQCKDPPCVKGCPVHIDIPEFIKLIAEGNFEGAARIILETNPLPAICGRVCPQERQ 80
|
90 100 110
....*....|....*....|....*....|...
gi 497534204 104 CEGSCTLN-DDFGAVTIGNIEKYINDKAFEMGW 135
Cdd:pfam14691 81 CEGACVLGkKGFEPVAIGRLERFAADWARENGI 113
|
|
| PRK12779 |
PRK12779 |
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; ... |
59-466 |
2.46e-57 |
|
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; Provisional
Pssm-ID: 183740 [Multi-domain] Cd Length: 944 Bit Score: 203.91 E-value: 2.46e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497534204 59 CPVHNYIPQWLKLANEGRIIEAAELSHQTNSLPEVCGRVCPQDRLCEGSCTLNDDfgAVTIGNIEKYINDKAFEMGwkPD 138
Cdd:PRK12779 214 CPVKIHIPEMLDLLGNGKHREALELIESCNPLPNVTGRVCPQELQCQGVCTHTKR--PIEIGQLEWYLPQHEKLVN--PN 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497534204 139 MSH---------VEWTDKKVAIIGAGPAGLAAADILVRNGVKAVVFDRYPEIGGLLTFGIPSFKLEKGIMENRRRIFSGM 209
Cdd:PRK12779 290 ANErfagrispwAAAVKPPIAVVGSGPSGLINAYLLAVEGFPVTVFEAFHDLGGVLRYGIPEFRLPNQLIDDVVEKIKLL 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497534204 210 GVEFKMNTEVGKDVQLQQL-VDDYDAVFLGVGtyknmrAGLDN------EEAPGVYDALPFLVS-NTYKVMELDNPTPFI 281
Cdd:PRK12779 370 GGRFVKNFVVGKTATLEDLkAAGFWKIFVGTG------AGLPTfmnvpgEHLLGVMSANEFLTRvNLMRGLDDDYETPLP 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497534204 282 DMKGKKVVVLGGGDTAMDCVRTSiRQHAANVVCAYRRDEANMPGSRREVKNAKEEGVKFMFNLQPLALETDSSGH-VTGV 360
Cdd:PRK12779 444 EVKGKEVFVIGGGNTAMDAARTA-KRLGGNVTIVYRRTKSEMPARVEELHHALEEGINLAVLRAPREFIGDDHTHfVTHA 522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497534204 361 KVVKTALGEPDEAGRRRPEPVEGSEHVlEADAVIMAFGFQPHA-MEWLEPfGVELDQWGRIK-APGKQefqyQTTNSKIF 438
Cdd:PRK12779 523 LLDVNELGEPDKSGRRSPKPTGEIERV-PVDLVIMALGNTANPiMKDAEP-GLKTNKWGTIEvEKGSQ----RTSIKGVY 596
|
410 420
....*....|....*....|....*...
gi 497534204 439 AGGDAVRGSDLVVTAIDEGRKAAEGILD 466
Cdd:PRK12779 597 SGGDAARGGSTAIRAAGDGQAAAKEIVG 624
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
167-469 |
3.30e-23 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 99.42 E-value: 3.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497534204 167 RNGVKAVVFDRyPEIGGLLT--------FGIPsfkleKGI-----MENRRRIFSGMGVEFKMnTEVgKDVQLQqlvDDY- 232
Cdd:COG0492 21 RAGLKTLVIEG-GEPGGQLAttkeienyPGFP-----EGIsgpelAERLREQAERFGAEILL-EEV-TSVDKD---DGPf 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497534204 233 ------------DAVFLGVGTYKNmRAGLDNEEAP---GVY-----DALPFlvsntykvmeldnptpfidmKGKKVVVLG 292
Cdd:COG0492 90 rvttddgteyeaKAVIIATGAGPR-KLGLPGEEEFegrGVSycatcDGFFF--------------------RGKDVVVVG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497534204 293 GGDTAMDCVRTsIRQHAANVVCAYRRDEANmpGSRREVKNAKE-EGVKFMFNLQPLALETDssGHVTGVKVVKTALGEpd 371
Cdd:COG0492 149 GGDSALEEALY-LTKFASKVTLIHRRDELR--ASKILVERLRAnPKIEVLWNTEVTEIEGD--GRVEGVTLKNVKTGE-- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497534204 372 eagrrrpepvegsEHVLEADAVIMAFGFQPHAmEWLEPFGVELDQWGRIKAPGKQEfqyqtTN-SKIFAGGDAVRGS-DL 449
Cdd:COG0492 222 -------------EKELEVDGVFVAIGLKPNT-ELLKGLGLELDEDGYIVVDEDME-----TSvPGVFAAGDVRDYKyRQ 282
|
330 340
....*....|....*....|
gi 497534204 450 VVTAIDEGRKAAEGILDYLE 469
Cdd:COG0492 283 AATAAGEGAIAALSAARYLE 302
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
147-457 |
5.96e-15 |
|
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: 75.43 E-value: 5.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497534204 147 KKVAIIGAGPAGLAAADILVRNGVKAVVFDR---YPEIGGLLTFGI-------PSFKLEKGIMENRRRIFSGMGVEFKMN 216
Cdd:pfam07992 1 YDVVVIGGGPAGLAAALTLAQLGGKVTLIEDegtCPYGGCVLSKALlgaaeapEIASLWADLYKRKEEVVKKLNNGIEVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497534204 217 TEVG--------KDVQLQQLVDD------YDAVFLGVGTyKNMRAGLdneeaPGVYDALPFLVSnTYKVMELdnptPFID 282
Cdd:pfam07992 81 LGTEvvsidpgaKKVVLEELVDGdgetitYDRLVIATGA-RPRLPPI-----PGVELNVGFLVR-TLDSAEA----LRLK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497534204 283 MKGKKVVVLGGGDTAMDCVrTSIRQHAANVVCAYRRDEANMP----GSRREVKNAKEEGVKFMFNlqplaletdssghvt 358
Cdd:pfam07992 150 LLPKRVVVVGGGYIGVELA-AALAKLGKEVTLIEALDRLLRAfdeeISAALEKALEKNGVEVRLG--------------- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497534204 359 gvKVVKTALGEPDEAgrrrpEPVEGSEHVLEADAVIMAFGFQPhAMEWLEPFGVELDQWGRIKApgkqEFQYQTTNSKIF 438
Cdd:pfam07992 214 --TSVKEIIGDGDGV-----EVILKDGTEIDADLVVVAIGRRP-NTELLEAAGLELDERGGIVV----DEYLRTSVPGIY 281
|
330 340
....*....|....*....|
gi 497534204 439 AGGD-AVRGSDLVVTAIDEG 457
Cdd:pfam07992 282 AAGDcRVGGPELAQNAVAQG 301
|
|
| PLN02852 |
PLN02852 |
ferredoxin-NADP+ reductase |
169-399 |
5.03e-11 |
|
ferredoxin-NADP+ reductase
Pssm-ID: 215457 Cd Length: 491 Bit Score: 64.72 E-value: 5.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497534204 169 GVKAVVFDRYPEIGGLLTFGIPSFKLEKGIMENR-RRIFSGMGVEFKMNTEVGKDVQLQQLVDDYDAVFLGVGTYKNMRA 247
Cdd:PLN02852 51 GARVDIIERLPTPFGLVRSGVAPDHPETKNVTNQfSRVATDDRVSFFGNVTLGRDVSLSELRDLYHVVVLAYGAESDRRL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497534204 248 GLDNEEAPGVYDALPFLV-SNTYKVMELDNPTPFidmKGKKVVVLGGGDTAMDCVR-----------TSIRQHA------ 309
Cdd:PLN02852 131 GIPGEDLPGVLSAREFVWwYNGHPDCVHLPPDLK---SSDTAVVLGQGNVALDCARillrptdelasTDIAEHAlealrg 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497534204 310 ---ANVVCAYRR-----------------------------------DEANMPGSRREvKNAKEEGVK------------ 339
Cdd:PLN02852 208 ssvRKVYLVGRRgpvqaactakelrellglknvrvrikeadltlspeDEEELKASRPK-RRVYELLSKaaaagkcapsgg 286
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 497534204 340 -----FMFNLQPLALE--TDSSGHVTGVKVVKTALgEPDEAGRRRPEPVEGSEHVLEADAVIMAFGF 399
Cdd:PLN02852 287 qrelhFVFFRNPTRFLdsGDGNGHVAGVKLERTVL-EGAAGSGKQVAVGTGEFEDLPCGLVLKSIGY 352
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
331-465 |
1.54e-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: 56.63 E-value: 1.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497534204 331 KNAKEEGVKFMFNLQPLALETDSSGhvtgvKVVKTAlgepdeagrrrpepVEGSEHVLEADAVIMAFGFQPHAMEW-LEP 409
Cdd:COG1249 217 KALEKEGIDILTGAKVTSVEKTGDG-----VTVTLE--------------DGGGEEAVEADKVLVATGRRPNTDGLgLEA 277
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 497534204 410 FGVELDQWGRIKApgkqEFQYQTTNSKIFAGGDAVRGSDLVVTAIDEGRKAAEGIL 465
Cdd:COG1249 278 AGVELDERGGIKV----DEYLRTSVPGIYAIGDVTGGPQLAHVASAEGRVAAENIL 329
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
358-467 |
2.68e-08 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 55.95 E-value: 2.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497534204 358 TGVKVVKTalgEPDEAGRRRPEPVEGSEHVLEADAVIMAFGFQPHAMEW-LEPFGVELDQWGRIKAPGKqefqYQTTNSK 436
Cdd:PRK06292 228 LGAKVTSV---EKSGDEKVEELEKGGKTETIEADYVLVATGRRPNTDGLgLENTGIELDERGRPVVDEH----TQTSVPG 300
|
90 100 110
....*....|....*....|....*....|.
gi 497534204 437 IFAGGDAVRGSDLVVTAIDEGRKAAEGILDY 467
Cdd:PRK06292 301 IYAAGDVNGKPPLLHEAADEGRIAAENAAGD 331
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
206-465 |
4.13e-06 |
|
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: 48.65 E-value: 4.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497534204 206 FSGMGVEFKMNTEV------GKDVQLQQ-LVDDYDAVFLGVGTyKNMRAGLDNEEAPGVY------DALpflvsNTYKVM 272
Cdd:COG0446 46 FERKGIDVRTGTEVtaidpeAKTVTLRDgETLSYDKLVLATGA-RPRPPPIPGLDLPGVFtlrtldDAD-----ALREAL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497534204 273 EldnptpfiDMKGKKVVVLGGG------DTAMdcvrtsiRQHAANVVCAYRRDEAnMPGSRREV-----KNAKEEGVKFM 341
Cdd:COG0446 120 K--------EFKGKRAVVIGGGpiglelAEAL-------RKRGLKVTLVERAPRL-LGVLDPEMaalleEELREHGVELR 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497534204 342 FNLQPLALETDssghvTGVKVVKTalgepdeagrrrpepvegSEHVLEADAVIMAFGFQPHAmEWLEPFGVELDQWGRIK 421
Cdd:COG0446 184 LGETVVAIDGD-----DKVAVTLT------------------DGEEIPADLVVVAPGVRPNT-ELAKDAGLALGERGWIK 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 497534204 422 APGKQefqyQTTNSKIFAGGDAVRGSDLVV----------TAIDEGRKAAEGIL 465
Cdd:COG0446 240 VDETL----QTSDPDVYAAGDCAEVPHPVTgktvyiplasAANKQGRVAAENIL 289
|
|
| PRK05249 |
PRK05249 |
Si-specific NAD(P)(+) transhydrogenase; |
337-466 |
2.75e-05 |
|
Si-specific NAD(P)(+) transhydrogenase;
Pssm-ID: 235373 [Multi-domain] Cd Length: 461 Bit Score: 46.30 E-value: 2.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497534204 337 GVKFMFNLQPLALETDSSGhvtgvkvVKTALgepdEAGRRrpepvegsehvLEADAVIMAFGFQPHAMEW-LEPFGVELD 415
Cdd:PRK05249 230 GVTIRHNEEVEKVEGGDDG-------VIVHL----KSGKK-----------IKADCLLYANGRTGNTDGLnLENAGLEAD 287
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 497534204 416 QWGRIKAPGkqefQYQTTNSKIFAGGDAVRGSDLVVTAIDEGRKAAEGILD 466
Cdd:PRK05249 288 SRGQLKVNE----NYQTAVPHIYAVGDVIGFPSLASASMDQGRIAAQHAVG 334
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
287-355 |
1.84e-04 |
|
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: 39.88 E-value: 1.84e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 497534204 287 KVVVLGGGDTAMDCVrTSIRQHAANVVCAYRRDEAnMPGSRREV-----KNAKEEGVKFMFNLQPLALETDSSG 355
Cdd:pfam00070 1 RVVVVGGGYIGLELA-GALARLGSKVTVVERRDRL-LPGFDPEIakilqEKLEKNGIEFLLNTTVEAIEGNGDG 72
|
|
| TRX_reduct |
TIGR01292 |
thioredoxin-disulfide reductase; This model describes thioredoxin-disulfide reductase, a ... |
148-468 |
2.91e-04 |
|
thioredoxin-disulfide reductase; This model describes thioredoxin-disulfide reductase, a member of the pyridine nucleotide-disulphide oxidoreductases (pfam00070). [Energy metabolism, Electron transport]
Pssm-ID: 273540 [Multi-domain] Cd Length: 299 Bit Score: 42.61 E-value: 2.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497534204 148 KVAIIGAGPAGLAAADILVRNGVKAVVFDRYPEIGGLLTFGI----PSFKleKGI-----MENRRRIFSGMGVEFKMNT- 217
Cdd:TIGR01292 1 DVIIIGAGPAGLTAAIYAARANLKPLLIEGMEPGGQLTTTTEvenyPGFP--EGIsgpelMEKMKEQAVKFGAEIIYEEv 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497534204 218 ---EVGKDVQLQQLVDDY----DAVFLGVGTyKNMRAGLDNEE--------APGVYDAlPFLvsntykvmeldnptpfid 282
Cdd:TIGR01292 79 ikvDKSDRPFKVYTGDGKeytaKAVIIATGA-SARKLGIPGEDefwgrgvsYCATCDG-PFF------------------ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497534204 283 mKGKKVVVLGGGDTAMDCVrTSIRQHAANVVCAYRRDEANMPGSRREvKNAKEEGVKFMFNLQPLALETDSSghVTGVKV 362
Cdd:TIGR01292 139 -KNKEVAVVGGGDSAIEEA-LYLTRIAKKVTLVHRRDKFRAEKILLD-RLKKNPKIEFLWNSTVEEIVGDNK--VEGVKI 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497534204 363 VKTalgepdeagrrrpepVEGSEHVLEADAVIMAFGFQPHAmewlEPFG--VELDQWGRIKApgkqEFQYQTTNSKIFAG 440
Cdd:TIGR01292 214 KNT---------------VTGEEEELEVDGVFIAIGHEPNT----ELLKglLELDENGYIVT----DEGMRTSVPGVFAA 270
|
330 340 350
....*....|....*....|....*....|
gi 497534204 441 GDaVRGSDL--VVTAIDEGRKAAEGILDYL 468
Cdd:TIGR01292 271 GD-VRDKGYrqAVTAAGDGCIAALSAERYL 299
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
229-466 |
3.04e-04 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 43.27 E-value: 3.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497534204 229 VDD----YDAVFLGVGTyknmRAGLdnEEAPGVyDALPFLVSNTykVMELDN-PtpfidmkgKKVVVLGGGDTAMDcvrt 303
Cdd:PRK06370 127 VGGetlrAKRIFINTGA----RAAI--PPIPGL-DEVGYLTNET--IFSLDElP--------EHLVIIGGGYIGLE---- 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497534204 304 sIRQhaanvvcAYRR----------DEANMPGSRREVKNA-----KEEGVKFMFNLQPLALETDSSGHVTGVKVvktalg 368
Cdd:PRK06370 186 -FAQ-------MFRRfgsevtvierGPRLLPREDEDVAAAvreilEREGIDVRLNAECIRVERDGDGIAVGLDC------ 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497534204 369 epdeagrrrpepvEGSEHVLEADAVIMAFGFQPHAMEW-LEPFGVELDQWGRIKAPGkqefQYQTTNSKIFAGGDAVRGS 447
Cdd:PRK06370 252 -------------NGGAPEITGSHILVAVGRVPNTDDLgLEAAGVETDARGYIKVDD----QLRTTNPGIYAAGDCNGRG 314
|
250
....*....|....*....
gi 497534204 448 DLVVTAIDEGRKAAEGILD 466
Cdd:PRK06370 315 AFTHTAYNDARIVAANLLD 333
|
|
| ACS_1 |
cd01916 |
Acetyl-CoA synthase (ACS), also known as acetyl-CoA decarbonylase, is found in acetogenic and ... |
21-100 |
6.85e-04 |
|
Acetyl-CoA synthase (ACS), also known as acetyl-CoA decarbonylase, is found in acetogenic and methanogenic organisms and is responsible for the synthesis and breakdown of acetyl-CoA. ACS forms a heterotetramer with carbon monoxide dehydrogenase (CODH) consisting of two ACS and two CODH subunits. CODH reduces carbon dioxide to carbon monoxide and ACS then synthesizes acetyl-CoA from carbon monoxide, CoA, and a methyl group donated by another protein (CoFeSP). ACS has three structural domains, an N-terminal rossman fold domain with a helical region at its N-terminus which interacts with CODH, and two alpha + beta fold domains. A Ni-Fe-S center referred to as the A-cluster is located in the C-terminal domain. A large cavity exists between the three domains which may bind CoA.
Pssm-ID: 238897 [Multi-domain] Cd Length: 731 Bit Score: 42.01 E-value: 6.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497534204 21 IKIRKIEFVEIYEPfTKQQAKAQADRCLDCGNpyCEWKCPVHNYIPQWLKLANEGRIIEAAELSHQTNSlpevCGR---V 97
Cdd:cd01916 342 MAVKPKRKGEKKLP-TDEEFQELAAKCTDCGW--CTRACPNSLRIKEAMEAAKEGDFSGLADLFDQCVG----CGRceqE 414
|
...
gi 497534204 98 CPQ 100
Cdd:cd01916 415 CPK 417
|
|
| PLN02507 |
PLN02507 |
glutathione reductase |
286-457 |
9.71e-04 |
|
glutathione reductase
Pssm-ID: 215281 [Multi-domain] Cd Length: 499 Bit Score: 41.73 E-value: 9.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497534204 286 KKVVVLGGGDTAMDCvrTSI-RQHAANVVCAYRRdEANMPG---SRREV--KNAKEEGVkfmfNLQPLALETDSSGHVTG 359
Cdd:PLN02507 204 KRAVVLGGGYIAVEF--ASIwRGMGATVDLFFRK-ELPLRGfddEMRAVvaRNLEGRGI----NLHPRTNLTQLTKTEGG 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497534204 360 VKVVKTalgepdeagrrrpepvEGSEHVleADAVIMAFGFQPHAMEW-LEPFGVELDQWGRIKAPgkqefQYQTTN-SKI 437
Cdd:PLN02507 277 IKVITD----------------HGEEFV--ADVVLFATGRAPNTKRLnLEAVGVELDKAGAVKVD-----EYSRTNiPSI 333
|
170 180
....*....|....*....|
gi 497534204 438 FAGGDAVRGSDLVVTAIDEG 457
Cdd:PLN02507 334 WAIGDVTNRINLTPVALMEG 353
|
|
| PRK12771 |
PRK12771 |
putative glutamate synthase (NADPH) small subunit; Provisional |
3-60 |
1.34e-03 |
|
putative glutamate synthase (NADPH) small subunit; Provisional
Pssm-ID: 237198 [Multi-domain] Cd Length: 564 Bit Score: 41.01 E-value: 1.34e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 497534204 3 QNVYQFIDVNRVDPAKKPIKIRKIEFVEIYEPFTKQQAKAQADRCLDCGNPY----CEWKCP 60
Cdd:PRK12771 462 LNLWYFTDAPRAQRPELDADERVGDFDEVLGGLTEEEARQEAARCLSCGNCFecdnCYGACP 523
|
|
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
357-465 |
2.53e-03 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 40.13 E-value: 2.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497534204 357 VTGVKVVKTALGEP-----DEAGrrrpepveGSEHVLEADAVIMAFGFQPHAMEW-LEPFGVELDQwGRIKAPGkqefQY 430
Cdd:PRK06416 231 KTGAKAKKVEQTDDgvtvtLEDG--------GKEETLEADYVLVAVGRRPNTENLgLEELGVKTDR-GFIEVDE----QL 297
|
90 100 110
....*....|....*....|....*....|....*
gi 497534204 431 QTTNSKIFAGGDAVRGSDLVVTAIDEGRKAAEGIL 465
Cdd:PRK06416 298 RTNVPNIYAIGDIVGGPMLAHKASAEGIIAAEAIA 332
|
|
| PRK06116 |
PRK06116 |
glutathione reductase; Validated |
286-462 |
3.22e-03 |
|
glutathione reductase; Validated
Pssm-ID: 235701 [Multi-domain] Cd Length: 450 Bit Score: 39.75 E-value: 3.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497534204 286 KKVVVLGGGDTAMD--CVrtsIRQHAANVVCAYRRDE--ANMPGSRRE--VKNAKEEGVKFMFNLQPLALETDSSGHVTg 359
Cdd:PRK06116 168 KRVAVVGAGYIAVEfaGV---LNGLGSETHLFVRGDAplRGFDPDIREtlVEEMEKKGIRLHTNAVPKAVEKNADGSLT- 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497534204 360 vkvVKTALGEpdeagrrrpepvegsehVLEADAVIMAFGFQP--HAMEwLEPFGVELDQWGRIKAPgkqefQYQTTNSK- 436
Cdd:PRK06116 244 ---LTLEDGE-----------------TLTVDCLIWAIGREPntDGLG-LENAGVKLNEKGYIIVD-----EYQNTNVPg 297
|
170 180
....*....|....*....|....*.
gi 497534204 437 IFAGGDAVRGSDLVVTAIDEGRKAAE 462
Cdd:PRK06116 298 IYAVGDVTGRVELTPVAIAAGRRLSE 323
|
|
| PRK06327 |
PRK06327 |
dihydrolipoamide dehydrogenase; Validated |
382-464 |
3.99e-03 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235779 [Multi-domain] Cd Length: 475 Bit Score: 39.52 E-value: 3.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497534204 382 EGSEHVLEADAVIMAFGFQPHAMEW-LEPFGVELDQWGRIKAPGKqefqYQTTNSKIFAGGDAVRGSDLVVTAIDEGRKA 460
Cdd:PRK06327 265 DGEAQTLEVDKLIVSIGRVPNTDGLgLEAVGLKLDERGFIPVDDH----CRTNVPNVYAIGDVVRGPMLAHKAEEEGVAV 340
|
....
gi 497534204 461 AEGI 464
Cdd:PRK06327 341 AERI 344
|
|
| |
