|
Name |
Accession |
Description |
Interval |
E-value |
| PRK12778 |
PRK12778 |
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ... |
1-765 |
0e+00 |
|
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;
Pssm-ID: 237200 [Multi-domain] Cd Length: 752 Bit Score: 1435.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 1 MNKIISKEHFSEKVFKLVIEAPLIAKSRKAGHFVIVRVGEKGERMPLTIAGADPVKGTITLVVQEVGLSSTRLCELNEGD 80
Cdd:PRK12778 1 MNKIVEKEIFSEKVFLLEIEAPLIAKSRKPGQFVIVRVGEKGERIPLTIADADPEKGTITLVIQEVGLSTTKLCELNEGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 81 YITDVVGPLGKATHIENFGTVVCAGGGVGVAPMLPIVQALKAAGNRVITVLAGRTKELIILEKEMRESSDEVIIMTDDGS 160
Cdd:PRK12778 81 YITDVVGPLGNPSEIENYGTVVCAGGGVGVAPMLPIVKALKAAGNRVITILGGRSKELIILEDEMRESSDEVIIMTDDGS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 161 YGHKGLVTEGVEEVIKRET-VNKCFAIGPAIMMKFVCLLTKKYEIPTDVSLNTIMVDGTGMCGACRITVGGKTRFVCVDG 239
Cdd:PRK12778 161 YGRKGLVTDGLEEVIKRETkVDKVFAIGPAIMMKFVCLLTKKYGIPTIVSLNTIMVDGTGMCGACRVTVGGKTKFACVDG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 240 PEFDGHQVDFDEMLKRMGAFKDIEKEEIHKLDTEKpttceatkeldgrdAEWRASLRKAMKPKERMAIPRVKMNELDAEY 319
Cdd:PRK12778 241 PEFDGHLVDFDEMLKRMGAYKTIEGEELLKLEERT--------------AAWRAELRKSMKPKERTAIERVPMPELDPEY 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 320 RSHSRKEEVNLGLNEEQAITEAKRCLDCPNPTCMNGCPVGINIPKFIKNIERGEFLEAAKTLKATSALPAVCGRVCPQEK 399
Cdd:PRK12778 307 RAHNRFEEVNLGLTKEQAMTEAKRCLDCKNPGCVEGCPVGIDIPRFIKNIERGNFLEAAKILKETSALPAVCGRVCPQEK 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 400 QCESQCTHLKAGHEAVAIGYLERFAADYERESGQISVPEVAEKNNIKVAVIGSGPAGLSFAGDMAKQGYDVTVFEALHEI 479
Cdd:PRK12778 387 QCESKCIHGKMGEEAVAIGYLERFVADYERESGNISVPEVAEKNGKKVAVIGSGPAGLSFAGDLAKRGYDVTVFEALHEI 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 480 GGVLKYGIPEFRLPNKIVDVEIDNLSKMGVKFMKDCIVGKTISVEDLEAEDFKGIFVASGAGLPNFMNIPGENSINIMSS 559
Cdd:PRK12778 467 GGVLKYGIPEFRLPKKIVDVEIENLKKLGVKFETDVIVGKTITIEELEEEGFKGIFIASGAGLPNFMNIPGENSNGVMSS 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 560 NEYLTRVNLMDAASEDSDTPVTFGKRVAVIGGGNTAMDSVRTARRLGAEHAMIIYRRSEEEMPARLEEVKHAKEEGVEFL 639
Cdd:PRK12778 547 NEYLTRVNLMDAASPDSDTPIKFGKKVAVVGGGNTAMDSARTAKRLGAERVTIVYRRSEEEMPARLEEVKHAKEEGIEFL 626
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 640 TLHNPIEYIADEKGRVKQVVLQKMELGEPDASGRRSPIAIPGATETIDIDMAIVSVGVSPNPIVPSSIPGLELGRKGTIA 719
Cdd:PRK12778 627 TLHNPIEYLADEKGWVKQVVLQKMELGEPDASGRRRPVAIPGSTFTVDVDLVIVSVGVSPNPLVPSSIPGLELNRKGTIV 706
|
730 740 750 760
....*....|....*....|....*....|....*....|....*.
gi 1474009758 720 VNENMQSSIPTIYAGGDIVRGGATVILAMGDGRKAAASMHAQLSSK 765
Cdd:PRK12778 707 VDEEMQSSIPGIYAGGDIVRGGATVILAMGDGKRAAAAIDEYLSSK 752
|
|
| PRK12775 |
PRK12775 |
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin ... |
1-763 |
0e+00 |
|
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin domain-containing protein; Provisional
Pssm-ID: 183738 [Multi-domain] Cd Length: 1006 Bit Score: 757.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 1 MNKIISKEHFSEKVFKLVIEAPLIAKSRKAGHFVIVRVGEKGERMPLTIAGADPVKGTITLVVQEVGlSSTR--LCELNE 78
Cdd:PRK12775 1 MYSIVRREAFSDTTFLWEVEAPDVAASAEPGHFVMLRLYEGAERIPLTVADFDRKKGTITMVVQALG-KTTRemMTKFKA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 79 GDYITDVVGPLGKATHIENFGTVVCAGGGVGVAPMLPIVQALKAAGNRVITVLAGRTKELIILEKEMRESSDEVIIMTDD 158
Cdd:PRK12775 80 GDTFEDFVGPLGLPQHIDKAGHVVLVGGGLGVAPVYPQLRAFKEAGARTTGIIGFRNKDLVFWEDKFGKYCDDLIVCTDD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 159 GSYGHKGLVTEGVEEVIKRETVNKCFAIGPAIMMKFVCLLTKKYEIPTDVSLNTIMVDGTGMCGACRITVGGKTRFVCVD 238
Cdd:PRK12775 160 GSYGKPGFVTAALKEVCEKDKPDLVVAIGPLPMMNACVETTRPFGVKTMVSLNAIMVDGTGMCGSCRVTVGGEVKFACVD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 239 GPEFDGHQVDFDEMLKRMGAFKDIEKeeihKLDTEKPTTCEATKEL--DGRdaewraslRKAMKPKErMAIPRVKMNELD 316
Cdd:PRK12775 240 GPDFDGHKVDFKELHARQKRFKSQED----RANEDYAHVCNLEKQLfeEGK--------RNYKKLKT-LVPHQTPMPERD 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 317 AEYRSHSRKeEVNLGLNEEQAITEAKRCLDCPNPTCMNGCPVGINIPKFIKNIERGEFLEAAKTLKATSALPAVCGRVCP 396
Cdd:PRK12775 307 AVERARNFK-EVNLGYSLEDALQEAERCIQCAKPTCIAGCPVQIDIPVFIRHVVVRDFDGALEVIYEASIFPSICGRVCP 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 397 QEKQCESQCThLKAGHEAVAIGYLERFAADYEReSGQISVPEVAEKNNiKVAVIGSGPAGLSFAGDMAKQGYDVTVFEAL 476
Cdd:PRK12775 386 QETQCEAQCI-IAKKHESVGIGRLERFVGDNAR-AKPVKPPRFSKKLG-KVAICGSGPAGLAAAADLVKYGVDVTVYEAL 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 477 HEIGGVLKYGIPEFRLPNKIVDVEIDNLSKMGVKFMKDCIVGKTISVEDLEAED-FKGIFVASGAGLPNFMNIPGENSIN 555
Cdd:PRK12775 463 HVVGGVLQYGIPSFRLPRDIIDREVQRLVDIGVKIETNKVIGKTFTVPQLMNDKgFDAVFLGVGAGAPTFLGIPGEFAGQ 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 556 IMSSNEYLTRVNLMDAAS-EDSDTPVTFGKRVAVIGGGNTAMDSVRTARRLGAEHAMIIYRRSEEEMPARLEEVKHAKEE 634
Cdd:PRK12775 543 VYSANEFLTRVNLMGGDKfPFLDTPISLGKSVVVIGAGNTAMDCLRVAKRLGAPTVRCVYRRSEAEAPARIEEIRHAKEE 622
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 635 GVEFLTLHNPIEYIADEKGRVKQVVLQKMELGEPDASGRRSPIAIpGATETIDIDMAIVSVGVSPNPIVPSSIPGLELGR 714
Cdd:PRK12775 623 GIDFFFLHSPVEIYVDAEGSVRGMKVEEMELGEPDEKGRRKPMPT-GEFKDLECDTVIYALGTKANPIITQSTPGLALNK 701
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....
gi 1474009758 715 KGTIAVN----ENMQSS-IPTIYAGGDIVRGGATVILAMGDGRKAAASMHAQLS 763
Cdd:PRK12775 702 WGNIAADdgklESTQSTnLPGVFAGGDIVTGGATVILAMGAGRRAARSIATYLR 755
|
|
| PRK12831 |
PRK12831 |
putative oxidoreductase; Provisional |
300-765 |
0e+00 |
|
putative oxidoreductase; Provisional
Pssm-ID: 183780 [Multi-domain] Cd Length: 464 Bit Score: 674.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 300 KPKERMaiPRVKMNELDAEYRSHSRkEEVNLGLNEEQAITEAKRCLDCPNPTCMNGCPVGINIPKFIKNIERGEFLEAAK 379
Cdd:PRK12831 1 MMKDRK--KRVPVREQDPEVRATNF-EEVCLGYNEEEAVKEASRCLQCKKPKCVKGCPVSINIPGFISKLKEGDFEEAAK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 380 TLKATSALPAVCGRVCPQEKQCESQCTHLKAGhEAVAIGYLERFAADYERESGqISVPEVAEKNNIKVAVIGSGPAGLSF 459
Cdd:PRK12831 78 IIAKYNALPAVCGRVCPQESQCEGKCVLGIKG-EPVAIGKLERFVADWARENG-IDLSETEEKKGKKVAVIGSGPAGLTC 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 460 AGDMAKQGYDVTVFEALHEIGGVLKYGIPEFRLP-NKIVDVEIDNLSKMGVKFMKDCIVGKTISVEDL-EAEDFKGIFVA 537
Cdd:PRK12831 156 AGDLAKMGYDVTIFEALHEPGGVLVYGIPEFRLPkETVVKKEIENIKKLGVKIETNVVVGKTVTIDELlEEEGFDAVFIG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 538 SGAGLPNFMNIPGENSINIMSSNEYLTRVNLMDAASEDSDTPVTFGKRVAVIGGGNTAMDSVRTARRLGAEhAMIIYRRS 617
Cdd:PRK12831 236 SGAGLPKFMGIPGENLNGVFSANEFLTRVNLMKAYKPEYDTPIKVGKKVAVVGGGNVAMDAARTALRLGAE-VHIVYRRS 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 618 EEEMPARLEEVKHAKEEGVEFLTLHNPIEYIADEKGRVKQVVLQKMELGEPDASGRRSPIAIPGATETIDIDMAIVSVGV 697
Cdd:PRK12831 315 EEELPARVEEVHHAKEEGVIFDLLTNPVEILGDENGWVKGMKCIKMELGEPDASGRRRPVEIEGSEFVLEVDTVIMSLGT 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1474009758 698 SPNPIVPSSIPGLELGRKGTIAVNENM-QSSIPTIYAGGDIVRGGATVILAMGDGRKAAASMHAQLSSK 765
Cdd:PRK12831 395 SPNPLISSTTKGLKINKRGCIVADEETgLTSKEGVFAGGDAVTGAATVILAMGAGKKAAKAIDEYLSKK 463
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
302-765 |
0e+00 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 663.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 302 KERMAIPRVKMNELDAEYRSHsRKEEVNLGLNEEQAITEAKRCLDCPNPTCMNGCPVGINIPKFIKNIERGEFLEAAKTL 381
Cdd:PRK11749 1 LKFLTTPRIPMPRQDAEERAQ-NFDEVAPGYTPEEAIEEASRCLQCKDAPCVKACPVSIDIPEFIRLIAEGNLKGAAETI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 382 KATSALPAVCGRVCPQEKQCESQCTHLKAGHeAVAIGYLERFAADYERESGQIsVPEVAEKNNIKVAVIGSGPAGLSFAG 461
Cdd:PRK11749 80 LETNPLPAVCGRVCPQERLCEGACVRGKKGE-PVAIGRLERYITDWAMETGWV-LFKRAPKTGKKVAVIGAGPAGLTAAH 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 462 DMAKQGYDVTVFEALHEIGGVLKYGIPEFRLPNKIVDVEIDNLSKMGVKFMKDCIVGKTISVEDLeAEDFKGIFVASGAG 541
Cdd:PRK11749 158 RLARKGYDVTIFEARDKAGGLLRYGIPEFRLPKDIVDREVERLLKLGVEIRTNTEVGRDITLDEL-RAGYDAVFIGTGAG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 542 LPNFMNIPGENSINIMSSNEYLTRVNLMDaasEDSDTPVtfGKRVAVIGGGNTAMDSVRTARRLGAEHAMIIYRRSEEEM 621
Cdd:PRK11749 237 LPRFLGIPGENLGGVYSAVDFLTRVNQAV---ADYDLPV--GKRVVVIGGGNTAMDAARTAKRLGAESVTIVYRRGREEM 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 622 PARLEEVKHAKEEGVEFLTLHNPIEYIADEKGRvKQVVLQKMELGEPDASGRRSpIAIPGATETIDIDMAIVSVGVSPNP 701
Cdd:PRK11749 312 PASEEEVEHAKEEGVEFEWLAAPVEILGDEGRV-TGVEFVRMELGEPDASGRRR-VPIEGSEFTLPADLVIKAIGQTPNP 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1474009758 702 IVPSSIPGLELGRKGT-IAVNENMQSSIPTIYAGGDIVRGGATVILAMGDGRKAAASMHAQLSSK 765
Cdd:PRK11749 390 LILSTTPGLELNRWGTiIADDETGRTSLPGVFAGGDIVTGAATVVWAVGDGKDAAEAIHEYLEGA 454
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
326-760 |
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: 614.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 326 EEVNLGLNEEQAITEAKRCLDCPNPTCMNGCPVGINIPKFIKNIERGEFLEAAKTLKATSALPAVCGRVCPQekQCESQC 405
Cdd:COG0493 6 REVYPGLSEEEAIEQAARCLDCGDPPCQTGCPVGNDIPEWIRLIAEGDYEEALELIHETNPFPEVCGRVCPA--PCEGAC 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 406 THLKaGHEAVAIGYLERFAADYERESGQISVPEVAEKNNIKVAVIGSGPAGLSFAGDMAKQGYDVTVFEALHEIGGVLKY 485
Cdd:COG0493 84 VRGI-VDEPVAIGALERFIADKAFEEGWVKPPPPAPRTGKKVAVVGSGPAGLAAAYQLARAGHEVTVFEALDKPGGLLRY 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 486 GIPEFRLPNKIVDVEIDNLSKMGVKFMKDCIVGKTISVEDLEaEDFKGIFVASGAGLPNFMNIPGENSINIMSSNEYLTR 565
Cdd:COG0493 163 GIPEFRLPKDVLDREIELIEALGVEFRTNVEVGKDITLDELL-EEFDAVFLATGAGKPRDLGIPGEDLKGVHSAMDFLTA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 566 VNLMDAAsedsDTPVTFGKRVAVIGGGNTAMDSVRTARRLGAEHAMIIYRRSEEEMPARLEEVKHAKEEGVEFLTLHNPI 645
Cdd:COG0493 242 VNLGEAP----DTILAVGKRVVVIGGGNTAMDCARTALRLGAESVTIVYRRTREEMPASKEEVEEALEEGVEFLFLVAPV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 646 EYIADEKGRVKQVVLQKMELGEPDASGRRSPIAIPGATETIDIDMAIVSVGVSPNPIVPSSIPGLELGRKGTIAVNE-NM 724
Cdd:COG0493 318 EIIGDENGRVTGLECVRMELGEPDESGRRRPVPIEGSEFTLPADLVILAIGQTPDPSGLEEELGLELDKRGTIVVDEeTY 397
|
410 420 430
....*....|....*....|....*....|....*.
gi 1474009758 725 QSSIPTIYAGGDIVRGGATVILAMGDGRKAAASMHA 760
Cdd:COG0493 398 QTSLPGVFAGGDAVRGPSLVVWAIAEGRKAARAIDR 433
|
|
| gltA |
TIGR01316 |
glutamate synthase (NADPH), homotetrameric; This protein is homologous to the small subunit of ... |
326-762 |
1.67e-167 |
|
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: 490.54 E-value: 1.67e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 326 EEVNLGLNEEQAITEAKRCLDCPNPT--CMNGCPVGINIPKFIKNIERGEFLEAAKTLKATSALPAVCGRVCPQEKQCES 403
Cdd:TIGR01316 10 QEAALGYTEQLALVEAQRCLNCKDATkpCIKGCPVHVPIPEFIAKIQEGDFKGAVDIIKTTSLLPAICGRVCPQERQCEG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 404 QCT---HLKAGHEAVAIGYLERFAADYERESGQISVPEVAEKNNIKVAVIGSGPAGLSFAGDMAKQGYDVTVFEALHEIG 480
Cdd:TIGR01316 90 QCTvgkMFKDVGKPVSIGALERFVADWERQHGIETEPEKAPSTHKKVAVIGAGPAGLACASELAKAGHSVTVFEALHKPG 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 481 GVLKYGIPEFRLPNKIVDVEIDNLSKMGVKFMKDCIVGKTISVEDLeAEDFKGIFVASGAGLPNFMNIPGENSINIMSSN 560
Cdd:TIGR01316 170 GVVTYGIPEFRLPKEIVVTEIKTLKKLGVTFRMNFLVGKTATLEEL-FSQYDAVFIGTGAGLPKLMNIPGEELCGVYSAN 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 561 EYLTRVNLMDA-ASEDSDTPVTFGKRVAVIGGGNTAMDSVRTARRLGAEhAMIIYRRSEEEMPARLEEVKHAKEEGVEFL 639
Cdd:TIGR01316 249 DFLTRANLMKAyEFPHADTPVYAGKSVVVIGGGNTAVDSARTALRLGAE-VHCLYRRTREDMTARVEEIAHAEEEGVKFH 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 640 TLHNPIEYIADEKGRVKQVVLQKMELGEPDASGRRSPIAIPGATETIDIDMAIVSVGVSPNPIVPSSiPGLELGRKGTIA 719
Cdd:TIGR01316 328 FLCQPVEIIGDEEGNVRAVKFRKMDCQEQIDSGERRFLPCGDAECKLEADAVIVAIGNGSNPIMAET-TRLKTSERGTIV 406
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1474009758 720 VNENMQSSIPTIYAGGDIVRGGATVILAMGDGRKAAASMHAQL 762
Cdd:TIGR01316 407 VDEDQRTSIPGVFAGGDIILGAATVIRAMGQGKRAAKSINEYL 449
|
|
| PRK06222 |
PRK06222 |
sulfide/dihydroorotate dehydrogenase-like FAD/NAD-binding protein; |
1-269 |
1.42e-156 |
|
sulfide/dihydroorotate dehydrogenase-like FAD/NAD-binding protein;
Pssm-ID: 235747 [Multi-domain] Cd Length: 281 Bit Score: 455.80 E-value: 1.42e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 1 MNKIISKEHFSEKVFKLVIEAPLIAKSRKAGHFVIVRVGEKGERMPLTIAGADPVKGTITLVVQEVGLSSTRLCELNEGD 80
Cdd:PRK06222 1 MYKILEKEELAPNVFLMEIEAPRVAKKAKPGQFVIVRIDEKGERIPLTIADYDREKGTITIVFQAVGKSTRKLAELKEGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 81 YITDVVGPLGKATHIENFGTVVCAGGGVGVAPMLPIVQALKAAGNRVITVLAGRTKELIILEKEMRESSDEVIIMTDDGS 160
Cdd:PRK06222 81 SILDVVGPLGKPSEIEKFGTVVCVGGGVGIAPVYPIAKALKEAGNKVITIIGARNKDLLILEDEMKAVSDELYVTTDDGS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 161 YGHKGLVTEGVEEVI-KRETVNKCFAIGPAIMMKFVCLLTKKYEIPTDVSLNTIMVDGTGMCGACRITVGGKTRFVCVDG 239
Cdd:PRK06222 161 YGRKGFVTDVLKELLeSGKKVDRVVAIGPVIMMKFVAELTKPYGIKTIVSLNPIMVDGTGMCGACRVTVGGETKFACVDG 240
|
250 260 270
....*....|....*....|....*....|
gi 1474009758 240 PEFDGHQVDFDEMLKRMGAFKDIEKEEIHK 269
Cdd:PRK06222 241 PEFDGHLVDFDELMRRLAMYKEEEKLALEK 270
|
|
| PRK12779 |
PRK12779 |
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; ... |
355-758 |
5.35e-138 |
|
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; Provisional
Pssm-ID: 183740 [Multi-domain] Cd Length: 944 Bit Score: 430.79 E-value: 5.35e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 355 GCPVGINIPKFIKNIERGEFLEAAKTLKATSALPAVCGRVCPQEKQCESQCTHLKaghEAVAIGYLERFAADYERE---- 430
Cdd:PRK12779 213 GCPVKIHIPEMLDLLGNGKHREALELIESCNPLPNVTGRVCPQELQCQGVCTHTK---RPIEIGQLEWYLPQHEKLvnpn 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 431 -----SGQISVPEVAEKNNIkvAVIGSGPAGLSFAGDMAKQGYDVTVFEALHEIGGVLKYGIPEFRLPNKIVDVEIDNLS 505
Cdd:PRK12779 290 anerfAGRISPWAAAVKPPI--AVVGSGPSGLINAYLLAVEGFPVTVFEAFHDLGGVLRYGIPEFRLPNQLIDDVVEKIK 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 506 KMGVKFMKDCIVGKTISVEDLEAEDFKGIFVASGAGLPNFMNIPGENSINIMSSNEYLTRVNLMDAASEDSDTPV--TFG 583
Cdd:PRK12779 368 LLGGRFVKNFVVGKTATLEDLKAAGFWKIFVGTGAGLPTFMNVPGEHLLGVMSANEFLTRVNLMRGLDDDYETPLpeVKG 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 584 KRVAVIGGGNTAMDSVRTARRLGAeHAMIIYRRSEEEMPARLEEVKHAKEEGVEFLTLHNPIEYIADEKGR-VKQVVLQK 662
Cdd:PRK12779 448 KEVFVIGGGNTAMDAARTAKRLGG-NVTIVYRRTKSEMPARVEELHHALEEGINLAVLRAPREFIGDDHTHfVTHALLDV 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 663 MELGEPDASGRRSPIAIpGATETIDIDMAIVSVGVSPNPIVPSSIPGLELGRKGTIAVNENMQ-SSIPTIYAGGDIVRGG 741
Cdd:PRK12779 527 NELGEPDKSGRRSPKPT-GEIERVPVDLVIMALGNTANPIMKDAEPGLKTNKWGTIEVEKGSQrTSIKGVYSGGDAARGG 605
|
410
....*....|....*..
gi 1474009758 742 ATVILAMGDGRKAAASM 758
Cdd:PRK12779 606 STAIRAAGDGQAAAKEI 622
|
|
| DHOD_e_trans_like1 |
cd06219 |
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase-like ... |
2-248 |
1.73e-130 |
|
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase-like proteins. Dihydroorotate dehydrogenases (DHODs) catalyze the only redox reaction in pyrimidine de novo biosynthesis. They catalyze the oxidation of (S)-dihydroorotate to orotate coupled with the reduction of NAD+. In L. lactis, DHOD B (encoded by pyrDa) is co-expressed with pyrK and both gene products are required for full activity, as well as NAD binding. NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer between an NAD(P)-binding domain of the alpha/beta class and a discrete (usually N-terminal) domain which vary in orientation with respect to the NAD(P) binding domain. The N-terminal domain may contain a flavin prosthetic group, as in flavoenzymes, or use flavin as a substrate. Ferredoxin is reduced in the final stage of photosystem I. The flavoprotein Ferredoxin-NADP+ reductase transfers electrons from reduced ferredoxin to FAD, forming FADH2 via a semiquinone intermediate, and then transfers a hydride ion to convert NADP+ to NADPH.
Pssm-ID: 99815 [Multi-domain] Cd Length: 248 Bit Score: 387.70 E-value: 1.73e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 2 NKIISKEHFSEKVFKLVIEAPLIAKSRKAGHFVIVRVGEKGERMPLTIAGADPVKGTITLVVQEVGLSSTRLCELNEGDY 81
Cdd:cd06219 1 YKILEKEELAPNVKLFEIEAPLIAKKAKPGQFVIVRADEKGERIPLTIADWDPEKGTITIVVQVVGKSTRELATLEEGDK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 82 ITDVVGPLGKATHIENFGTVVCAGGGVGVAPMLPIVQALKAAGNRVITVLAGRTKELIILEKEMRESSDEVIIMTDDGSY 161
Cdd:cd06219 81 IHDVVGPLGKPSEIENYGTVVFVGGGVGIAPIYPIAKALKEAGNRVITIIGARTKDLVILEDEFRAVSDELIITTDDGSY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 162 GHKGLVTEGVEEVIKR-ETVNKCFAIGPAIMMKFVCLLTKKYEIPTDVSLNTIMVDGTGMCGACRITVGGKTRFVCVDGP 240
Cdd:cd06219 161 GEKGFVTDPLKELIESgEKVDLVIAIGPPIMMKAVSELTRPYGIPTVVSLNPIMVDGTGMCGACRVTVGGETKFACVDGP 240
|
....*...
gi 1474009758 241 EFDGHQVD 248
Cdd:cd06219 241 EFDAHKVD 248
|
|
| gltD |
PRK12810 |
glutamate synthase subunit beta; Reviewed |
300-762 |
3.22e-121 |
|
glutamate synthase subunit beta; Reviewed
Pssm-ID: 237213 [Multi-domain] Cd Length: 471 Bit Score: 372.19 E-value: 3.22e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 300 KPKERMAIPRVKMNELDAEYRSHSRKEeVNLGLNEEQAITEAKRCLDCPNPTCMNGCPVGINIPKFIKNIERGEFLEAAK 379
Cdd:PRK12810 3 KPTGFLEYDRVDPKKRPVAERIKDFKE-FYEPFSEEQAKIQAARCMDCGIPFCHWGCPVHNYIPEWNDLVYRGRWEEAAE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 380 TLKATSALPAVCGRVCPQEkqCESQCThLKAGHEAVAIGYLERFAADYERESGQIsVPEV-AEKNNIKVAVIGSGPAGLS 458
Cdd:PRK12810 82 RLHQTNNFPEFTGRVCPAP--CEGACT-LNINFGPVTIKNIERYIIDKAFEEGWV-KPDPpVKRTGKKVAVVGSGPAGLA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 459 FAGDMAKQGYDVTVFEALHEIGGVLKYGIPEFRLPNKIVDVEIDNLSKMGVKFMKDCIVGKTISVEDLEAEdFKGIFVAS 538
Cdd:PRK12810 158 AADQLARAGHKVTVFERADRIGGLLRYGIPDFKLEKEVIDRRIELMEAEGIEFRTNVEVGKDITAEELLAE-YDAVFLGT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 539 GAGLPNFMNIPGENSINIMSSNEYLTRVNLMDAASEDSDTPVTFGKRVAVIGGGNTAMDSVRTARRLGAEHamiIYRRSE 618
Cdd:PRK12810 237 GAYKPRDLGIPGRDLDGVHFAMDFLIQNTRRVLGDETEPFISAKGKHVVVIGGGDTGMDCVGTAIRQGAKS---VTQRDI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 619 EEMPARLE-------------EVKHAKEEGVEFLTLHNPIEYIAdEKGRVKQVVLQKMELGEPDasgrrsPIAIPGATET 685
Cdd:PRK12810 314 MPMPPSRRnknnpwpywpmklEVSNAHEEGVEREFNVQTKEFEG-ENGKVTGVKVVRTELGEGD------FEPVEGSEFV 386
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1474009758 686 IDIDMAIVSVG-VSPNPIVPSSiPGLELGRKGTIAVNE-NMQSSIPTIYAGGDIVRGGATVILAMGDGRKAAASMHAQL 762
Cdd:PRK12810 387 LPADLVLLAMGfTGPEAGLLAQ-FGVELDERGRVAAPDnAYQTSNPKVFAAGDMRRGQSLVVWAIAEGRQAARAIDAYL 464
|
|
| gltD_gamma_fam |
TIGR01318 |
glutamate synthase small subunit family protein, proteobacterial; This model represents one of ... |
308-758 |
4.82e-113 |
|
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: 350.64 E-value: 4.82e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 308 PRVKMNELDAEYR-SHSRkeEVNLGLNEEQAITEAKRCLDCPNPTCMNGCPVGINIPKFIKNIERGEFLEAAKTLKATSA 386
Cdd:TIGR01318 7 PRQDPDKIPVEERkTDFR--EIYGPFDKGQAQYQADRCLDCGNPYCEWKCPVHNAIPQWLQLVQEGRIDEAAELSHQTNT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 387 LPAVCGRVCPQEKQCESQCThLKAGHEAVAIGYLERFAADYERESG-QISVPEVaEKNNIKVAVIGSGPAGLSFAGDMAK 465
Cdd:TIGR01318 85 LPEICGRVCPQDRLCEGACT-LNDEGGAVTIGNLERYITDTALAMGwRPDLSHV-QPTGKRVAVIGAGPAGLACADILAR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 466 QGYDVTVFEALHEIGGVLKYGIPEFRLPNKIVDVEIDNLSKMGVKFMKDCIVGKTISVEDLeAEDFKGIFVASGAGLPNF 545
Cdd:TIGR01318 163 AGVQVVVFDRHPEIGGLLTFGIPSFKLDKAVLSRRREIFTAMGIEFRLNCEVGRDISLDDL-LEDYDAVFLGVGTYRSMR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 546 MNIPGENSINIMSSNEYL---TRVNLMDAASEDSDTPVTFGKRVAVIGGGNTAMDSVRTARRLGAEHAMIIYRRSEEEMP 622
Cdd:TIGR01318 242 GGLPGEDAPGVLPALPFLianTRQLMGLPEEPEEPLIDVEGKRVVVLGGGDTAMDCVRTAIRLGATKVTCAYRRDEANMP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 623 ARLEEVKHAKEEGVEFLTLHNPIEYIADEKGRVKQVVLQKMELGEPDASGRRSPIAIPGATETIDIDMAIVSVGVSPNPI 702
Cdd:TIGR01318 322 GSRREVANAREEGVEFLFNVQPVSIESDEDGQVIGVTVVRTKLGEPDANGRRRPVPVAGSEFVLPADVVIMAFGFSPHLM 401
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 703 VPSSIPGLELGRKGTIAVNEN----MQSSIPTIYAGGDIVRGGATVILAMGDGRKAAASM 758
Cdd:TIGR01318 402 PWLAAHGITLDSWGRIITALSsgltYQTTNPKIFAGGDAVRGADLVVTAVAEGRDAAQGI 461
|
|
| PRK12814 |
PRK12814 |
putative NADPH-dependent glutamate synthase small subunit; Provisional |
341-765 |
1.42e-110 |
|
putative NADPH-dependent glutamate synthase small subunit; Provisional
Pssm-ID: 139246 [Multi-domain] Cd Length: 652 Bit Score: 350.57 E-value: 1.42e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 341 AKRCLDCPNPtCMNGCPVGINIPKFIKNIERGEFLEAAKTLKATSALPAVCGRVCPQEkqCESQCTHlkagH---EAVAI 417
Cdd:PRK12814 94 EQHCGDCLGP-CELACPAGCNIPGFIAAIARGDDREAIRIIKETIPLPGILGRICPAP--CEEACRR----HgvdEPVSI 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 418 GYLERFAADYERESGQISVPEVAEKNNIKVAVIGSGPAGLSFAGDMAKQGYDVTVFEALHEIGGVLKYGIPEFRLPNKIV 497
Cdd:PRK12814 167 CALKRYAADRDMESAERYIPERAPKSGKKVAIIGAGPAGLTAAYYLLRKGHDVTIFDANEQAGGMMRYGIPRFRLPESVI 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 498 DVEIDNLSKMGVKFMKDCIVGKTISVEDLEAEdFKGIFVASGAGLPNFMNIPGENSINIMSSNEYLTRVNlmdaasedSD 577
Cdd:PRK12814 247 DADIAPLRAMGAEFRFNTVFGRDITLEELQKE-FDAVLLAVGAQKASKMGIPGEELPGVISGIDFLRNVA--------LG 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 578 TPVTFGKRVAVIGGGNTAMDSVRTARRLGAEHAMIIYRRSEEEMPARLEEVKHAKEEGVEFLTLHNPIEYIADEKGRVKQ 657
Cdd:PRK12814 318 TALHPGKKVVVIGGGNTAIDAARTALRLGAESVTILYRRTREEMPANRAEIEEALAEGVSLRELAAPVSIERSEGGLELT 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 658 VVlqKMELGEPDASGRRSPIAIPGATETIDIDMAIVSVGVSPNPIVpSSIPGLELGRKGTIAVN-ENMQSSIPTIYAGGD 736
Cdd:PRK12814 398 AI--KMQQGEPDESGRRRPVPVEGSEFTLQADTVISAIGQQVDPPI-AEAAGIGTSRNGTVKVDpETLQTSVAGVFAGGD 474
|
410 420
....*....|....*....|....*....
gi 1474009758 737 IVRGGATVILAMGDGRKAAASMHAQLSSK 765
Cdd:PRK12814 475 CVTGADIAINAVEQGKRAAHAIDLFLNGK 503
|
|
| PRK12771 |
PRK12771 |
putative glutamate synthase (NADPH) small subunit; Provisional |
350-763 |
6.42e-106 |
|
putative glutamate synthase (NADPH) small subunit; Provisional
Pssm-ID: 237198 [Multi-domain] Cd Length: 564 Bit Score: 335.31 E-value: 6.42e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 350 PTCMNGCPVGINIPKFIKNIERGEFLEAAKTLKATSALPAVCGRVCPQEkqCESQC--THLKaghEAVAIGYLERFAADY 427
Cdd:PRK12771 47 PPCNAACPAGEDIRGWLALVRGGDYEYAWRRLTKDNPFPAVMGRVCYHP--CESGCnrGQVD---DAVGINAVERFLGDY 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 428 ERESGqISVPEVAEKNNIKVAVIGSGPAGLSFAGDMAKQGYDVTVFEALHEIGGVLKYGIPEFRLPNKIVDVEIDNLSKM 507
Cdd:PRK12771 122 AIANG-WKFPAPAPDTGKRVAVIGGGPAGLSAAYHLRRMGHAVTIFEAGPKLGGMMRYGIPAYRLPREVLDAEIQRILDL 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 508 GVKFMKDCIVGKTISVEDLEAeDFKGIFVASGAGLPNFMNIPGENSINIMSSNEYLTRVNLMDaasedsdtPVTFGKRVA 587
Cdd:PRK12771 201 GVEVRLGVRVGEDITLEQLEG-EFDAVFVAIGAQLGKRLPIPGEDAAGVLDAVDFLRAVGEGE--------PPFLGKRVV 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 588 VIGGGNTAMDSVRTARRLGAEHAMIIYRRSEEEMPARLEEVKHAKEEGVEFLTLHNPIEYIADEKGRVKQVVlQKMELGE 667
Cdd:PRK12771 272 VIGGGNTAMDAARTARRLGAEEVTIVYRRTREDMPAHDEEIEEALREGVEINWLRTPVEIEGDENGATGLRV-ITVEKME 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 668 PDASGRRSPIAipGATETIDIDMAIVSVGVSPNPIVPSSIPGLELGRkGTIAVNEN-MQSSIPTIYAGGDIVRGGATVIL 746
Cdd:PRK12771 351 LDEDGRPSPVT--GEEETLEADLVVLAIGQDIDSAGLESVPGVEVGR-GVVQVDPNfMMTGRPGVFAGGDMVPGPRTVTT 427
|
410
....*....|....*..
gi 1474009758 747 AMGDGRKAAASMHAQLS 763
Cdd:PRK12771 428 AIGHGKKAARNIDAFLG 444
|
|
| PRK12769 |
PRK12769 |
putative oxidoreductase Fe-S binding subunit; Reviewed |
298-758 |
7.96e-98 |
|
putative oxidoreductase Fe-S binding subunit; Reviewed
Pssm-ID: 183733 [Multi-domain] Cd Length: 654 Bit Score: 317.07 E-value: 7.96e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 298 AMKPKERMAI--PRVKMNELDAEYRShSRKEEVNLGLNEEQAITEAKRCLDCPNPT-CMNGCPVGINIPKFIKNIERGEF 374
Cdd:PRK12769 180 AMSKVEQMQAtpPRGEPDKLAIEARK-TGFDEIYLPFRADQAQREASRCLKCGEHSiCEWTCPLHNHIPQWIELVKAGNI 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 375 LEAAKTLKATSALPAVCGRVCPQEKQCESQCThLKAGHEAVAIGYLERFAADYERESG-QISVPEVaEKNNIKVAVIGSG 453
Cdd:PRK12769 259 DAAVELSHQTNSLPEITGRVCPQDRLCEGACT-LRDEYGAVTIGNIERYISDQALAKGwRPDLSQV-TKSDKRVAIIGAG 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 454 PAGLSFAGDMAKQGYDVTVFEALHEIGGVLKYGIPEFRLPNKIVDVEIDNLSKMGVKFMKDCIVGKTISVEDLeAEDFKG 533
Cdd:PRK12769 337 PAGLACADVLARNGVAVTVYDRHPEIGGLLTFGIPAFKLDKSLLARRREIFSAMGIEFELNCEVGKDISLESL-LEDYDA 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 534 IFVASG------AGLPNfmnipgENSINIMSSNEYL---TRvNLMD-AASEDSDTPVTFGKRVAVIGGGNTAMDSVRTAR 603
Cdd:PRK12769 416 VFVGVGtyrsmkAGLPN------EDAPGVYDALPFLianTK-QVMGlEELPEEPFINTAGLNVVVLGGGDTAMDCVRTAL 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 604 RLGAEHAMIIYRRSEEEMPARLEEVKHAKEEGVEFLTLHNPIEYIADEKGRVKQVVLQKMELGEPDASGRRSPIAIPGAT 683
Cdd:PRK12769 489 RHGASNVTCAYRRDEANMPGSKKEVKNAREEGANFEFNVQPVALELNEQGHVCGIRFLRTRLGEPDAQGRRRPVPIPGSE 568
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1474009758 684 ETIDIDMAIVSVGVSPNPIVPSSIPGLELGRKGTIAVNEN----MQSSIPTIYAGGDIVRGGATVILAMGDGRKAAASM 758
Cdd:PRK12769 569 FVMPADAVIMAFGFNPHGMPWLESHGVTVDKWGRIIADVEsqyrYQTSNPKIFAGGDAVRGADLVVTAMAEGRHAAQGI 647
|
|
| PRK12809 |
PRK12809 |
putative oxidoreductase Fe-S binding subunit; Reviewed |
292-758 |
4.86e-89 |
|
putative oxidoreductase Fe-S binding subunit; Reviewed
Pssm-ID: 183762 [Multi-domain] Cd Length: 639 Bit Score: 293.47 E-value: 4.86e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 292 RASLRKAMKPKErmaiPRVKMNELDAEYRSHsRKEEVNLGLNEEQAITEAKRCLDCPNPT-CMNGCPVGINIPKFIKNIE 370
Cdd:PRK12809 163 QPSRSAALLPVN----SRKGADKISASERKT-HFGEIYCGLDPQQATYESDRCVYCAEKAnCNWHCPLHNAIPDYIRLVQ 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 371 RGEFLEAAKTLKATSALPAVCGRVCPQEKQCESQCThLKAGHEAVAIGYLERFAADYERESGQI-SVPEVAEKNNiKVAV 449
Cdd:PRK12809 238 EGKIIEAAELCHQTSSLPEICGRVCPQDRLCEGACT-LKDHSGAVSIGNLERYITDTALAMGWRpDVSKVVPRSE-KVAV 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 450 IGSGPAGLSFAGDMAKQGYDVTVFEALHEIGGVLKYGIPEFRLPNKIVDVEIDNLSKMGVKFMKDCIVGKTISVEDLeAE 529
Cdd:PRK12809 316 IGAGPAGLGCADILARAGVQVDVFDRHPEIGGMLTFGIPPFKLDKTVLSQRREIFTAMGIDFHLNCEIGRDITFSDL-TS 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 530 DFKGIFVasGAGLPNFM--NIPGENSINIMSSNEYLT--RVNLMdAASEDSDTPVTF--GKRVAVIGGGNTAMDSVRTAR 603
Cdd:PRK12809 395 EYDAVFI--GVGTYGMMraDLPHEDAPGVIQALPFLTahTRQLM-GLPESEEYPLTDveGKRVVVLGGGDTTMDCLRTSI 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 604 RLGAEHAMIIYRRSEEEMPARLEEVKHAKEEGVEFLTLHNPIEYIADEKGRVKQVVLQKMELGEPDASGRRSPIAIPGAT 683
Cdd:PRK12809 472 RLNAASVTCAYRRDEVSMPGSRKEVVNAREEGVEFQFNVQPQYIACDEDGRLTAVGLIRTAMGEPGPDGRRRPRPVAGSE 551
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1474009758 684 ETIDIDMAIVSVGVSPNPIVPSSIPGLELGRKGTIAVNE----NMQSSIPTIYAGGDIVRGGATVILAMGDGRKAAASM 758
Cdd:PRK12809 552 FELPADVLIMAFGFQAHAMPWLQGSGIKLDKWGLIQTGDvgylPTQTHLKKVFAGGDAVHGADLVVTAMAAGRQAARDM 630
|
|
| PRK13984 |
PRK13984 |
putative oxidoreductase; Provisional |
309-765 |
4.25e-85 |
|
putative oxidoreductase; Provisional
Pssm-ID: 172486 [Multi-domain] Cd Length: 604 Bit Score: 281.66 E-value: 4.25e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 309 RVKMNELDAEYRSHSRKEEVNlGLNEEQAITEAKRCLDCPnpTCMNGCPVGINIPKFIKNIERGEFLEAAKTLKATSALP 388
Cdd:PRK13984 153 RVEMEEIPPEERVKSFIEIVK-GYSKEQAMQEAARCVECG--ICTDTCPAHMDIPQYIKAIYKDDLEEGLRWLYKTNPLS 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 389 AVCGRVCPQekQCESQCThlkAGH--EAVAIGYLERFAADY--ERESGQIsVPEVAEKNNIKVAVIGSGPAGLSFAGDMA 464
Cdd:PRK13984 230 MVCGRVCTH--KCETVCS---IGHrgEPIAIRWLKRYIVDNvpVEKYSEI-LDDEPEKKNKKVAIVGSGPAGLSAAYFLA 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 465 KQGYDVTVFEALHEIGGVLKYGIPEFRLPNKIVDVEIDNLSKMGVKFMKDCIVGKTISVEDLEaEDFKGIFVASGAGLPN 544
Cdd:PRK13984 304 TMGYEVTVYESLSKPGGVMRYGIPSYRLPDEALDKDIAFIEALGVKIHLNTRVGKDIPLEELR-EKHDAVFLSTGFTLGR 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 545 FMNIPGENSINIMSSNEYLTRV-NLMDAASEDSDTPvtfgKRVAVIGGGNTAMDSVRTARRLG------AEHAMIIYRRS 617
Cdd:PRK13984 383 STRIPGTDHPDVIQALPLLREIrDYLRGEGPKPKIP----RSLVVIGGGNVAMDIARSMARLQkmeygeVNVKVTSLERT 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 618 EEEMPARLEEVKHAKEEGVEFLTLHNPIEYIADEkGRVKQVVLQKMeLGEPDASGRRSPIAIPGATETIDIDMAIVSVGV 697
Cdd:PRK13984 459 FEEMPADMEEIEEGLEEGVVIYPGWGPMEVVIEN-DKVKGVKFKKC-VEVFDEEGRFNPKFDESDQIIVEADMVVEAIGQ 536
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 698 SPN-PIVPSSI-PGLELGRkGTIAVNENMQSSIPTIYAGGDIVRgGATVILAMGDGRKAAASMHAQLSSK 765
Cdd:PRK13984 537 APDySYLPEELkSKLEFVR-GRILTNEYGQTSIPWLFAGGDIVH-GPDIIHGVADGYWAAEGIDMYLRKQ 604
|
|
| PRK12770 |
PRK12770 |
putative glutamate synthase subunit beta; Provisional |
438-765 |
2.58e-83 |
|
putative glutamate synthase subunit beta; Provisional
Pssm-ID: 237197 [Multi-domain] Cd Length: 352 Bit Score: 268.78 E-value: 2.58e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 438 EVAEKNNIKVAVIGSGPAGLSFAGDMAKQGYDVTVFEALHEIGGVLKYGIPEFRLPNKIVDVEIDNLSKMGVKF------ 511
Cdd:PRK12770 12 EKPPPTGKKVAIIGAGPAGLAAAGYLACLGYEVHVYDKLPEPGGLMLFGIPEFRIPIERVREGVKELEEAGVVFhtrtkv 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 512 ---------MKDCIVGKTISVEDLeAEDFKGIFVASGAGLPNFMNIPGENSINIMSSNEYLTRVNLMDAASEDSDT-PVT 581
Cdd:PRK12770 92 ccgeplheeEGDEFVERIVSLEEL-VKKYDAVLIATGTWKSRKLGIPGEDLPGVYSALEYLFRIRAAKLGYLPWEKvPPV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 582 FGKRVAVIGGGNTAMDSVRTARRLGAEHAMIIYRRSEEEMPARLEEVKHAKEEGVEFLTLHNPIEYIADekGRVKQVVLQ 661
Cdd:PRK12770 171 EGKKVVVVGAGLTAVDAALEAVLLGAEKVYLAYRRTINEAPAGKYEIERLIARGVEFLELVTPVRIIGE--GRVEGVELA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 662 KMELGEPDASGRRSPIAIPGATETIDIDMAIVSVGVSPNPIVPSSIPGLELGRKGTIAVNENMQSSIPTIYAGGDIVRGG 741
Cdd:PRK12770 249 KMRLGEPDESGRPRPVPIPGSEFVLEADTVVFAIGEIPTPPFAKECLGIELNRKGEIVVDEKHMTSREGVFAAGDVVTGP 328
|
330 340
....*....|....*....|....
gi 1474009758 742 ATVILAMGDGRKAAASMHAQLSSK 765
Cdd:PRK12770 329 SKIGKAIKSGLRAAQSIHEWLDLK 352
|
|
| Mcr1 |
COG0543 |
NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion]; ... |
3-249 |
2.97e-80 |
|
NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion];
Pssm-ID: 440309 [Multi-domain] Cd Length: 247 Bit Score: 257.10 E-value: 2.97e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 3 KIISKEHFSEKVFKLVIEAPLIAKSRKAGHFVIVRVGEKGERMPLTIAGADPVKGTITLVVQEVGLSSTRLCELNEGDYI 82
Cdd:COG0543 1 KVVSVERLAPDVYLLRLEAPLIALKFKPGQFVMLRVPGDGLRRPFSIASAPREDGTIELHIRVVGKGTRALAELKPGDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 83 tDVVGPLGKATHIENF-----------GTvvcagggvgvAPMLPIVQALKAAGNRVITVLAGRTKELIILEKEMRESSD- 150
Cdd:COG0543 81 -DVRGPLGNGFPLEDSgrpvllvaggtGL----------APLRSLAEALLARGRRVTLYLGARTPEDLYLLDELEALADf 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 151 EVIIMTDDGSYGHKGLVTEGVEEVIKRETVNKCFAIGPAIMMKFVCLLTKKYEIPTD---VSLNTIMVDGTGMCGACRIT 227
Cdd:COG0543 150 RVVVTTDDGWYGRKGFVTDALKELLAEDSGDDVYACGPPPMMKAVAELLLERGVPPEriyVSLERRMACGIGMCGGCVVP 229
|
250 260
....*....|....*....|..
gi 1474009758 228 VGGktrfVCVDGPEFDGHQVDF 249
Cdd:COG0543 230 VGG----GCKDGPVFDAAEVDW 247
|
|
| GOGAT_sm_gam |
TIGR01317 |
glutamate synthases, NADH/NADPH, small subunit; This model represents one of three built for ... |
300-757 |
3.55e-73 |
|
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: 246.28 E-value: 3.55e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 300 KPKERMAIPRVKMNELDAEYRSHSRKEeVNLGLNEEQAITEAKRCLDCPNPTCMN--GCPVGINIPKFIKNIERGEFLEA 377
Cdd:TIGR01317 1 KPTGFLEYKRRKPTERDPRTRLKDWKE-FTNPFDKESAKYQAARCMDCGTPFCHNdsGCPLNNLIPEFNDLVFRGRWKEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 378 AKTLKATSALPAVCGRVCPQEkqCESQCThLKAGHEAVAIGYLERFAADYERESGQISvPEVAEK-NNIKVAVIGSGPAG 456
Cdd:TIGR01317 80 LDRLHATNNFPEFTGRVCPAP--CEGACT-LGISEDPVGIKSIERIIIDKGFQEGWVQ-PRPPSKrTGKKVAVVGSGPAG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 457 LSFAGDMAKQGYDVTVFEALHEIGGVLKYGIPEFRLPNKIVDVEIDNLSKMGVKFMKDCIVGKTISVEDLEaEDFKGIFV 536
Cdd:TIGR01317 156 LAAADQLNRAGHTVTVFEREDRCGGLLMYGIPNMKLDKAIVDRRIDLLSAEGIDFVTNTEIGVDISADELK-EQFDAVVL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 537 ASGAGLPNFMNIPGENSINIMSSNEYL---TRVNLmDAASEDSDTPVTFGKRVAVIGGGNTAMDSVRTARRLGAE--HAM 611
Cdd:TIGR01317 235 AGGATKPRDLPIPGRELKGIHYAMEFLpsaTKALL-GKDFKDIIFIKAKGKKVVVIGGGDTGADCVGTSLRHGAAsvHQF 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 612 IIYRRSEEEMPA--------RLEEVKHAKEEGVEFLTlHNPIEY-------IADEKGRVKQVVLQKMELgEPDASGRRSP 676
Cdd:TIGR01317 314 EIMPKPPEARAKdnpwpewpRVYRVDYAHEEAAAHYG-RDPREYsiltkefIGDDEGKVTALRTVRVEW-KKSQDGKWQF 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 677 IAIPGATETIDIDMAIVSVG-VSPNPIVPSSIpGLELGRKGTI-AVNENMQSSIPTIYAGGDIVRGGATVILAMGDGRKA 754
Cdd:TIGR01317 392 VEIPGSEEVFEADLVLLAMGfVGPEQILLDDF-GVKKTRRGNIsAGYDDYSTSIPGVFAAGDCRRGQSLIVWAINEGRKA 470
|
...
gi 1474009758 755 AAS 757
Cdd:TIGR01317 471 AAA 473
|
|
| PRK12779 |
PRK12779 |
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; ... |
3-269 |
3.64e-63 |
|
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; Provisional
Pssm-ID: 183740 [Multi-domain] Cd Length: 944 Bit Score: 228.18 E-value: 3.64e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 3 KIISKEHFSEKVFKLVIEAPLIAKSRKAGHFVIVRVGEKGERMPLTIAGADPVKGTITLVVQEVGLSSTRLCELNEGDYI 82
Cdd:PRK12779 652 TIVGKVQLAGGIVEFTVRAPMVARSAQAGQFVRVLPWEKGELIPLTLADWDAEKGTIDLVVQGMGTSSLEINRMAIGDAF 731
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 83 TDVVGPLGKATHIENF---GTVVCAGGGVGVAPMLPIVQALKAAGNRVITVLAGRTKELII-------LEKEMRESSD-- 150
Cdd:PRK12779 732 SGIAGPLGRASELHRYegnQTVVFCAGGVGLPPVYPIMRAHLRLGNHVTLISGFRAKEFLFwtgdderVGKLKAEFGDql 811
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 151 EVIIMTDDGSYGHKGLVTEGVEEVIKR------ETVNKCFAIGPAIMMKFVCLLTKKYEIPTDVSLNTIMVDGTGMCGAC 224
Cdd:PRK12779 812 DVIYTTNDGSFGVKGFVTGPLEEMLKAnqqgkgRTIAEVIAIGPPLMMRAVSDLTKPYGVKTVASLNSIMVDATGMCGAC 891
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1474009758 225 RI--TVGGKT--RFVCVDGPEFDGHQVDFDEMLKRMGAFKDIEKEEIHK 269
Cdd:PRK12779 892 MVpvTIDGKMvrKHACIDGPEIDAHIIDWDKFLPRFNQFKAQELESKKK 940
|
|
| Fer4_20 |
pfam14691 |
Dihydroprymidine dehydrogenase domain II, 4Fe-4S cluster; Domain II of the enzyme ... |
326-432 |
3.22e-56 |
|
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: 187.75 E-value: 3.22e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 326 EEVNLGLNEEQAITEAKRCLDCPNPTCMNGCPVGINIPKFIKNIERGEFLEAAKTLKATSALPAVCGRVCPQEKQCESQC 405
Cdd:pfam14691 6 EEVALGYTEEEAIAEASRCLQCKDPPCVKGCPVHIDIPEFIKLIAEGNFEGAARIILETNPLPAICGRVCPQERQCEGAC 85
|
90 100
....*....|....*....|....*..
gi 1474009758 406 THLKAGHEAVAIGYLERFAADYERESG 432
Cdd:pfam14691 86 VLGKKGFEPVAIGRLERFAADWARENG 112
|
|
| DHOD_e_trans_like |
cd06192 |
FAD/NAD binding domain (electron transfer subunit) of dihydroorotate dehydrogenase-like ... |
4-243 |
6.99e-50 |
|
FAD/NAD binding domain (electron transfer subunit) of dihydroorotate dehydrogenase-like proteins. Dihydroorotate dehydrogenases (DHODs) catalyze the only redox reaction in pyrimidine de novo biosynthesis. They catalyze the oxidation of (S)-dihydroorotate to orotate coupled with the reduction of NAD+. In L. lactis, DHOD B (encoded by pyrDa) is co-expressed with pyrK and both gene products are required for full activity, as well as NAD binding. NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer between an NAD(P)-binding domain of the alpha/beta class and a discrete (usually N-terminal) domain which vary in orientation with respect to the NAD(P) binding domain. The N-terminal domain may contain a flavin prosthetic group (as in flavoenzymes) or use flavin as a substrate. Ferredoxin is reduced in the final stage of photosystem I. The flavoprotein Ferredoxin-NADP+ reductase transfers electrons from reduced ferredoxin to FAD (forming FADH2 via a semiquinone intermediate) which then transfers a hydride ion to convert NADP+ to NADPH.
Pssm-ID: 99789 [Multi-domain] Cd Length: 243 Bit Score: 175.21 E-value: 6.99e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 4 IISKEHFSEKVFKLVIEAPLIAKSRKAGHFVIVRVGE--KGERMPLTIAGADPVKGTITLVVQEVGLSSTRLCELNEGDY 81
Cdd:cd06192 1 IVKKEQLEPNLVLLTIKAPLAARLFRPGQFVFLRNFEspGLERIPLSLAGVDPEEGTISLLVEIRGPKTKLIAELKPGEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 82 ItDVVGPLGKATHIENF-GTVVCAGGGVGVAPMLPIVQALKAAGNRVITVLAGRTKELIILEKEMRESSDEVIIMTDDGS 160
Cdd:cd06192 81 L-DVMGPLGNGFEGPKKgGTVLLVAGGIGLAPLLPIAKKLAANGNKVTVLAGAKKAKEEFLDEYFELPADVEIWTTDDGE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 161 YGHKGLVTEgVEEVIKRETVNKCFAIGPAIMMKFVC--LLTKKYEIPTDVSLNTIMVDGTGMCGACRITVGGKTRFVCVD 238
Cdd:cd06192 160 LGLEGKVTD-SDKPIPLEDVDRIIVAGSDIMMKAVVeaLDEWLQLIKASVSNNSPMCCGIGICGACTIETKHGVKRLCKD 238
|
....*
gi 1474009758 239 GPEFD 243
Cdd:cd06192 239 GPVFR 243
|
|
| DHOD_e_trans |
cd06218 |
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase. ... |
4-243 |
2.29e-49 |
|
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase. Dihydroorotate dehydrogenases (DHODs) catalyze the only redox reaction in pyrimidine de novo biosynthesis. They catalyze the oxidation of (S)-dihydroorotate to orotate coupled with the reduction of NAD+. In L. lactis, DHOD B (encoded by pyrDa) is co-expressed with pyrK and both gene products are required for full activity, as well as 3 cofactors: FMN, FAD, and an [2Fe-2S] cluster.
Pssm-ID: 99814 [Multi-domain] Cd Length: 246 Bit Score: 173.89 E-value: 2.29e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 4 IISKEHFSEKVFKLVIEAPLIAKSRKAGHFVIVRVGEKGE---RMPLTIAGADPVKGTITLVVQEVGLSSTRLCELNEGD 80
Cdd:cd06218 1 VLSNREIADDIYRLVLEAPEIAAAAKPGQFVMLRVPDGSDpllRRPISIHDVDPEEGTITLLYKVVGKGTRLLSELKAGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 81 YItDVVGPLGKATHIENF-----------GTVvcagggvgvaPMLPIVQALKAAGNRVITVLAGRTKELIILEKEMRESS 149
Cdd:cd06218 81 EL-DVLGPLGNGFDLPDDdgkvllvgggiGIA----------PLLFLAKQLAERGIKVTVLLGFRSADDLFLVEEFEALG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 150 DEVIIMTDDGSYGHKGLVTEGVEEVIKRETVNKCFAIGPAIMMKFVCLLTKKYEIPTDVSLNTIMVDGTGMCGACRITVG 229
Cdd:cd06218 150 AEVYVATDDGSAGTKGFVTDLLKELLAEARPDVVYACGPEPMLKAVAELAAERGVPCQVSLEERMACGIGACLGCVVKTK 229
|
250
....*....|....*..
gi 1474009758 230 GKTRF---VCVDGPEFD 243
Cdd:cd06218 230 DDEGGykrVCKDGPVFD 246
|
|
| PRK00054 |
PRK00054 |
dihydroorotate dehydrogenase electron transfer subunit; Reviewed |
3-247 |
3.63e-36 |
|
dihydroorotate dehydrogenase electron transfer subunit; Reviewed
Pssm-ID: 234601 [Multi-domain] Cd Length: 250 Bit Score: 136.93 E-value: 3.63e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 3 KIISKEHFSEKVFKLVIEAPLIAKSrKAGHFVIVRV--GEKGERMPLTIAGADpvKGTITLVVQEVGLSSTRLCELNEGD 80
Cdd:PRK00054 8 KIVENKEIAPNIYTLVLDGEKVFDM-KPGQFVMVWVpgVEPLLERPISISDID--KNEITILYRKVGEGTKKLSKLKEGD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 81 YItDVVGPLGKATHIENFG-TVVCAGGGVGVAPMLPIVQALKAAGNRVITVLAGRTKELIILEKEMrESSDEVIIMTDDG 159
Cdd:PRK00054 85 EL-DIRGPLGNGFDLEEIGgKVLLVGGGIGVAPLYELAKELKKKGVEVTTVLGARTKDEVIFEEEF-AKVGDVYVTTDDG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 160 SYGHKGLVTEGVEEVikRETVNKCFAIGPAIMMKFVCLLTKKYEIPTDVSLNTIMVDGTGMCGACRITVGGKTRFVCVDG 239
Cdd:PRK00054 163 SYGFKGFVTDVLDEL--DSEYDAIYSCGPEIMMKKVVEILKEKKVPAYVSLERRMKCGIGACGACVCDTETGGKRVCKDG 240
|
....*...
gi 1474009758 240 PEFDGHQV 247
Cdd:PRK00054 241 PVFSGGEL 248
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
446-751 |
5.62e-33 |
|
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: 129.36 E-value: 5.62e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 446 KVAVIGSGPAGLSFAGDMAKQGYDVTVFEA---LHEIGGVLKYGI-------PEFRLPNKIVDV--EIDNLSKMGVKFM- 512
Cdd:pfam07992 2 DVVVIGGGPAGLAAALTLAQLGGKVTLIEDegtCPYGGCVLSKALlgaaeapEIASLWADLYKRkeEVVKKLNNGIEVLl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 513 ----------KDCIVGKTISVEDLEAEDFKGIFVASGAGlPNFMNIPGENSINImssneYLTRVnLMDA-ASEDSDTPvt 581
Cdd:pfam07992 82 gtevvsidpgAKKVVLEELVDGDGETITYDRLVIATGAR-PRLPPIPGVELNVG-----FLVRT-LDSAeALRLKLLP-- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 582 fgKRVAVIGGGNTAMDSVRTARRLGAEhAMIIYRRSE--EEMPARLEEV--KHAKEEGVEFLTLHNPIEYIADEKGrvkq 657
Cdd:pfam07992 153 --KRVVVVGGGYIGVELAAALAKLGKE-VTLIEALDRllRAFDEEISAAleKALEKNGVEVRLGTSVKEIIGDGDG---- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 658 vvlQKMELGEPDasgrrspiaipgateTIDIDMAIVSVGVSPNPIVPSSIpGLELGRKGTIAVNENMQSSIPTIYAGGDI 737
Cdd:pfam07992 226 ---VEVILKDGT---------------EIDADLVVVAIGRRPNTELLEAA-GLELDERGGIVVDEYLRTSVPGIYAAGDC 286
|
330
....*....|....*
gi 1474009758 738 -VRGGATVILAMGDG 751
Cdd:pfam07992 287 rVGGPELAQNAVAQG 301
|
|
| DHOD_e_trans_like2 |
cd06220 |
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase-like ... |
31-246 |
5.85e-31 |
|
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase-like proteins. Dihydroorotate dehydrogenases (DHODs) catalyze the only redox reaction in pyrimidine de novo biosynthesis. They catalyze the oxidation of (S)-dihydroorotate to orotate coupled with the reduction of NAD+. In L. lactis, DHOD B (encoded by pyrDa) is co-expressed with pyrK and both gene products are required for full activity, as well as 3 cofactors: FMN, FAD, and an [2Fe-2S] cluster.
Pssm-ID: 99816 [Multi-domain] Cd Length: 233 Bit Score: 121.20 E-value: 5.85e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 31 GHFVIV---RVGEKgermPLTIAGADPVKGtitLVVQEVGLSSTRLCELNEGDYITdVVGPLGKATHIENfGTVVCAGGG 107
Cdd:cd06220 27 GQFVMVwvpGVDEI----PMSLSYIDGPNS---ITVKKVGEATSALHDLKEGDKLG-IRGPYGNGFELVG-GKVLLIGGG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 108 VGVAPMLPIVQALKAAgNRVITVLAGRTKELIILEKEMReSSDEVIIMTDDGSYGHKGLVTEGVEEvIKRETVNKCFAIG 187
Cdd:cd06220 98 IGIAPLAPLAERLKKA-ADVTVLLGARTKEELLFLDRLR-KSDELIVTTDDGSYGFKGFVTDLLKE-LDLEEYDAIYVCG 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1474009758 188 PAIMMKFVCLLTKKYEIPTDVSLNTIMVDGTGMCGACRITVGGKTrfVCVDGPEFDGHQ 246
Cdd:cd06220 175 PEIMMYKVLEILDERGVRAQFSLERYMKCGIGICGSCCIDPTGLR--VCRDGPVFDGEQ 231
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
446-765 |
6.00e-28 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 114.83 E-value: 6.00e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 446 KVAVIGSGPAGLSFAGDMAKQGYDVTVFEALhEIGGVLK--------YGIPEFRLPNKIVDVEIDNLSKMGVKFMKDCIV 517
Cdd:COG0492 2 DVVIIGAGPAGLTAAIYAARAGLKTLVIEGG-EPGGQLAttkeienyPGFPEGISGPELAERLREQAERFGAEILLEEVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 518 G-------KTISVEDLEAEDFKGIFVASGAGlPNFMNIPGENsinimssnEYLTRvNLMDAASedSDTPVTFGKRVAVIG 590
Cdd:COG0492 81 SvdkddgpFRVTTDDGTEYEAKAVIIATGAG-PRKLGLPGEE--------EFEGR-GVSYCAT--CDGFFFRGKDVVVVG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 591 GGNTAMDSVRTARRLGAEHAMIIYR---RSEEEMPARLEEVkhakeEGVEFLTLHNPIEYIADekGRVKQVVLQKMELGE 667
Cdd:COG0492 149 GGDSALEEALYLTKFASKVTLIHRRdelRASKILVERLRAN-----PKIEVLWNTEVTEIEGD--GRVEGVTLKNVKTGE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 668 pdasgrrspiaipgaTETIDIDMAIVSVGVSPNP-IVPSSipGLELGRKGTIAVNENMQSSIPTIYAGGDIVRGG-ATVI 745
Cdd:COG0492 222 ---------------EKELEVDGVFVAIGLKPNTeLLKGL--GLELDEDGYIVVDEDMETSVPGVFAAGDVRDYKyRQAA 284
|
330 340
....*....|....*....|
gi 1474009758 746 LAMGDGRKAAASMHAQLSSK 765
Cdd:COG0492 285 TAAGEGAIAALSAARYLEPL 304
|
|
| sulfite_reductase_like |
cd06221 |
Anaerobic sulfite reductase contains an FAD and NADPH binding module with structural ... |
12-243 |
7.20e-22 |
|
Anaerobic sulfite reductase contains an FAD and NADPH binding module with structural similarity to ferredoxin reductase and sequence similarity to dihydroorotate dehydrogenases. Clostridium pasteurianum inducible dissimilatory type sulfite reductase is linked to ferredoxin and reduces NH2OH and SeO3 at a lesser rate than it's normal substate SO3(2-). Dihydroorotate dehydrogenases (DHODs) catalyze the only redox reaction in pyrimidine de novo biosynthesis. They catalyze the oxidation of (S)-dihydroorotate to orotate coupled with the reduction of NAD+.
Pssm-ID: 99817 [Multi-domain] Cd Length: 253 Bit Score: 95.75 E-value: 7.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 12 EKVFKLVIEAPLIAKSR-KAGHFVIV---RVGEKgermPLTIAGADPVKGTITLVVQEVGLSSTRLCELNEGDYITdVVG 87
Cdd:cd06221 11 IKTFTLRLEDDDEELFTfKPGQFVMLslpGVGEA----PISISSDPTRRGPLELTIRRVGRVTEALHELKPGDTVG-LRG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 88 PLGKATHIENFGTVVCAGGG--VGVAPMLPIVQALKAAGNRV--ITVLAG-RTKELIILEKEM---RESSD-EVIIMTDD 158
Cdd:cd06221 86 PFGNGFPVEEMKGKDLLLVAggLGLAPLRSLINYILDNREDYgkVTLLYGaRTPEDLLFKEELkewAKRSDvEVILTVDR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 159 GSY---GHKGLVTEGVEEVikRETVNKCFAI--GPAIMMKFVCLLTKKYEIPTD---VSLNTIMVDGTGMCGACRItvGG 230
Cdd:cd06221 166 AEEgwtGNVGLVTDLLPEL--TLDPDNTVAIvcGPPIMMRFVAKELLKLGVPEEqiwVSLERRMKCGVGKCGHCQI--GP 241
|
250
....*....|...
gi 1474009758 231 KtrFVCVDGPEFD 243
Cdd:cd06221 242 K--YVCKDGPVFS 252
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
447-756 |
1.26e-21 |
|
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: 98.62 E-value: 1.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 447 VAVIGSGPAGLSFAGDMAKQGYDVTVFEAlHEIGGV-------------------------LKYGI----PEFRLP--NK 495
Cdd:COG1249 6 LVVIGAGPGGYVAAIRAAQLGLKVALVEK-GRLGGTclnvgcipskallhaaevahearhaAEFGIsagaPSVDWAalMA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 496 IVDVEIDNLSKMGVKFMK----DCIVG-------KTISVEDLEAEDFKGIFVASGAgLPNFMNIPGENSINIMSSNE--Y 562
Cdd:COG1249 85 RKDKVVDRLRGGVEELLKkngvDVIRGrarfvdpHTVEVTGGETLTADHIVIATGS-RPRVPPIPGLDEVRVLTSDEalE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 563 LTRVnlmdaasedsdtPvtfgKRVAVIGGGNTAMD--SVrtARRLGAEHAMIIY-----RRSEEEMPARLEevKHAKEEG 635
Cdd:COG1249 164 LEEL------------P----KSLVVIGGGYIGLEfaQI--FARLGSEVTLVERgdrllPGEDPEISEALE--KALEKEG 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 636 VEFLTLHNPIEYIADEKGrvKQVVLQKmelgepdasgrrspiaiPGATETIDIDMAIVSVGVSPNpivpssIPGL----- 710
Cdd:COG1249 224 IDILTGAKVTSVEKTGDG--VTVTLED-----------------GGGEEAVEADKVLVATGRRPN------TDGLgleaa 278
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1474009758 711 --ELGRKGTIAVNENMQSSIPTIYAGGDIVRGGATVILAMGDGRKAAA 756
Cdd:COG1249 279 gvELDERGGIKVDEYLRTSVPGIYAIGDVTGGPQLAHVASAEGRVAAE 326
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
469-758 |
1.81e-19 |
|
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: 90.26 E-value: 1.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 469 DVTVFEALHEIGGvLKYGIP-----EFRLPNKIVDVEIDNLSKMGVKFMKDCIV------GKTISVEDLEAEDFKGIFVA 537
Cdd:COG0446 7 EITVIEKGPHHSY-QPCGLPyyvggGIKDPEDLLVRTPESFERKGIDVRTGTEVtaidpeAKTVTLRDGETLSYDKLVLA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 538 SGAgLPNFMNIPGENSINIMSsneyLTRVNLMDAASEDSDTPVtfGKRVAVIGGGNTAMDSVRTARRLGAEhAMIIYR-- 615
Cdd:COG0446 86 TGA-RPRPPPIPGLDLPGVFT----LRTLDDADALREALKEFK--GKRAVVIGGGPIGLELAEALRKRGLK-VTLVERap 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 616 ----RSEEEMPARLEEvkHAKEEGVEFLTLHNPIEYIADEKGRVKQvvlqkmelgepdASGrrspiaipgatETIDIDMA 691
Cdd:COG0446 158 rllgVLDPEMAALLEE--ELREHGVELRLGETVVAIDGDDKVAVTL------------TDG-----------EEIPADLV 212
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1474009758 692 IVSVGVSPNPIVPSSIpGLELGRKGTIAVNENMQSSIPTIYAGGDIVR-----GGATVILAMGD-----GRKAAASM 758
Cdd:COG0446 213 VVAPGVRPNTELAKDA-GLALGERGWIKVDETLQTSDPDVYAAGDCAEvphpvTGKTVYIPLASaankqGRVAAENI 288
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
447-738 |
2.05e-13 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 73.29 E-value: 2.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 447 VAVIGSGPAGLSFAGDMAKQGYDVTVFE------------------------ALHEIGGVLKYGI----PEFRLP----- 493
Cdd:PRK06292 6 VIVIGAGPAGYVAARRAAKLGKKVALIEkgplggtclnvgcipskaliaaaeAFHEAKHAEEFGIhadgPKIDFKkvmar 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 494 -NKIVD-----VEIDNLSKMGVKFMKDC--IVG-KTISVEDLEAEdFKGIFVASGAGLPNfmnIPGENSINimsSNEYLT 564
Cdd:PRK06292 86 vRRERDrfvggVVEGLEKKPKIDKIKGTarFVDpNTVEVNGERIE-AKNIVIATGSRVPP---IPGVWLIL---GDRLLT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 565 rvnlMDAASEDSDTPvtfgKRVAVIGGGNTAMDsvrTA---RRLGAEHAMI-----IYRRSEEEMPARLEEvKHAKEegV 636
Cdd:PRK06292 159 ----SDDAFELDKLP----KSLAVIGGGVIGLE---LGqalSRLGVKVTVFergdrILPLEDPEVSKQAQK-ILSKE--F 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 637 EFLTLHNPIEYiadEKGRVKQVVLQKMElgepdasgrrspiaipGATETIDIDMAIVSVGVSPNpiVPSSIP---GLELG 713
Cdd:PRK06292 225 KIKLGAKVTSV---EKSGDEKVEELEKG----------------GKTETIEADYVLVATGRRPN--TDGLGLentGIELD 283
|
330 340
....*....|....*....|....*
gi 1474009758 714 RKGTIAVNENMQSSIPTIYAGGDIV 738
Cdd:PRK06292 284 ERGRPVVDEHTQTSVPGIYAAGDVN 308
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
446-758 |
2.82e-13 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 72.48 E-value: 2.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 446 KVAVIGSGPAGLSFAGDMAKQGYD--VTVFEA-------------------------LHEIGGVLKYGIpEFRLPNKIVD 498
Cdd:COG1251 3 RIVIIGAGMAGVRAAEELRKLDPDgeITVIGAephppynrpplskvlagetdeedllLRPADFYEENGI-DLRLGTRVTA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 499 VEIDNlskmgvkfmkdcivgKTISVEDLEAEDFKGIFVASGAGlPNFMNIPGENSINIMSsneYLTR---VNLMDAASEd 575
Cdd:COG1251 82 IDRAA---------------RTVTLADGETLPYDKLVLATGSR-PRVPPIPGADLPGVFT---LRTLddaDALRAALAP- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 576 sdtpvtfGKRVAVIGGGNTAMDSVRTARRLGAE----HAM--IIYRRSEEEMPARLEEvkHAKEEGVEFLTLHNPIEYIA 649
Cdd:COG1251 142 -------GKRVVVIGGGLIGLEAAAALRKRGLEvtvvERAprLLPRQLDEEAGALLQR--LLEALGVEVRLGTGVTEIEG 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 650 DekGRVKQVVLqkmelgepdASGrrspiaipgatETIDIDMAIVSVGVSPN-PIVPSSipGLELGRkGtIAVNENMQSSI 728
Cdd:COG1251 213 D--DRVTGVRL---------ADG-----------EELPADLVVVAIGVRPNtELARAA--GLAVDR-G-IVVDDYLRTSD 266
|
330 340 350
....*....|....*....|....*....|....*....
gi 1474009758 729 PTIYAGGDIVR------GGATVIL---AMGDGRKAAASM 758
Cdd:COG1251 267 PDIYAAGDCAEhpgpvyGRRVLELvapAYEQARVAAANL 305
|
|
| PRK05802 |
PRK05802 |
sulfide/dihydroorotate dehydrogenase-like FAD/NAD-binding protein; |
3-231 |
1.63e-12 |
|
sulfide/dihydroorotate dehydrogenase-like FAD/NAD-binding protein;
Pssm-ID: 235613 [Multi-domain] Cd Length: 320 Bit Score: 69.24 E-value: 1.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 3 KIISKEHFSEKVFKLVIEAP--LIAKSRKAGHFVIVRVGEKGE--RMPLTIAGADPVKGTITLVVQEVGLSSTRLCELNE 78
Cdd:PRK05802 68 KIIKKENIEDNLIILTLKVPhkLARDLVYPGSFVFLRNKNSSSffDVPISIMEADTEENIIKVAIEIRGVKTKKIAKLNK 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 79 GDYITdVVGP-----LGkATHIENF--GTVVCAGGGVGVAPMLPIVQALKAAGNRVITVL-AGRTKELIIlEKEMRESSD 150
Cdd:PRK05802 148 GDEIL-LRGPywngiLG-LKNIKSTknGKSLVIARGIGQAPGVPVIKKLYSNGNKIIVIIdKGPFKNNFI-KEYLELYNI 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 151 EVIIMT--DDGSYGHKGlvTEGVEEVIKRETVNKCFAIGPAIMMKFVCLLTKKY--EIPTDVSLNTIMVDGTGMCGACRI 226
Cdd:PRK05802 225 EIIELNllDDGELSEEG--KDILKEIIKKEDINLIHCGGSDILHYKIIEYLDKLneKIKLSCSNNAKMCCGEGICGACTV 302
|
....*
gi 1474009758 227 TVGGK 231
Cdd:PRK05802 303 RYGGH 307
|
|
| DHODB_Fe-S_bind |
pfam10418 |
Iron-sulfur cluster binding domain of dihydroorotate dehydrogenase B; Lactococcus lactis is ... |
211-247 |
2.27e-12 |
|
Iron-sulfur cluster binding domain of dihydroorotate dehydrogenase B; Lactococcus lactis is one of the few organizms with two dihydroorotate dehydrogenases, DHODs, A and B. The B enzyme is a prototype for DHODs in Gram-positive bacteria that use NAD+ as the second substrate. DHODB is a hetero-tetramer composed of a central homodimer of PyrDB subunits resembling the DHODA structure and two PyrK subunits along with three different cofactors: FMN, FAD, and a [2Fe-2S] cluster. The [2Fe-2S] iron-sulfur cluster binds to this C-terminal domain of the PyrK subunit, which is at the interface between the flavin and NAD binding domains and contains three beta-strands. The four cysteine residues at the N-terminal part of this domain are the ones that bind, in pairs, to the iron-sulfur cluster. The conformation of the whole molecule means that the iron-sulfur cluster is localized in a well-ordered part of this domain close to the FAD binding site. The FAD and and NAD binding domains are FAD_binding_6, pfam00970 and NAD_binding_1, pfam00175.
Pssm-ID: 463084 [Multi-domain] Cd Length: 40 Bit Score: 61.85 E-value: 2.27e-12
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1474009758 211 NTIMVDGTGMCGACRITV---GGKTRFVCVDGPEFDGHQV 247
Cdd:pfam10418 1 EERMACGVGACGGCVVKTkggDGEYKRVCVDGPVFDADEV 40
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
449-758 |
5.44e-12 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 68.69 E-value: 5.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 449 VIGSGPAGLSFAGDMAKQGYDVTVFE------------------------ALHEIGGVLKYGIP-------EF-----RL 492
Cdd:PRK06370 10 VIGAGQAGPPLAARAAGLGMKVALIErgllggtcvntgcvptktliasarAAHLARRAAEYGVSvggpvsvDFkavmaRK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 493 pNKIV-----DVE--IDNLSKMGVKFMKDCIVG-KTISVEDlEAEDFKGIFVASGAGlPNFMNIPGENSINimssneYLT 564
Cdd:PRK06370 90 -RRIRarsrhGSEqwLRGLEGVDVFRGHARFESpNTVRVGG-ETLRAKRIFINTGAR-AAIPPIPGLDEVG------YLT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 565 RVNLMDaasedsdtpVTF-GKRVAVIGGGNTAMDSVRTARRLGAEHAMI-----IYRRSEEEMPARLEEVkhAKEEGVEF 638
Cdd:PRK06370 161 NETIFS---------LDElPEHLVIIGGGYIGLEFAQMFRRFGSEVTVIergprLLPREDEDVAAAVREI--LEREGIDV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 639 LTLHNPIEYiadekgrvkqvvlqkmelgEPDASGRRSPIAIPGATETIDIDMAIVSVGVSPNpivpssIPGL-------E 711
Cdd:PRK06370 230 RLNAECIRV-------------------ERDGDGIAVGLDCNGGAPEITGSHILVAVGRVPN------TDDLgleaagvE 284
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1474009758 712 LGRKGTIAVNENMQSSIPTIYAGGDIVRGGATVILAMGDGRKAAASM 758
Cdd:PRK06370 285 TDARGYIKVDDQLRTTNPGIYAAGDCNGRGAFTHTAYNDARIVAANL 331
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
446-738 |
9.08e-12 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 67.47 E-value: 9.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 446 KVAVIGSGPAGLSFA---GDMAKQGYDVTVFEA---------LHEI-GGVLKYGipefrlpnkivDVEIDN---LSKMGV 509
Cdd:COG1252 3 RIVIVGGGFAGLEAArrlRKKLGGDAEVTLIDPnpyhlfqplLPEVaAGTLSPD-----------DIAIPLrelLRRAGV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 510 KFMKDCIVG-----KTISVEDLEAEDFKGIFVASGAGlPNFMNIPG--ENSINIMSSNEYLTR----VNLMDAASEDSdt 578
Cdd:COG1252 72 RFIQGEVTGidpeaRTVTLADGRTLSYDYLVIATGSV-TNFFGIPGlaEHALPLKTLEDALALrerlLAAFERAERRR-- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 579 pvtfGKRVAVIGGGNTA----------MDSVRTARRLGAEHA-MIIYRRSEE---EMPARLEE--VKHAKEEGVEFLTlh 642
Cdd:COG1252 149 ----LLTIVVVGGGPTGvelagelaelLRKLLRYPGIDPDKVrITLVEAGPRilpGLGEKLSEaaEKELEKRGVEVHT-- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 643 npieyiadeKGRVKQVVLQKMELgepdASGrrspiaipgatETIDIDMAIVSVGVSPNPIVPSSipGLELGRKGTIAVNE 722
Cdd:COG1252 223 ---------GTRVTEVDADGVTL----EDG-----------EEIPADTVIWAAGVKAPPLLADL--GLPTDRRGRVLVDP 276
|
330
....*....|....*..
gi 1474009758 723 NMQS-SIPTIYAGGDIV 738
Cdd:COG1252 277 TLQVpGHPNVFAIGDCA 293
|
|
| PLN02852 |
PLN02852 |
ferredoxin-NADP+ reductase |
447-745 |
2.33e-11 |
|
ferredoxin-NADP+ reductase
Pssm-ID: 215457 Cd Length: 491 Bit Score: 66.64 E-value: 2.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 447 VAVIGSGPAGLSFAGDMAK--QGYDVTVFEALHEIGGVLKYGI----PEfrlpNKIVDVEIDNLSKMG-VKFMKDCIVGK 519
Cdd:PLN02852 29 VCVVGSGPAGFYTADKLLKahDGARVDIIERLPTPFGLVRSGVapdhPE----TKNVTNQFSRVATDDrVSFFGNVTLGR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 520 TISVEDLEAEdFKGIFVASGAGLPNFMNIPGENSINIMSSNEYLTRVNLMDAASEDSDTPVTfGKRVAVIGGGNTAMDSV 599
Cdd:PLN02852 105 DVSLSELRDL-YHVVVLAYGAESDRRLGIPGEDLPGVLSAREFVWWYNGHPDCVHLPPDLKS-SDTAVVLGQGNVALDCA 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 600 RTARRLG--------AEHAM------------IIYRR-----------------------------------SEEEMPA- 623
Cdd:PLN02852 183 RILLRPTdelastdiAEHALealrgssvrkvyLVGRRgpvqaactakelrellglknvrvrikeadltlspeDEEELKAs 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 624 RL-----EEVKHAKEEG----------VEFLTLHNPIEYIA--DEKGRVKQVVLQKMELgEPDASGRRSPIAIPGATETI 686
Cdd:PLN02852 263 RPkrrvyELLSKAAAAGkcapsggqreLHFVFFRNPTRFLDsgDGNGHVAGVKLERTVL-EGAAGSGKQVAVGTGEFEDL 341
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1474009758 687 DIDMAIVSVGVSPNPIvpSSIP-----GLELGRKGTIAVNENMQSSIPTIYAGGDIVRGGATVI 745
Cdd:PLN02852 342 PCGLVLKSIGYKSLPV--DGLPfdhkrGVVPNVHGRVLSSASGADTEPGLYVVGWLKRGPTGII 403
|
|
| PRK08345 |
PRK08345 |
cytochrome-c3 hydrogenase subunit gamma; Provisional |
12-242 |
2.04e-10 |
|
cytochrome-c3 hydrogenase subunit gamma; Provisional
Pssm-ID: 236247 [Multi-domain] Cd Length: 289 Bit Score: 62.52 E-value: 2.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 12 EKVFKLVIEAPLIAKS--RKAGHFVIVRVGEKGErMPLTIAGADPVKGTITLVVQEVGLSSTRLCELNEGDyITDVVGPL 89
Cdd:PRK08345 20 EKLFLLRFEDPELAESftFKPGQFVQVTIPGVGE-VPISICSSPTRKGFFELCIRRAGRVTTVIHRLKEGD-IVGVRGPY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 90 GKATHIENF--GTVVCAGGGVGVAPMLPIVqaLKAAGNRV----ITVLAG-RTKELIILEKE----MRESSDEVIIMT-- 156
Cdd:PRK08345 98 GNGFPVDEMegMDLLLIAGGLGMAPLRSVL--LYAMDNRWkygnITLIYGaKYYEDLLFYDElikdLAEAENVKIIQSvt 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 157 -DDGSYGHKGL-------VTEGVEEVIKRET---VNKCFAI--GPAIMMKFVCLLTKKYEIPTD---VSLNTIMVDGTGM 220
Cdd:PRK08345 176 rDPEWPGCHGLpqgfierVCKGVVTDLFREAntdPKNTYAAicGPPVMYKFVFKELINRGYRPEriyVTLERRMRCGIGK 255
|
250 260
....*....|....*....|..
gi 1474009758 221 CGACRITVGGKTRFVCVDGPEF 242
Cdd:PRK08345 256 CGHCIVGTSTSIKYVCKDGPVF 277
|
|
| PRK06327 |
PRK06327 |
dihydrolipoamide dehydrogenase; Validated |
584-740 |
1.15e-09 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235779 [Multi-domain] Cd Length: 475 Bit Score: 61.48 E-value: 1.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 584 KRVAVIGGG--NTAMDSVrtARRLGAEHAMIiyrrseEEMParleevkhakeegvEFLTLHNpiEYIADE--KGRVKQ-- 657
Cdd:PRK06327 184 KKLAVIGAGviGLELGSV--WRRLGAEVTIL------EALP--------------AFLAAAD--EQVAKEaaKAFTKQgl 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 658 VVLQKMELGEPDASGRRSPIAI---PGATETIDIDMAIVSVGVSPNP--IVPSSIpGLELGRKGTIAVNENMQSSIPTIY 732
Cdd:PRK06327 240 DIHLGVKIGEIKTGGKGVSVAYtdaDGEAQTLEVDKLIVSIGRVPNTdgLGLEAV-GLKLDERGFIPVDDHCRTNVPNVY 318
|
....*...
gi 1474009758 733 AGGDIVRG 740
Cdd:PRK06327 319 AIGDVVRG 326
|
|
| FNR_like |
cd00322 |
Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a ... |
5-207 |
1.46e-09 |
|
Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a chloroplast reductase activity, catalyzing the electron transfer from reduced iron-sulfur protein ferredoxin to NADP+ as the final step in the electron transport mechanism of photosystem I. FNR transfers electrons from reduced ferredoxin to FAD (forming FADH2 via a semiquinone intermediate) and then transfers a hydride ion to convert NADP+ to NADPH. FNR has since been shown to utilize a variety of electron acceptors and donors and has a variety of physiological functions including nitrogen assimilation, dinitrogen fixation, steroid hydroxylation, fatty acid metabolism, oxygenase activity, and methane assimilation in many organisms. FNR has an NAD(P)-binding sub-domain of the alpha/beta class and a discrete (usually N-terminal) flavin sub-domain which vary in orientation with respect to the NAD(P) binding domain. The N-terminal moeity may contain a flavin prosthetic group (as in flavoenzymes) or use flavin as a substrate. Because flavins such as FAD can exist in oxidized, semiquinone (one- electron reduced), or fully reduced hydroquinone forms, FNR can interact with one and 2 electron carriers. FNR has a strong preference for NADP(H) vs NAD(H).
Pssm-ID: 99778 [Multi-domain] Cd Length: 223 Bit Score: 59.00 E-value: 1.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 5 ISKEHFSEKVFKLVIEAPLIAKSrKAGHFVIVRVGEKGERM--PLTIAGADPVKGTITLVVQEV--GLSSTRLCELNEGD 80
Cdd:cd00322 1 VATEDVTDDVRLFRLQLPNGFSF-KPGQYVDLHLPGDGRGLrrAYSIASSPDEEGELELTVKIVpgGPFSAWLHDLKPGD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 81 YITdVVGPLGKATHIENFG------------TvvcagggvgvaPMLPIVQALKAAG-NRVITVLAG-RTKELIILEKEMR 146
Cdd:cd00322 80 EVE-VSGPGGDFFLPLEESgpvvliaggigiT-----------PFRSMLRHLAADKpGGEITLLYGaRTPADLLFLDELE 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1474009758 147 ESSDE-----VIIMTDDGSYGHKGLVTEGVEEVIKRETVNK-----CFAIGPAIMMKFVCLLTKKYEIPTD 207
Cdd:cd00322 148 ELAKEgpnfrLVLALSRESEAKLGPGGRIDREAEILALLPDdsgalVYICGPPAMAKAVREALVSLGVPEE 218
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
446-736 |
1.84e-09 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 60.44 E-value: 1.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 446 KVAVIGSGPAGLSFAgdmAK-----QGYDVTVFEALHEIG----GVLKYGIPEFRLPNKIVDVEIDNLSKMGV------K 510
Cdd:PRK09564 2 KIIIIGGTAAGMSAA---AKakrlnKELEITVYEKTDIVSfgacGLPYFVGGFFDDPNTMIARTPEEFIKSGIdvktehE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 511 FMKDCIVGKTISVEDLEAED-----FKGIFVASGAG--LPNFMNIPGENSINIMSSNEYLTRVNLMDaaseDSDTpvtfg 583
Cdd:PRK09564 79 VVKVDAKNKTITVKNLKTGSifndtYDKLMIATGARpiIPPIKNINLENVYTLKSMEDGLALKELLK----DEEI----- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 584 KRVAVIGGGNTAMDSVRTARRLGAEHAMI------IYRRSEEEMPARLEEvkHAKEEGVEFLTLHNPIEYIADEKgrVKQ 657
Cdd:PRK09564 150 KNIVIIGAGFIGLEAVEAAKHLGKNVRIIqledriLPDSFDKEITDVMEE--ELRENGVELHLNEFVKSLIGEDK--VEG 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1474009758 658 VVLQKMElgepdasgrrspiaipgatetIDIDMAIVSVGVSPNPIVPSSiPGLELGRKGTIAVNENMQSSIPTIYAGGD 736
Cdd:PRK09564 226 VVTDKGE---------------------YEADVVIVATGVKPNTEFLED-TGLKTLKNGAIIVDEYGETSIENIYAAGD 282
|
|
| COG1233 |
COG1233 |
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ... |
446-481 |
2.23e-09 |
|
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440846 [Multi-domain] Cd Length: 491 Bit Score: 60.63 E-value: 2.23e-09
10 20 30
....*....|....*....|....*....|....*.
gi 1474009758 446 KVAVIGSGPAGLSFAGDMAKQGYDVTVFEALHEIGG 481
Cdd:COG1233 5 DVVVIGAGIGGLAAAALLARAGYRVTVLEKNDTPGG 40
|
|
| CzcO |
COG2072 |
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ... |
445-605 |
1.55e-08 |
|
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: 57.57 E-value: 1.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 445 IKVAVIGSGPAGLSFAGDMAKQGYDVTVFEALHEIGG--------------------------------------VL--- 483
Cdd:COG2072 7 VDVVVIGAGQAGLAAAYHLRRAGIDFVVLEKADDVGGtwrdnrypglrldtpshlyslpffpnwsddpdfptgdeILayl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 484 -----KYGI-PEFRLPNKIVDVEIDNLSKmgvkfmkdcivGKTISVEDLEAEDFKGIFVASGA-GLPNFMNIPGENS--I 554
Cdd:COG2072 87 eayadKFGLrRPIRFGTEVTSARWDEADG-----------RWTVTTDDGETLTARFVVVATGPlSRPKIPDIPGLEDfaG 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1474009758 555 NIMSSNEYltrvnlmdaasedsDTPVTF-GKRVAVIGGGNTAMDSV----RTARRL 605
Cdd:COG2072 156 EQLHSADW--------------RNPVDLaGKRVLVVGTGASAVQIApelaRVAAHV 197
|
|
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
447-740 |
1.81e-08 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 57.46 E-value: 1.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 447 VAVIGSGPAGLSFAGDMAKQGYDVTVFEALHeIGGV-LKYG-IPEFRLPN--KIVDvEIDNLSKMGVKFM---------- 512
Cdd:PRK06416 7 VIVIGAGPGGYVAAIRAAQLGLKVAIVEKEK-LGGTcLNRGcIPSKALLHaaERAD-EARHSEDFGIKAEnvgidfkkvq 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 513 --KDCIVGK---------------------------TISVEDLEAED---FKGIFVASGA---GLPNFmNIPGENsinIM 557
Cdd:PRK06416 85 ewKNGVVNRltggvegllkknkvdiirgeaklvdpnTVRVMTEDGEQtytAKNIILATGSrprELPGI-EIDGRV---IW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 558 SSNEYLTrvnlmdaasedsdtPVTFGKRVAVIGGG--NTAMDSVRTArrLGAEHAMI-----IYRRSEEEMPARLEevKH 630
Cdd:PRK06416 161 TSDEALN--------------LDEVPKSLVVIGGGyiGVEFASAYAS--LGAEVTIVealprILPGEDKEISKLAE--RA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 631 AKEEGVEFLTlhnpieyiadeKGRVKQVvlqkmelgEPDASGRRSPIAIPGATETIDIDMAIVSVGVSPNpivpSSIPGL 710
Cdd:PRK06416 223 LKKRGIKIKT-----------GAKAKKV--------EQTDDGVTVTLEDGGKEETLEADYVLVAVGRRPN----TENLGL 279
|
330 340 350
....*....|....*....|....*....|....
gi 1474009758 711 E-LGRK---GTIAVNENMQSSIPTIYAGGDIVRG 740
Cdd:PRK06416 280 EeLGVKtdrGFIEVDEQLRTNVPNIYAIGDIVGG 313
|
|
| PRK07233 |
PRK07233 |
hypothetical protein; Provisional |
446-481 |
2.49e-08 |
|
hypothetical protein; Provisional
Pssm-ID: 235977 [Multi-domain] Cd Length: 434 Bit Score: 56.82 E-value: 2.49e-08
10 20 30
....*....|....*....|....*....|....*.
gi 1474009758 446 KVAVIGSGPAGLSFAGDMAKQGYDVTVFEALHEIGG 481
Cdd:PRK07233 1 KIAIVGGGIAGLAAAYRLAKRGHEVTVFEADDQLGG 36
|
|
| NAD_binding_8 |
pfam13450 |
NAD(P)-binding Rossmann-like domain; |
449-499 |
1.14e-07 |
|
NAD(P)-binding Rossmann-like domain;
Pssm-ID: 433218 [Multi-domain] Cd Length: 67 Bit Score: 49.07 E-value: 1.14e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1474009758 449 VIGSGPAGLSFAGDMAKQGYDVTVFEALHEIGGVlkygIPEFRLPNKIVDV 499
Cdd:pfam13450 1 IVGAGLAGLVAAALLAKRGFRVLVLEKRDRLGGN----AYSYRVPGYVFDY 47
|
|
| HemY |
COG1232 |
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ... |
446-484 |
1.37e-07 |
|
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen oxidase HemY/PPOX is part of the Pathway/BioSystem: Heme biosynthesis
Pssm-ID: 440845 [Multi-domain] Cd Length: 443 Bit Score: 54.84 E-value: 1.37e-07
10 20 30
....*....|....*....|....*....|....*....
gi 1474009758 446 KVAVIGSGPAGLSFAGDMAKQGYDVTVFEALHEIGGVLK 484
Cdd:COG1232 3 RVAVIGGGIAGLTAAYRLAKAGHEVTVLEASDRVGGLIR 41
|
|
| PRK07208 |
PRK07208 |
hypothetical protein; Provisional |
443-482 |
6.54e-07 |
|
hypothetical protein; Provisional
Pssm-ID: 235967 [Multi-domain] Cd Length: 479 Bit Score: 52.58 E-value: 6.54e-07
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1474009758 443 NNIKVAVIGSGPAGLSFAGDMAKQGYDVTVFEALHEIGGV 482
Cdd:PRK07208 3 NKKSVVIIGAGPAGLTAAYELLKRGYPVTVLEADPVVGGI 42
|
|
| PRK13512 |
PRK13512 |
coenzyme A disulfide reductase; Provisional |
681-761 |
8.52e-07 |
|
coenzyme A disulfide reductase; Provisional
Pssm-ID: 184103 [Multi-domain] Cd Length: 438 Bit Score: 52.09 E-value: 8.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 681 GATETIDIdmAIVSVGVSPNP-IVPSSipGLELGRKGTIAVNENMQSSIPTIYAGGDIVRG-------GATVILAMGDGR 752
Cdd:PRK13512 225 GKVEHYDM--IIEGVGTHPNSkFIESS--NIKLDDKGFIPVNDKFETNVPNIYAIGDIITShyrhvdlPASVPLAWGAHR 300
|
....*....
gi 1474009758 753 kaAASMHAQ 761
Cdd:PRK13512 301 --AASIVAE 307
|
|
| nitri_red_nirB |
TIGR02374 |
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ... |
584-736 |
8.67e-07 |
|
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen metabolism]
Pssm-ID: 162827 [Multi-domain] Cd Length: 785 Bit Score: 52.52 E-value: 8.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 584 KRVAVIGGGNTAMDSVRTARRLG-----AEHAMIIYRRSEEEMPARLEEVKHAKEeGVEFLTLHNPIEYIADekGRVKQV 658
Cdd:TIGR02374 141 KKAAVIGGGLLGLEAAVGLQNLGmdvsvIHHAPGLMAKQLDQTAGRLLQRELEQK-GLTFLLEKDTVEIVGA--TKADRI 217
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1474009758 659 VLqkmelgepdASGrrspiaipgatETIDIDMAIVSVGVSPNPIVPSSiPGLELGRKgtIAVNENMQSSIPTIYAGGD 736
Cdd:TIGR02374 218 RF---------KDG-----------SSLEADLIVMAAGIRPNDELAVS-AGIKVNRG--IIVNDSMQTSDPDIYAVGE 272
|
|
| Fpr |
COG1018 |
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion]; |
3-195 |
1.05e-06 |
|
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion];
Pssm-ID: 440641 [Multi-domain] Cd Length: 231 Bit Score: 50.56 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 3 KIISKEHFSEKVFKLVIEAPLIAKSR--KAGHFVIVRVGEKGERM--PLTIAGAdPVKGTITLVVQEV--GLSSTRLCE- 75
Cdd:COG1018 7 RVVEVRRETPDVVSFTLEPPDGAPLPrfRPGQFVTLRLPIDGKPLrrAYSLSSA-PGDGRLEITVKRVpgGGGSNWLHDh 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 76 LNEGDYITdVVGPLGKATHIENFG------------TvvcagggvgvaPMLPIVQALKAAGNRV-ITVL-AGRTKELIIL 141
Cdd:COG1018 86 LKVGDTLE-VSGPRGDFVLDPEPArpllliaggigiT-----------PFLSMLRTLLARGPFRpVTLVyGARSPADLAF 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 142 EKEMRESSDE-----VIIMTDDGSYGHKGLVT-EGVEEVIKRETVNKCFAIGPAIMMKFV 195
Cdd:COG1018 154 RDELEALAARhprlrLHPVLSREPAGLQGRLDaELLAALLPDPADAHVYLCGPPPMMEAV 213
|
|
| PRK13748 |
PRK13748 |
putative mercuric reductase; Provisional |
531-758 |
1.19e-06 |
|
putative mercuric reductase; Provisional
Pssm-ID: 184298 [Multi-domain] Cd Length: 561 Bit Score: 52.08 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 531 FKGIFVASGAGlPNFMNIPGENSINIMSSNEYLtrvnlmdaASEdsdtpvTFGKRVAVIGGGNTAMDSVRTARRLGAEhA 610
Cdd:PRK13748 233 FDRCLIATGAS-PAVPPIPGLKETPYWTSTEAL--------VSD------TIPERLAVIGSSVVALELAQAFARLGSK-V 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 611 MIIYRRS--EEEMPARLEEVKHA-KEEGVEFLTlHNPIEYIADEKGrvkQVVLqKMELGEpdasgrrspiaipgatetID 687
Cdd:PRK13748 297 TILARSTlfFREDPAIGEAVTAAfRAEGIEVLE-HTQASQVAHVDG---EFVL-TTGHGE------------------LR 353
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1474009758 688 IDMAIVSVGVSPNPivpSSI----PGLELGRKGTIAVNENMQSSIPTIYAGGDIVRGGATVILAMGDGRKAAASM 758
Cdd:PRK13748 354 ADKLLVATGRAPNT---RSLaldaAGVTVNAQGAIVIDQGMRTSVPHIYAAGDCTDQPQFVYVAAAAGTRAAINM 425
|
|
| YobN |
COG1231 |
Monoamine oxidase [Amino acid transport and metabolism]; |
446-481 |
1.35e-06 |
|
Monoamine oxidase [Amino acid transport and metabolism];
Pssm-ID: 440844 [Multi-domain] Cd Length: 440 Bit Score: 51.46 E-value: 1.35e-06
10 20 30
....*....|....*....|....*....|....*.
gi 1474009758 446 KVAVIGSGPAGLSFAGDMAKQGYDVTVFEALHEIGG 481
Cdd:COG1231 9 DVVIVGAGLAGLAAARELRKAGLDVTVLEARDRVGG 44
|
|
| UbiH |
COG0654 |
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ... |
446-475 |
8.02e-06 |
|
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme transport and metabolism, Energy production and conversion]; 2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases is part of the Pathway/BioSystem: Ubiquinone biosynthesis
Pssm-ID: 440419 [Multi-domain] Cd Length: 326 Bit Score: 48.78 E-value: 8.02e-06
10 20 30
....*....|....*....|....*....|
gi 1474009758 446 KVAVIGSGPAGLSFAGDMAKQGYDVTVFEA 475
Cdd:COG0654 5 DVLIVGGGPAGLALALALARAGIRVTVVER 34
|
|
| PRK15317 |
PRK15317 |
alkyl hydroperoxide reductase subunit F; Provisional |
532-757 |
9.70e-06 |
|
alkyl hydroperoxide reductase subunit F; Provisional
Pssm-ID: 237942 [Multi-domain] Cd Length: 517 Bit Score: 49.00 E-value: 9.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 532 KGIFVASGAGLPNfMNIPGENsinimssnEYLTR-VnlmdAASEDSDTPVTFGKRVAVIGGGNTAmdsVRTARRLG--AE 608
Cdd:PRK15317 312 KTVILATGARWRN-MNVPGED--------EYRNKgV----AYCPHCDGPLFKGKRVAVIGGGNSG---VEAAIDLAgiVK 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 609 HAMIIyrrseEEMPA-RLEEV---KHAKEEGVEFLTLHNPIEYIADEKgRVKQVVLQKMELGEpdasgrrspiaipgaTE 684
Cdd:PRK15317 376 HVTVL-----EFAPElKADQVlqdKLRSLPNVTIITNAQTTEVTGDGD-KVTGLTYKDRTTGE---------------EH 434
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1474009758 685 TIDIDMAIVSVGVSPNP-IVPSSIpglELGRKGTIAVNENMQSSIPTIYAGGDIvrggATV-----ILAMGDGRKAAAS 757
Cdd:PRK15317 435 HLELEGVFVQIGLVPNTeWLKGTV---ELNRRGEIIVDARGATSVPGVFAAGDC----TTVpykqiIIAMGEGAKAALS 506
|
|
| PRK12814 |
PRK12814 |
putative NADPH-dependent glutamate synthase small subunit; Provisional |
306-347 |
1.15e-05 |
|
putative NADPH-dependent glutamate synthase small subunit; Provisional
Pssm-ID: 139246 [Multi-domain] Cd Length: 652 Bit Score: 48.96 E-value: 1.15e-05
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1474009758 306 AIPRVKMNELDAEYRSHSRkEEVNLGLNEEQAITEAKRCLDC 347
Cdd:PRK12814 532 PAPRVALPELPLEERTGGF-EEVVTGYSPEQAREEALRCLRC 572
|
|
| PLN02976 |
PLN02976 |
amine oxidase |
446-481 |
2.13e-05 |
|
amine oxidase
Pssm-ID: 215527 [Multi-domain] Cd Length: 1713 Bit Score: 48.33 E-value: 2.13e-05
10 20 30
....*....|....*....|....*....|....*.
gi 1474009758 446 KVAVIGSGPAGLSFAGDMAKQGYDVTVFEALHEIGG 481
Cdd:PLN02976 695 KIIVVGAGPAGLTAARHLQRQGFSVTVLEARSRIGG 730
|
|
| PRK05249 |
PRK05249 |
Si-specific NAD(P)(+) transhydrogenase; |
709-758 |
2.26e-05 |
|
Si-specific NAD(P)(+) transhydrogenase;
Pssm-ID: 235373 [Multi-domain] Cd Length: 461 Bit Score: 47.46 E-value: 2.26e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1474009758 709 GLELGRKGTIAVNENMQSSIPTIYAGGDIVRGGATVILAMGDGRKAAASM 758
Cdd:PRK05249 283 GLEADSRGQLKVNENYQTAVPHIYAVGDVIGFPSLASASMDQGRIAAQHA 332
|
|
| PRK07251 |
PRK07251 |
FAD-containing oxidoreductase; |
449-741 |
2.53e-05 |
|
FAD-containing oxidoreductase;
Pssm-ID: 180907 [Multi-domain] Cd Length: 438 Bit Score: 47.44 E-value: 2.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 449 VIGSGPAGLSFAGDMAKQGYDVTVFE-ALHEIGGVLkygIPEFRLPNKIVDVEID-NLSKMGVKFMKDCIVG-------- 518
Cdd:PRK07251 8 VIGFGKAGKTLAAKLASAGKKVALVEeSKAMYGGTC---INIGCIPTKTLLVAAEkNLSFEQVMATKNTVTSrlrgknya 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 519 -------------------KTISVE------DLEAEDfkgIFVASGAgLPNFMNIPG-ENSINIMSSNEYLTRVNLmdaa 572
Cdd:PRK07251 85 mlagsgvdlydaeahfvsnKVIEVQagdekiELTAET---IVINTGA-VSNVLPIPGlADSKHVYDSTGIQSLETL---- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 573 sedsdtPvtfgKRVAVIGGGNTAMDSVRTARRLGAEHAMI-----IYRRSEEEMPARLEEvkHAKEEGVEFLtLHNPIEY 647
Cdd:PRK07251 157 ------P----ERLGIIGGGNIGLEFAGLYNKLGSKVTVLdaastILPREEPSVAALAKQ--YMEEDGITFL-LNAHTTE 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 648 IADEKGRVkqVVLQKMELGEPD----ASGRRSPIAiPGATETIDIdmaivsvgvspnpivpssipglELGRKGTIAVNEN 723
Cdd:PRK07251 224 VKNDGDQV--LVVTEDETYRFDallyATGRKPNTE-PLGLENTDI----------------------ELTERGAIKVDDY 278
|
330
....*....|....*...
gi 1474009758 724 MQSSIPTIYAGGDiVRGG 741
Cdd:PRK07251 279 CQTSVPGVFAVGD-VNGG 295
|
|
| PRK06567 |
PRK06567 |
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; Validated |
434-620 |
3.00e-05 |
|
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; Validated
Pssm-ID: 235832 [Multi-domain] Cd Length: 1028 Bit Score: 47.59 E-value: 3.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 434 ISVPEVAEKNNIKVAVIGSGPAGLSFAGDMAKQGYDVTVFEAL----------------HE------------IGGVLKY 485
Cdd:PRK06567 373 IYAPLPKEPTNYNILVTGLGPAGFSLSYYLLRSGHNVTAIDGLkitllpfdvhkpikfwHEyknllsermprgFGGVAEY 452
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 486 GIpEFRLPNKIVDV-----EIDNlskmGVKFMKDCIVGKTISVEDLEAEDFKGIFVASGAGLPNFMNIPGENSINIMSSN 560
Cdd:PRK06567 453 GI-TVRWDKNNLDIlrlilERNN----NFKYYDGVALDFNITKEQAFDLGFDHIAFCIGAGQPKVLDIENFEAKGVKTAS 527
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 561 EYLTRVNLMDAASEDSDTPVTFGKRVAVIGGGNTAMDSvrtarrlgAEHAMIIYRRSEEE 620
Cdd:PRK06567 528 DFLMTLQSGGAFLKNSNTNMVIRMPIAVIGGGLTSLDA--------ATESLYYYKKQVEE 579
|
|
| Ppro0129 |
COG2907 |
Predicted flavin-containing amine oxidase [General function prediction only]; |
446-481 |
3.17e-05 |
|
Predicted flavin-containing amine oxidase [General function prediction only];
Pssm-ID: 442151 [Multi-domain] Cd Length: 423 Bit Score: 47.03 E-value: 3.17e-05
10 20 30
....*....|....*....|....*....|....*.
gi 1474009758 446 KVAVIGSGPAGLSFAGDMAKQgYDVTVFEALHEIGG 481
Cdd:COG2907 5 RIAVIGSGISGLTAAWLLSRR-HDVTLFEANDRLGG 39
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
585-658 |
3.74e-05 |
|
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: 42.58 E-value: 3.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 585 RVAVIGGGNTAMDSVRTARRLGAEhAMIIYRRSE------EEMPARLEEvkHAKEEGVEFLTLHNPIEYIADEKGRVKQV 658
Cdd:pfam00070 1 RVVVVGGGYIGLELAGALARLGSK-VTVVERRDRllpgfdPEIAKILQE--KLEKNGIEFLLNTTVEAIEGNGDGVVVVL 77
|
|
| PRK06567 |
PRK06567 |
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; Validated |
4-256 |
4.87e-05 |
|
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; Validated
Pssm-ID: 235832 [Multi-domain] Cd Length: 1028 Bit Score: 46.82 E-value: 4.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 4 IISKEH----FSEKVFKLVIEAPLIAKSRKAGHFVIVR-----VGEKGERMPLTIAGADPVKGTITLVVQEVGlSSTRLC 74
Cdd:PRK06567 791 LTSRVNkiniLDDKTFELIIHSPLAAKNFKFGQFFRLQnysedAAKLIEPVALSPIDIDVEKGLISFIVFEVG-KSTSLC 869
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 75 ELNEGDYITDVVGPLGkathienfgtvvcagggvgvapmLPivqaLKAAGNRVITVLAGRTKELIILeKEMRESSDEVII 154
Cdd:PRK06567 870 KTLSENEKVVLMGPTG-----------------------SP----LEIPQNKKIVIVDFEVGNIGLL-KVLKENNNEVIF 921
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 155 MTDDGSYGHKgLVTegVEEVIkretVNKcfaiGPAIMMKFVCLLTKKYEIPTD--VSLNTIM-VDGTGMCGACRITVGGK 231
Cdd:PRK06567 922 VTYPDIKIRK-LVS--VDIVI----INA----SPEIIEELQSLKNEIFGENTEiiVSVNSSMqCMMKGICGQCIQKVKGE 990
|
250 260
....*....|....*....|....*..
gi 1474009758 232 TR--FVCvDGPEFDGHQVDFDEMLKRM 256
Cdd:PRK06567 991 QKyiFAC-SQQNQNAEIVDFKSLKTRL 1016
|
|
| PRK12771 |
PRK12771 |
putative glutamate synthase (NADPH) small subunit; Provisional |
308-357 |
8.12e-05 |
|
putative glutamate synthase (NADPH) small subunit; Provisional
Pssm-ID: 237198 [Multi-domain] Cd Length: 564 Bit Score: 46.02 E-value: 8.12e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1474009758 308 PRVKMNELDAEYRSHSRkEEVNLGLNEEQAITEAKRCLDCPN----PTCMNGCP 357
Cdd:PRK12771 471 PRAQRPELDADERVGDF-DEVLGGLTEEEARQEAARCLSCGNcfecDNCYGACP 523
|
|
| trypano_reduc |
TIGR01423 |
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ... |
519-737 |
9.69e-05 |
|
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of spermidine, is (in its reduced form) an important antioxidant found in trypanosomatids (Crithidia, Leishmania, Trypanosoma). This model describes trypanothione reductase, a possible antitrypanosomal drug target closely related to some forms of glutathione reductase.
Pssm-ID: 200098 [Multi-domain] Cd Length: 486 Bit Score: 45.73 E-value: 9.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 519 KTISVEDLEAEDfkgIFVASGAgLPNFMNIPGENsiNIMSSNE--YLtrvnlmdaasedSDTPvtfgKRVAVIGGGNTAM 596
Cdd:TIGR01423 143 KSAVKERLQAEH---ILLATGS-WPQMLGIPGIE--HCISSNEafYL------------DEPP----RRVLTVGGGFISV 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 597 D--SVRTARRLGAEHAMIIYRRS------EEEMpaRLEEVKHAKEEGVEFLTLHNPIEYIADEKGRvKQVVLQkmelgep 668
Cdd:TIGR01423 201 EfaGIFNAYKPRGGKVTLCYRNNmilrgfDSTL--RKELTKQLRANGINIMTNENPAKVTLNADGS-KHVTFE------- 270
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 669 daSGRrspiaipgateTIDIDMAIVSVGVSPNP-IVPSSIPGLELGRKGTIAVNENMQSSIPTIYAGGDI 737
Cdd:TIGR01423 271 --SGK-----------TLDVDVVMMAIGRVPRTqTLQLDKVGVELTKKGAIQVDEFSRTNVPNIYAIGDV 327
|
|
| PRK06116 |
PRK06116 |
glutathione reductase; Validated |
534-737 |
1.06e-04 |
|
glutathione reductase; Validated
Pssm-ID: 235701 [Multi-domain] Cd Length: 450 Bit Score: 45.53 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 534 IFVASGaGLPNFMNIPG-ENSInimSSNE--YLTRVnlmdaasedsdtPvtfgKRVAVIGGGNTAMDSVRTARRLGAEhA 610
Cdd:PRK06116 135 ILIATG-GRPSIPDIPGaEYGI---TSDGffALEEL------------P----KRVAVVGAGYIAVEFAGVLNGLGSE-T 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 611 MIIYRRseeEMPAR---------LEEVkhAKEEGVEFLTLHNPIEYIADEKGRVKqVVLQKMELGEPD----ASGRRspi 677
Cdd:PRK06116 194 HLFVRG---DAPLRgfdpdiretLVEE--MEKKGIRLHTNAVPKAVEKNADGSLT-LTLEDGETLTVDcliwAIGRE--- 264
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 678 aiPgATETIDIDMAivsvgvspnpivpssipGLELGRKGTIAVNENMQSSIPTIYAGGDI 737
Cdd:PRK06116 265 --P-NTDGLGLENA-----------------GVKLNEKGYIIVDEYQNTNVPGIYAVGDV 304
|
|
| COG3380 |
COG3380 |
Predicted NAD/FAD-dependent oxidoreductase [General function prediction only]; |
446-481 |
1.10e-04 |
|
Predicted NAD/FAD-dependent oxidoreductase [General function prediction only];
Pssm-ID: 442607 [Multi-domain] Cd Length: 331 Bit Score: 44.87 E-value: 1.10e-04
10 20 30
....*....|....*....|....*....|....*.
gi 1474009758 446 KVAVIGSGPAGLSFAGDMAKQGYDVTVFEALHEIGG 481
Cdd:COG3380 5 DIAIIGAGIAGLAAARALQDAGHEVTVFEKSRGVGG 40
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
446-517 |
1.13e-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: 41.04 E-value: 1.13e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1474009758 446 KVAVIGSGPAGLSFAGDMAKQGYDVTVFEALHEIGGVlkygipefrLPNKIVDVEIDNLSKMGVKFMKDCIV 517
Cdd:pfam00070 1 RVVVVGGGYIGLELAGALARLGSKVTVVERRDRLLPG---------FDPEIAKILQEKLEKNGIEFLLNTTV 63
|
|
| PLN02487 |
PLN02487 |
zeta-carotene desaturase |
437-481 |
1.42e-04 |
|
zeta-carotene desaturase
Pssm-ID: 215268 [Multi-domain] Cd Length: 569 Bit Score: 45.18 E-value: 1.42e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1474009758 437 PEVAEKNNIKVAVIGSGPAGLSFAGDMAKQGYDVTVFEALHEIGG 481
Cdd:PLN02487 68 PEAYKGPKLKVAIIGAGLAGMSTAVELLDQGHEVDIYESRPFIGG 112
|
|
| COG3349 |
COG3349 |
Uncharacterized protein, contains NAD-binding domain and a Fe-S cluster [General function ... |
446-481 |
1.68e-04 |
|
Uncharacterized protein, contains NAD-binding domain and a Fe-S cluster [General function prediction only];
Pssm-ID: 442577 [Multi-domain] Cd Length: 445 Bit Score: 44.85 E-value: 1.68e-04
10 20 30
....*....|....*....|....*....|....*.
gi 1474009758 446 KVAVIGSGPAGLSFAGDMAKQGYDVTVFEALHEIGG 481
Cdd:COG3349 5 RVVVVGGGLAGLAAAVELAEAGFRVTLLEARPRLGG 40
|
|
| FixC |
COG0644 |
Dehydrogenase (flavoprotein) [Energy production and conversion]; |
453-528 |
2.17e-04 |
|
Dehydrogenase (flavoprotein) [Energy production and conversion];
Pssm-ID: 440409 [Multi-domain] Cd Length: 281 Bit Score: 43.80 E-value: 2.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 453 GPAGLSFAGDMAKQGYDVTVFEALHEI------GGVLKYGIPEFR-------LPNKIVDVEIDNLSKMGVKFMKDCIVGK 519
Cdd:COG0644 2 GPAGSAAARRLARAGLSVLLLEKGSFPgdkicgGGLLPRALEELEplgldepLERPVRGARFYSPGGKSVELPPGRGGGY 81
|
....*....
gi 1474009758 520 TISVEDLEA 528
Cdd:COG0644 82 VVDRARFDR 90
|
|
| PRK10262 |
PRK10262 |
thioredoxin reductase; Provisional |
446-738 |
2.19e-04 |
|
thioredoxin reductase; Provisional
Pssm-ID: 182343 [Multi-domain] Cd Length: 321 Bit Score: 44.28 E-value: 2.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 446 KVAVIGSGPAGLSFAGDMAKQGYDVTVFEALhEIGGVLKYGIPEFRLPNKIVDVE----IDNLSKMGVKFMKDCIVGKTI 521
Cdd:PRK10262 8 KLLILGSGPAGYTAAVYAARANLQPVLITGM-EKGGQLTTTTEVENWPGDPNDLTgpllMERMHEHATKFETEIIFDHIN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 522 SVeDLEAEDFK-----------GIFVASGAGlPNFMNIPGENSINIMSSneyltrvnlmdAASEDSDTPVTFGKRVAVIG 590
Cdd:PRK10262 87 KV-DLQNRPFRltgdsgeytcdALIIATGAS-ARYLGLPSEEAFKGRGV-----------SACATCDGFFYRNQKVAVIG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 591 GGNTAMDSVRTARRLGAEHAMIIYR---RSEEEMPARLEEvkhAKEEGVEFLTLHNPIEYIADEKGRVKQVVLQKMElge 667
Cdd:PRK10262 154 GGNTAVEEALYLSNIASEVHLIHRRdgfRAEKILIKRLMD---KVENGNIILHTNRTLEEVTGDQMGVTGVRLRDTQ--- 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1474009758 668 pdasgrrspiaIPGATETIDIDMAIVSVGVSPNPIVPSSIPGLElgrKGTIAVNENM-----QSSIPTIYAGGDIV 738
Cdd:PRK10262 228 -----------NSDNIESLDVAGLFVAIGHSPNTAIFEGQLELE---NGYIKVQSGIhgnatQTSIPGVFAAGDVM 289
|
|
| DadA |
COG0665 |
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism]; |
446-481 |
5.31e-04 |
|
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
Pssm-ID: 440429 [Multi-domain] Cd Length: 364 Bit Score: 42.97 E-value: 5.31e-04
10 20 30
....*....|....*....|....*....|....*.
gi 1474009758 446 KVAVIGSGPAGLSFAGDMAKQGYDVTVFEAlHEIGG 481
Cdd:COG0665 4 DVVVIGGGIAGLSTAYHLARRGLDVTVLER-GRPGS 38
|
|
| HdrA |
COG1148 |
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion]; |
446-500 |
5.38e-04 |
|
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
Pssm-ID: 440762 [Multi-domain] Cd Length: 563 Bit Score: 43.31 E-value: 5.38e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1474009758 446 KVAVIGSGPAGLSFAGDMAKQGYDVTVFEALHEIGGV---LKYGIPEFR-----LPNKIVDVE 500
Cdd:COG1148 142 RALVIGGGIAGMTAALELAEQGYEVYLVEKEPELGGRaaqLHKTFPGLDcpqciLEPLIAEVE 204
|
|
| PTZ00058 |
PTZ00058 |
glutathione reductase; Provisional |
520-738 |
6.81e-04 |
|
glutathione reductase; Provisional
Pssm-ID: 185420 [Multi-domain] Cd Length: 561 Bit Score: 43.07 E-value: 6.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 520 TISVEDLEAED------FKGIFVASGaGLPNFMNIPGENsiNIMSSNEYLTrvnlmdaasedsdtpVTFGKRVAVIGGGN 593
Cdd:PTZ00058 186 TIVSAGVSQLDdgqvieGKNILIAVG-NKPIFPDVKGKE--FTISSDDFFK---------------IKEAKRIGIAGSGY 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 594 TAMDSVRTARRLGAEHAMII-----YRRSEEEMPARLEevKHAKEEGVEFLTLHNPIEYIADEKGRVKQVVlqkmelgep 668
Cdd:PTZ00058 248 IAVELINVVNRLGAESYIFArgnrlLRKFDETIINELE--NDMKKNNINIITHANVEEIEKVKEKNLTIYL--------- 316
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 669 dASGRRSpiaipgatetIDIDMAIVSVGVSPNPIVPSSIPGLELGRKGTIAVNENMQSSIPTIYAGGDIV 738
Cdd:PTZ00058 317 -SDGRKY----------EHFDYVIYCVGRSPNTEDLNLKALNIKTPKGYIKVDDNQRTSVKHIYAVGDCC 375
|
|
| PRK06753 |
PRK06753 |
hypothetical protein; Provisional |
446-479 |
1.09e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 168661 [Multi-domain] Cd Length: 373 Bit Score: 41.98 E-value: 1.09e-03
10 20 30
....*....|....*....|....*....|....
gi 1474009758 446 KVAVIGSGPAGLSFAGDMAKQGYDVTVFEALHEI 479
Cdd:PRK06753 2 KIAIIGAGIGGLTAAALLQEQGHEVKVFEKNESV 35
|
|
| PLN02172 |
PLN02172 |
flavin-containing monooxygenase FMO GS-OX |
443-485 |
1.23e-03 |
|
flavin-containing monooxygenase FMO GS-OX
Pssm-ID: 215116 [Multi-domain] Cd Length: 461 Bit Score: 42.16 E-value: 1.23e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1474009758 443 NNIKVAVIGSGPAGLSFAGDMAKQGYDVTVFEALHEIGGVLKY 485
Cdd:PLN02172 9 NSQHVAVIGAGAAGLVAARELRREGHTVVVFEREKQVGGLWVY 51
|
|
| PRK09126 |
PRK09126 |
FAD-dependent hydroxylase; |
447-474 |
1.47e-03 |
|
FAD-dependent hydroxylase;
Pssm-ID: 236385 [Multi-domain] Cd Length: 392 Bit Score: 41.85 E-value: 1.47e-03
10 20
....*....|....*....|....*...
gi 1474009758 447 VAVIGSGPAGLSFAGDMAKQGYDVTVFE 474
Cdd:PRK09126 6 IVVVGAGPAGLSFARSLAGSGLKVTLIE 33
|
|
| FAD_binding_2 |
pfam00890 |
FAD binding domain; This family includes members that bind FAD. This family includes the ... |
447-481 |
3.08e-03 |
|
FAD binding domain; This family includes members that bind FAD. This family includes the flavoprotein subunits from succinate and fumarate dehydrogenase, aspartate oxidase and the alpha subunit of adenylylsulphate reductase.
Pssm-ID: 395718 [Multi-domain] Cd Length: 398 Bit Score: 40.73 E-value: 3.08e-03
10 20 30
....*....|....*....|....*....|....*
gi 1474009758 447 VAVIGSGPAGLSFAGDMAKQGYDVTVFEALHEIGG 481
Cdd:pfam00890 2 VLVIGGGLAGLAAALAAAEAGLKVAVVEKGQPFGG 36
|
|
| Pyr_redox_3 |
pfam13738 |
Pyridine nucleotide-disulphide oxidoreductase; |
522-735 |
3.44e-03 |
|
Pyridine nucleotide-disulphide oxidoreductase;
Pssm-ID: 404603 [Multi-domain] Cd Length: 296 Bit Score: 40.28 E-value: 3.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 522 SVEDLEAEDfkgIFVASGA-GLPNFMNIPgENSINimssneyltrvnlmdaASEDSDTPVTFGKRVAVIGGGNTAMD-SV 599
Cdd:pfam13738 113 SKGTYQARY---VIIATGEfDFPNKLGVP-ELPKH----------------YSYVKDFHPYAGQKVVVIGGYNSAVDaAL 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 600 RTARRlGAEHAMiIYRRSE-EEMPAR---------LEEVKHAKEEGVEFLTLHNPIEYIADEKGRVKqvvlqkmelgepd 669
Cdd:pfam13738 173 ELVRK-GARVTV-LYRGSEwEDRDSDpsyslspdtLNRLEELVKNGKIKAHFNAEVKEITEVDVSYK------------- 237
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1474009758 670 asgrrspIAIPGATETIDIDMAIVSVGVSPN--PIVPssiPGLELGRKGTIAVNENMQSSI-PTIYAGG 735
Cdd:pfam13738 238 -------VHTEDGRKVTSNDDPILATGYHPDlsFLKK---GLFELDEDGRPVLTEETESTNvPGLFLAG 296
|
|
| GG-red-SF |
TIGR02032 |
geranylgeranyl reductase family; This model represents a subfamily which includes ... |
447-502 |
6.44e-03 |
|
geranylgeranyl reductase family; This model represents a subfamily which includes geranylgeranyl reductases involved in chlorophyll and bacteriochlorophyll biosynthesis as well as other related enzymes which may also act on geranylgeranyl groups or related substrates. [Biosynthesis of cofactors, prosthetic groups, and carriers, Chlorophyll and bacteriochlorphyll]
Pssm-ID: 273936 [Multi-domain] Cd Length: 295 Bit Score: 39.22 E-value: 6.44e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1474009758 447 VAVIGSGPAGLSFAGDMAKQGYDVTVFEALHEI------GGVLKYGIPEFRLPNKIVDVEID 502
Cdd:TIGR02032 3 VVVVGAGPAGASAAYRLADKGLRVLLLEKKSFPrykpcgGALSPRALEELDLPGELIVNLVR 64
|
|
| PRK07251 |
PRK07251 |
FAD-containing oxidoreductase; |
446-553 |
7.81e-03 |
|
FAD-containing oxidoreductase;
Pssm-ID: 180907 [Multi-domain] Cd Length: 438 Bit Score: 39.35 E-value: 7.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474009758 446 KVAVIGSGPAGLSFAGDMAKQGYDVTVFEALHEIGGvlkygipefRLPNKIVDVEIDNLSKMGVKFMKDCIV-------G 518
Cdd:PRK07251 159 RLGIIGGGNIGLEFAGLYNKLGSKVTVLDAASTILP---------REEPSVAALAKQYMEEDGITFLLNAHTtevkndgD 229
|
90 100 110
....*....|....*....|....*....|....*
gi 1474009758 519 KTISVEDLEAEDFKGIFVASGAGlPNFMNIPGENS 553
Cdd:PRK07251 230 QVLVVTEDETYRFDALLYATGRK-PNTEPLGLENT 263
|
|
| PRK11883 |
PRK11883 |
protoporphyrinogen oxidase; Reviewed |
446-483 |
9.25e-03 |
|
protoporphyrinogen oxidase; Reviewed
Pssm-ID: 237009 [Multi-domain] Cd Length: 451 Bit Score: 39.06 E-value: 9.25e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1474009758 446 KVAVIGSGPAGLSFAGDMAKQG--YDVTVFEALHEIGGVL 483
Cdd:PRK11883 2 KVAIIGGGITGLSAAYRLHKKGpdADITLLEASDRLGGKI 41
|
|
| PRK12409 |
PRK12409 |
D-amino acid dehydrogenase small subunit; Provisional |
446-474 |
9.37e-03 |
|
D-amino acid dehydrogenase small subunit; Provisional
Pssm-ID: 237093 [Multi-domain] Cd Length: 410 Bit Score: 39.24 E-value: 9.37e-03
10 20
....*....|....*....|....*....
gi 1474009758 446 KVAVIGSGPAGLSFAGDMAKQGYDVTVFE 474
Cdd:PRK12409 3 HIAVIGAGITGVTTAYALAQRGYQVTVFD 31
|
|
| |
