|
Name |
Accession |
Description |
Interval |
E-value |
| PRK12831 |
PRK12831 |
putative oxidoreductase; Provisional |
1-454 |
0e+00 |
|
putative oxidoreductase; Provisional
Pssm-ID: 183780 [Multi-domain] Cd Length: 464 Bit Score: 723.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 1 MPERDALERARDFDEVSLGYSEEQALAEANRCIQCKNPTCIEGCPVNIDIKSFIARIIDGDYAGGVSVLKERNALPAVCG 80
Cdd:PRK12831 11 VREQDPEVRATNFEEVCLGYNEEEAVKEASRCLQCKKPKCVKGCPVSINIPGFISKLKEGDFEEAAKIIAKYNALPAVCG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 81 RVCPQEEQCEASCVLARKGEPIAIGRLERWLGDFDLACDLEHRCAPevgEPTGKRVAVVGSGPAGLACAGELRRFGHAVT 160
Cdd:PRK12831 91 RVCPQESQCEGKCVLGIKGEPVAIGKLERFVADWARENGIDLSETE---EKKGKKVAVIGSGPAGLTCAGDLAKMGYDVT 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 161 IFESLHAPGGVLTYGIPEFRLPK-AIVQAEIEMLGVMGAELVTDIVVGATHTLDELLAEEGFDAVFVGSGAGLPLFLGIP 239
Cdd:PRK12831 168 IFEALHEPGGVLVYGIPEFRLPKeTVVKKEIENIKKLGVKIETNVVVGKTVTIDELLEEEGFDAVFIGSGAGLPKFMGIP 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 240 GENLNGVYSANEFLTRVNLMKAYEfPSYDTPVWRGRKVAVVGGGNVAMDAARTAKRLGAeEVFLVYRRSEEEMPARREEV 319
Cdd:PRK12831 248 GENLNGVFSANEFLTRVNLMKAYK-PEYDTPIKVGKKVAVVGGGNVAMDAARTALRLGA-EVHIVYRRSEEELPARVEEV 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 320 HHARQEGIEFKMLCSPQEIVG-HDGWVTGMVATRMELGEPDASGRRAPVCVMDSDFVIDCDTVIVALGTRSNPLISQTTP 398
Cdd:PRK12831 326 HHAKEEGVIFDLLTNPVEILGdENGWVKGMKCIKMELGEPDASGRRRPVEIEGSEFVLEVDTVIMSLGTSPNPLISSTTK 405
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1309180661 399 DLEVTSRGYIATDEN-GATNKPGVFAGGDIVTGSATVILAMGAGKKAARAIDSWLGG 454
Cdd:PRK12831 406 GLKINKRGCIVADEEtGLTSKEGVFAGGDAVTGAATVILAMGAGKKAAKAIDEYLSK 462
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
1-457 |
0e+00 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 681.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 1 MPERDALERARDFDEVSLGYSEEQALAEANRCIQCKNPTCIEGCPVNIDIKSFIARIIDGDYAGGVSVLKERNALPAVCG 80
Cdd:PRK11749 11 MPRQDAEERAQNFDEVAPGYTPEEAIEEASRCLQCKDAPCVKACPVSIDIPEFIRLIAEGNLKGAAETILETNPLPAVCG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 81 RVCPQEEQCEASCVLARKGEPIAIGRLERWLGDFDLAcdlEHRCAPEVGEPTGKRVAVVGSGPAGLACAGELRRFGHAVT 160
Cdd:PRK11749 91 RVCPQERLCEGACVRGKKGEPVAIGRLERYITDWAME---TGWVLFKRAPKTGKKVAVIGAGPAGLTAAHRLARKGYDVT 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 161 IFESLHAPGGVLTYGIPEFRLPKAIVQAEIEMLGVMGAELVTDIVVGATHTLDELLaeEGFDAVFVGSGAGLPLFLGIPG 240
Cdd:PRK11749 168 IFEARDKAGGLLRYGIPEFRLPKDIVDREVERLLKLGVEIRTNTEVGRDITLDELR--AGYDAVFIGTGAGLPRFLGIPG 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 241 ENLNGVYSANEFLTRVNLMKAYefpsYDTPVwrGRKVAVVGGGNVAMDAARTAKRLGAEEVFLVYRRSEEEMPARREEVH 320
Cdd:PRK11749 246 ENLGGVYSAVDFLTRVNQAVAD----YDLPV--GKRVVVIGGGNTAMDAARTAKRLGAESVTIVYRRGREEMPASEEEVE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 321 HARQEGIEFKMLCSPQEIVGHDGWVTGMVATRMELGEPDASGRRaPVCVMDSDFVIDCDTVIVALGTRSNPLISQTTPDL 400
Cdd:PRK11749 320 HAKEEGVEFEWLAAPVEILGDEGRVTGVEFVRMELGEPDASGRR-RVPIEGSEFTLPADLVIKAIGQTPNPLILSTTPGL 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1309180661 401 EVTSRGYIATDE-NGATNKPGVFAGGDIVTGSATVILAMGAGKKAARAIDSWLGGAAR 457
Cdd:PRK11749 399 ELNRWGTIIADDeTGRTSLPGVFAGGDIVTGAATVVWAVGDGKDAAEAIHEYLEGAAS 456
|
|
| PRK12778 |
PRK12778 |
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ... |
1-452 |
0e+00 |
|
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;
Pssm-ID: 237200 [Multi-domain] Cd Length: 752 Bit Score: 660.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 1 MPERDALERARD-FDEVSLGYSEEQALAEANRCIQCKNPTCIEGCPVNIDIKSFIARIIDGDYAGGVSVLKERNALPAVC 79
Cdd:PRK12778 299 MPELDPEYRAHNrFEEVNLGLTKEQAMTEAKRCLDCKNPGCVEGCPVGIDIPRFIKNIERGNFLEAAKILKETSALPAVC 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 80 GRVCPQEEQCEASCVLARKG-EPIAIGRLERWLGDFdlACDLEHRCAPEVGEPTGKRVAVVGSGPAGLACAGELRRFGHA 158
Cdd:PRK12778 379 GRVCPQEKQCESKCIHGKMGeEAVAIGYLERFVADY--ERESGNISVPEVAEKNGKKVAVIGSGPAGLSFAGDLAKRGYD 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 159 VTIFESLHAPGGVLTYGIPEFRLPKAIVQAEIEMLGVMGAELVTDIVVGATHTLDELlAEEGFDAVFVGSGAGLPLFLGI 238
Cdd:PRK12778 457 VTVFEALHEIGGVLKYGIPEFRLPKKIVDVEIENLKKLGVKFETDVIVGKTITIEEL-EEEGFKGIFIASGAGLPNFMNI 535
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 239 PGENLNGVYSANEFLTRVNLMKAYEfPSYDTPVWRGRKVAVVGGGNVAMDAARTAKRLGAEEVFLVYRRSEEEMPARREE 318
Cdd:PRK12778 536 PGENSNGVMSSNEYLTRVNLMDAAS-PDSDTPIKFGKKVAVVGGGNTAMDSARTAKRLGAERVTIVYRRSEEEMPARLEE 614
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 319 VHHARQEGIEFKMLCSPQEIVG-HDGWVTGMVATRMELGEPDASGRRAPVCVMDSDFVIDCDTVIVALGTRSNPLISQTT 397
Cdd:PRK12778 615 VKHAKEEGIEFLTLHNPIEYLAdEKGWVKQVVLQKMELGEPDASGRRRPVAIPGSTFTVDVDLVIVSVGVSPNPLVPSSI 694
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1309180661 398 PDLEVTSRGYIATDENGATNKPGVFAGGDIVTGSATVILAMGAGKKAARAIDSWL 452
Cdd:PRK12778 695 PGLELNRKGTIVVDEEMQSSIPGIYAGGDIVRGGATVILAMGDGKRAAAAIDEYL 749
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
9-451 |
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: 623.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 9 RARDFDEVSLGYSEEQALAEANRCIQCKNPTCIEGCPVNIDIKSFIARIIDGDYAGGVSVLKERNALPAVCGRVCPQeeQ 88
Cdd:COG0493 1 RIKDFREVYPGLSEEEAIEQAARCLDCGDPPCQTGCPVGNDIPEWIRLIAEGDYEEALELIHETNPFPEVCGRVCPA--P 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 89 CEASCVLARKGEPIAIGRLERWLGDFDLACDLEHRcaPEVGEPTGKRVAVVGSGPAGLACAGELRRFGHAVTIFESLHAP 168
Cdd:COG0493 79 CEGACVRGIVDEPVAIGALERFIADKAFEEGWVKP--PPPAPRTGKKVAVVGSGPAGLAAAYQLARAGHEVTVFEALDKP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 169 GGVLTYGIPEFRLPKAIVQAEIEMLGVMGAELVTDIVVGATHTLDELLAEegFDAVFVGSGAGLPLFLGIPGENLNGVYS 248
Cdd:COG0493 157 GGLLRYGIPEFRLPKDVLDREIELIEALGVEFRTNVEVGKDITLDELLEE--FDAVFLATGAGKPRDLGIPGEDLKGVHS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 249 ANEFLTRVNLMKAyefpsYDTPVWRGRKVAVVGGGNVAMDAARTAKRLGAEEVFLVYRRSEEEMPARREEVHHARQEGIE 328
Cdd:COG0493 235 AMDFLTAVNLGEA-----PDTILAVGKRVVVIGGGNTAMDCARTALRLGAESVTIVYRRTREEMPASKEEVEEALEEGVE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 329 FKMLCSPQEIVG-HDGWVTGMVATRMELGEPDASGRRAPVCVMDSDFVIDCDTVIVALGTRSNPLISQTTPDLEVTSRGY 407
Cdd:COG0493 310 FLFLVAPVEIIGdENGRVTGLECVRMELGEPDESGRRRPVPIEGSEFTLPADLVILAIGQTPDPSGLEEELGLELDKRGT 389
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1309180661 408 IATDE-NGATNKPGVFAGGDIVTGSATVILAMGAGKKAARAIDSW 451
Cdd:COG0493 390 IVVDEeTYQTSLPGVFAGGDAVRGPSLVVWAIAEGRKAARAIDRY 434
|
|
| PRK12775 |
PRK12775 |
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin ... |
1-452 |
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: 552.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 1 MPERDALERARDFDEVSLGYSEEQALAEANRCIQCKNPTCIEGCPVNIDIKSFIARIIDGDYAGGVSVLKERNALPAVCG 80
Cdd:PRK12775 302 MPERDAVERARNFKEVNLGYSLEDALQEAERCIQCAKPTCIAGCPVQIDIPVFIRHVVVRDFDGALEVIYEASIFPSICG 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 81 RVCPQEEQCEASCVLARKGEPIAIGRLERWLGDFDLACDLEhrcAPEVGEPTGKrVAVVGSGPAGLACAGELRRFGHAVT 160
Cdd:PRK12775 382 RVCPQETQCEAQCIIAKKHESVGIGRLERFVGDNARAKPVK---PPRFSKKLGK-VAICGSGPAGLAAAADLVKYGVDVT 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 161 IFESLHAPGGVLTYGIPEFRLPKAIVQAEIEMLGVMGAELVTDIVVGATHTLDELLAEEGFDAVFVGSGAGLPLFLGIPG 240
Cdd:PRK12775 458 VYEALHVVGGVLQYGIPSFRLPRDIIDREVQRLVDIGVKIETNKVIGKTFTVPQLMNDKGFDAVFLGVGAGAPTFLGIPG 537
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 241 ENLNGVYSANEFLTRVNLMKAYEFPSYDTPVWRGRKVAVVGGGNVAMDAARTAKRLGAEEVFLVYRRSEEEMPARREEVH 320
Cdd:PRK12775 538 EFAGQVYSANEFLTRVNLMGGDKFPFLDTPISLGKSVVVIGAGNTAMDCLRVAKRLGAPTVRCVYRRSEAEAPARIEEIR 617
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 321 HARQEGIEFKMLCSPQEI-VGHDGWVTGMVATRMELGEPDASGRRAPVcVMDSDFVIDCDTVIVALGTRSNPLISQTTPD 399
Cdd:PRK12775 618 HAKEEGIDFFFLHSPVEIyVDAEGSVRGMKVEEMELGEPDEKGRRKPM-PTGEFKDLECDTVIYALGTKANPIITQSTPG 696
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1309180661 400 LEVTSRGYIATDENG-----ATNKPGVFAGGDIVTGSATVILAMGAGKKAARAIDSWL 452
Cdd:PRK12775 697 LALNKWGNIAADDGKlestqSTNLPGVFAGGDIVTGGATVILAMGAGRRAARSIATYL 754
|
|
| gltA |
TIGR01316 |
glutamate synthase (NADPH), homotetrameric; This protein is homologous to the small subunit of ... |
8-452 |
0e+00 |
|
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: 517.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 8 ERARDFDEVSLGYSEEQALAEANRCIQCKNPT--CIEGCPVNIDIKSFIARIIDGDYAGGVSVLKERNALPAVCGRVCPQ 85
Cdd:TIGR01316 4 ERSKLFQEAALGYTEQLALVEAQRCLNCKDATkpCIKGCPVHVPIPEFIAKIQEGDFKGAVDIIKTTSLLPAICGRVCPQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 86 EEQCEASCVLAR----KGEPIAIGRLERWLGDFDLACDLEHrcAPEVGEPTGKRVAVVGSGPAGLACAGELRRFGHAVTI 161
Cdd:TIGR01316 84 ERQCEGQCTVGKmfkdVGKPVSIGALERFVADWERQHGIET--EPEKAPSTHKKVAVIGAGPAGLACASELAKAGHSVTV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 162 FESLHAPGGVLTYGIPEFRLPKAIVQAEIEMLGVMGAELVTDIVVGATHTLDELLAEegFDAVFVGSGAGLPLFLGIPGE 241
Cdd:TIGR01316 162 FEALHKPGGVVTYGIPEFRLPKEIVVTEIKTLKKLGVTFRMNFLVGKTATLEELFSQ--YDAVFIGTGAGLPKLMNIPGE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 242 NLNGVYSANEFLTRVNLMKAYEFPSYDTPVWRGRKVAVVGGGNVAMDAARTAKRLGAeEVFLVYRRSEEEMPARREEVHH 321
Cdd:TIGR01316 240 ELCGVYSANDFLTRANLMKAYEFPHADTPVYAGKSVVVIGGGNTAVDSARTALRLGA-EVHCLYRRTREDMTARVEEIAH 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 322 ARQEGIEFKMLCSPQEIVGHD-GWVTGMVATRMELGEPDASGRRAPVCVMDSDFVIDCDTVIVALGTRSNPLISQTTpDL 400
Cdd:TIGR01316 319 AEEEGVKFHFLCQPVEIIGDEeGNVRAVKFRKMDCQEQIDSGERRFLPCGDAECKLEADAVIVAIGNGSNPIMAETT-RL 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1309180661 401 EVTSRGYIATDENGATNKPGVFAGGDIVTGSATVILAMGAGKKAARAIDSWL 452
Cdd:TIGR01316 398 KTSERGTIVVDEDQRTSIPGVFAGGDIILGAATVIRAMGQGKRAAKSINEYL 449
|
|
| gltD |
PRK12810 |
glutamate synthase subunit beta; Reviewed |
2-456 |
3.55e-135 |
|
glutamate synthase subunit beta; Reviewed
Pssm-ID: 237213 [Multi-domain] Cd Length: 471 Bit Score: 397.23 E-value: 3.55e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 2 PERDALERARDFDEVSLGYSEEQALAEANRCIQCKNPTCIEGCPVNIDIKSFIARIIDGDYAGGVSVLKERNALPAVCGR 81
Cdd:PRK12810 16 KKRPVAERIKDFKEFYEPFSEEQAKIQAARCMDCGIPFCHWGCPVHNYIPEWNDLVYRGRWEEAAERLHQTNNFPEFTGR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 82 VCPQEeqCEASCVLARKGEPIAIGRLERWLGD--FDlacdlEHRCAPEVG-EPTGKRVAVVGSGPAGLACAGELRRFGHA 158
Cdd:PRK12810 96 VCPAP--CEGACTLNINFGPVTIKNIERYIIDkaFE-----EGWVKPDPPvKRTGKKVAVVGSGPAGLAAADQLARAGHK 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 159 VTIFESLHAPGGVLTYGIPEFRLPKAIVQAEIEMLGVMGAELVTDIVVGATHTLDELLAEegFDAVFVGSGAGLPLFLGI 238
Cdd:PRK12810 169 VTVFERADRIGGLLRYGIPDFKLEKEVIDRRIELMEAEGIEFRTNVEVGKDITAEELLAE--YDAVFLGTGAYKPRDLGI 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 239 PGENLNGVYSANEFL---TRVNLmkAYEFPSYDTPVwrGRKVAVVGGGNVAMDAARTAKRLGAEEvflVYRRSEEEMPAR 315
Cdd:PRK12810 247 PGRDLDGVHFAMDFLiqnTRRVL--GDETEPFISAK--GKHVVVIGGGDTGMDCVGTAIRQGAKS---VTQRDIMPMPPS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 316 RE-------------EVHHARQEGIEFKMLCSPQEIVGHDGWVTGMVATRMELGEPDasgrraPVCVMDSDFVIDCDTVI 382
Cdd:PRK12810 320 RRnknnpwpywpmklEVSNAHEEGVEREFNVQTKEFEGENGKVTGVKVVRTELGEGD------FEPVEGSEFVLPADLVL 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1309180661 383 VALGTRSNPLISQTTPDLEVTSRGYIATDENG-ATNKPGVFAGGDIVTGSATVILAMGAGKKAARAIDSWLGGAA 456
Cdd:PRK12810 394 LAMGFTGPEAGLLAQFGVELDERGRVAAPDNAyQTSNPKVFAAGDMRRGQSLVVWAIAEGRQAARAIDAYLMGST 468
|
|
| PRK12779 |
PRK12779 |
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; ... |
4-448 |
8.38e-131 |
|
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; Provisional
Pssm-ID: 183740 [Multi-domain] Cd Length: 944 Bit Score: 400.75 E-value: 8.38e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 4 RDALERARDFDEVSLGYSEEQALA------------EANRCIQCKNPTC------------IEGCPVNIDIKSFIARIID 59
Cdd:PRK12779 150 RPAEERAVDFDLVNQGYLGYQSLGysvrevelfvwlEVMRDKQCDDKPCelgvlvqgkaepKGGCPVKIHIPEMLDLLGN 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 60 GDYAGGVSVLKERNALPAVCGRVCPQEEQCEASCVlaRKGEPIAIGRLERWLGDF------DLACDLEHRCAPEVGePTG 133
Cdd:PRK12779 230 GKHREALELIESCNPLPNVTGRVCPQELQCQGVCT--HTKRPIEIGQLEWYLPQHeklvnpNANERFAGRISPWAA-AVK 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 134 KRVAVVGSGPAGLACAGELRRFGHAVTIFESLHAPGGVLTYGIPEFRLPKAIVQAEIEMLGVMGAELVTDIVVGATHTLD 213
Cdd:PRK12779 307 PPIAVVGSGPSGLINAYLLAVEGFPVTVFEAFHDLGGVLRYGIPEFRLPNQLIDDVVEKIKLLGGRFVKNFVVGKTATLE 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 214 ELLAeEGFDAVFVGSGAGLPLFLGIPGENLNGVYSANEFLTRVNLMKAYEfPSYDTPV--WRGRKVAVVGGGNVAMDAAR 291
Cdd:PRK12779 387 DLKA-AGFWKIFVGTGAGLPTFMNVPGEHLLGVMSANEFLTRVNLMRGLD-DDYETPLpeVKGKEVFVIGGGNTAMDAAR 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 292 TAKRLGAeEVFLVYRRSEEEMPARREEVHHARQEGIEFKMLCSPQEIVG--HDGWVTGMVATRMELGEPDASGRRAPVCV 369
Cdd:PRK12779 465 TAKRLGG-NVTIVYRRTKSEMPARVEELHHALEEGINLAVLRAPREFIGddHTHFVTHALLDVNELGEPDKSGRRSPKPT 543
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 370 MDSDFViDCDTVIVALGTRSNPLISQTTPDLEVTSRGYIATDENG-ATNKPGVFAGGDIVTGSATVILAMGAGKKAARAI 448
Cdd:PRK12779 544 GEIERV-PVDLVIMALGNTANPIMKDAEPGLKTNKWGTIEVEKGSqRTSIKGVYSGGDAARGGSTAIRAAGDGQAAAKEI 622
|
|
| PRK12771 |
PRK12771 |
putative glutamate synthase (NADPH) small subunit; Provisional |
38-455 |
5.75e-128 |
|
putative glutamate synthase (NADPH) small subunit; Provisional
Pssm-ID: 237198 [Multi-domain] Cd Length: 564 Bit Score: 382.30 E-value: 5.75e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 38 PTCIEGCPVNIDIKSFIARIIDGDYAGGVSVLKERNALPAVCGRVCPQEeqCEASCVLARKGEPIAIGRLERWLGDFDLA 117
Cdd:PRK12771 47 PPCNAACPAGEDIRGWLALVRGGDYEYAWRRLTKDNPFPAVMGRVCYHP--CESGCNRGQVDDAVGINAVERFLGDYAIA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 118 CDLEHrcaPEVGEPTGKRVAVVGSGPAGLACAGELRRFGHAVTIFESLHAPGGVLTYGIPEFRLPKAIVQAEIEMLGVMG 197
Cdd:PRK12771 125 NGWKF---PAPAPDTGKRVAVIGGGPAGLSAAYHLRRMGHAVTIFEAGPKLGGMMRYGIPAYRLPREVLDAEIQRILDLG 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 198 AELVTDIVVGATHTLDELlaEEGFDAVFVGSGAGLPLFLGIPGENLNGVYSANEFLTRVNLMKayefpsydtPVWRGRKV 277
Cdd:PRK12771 202 VEVRLGVRVGEDITLEQL--EGEFDAVFVAIGAQLGKRLPIPGEDAAGVLDAVDFLRAVGEGE---------PPFLGKRV 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 278 AVVGGGNVAMDAARTAKRLGAEEVFLVYRRSEEEMPARREEVHHARQEGIEFKMLCSPQEIVGHDGWVTGMVATRMELGE 357
Cdd:PRK12771 271 VVIGGGNTAMDAARTARRLGAEEVTIVYRRTREDMPAHDEEIEEALREGVEINWLRTPVEIEGDENGATGLRVITVEKME 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 358 PDASGRRAPVCvmDSDFVIDCDTVIVALG--TRSNPLisQTTPDLEVtSRGYIATDENGA-TNKPGVFAGGDIVTGSATV 434
Cdd:PRK12771 351 LDEDGRPSPVT--GEEETLEADLVVLAIGqdIDSAGL--ESVPGVEV-GRGVVQVDPNFMmTGRPGVFAGGDMVPGPRTV 425
|
410 420
....*....|....*....|.
gi 1309180661 435 ILAMGAGKKAARAIDSWLGGA 455
Cdd:PRK12771 426 TTAIGHGKKAARNIDAFLGGE 446
|
|
| gltD_gamma_fam |
TIGR01318 |
glutamate synthase small subunit family protein, proteobacterial; This model represents one of ... |
1-453 |
4.22e-120 |
|
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: 358.73 E-value: 4.22e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 1 MPERDALE-RARDFDEVSLGYSEEQALAEANRCIQCKNPTCIEGCPVNIDIKSFIARIIDGDYAGGVSVLKERNALPAVC 79
Cdd:TIGR01318 10 DPDKIPVEeRKTDFREIYGPFDKGQAQYQADRCLDCGNPYCEWKCPVHNAIPQWLQLVQEGRIDEAAELSHQTNTLPEIC 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 80 GRVCPQEEQCEASCVLARKGEPIAIGRLERWLGDFDLAC----DLEHRcapevgEPTGKRVAVVGSGPAGLACAGELRRF 155
Cdd:TIGR01318 90 GRVCPQDRLCEGACTLNDEGGAVTIGNLERYITDTALAMgwrpDLSHV------QPTGKRVAVIGAGPAGLACADILARA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 156 GHAVTIFESLHAPGGVLTYGIPEFRLPKAIVQAEIEMLGVMGAELVTDIVVGATHTLDELLaeEGFDAVFVGSGAGLPLF 235
Cdd:TIGR01318 164 GVQVVVFDRHPEIGGLLTFGIPSFKLDKAVLSRRREIFTAMGIEFRLNCEVGRDISLDDLL--EDYDAVFLGVGTYRSMR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 236 LGIPGENLNGVYSANEFL---TRvNLMKAYEFPSYDTPVWRGRKVAVVGGGNVAMDAARTAKRLGAEEVFLVYRRSEEEM 312
Cdd:TIGR01318 242 GGLPGEDAPGVLPALPFLianTR-QLMGLPEEPEEPLIDVEGKRVVVLGGGDTAMDCVRTAIRLGATKVTCAYRRDEANM 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 313 PARREEVHHARQEGIEFKMLCSPQEIVGH-DGWVTGMVATRMELGEPDASGRRAPVCVMDSDFVIDCDTVIVALGTRSNP 391
Cdd:TIGR01318 321 PGSRREVANAREEGVEFLFNVQPVSIESDeDGQVIGVTVVRTKLGEPDANGRRRPVPVAGSEFVLPADVVIMAFGFSPHL 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1309180661 392 LISQTTPDLEVTSRGYIATDENGA----TNKPGVFAGGDIVTGSATVILAMGAGKKAARAIDSWLG 453
Cdd:TIGR01318 401 MPWLAAHGITLDSWGRIITALSSGltyqTTNPKIFAGGDAVRGADLVVTAVAEGRDAAQGILDWLG 466
|
|
| PRK12814 |
PRK12814 |
putative NADPH-dependent glutamate synthase small subunit; Provisional |
29-454 |
4.06e-118 |
|
putative NADPH-dependent glutamate synthase small subunit; Provisional
Pssm-ID: 139246 [Multi-domain] Cd Length: 652 Bit Score: 359.81 E-value: 4.06e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 29 ANRCIQCKNPtCIEGCPVNIDIKSFIARIIDGDYAGGVSVLKERNALPAVCGRVCPQEeqCEASCvlARKG--EPIAIGR 106
Cdd:PRK12814 94 EQHCGDCLGP-CELACPAGCNIPGFIAAIARGDDREAIRIIKETIPLPGILGRICPAP--CEEAC--RRHGvdEPVSICA 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 107 LERWLGDFDLACdlEHRCAPEVGEPTGKRVAVVGSGPAGLACAGELRRFGHAVTIFESLHAPGGVLTYGIPEFRLPKAIV 186
Cdd:PRK12814 169 LKRYAADRDMES--AERYIPERAPKSGKKVAIIGAGPAGLTAAYYLLRKGHDVTIFDANEQAGGMMRYGIPRFRLPESVI 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 187 QAEIEMLGVMGAELVTDIVVGATHTLDELLAEegFDAVFVGSGAGLPLFLGIPGENLNGVYSANEFLTRVNLMKAYEFps 266
Cdd:PRK12814 247 DADIAPLRAMGAEFRFNTVFGRDITLEELQKE--FDAVLLAVGAQKASKMGIPGEELPGVISGIDFLRNVALGTALHP-- 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 267 ydtpvwrGRKVAVVGGGNVAMDAARTAKRLGAEEVFLVYRRSEEEMPARREEVHHARQEGIEFKMLCSPQEIVGHDGWVT 346
Cdd:PRK12814 323 -------GKKVVVIGGGNTAIDAARTALRLGAESVTILYRRTREEMPANRAEIEEALAEGVSLRELAAPVSIERSEGGLE 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 347 gMVATRMELGEPDASGRRAPVCVMDSDFVIDCDTVIVALGTRSNPLIsQTTPDLEVTSRGYIATD-ENGATNKPGVFAGG 425
Cdd:PRK12814 396 -LTAIKMQQGEPDESGRRRPVPVEGSEFTLQADTVISAIGQQVDPPI-AEAAGIGTSRNGTVKVDpETLQTSVAGVFAGG 473
|
410 420
....*....|....*....|....*....
gi 1309180661 426 DIVTGSATVILAMGAGKKAARAIDSWLGG 454
Cdd:PRK12814 474 DCVTGADIAINAVEQGKRAAHAIDLFLNG 502
|
|
| PRK12769 |
PRK12769 |
putative oxidoreductase Fe-S binding subunit; Reviewed |
2-453 |
1.53e-105 |
|
putative oxidoreductase Fe-S binding subunit; Reviewed
Pssm-ID: 183733 [Multi-domain] Cd Length: 654 Bit Score: 327.47 E-value: 1.53e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 2 PERDALE-RARDFDEVSLGYSEEQALAEANRCIQC-KNPTCIEGCPVNIDIKSFIARIIDGDYAGGVSVLKERNALPAVC 79
Cdd:PRK12769 196 PDKLAIEaRKTGFDEIYLPFRADQAQREASRCLKCgEHSICEWTCPLHNHIPQWIELVKAGNIDAAVELSHQTNSLPEIT 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 80 GRVCPQEEQCEASCVLARKGEPIAIGRLERWLGDFDLAC----DLEHRcapevgEPTGKRVAVVGSGPAGLACAGELRRF 155
Cdd:PRK12769 276 GRVCPQDRLCEGACTLRDEYGAVTIGNIERYISDQALAKgwrpDLSQV------TKSDKRVAIIGAGPAGLACADVLARN 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 156 GHAVTIFESLHAPGGVLTYGIPEFRLPKAIVQAEIEMLGVMGAELVTDIVVGATHTLDELLAEegFDAVFVGSGAGLPLF 235
Cdd:PRK12769 350 GVAVTVYDRHPEIGGLLTFGIPAFKLDKSLLARRREIFSAMGIEFELNCEVGKDISLESLLED--YDAVFVGVGTYRSMK 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 236 LGIPGENLNGVYSANEFL---TRvNLMKAYEFPSYDTPVWRGRKVAVVGGGNVAMDAARTAKRLGAEEVFLVYRRSEEEM 312
Cdd:PRK12769 428 AGLPNEDAPGVYDALPFLianTK-QVMGLEELPEEPFINTAGLNVVVLGGGDTAMDCVRTALRHGASNVTCAYRRDEANM 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 313 PARREEVHHARQEGIEFKMLCSPQEIV-GHDGWVTGMVATRMELGEPDASGRRAPVCVMDSDFVIDCDTVIVALGTRSNP 391
Cdd:PRK12769 507 PGSKKEVKNAREEGANFEFNVQPVALElNEQGHVCGIRFLRTRLGEPDAQGRRRPVPIPGSEFVMPADAVIMAFGFNPHG 586
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1309180661 392 LISQTTPDLEVTSRGYIATDENGA----TNKPGVFAGGDIVTGSATVILAMGAGKKAARAIDSWLG 453
Cdd:PRK12769 587 MPWLESHGVTVDKWGRIIADVESQyryqTSNPKIFAGGDAVRGADLVVTAMAEGRHAAQGIIDWLG 652
|
|
| PRK13984 |
PRK13984 |
putative oxidoreductase; Provisional |
1-455 |
5.15e-92 |
|
putative oxidoreductase; Provisional
Pssm-ID: 172486 [Multi-domain] Cd Length: 604 Bit Score: 290.90 E-value: 5.15e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 1 MPERDALERARDFDEVSLGYSEEQALAEANRCIQCKnpTCIEGCPVNIDIKSFIARIIDGDYAGGVSVLKERNALPAVCG 80
Cdd:PRK13984 156 MEEIPPEERVKSFIEIVKGYSKEQAMQEAARCVECG--ICTDTCPAHMDIPQYIKAIYKDDLEEGLRWLYKTNPLSMVCG 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 81 RVCPQeeQCEASCVLARKGEPIAIGRLERWLGDfDLACDLEHRCAPEVGEPTGKRVAVVGSGPAGLACAGELRRFGHAVT 160
Cdd:PRK13984 234 RVCTH--KCETVCSIGHRGEPIAIRWLKRYIVD-NVPVEKYSEILDDEPEKKNKKVAIVGSGPAGLSAAYFLATMGYEVT 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 161 IFESLHAPGGVLTYGIPEFRLPKAIVQAEIEMLGVMGAELVTDIVVGATHTLDELlaEEGFDAVFVGSGAGLPLFLGIPG 240
Cdd:PRK13984 311 VYESLSKPGGVMRYGIPSYRLPDEALDKDIAFIEALGVKIHLNTRVGKDIPLEEL--REKHDAVFLSTGFTLGRSTRIPG 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 241 ENLNGVYSANEFLTRVNLMKAYEFPSYDTPvwrgRKVAVVGGGNVAMDAARTAKRL-----GAEEVFLV-YRRSEEEMPA 314
Cdd:PRK13984 389 TDHPDVIQALPLLREIRDYLRGEGPKPKIP----RSLVVIGGGNVAMDIARSMARLqkmeyGEVNVKVTsLERTFEEMPA 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 315 RREEVHHARQEGIEFKMLCSPQEIVGHDGWVTGmVATRMELGEPDASGRRAPVCVMDSDFVIDCDTVIVALGTRSNP--L 392
Cdd:PRK13984 465 DMEEIEEGLEEGVVIYPGWGPMEVVIENDKVKG-VKFKKCVEVFDEEGRFNPKFDESDQIIVEADMVVEAIGQAPDYsyL 543
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1309180661 393 ISQTTPDLEVTsRGYIATDENGATNKPGVFAGGDIVTGsATVILAMGAGKKAARAIDSWLGGA 455
Cdd:PRK13984 544 PEELKSKLEFV-RGRILTNEYGQTSIPWLFAGGDIVHG-PDIIHGVADGYWAAEGIDMYLRKQ 604
|
|
| PRK12770 |
PRK12770 |
putative glutamate synthase subunit beta; Provisional |
123-452 |
7.64e-92 |
|
putative glutamate synthase subunit beta; Provisional
Pssm-ID: 237197 [Multi-domain] Cd Length: 352 Bit Score: 282.26 E-value: 7.64e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 123 RCApEVGEPTGKRVAVVGSGPAGLACAGELRRFGHAVTIFESLHAPGGVLTYGIPEFRLPKAIVQA---EIEMLGV---- 195
Cdd:PRK12770 9 MCK-EKPPPTGKKVAIIGAGPAGLAAAGYLACLGYEVHVYDKLPEPGGLMLFGIPEFRIPIERVREgvkELEEAGVvfht 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 196 -------------MGAELVTDIVvgathTLDELLAEegFDAVFVGSGAGLPLFLGIPGENLNGVYSANEFLTRVNLMKAY 262
Cdd:PRK12770 88 rtkvccgeplheeEGDEFVERIV-----SLEELVKK--YDAVLIATGTWKSRKLGIPGEDLPGVYSALEYLFRIRAAKLG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 263 EFPSYDTPVWRGRKVAVVGGGNVAMDAARTAKRLGAEEVFLVYRRSEEEMPARREEVHHARQEGIEFKMLCSPQEIVGhD 342
Cdd:PRK12770 161 YLPWEKVPPVEGKKVVVVGAGLTAVDAALEAVLLGAEKVYLAYRRTINEAPAGKYEIERLIARGVEFLELVTPVRIIG-E 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 343 GWVTGMVATRMELGEPDASGRRAPVCVMDSDFVIDCDTVIVALGTRSNPLISQTTPDLEVTSRGYIATDENGATNKPGVF 422
Cdd:PRK12770 240 GRVEGVELAKMRLGEPDESGRPRPVPIPGSEFVLEADTVVFAIGEIPTPPFAKECLGIELNRKGEIVVDEKHMTSREGVF 319
|
330 340 350
....*....|....*....|....*....|
gi 1309180661 423 AGGDIVTGSATVILAMGAGKKAARAIDSWL 452
Cdd:PRK12770 320 AAGDVVTGPSKIGKAIKSGLRAAQSIHEWL 349
|
|
| PRK12809 |
PRK12809 |
putative oxidoreductase Fe-S binding subunit; Reviewed |
6-446 |
2.54e-89 |
|
putative oxidoreductase Fe-S binding subunit; Reviewed
Pssm-ID: 183762 [Multi-domain] Cd Length: 639 Bit Score: 284.61 E-value: 2.54e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 6 ALERARDFDEVSLGYSEEQALAEANRCIQC-KNPTCIEGCPVNIDIKSFIARIIDGDYAGGVSVLKERNALPAVCGRVCP 84
Cdd:PRK12809 184 ASERKTHFGEIYCGLDPQQATYESDRCVYCaEKANCNWHCPLHNAIPDYIRLVQEGKIIEAAELCHQTSSLPEICGRVCP 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 85 QEEQCEASCVLARKGEPIAIGRLERWLGDFDLACDLEhrcaPEVGE--PTGKRVAVVGSGPAGLACAGELRRFGHAVTIF 162
Cdd:PRK12809 264 QDRLCEGACTLKDHSGAVSIGNLERYITDTALAMGWR----PDVSKvvPRSEKVAVIGAGPAGLGCADILARAGVQVDVF 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 163 ESLHAPGGVLTYGIPEFRLPKAIVQAEIEMLGVMGAELVTDIVVGATHTLDELLAEegFDAVFVGSGAGLPLFLGIPGEN 242
Cdd:PRK12809 340 DRHPEIGGMLTFGIPPFKLDKTVLSQRREIFTAMGIDFHLNCEIGRDITFSDLTSE--YDAVFIGVGTYGMMRADLPHED 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 243 LNGVYSANEFLT--RVNLMKAYEFPSYDTPVWRGRKVAVVGGGNVAMDAARTAKRLGAEEVFLVYRRSEEEMPARREEVH 320
Cdd:PRK12809 418 APGVIQALPFLTahTRQLMGLPESEEYPLTDVEGKRVVVLGGGDTTMDCLRTSIRLNAASVTCAYRRDEVSMPGSRKEVV 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 321 HARQEGIEFKMLCSPQEIV-GHDGWVTGMVATRMELGEPDASGRRAPVCVMDSDFVIDCDTVIVALGTRSNPLISQTTPD 399
Cdd:PRK12809 498 NAREEGVEFQFNVQPQYIAcDEDGRLTAVGLIRTAMGEPGPDGRRRPRPVAGSEFELPADVLIMAFGFQAHAMPWLQGSG 577
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1309180661 400 LEVTSRGYIATDENG----ATNKPGVFAGGDIVTGSATVILAMGAGKKAAR 446
Cdd:PRK12809 578 IKLDKWGLIQTGDVGylptQTHLKKVFAGGDAVHGADLVVTAMAAGRQAAR 628
|
|
| GOGAT_sm_gam |
TIGR01317 |
glutamate synthases, NADH/NADPH, small subunit; This model represents one of three built for ... |
2-454 |
3.10e-84 |
|
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: 267.08 E-value: 3.10e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 2 PERDALERARDFDEVSLGYSEEQALAEANRCIQCKNPTC--IEGCPVNIDIKSFIARIIDGDYAGGVSVLKERNALPAVC 79
Cdd:TIGR01317 14 TERDPRTRLKDWKEFTNPFDKESAKYQAARCMDCGTPFChnDSGCPLNNLIPEFNDLVFRGRWKEALDRLHATNNFPEFT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 80 GRVCPQEeqCEASCVLARKGEPIAIGRLERWLGDFDLACDLEHRCAPEVgePTGKRVAVVGSGPAGLACAGELRRFGHAV 159
Cdd:TIGR01317 94 GRVCPAP--CEGACTLGISEDPVGIKSIERIIIDKGFQEGWVQPRPPSK--RTGKKVAVVGSGPAGLAAADQLNRAGHTV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 160 TIFESLHAPGGVLTYGIPEFRLPKAIVQAEIEMLGVMGAELVTDIVVGATHTLDELLAEegFDAVFVGSGAGLPLFLGIP 239
Cdd:TIGR01317 170 TVFEREDRCGGLLMYGIPNMKLDKAIVDRRIDLLSAEGIDFVTNTEIGVDISADELKEQ--FDAVVLAGGATKPRDLPIP 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 240 GENLNGVYSANEFL---TRVNLMKAYEFPSYDTPvwRGRKVAVVGGGNVAMDAARTAKRLGAEEV--FLVYRRSEEEMPA 314
Cdd:TIGR01317 248 GRELKGIHYAMEFLpsaTKALLGKDFKDIIFIKA--KGKKVVVIGGGDTGADCVGTSLRHGAASVhqFEIMPKPPEARAK 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 315 --------RREEVHHARQEGIEF------KMLCSPQEIVGHD-GWVTGMVATRMELgEPDASGRRAPVCVMDSDFVIDCD 379
Cdd:TIGR01317 326 dnpwpewpRVYRVDYAHEEAAAHygrdprEYSILTKEFIGDDeGKVTALRTVRVEW-KKSQDGKWQFVEIPGSEEVFEAD 404
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1309180661 380 TVIVALGTRSNPLISQTTPDLEVTSRGYI-ATDENGATNKPGVFAGGDIVTGSATVILAMGAGKKAARAIDSWLGG 454
Cdd:TIGR01317 405 LVLLAMGFVGPEQILLDDFGVKKTRRGNIsAGYDDYSTSIPGVFAAGDCRRGQSLIVWAINEGRKAAAAVDRYLMG 480
|
|
| Fer4_20 |
pfam14691 |
Dihydroprymidine dehydrogenase domain II, 4Fe-4S cluster; Domain II of the enzyme ... |
9-117 |
3.12e-57 |
|
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: 184.66 E-value: 3.12e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 9 RARDFDEVSLGYSEEQALAEANRCIQCKNPTCIEGCPVNIDIKSFIARIIDGDYAGGVSVLKERNALPAVCGRVCPQEEQ 88
Cdd:pfam14691 1 RIKNFEEVALGYTEEEAIAEASRCLQCKDPPCVKGCPVHIDIPEFIKLIAEGNFEGAARIILETNPLPAICGRVCPQERQ 80
|
90 100 110
....*....|....*....|....*....|
gi 1309180661 89 CEASCVLARKG-EPIAIGRLERWLGDFDLA 117
Cdd:pfam14691 81 CEGACVLGKKGfEPVAIGRLERFAADWARE 110
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
136-455 |
2.81e-38 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 141.03 E-value: 2.81e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 136 VAVVGSGPAGLACAGELRRFGHAVTIFESLhAPGGVLT--------YGIPEFRLPKAIVQAEIEMLGVMGAELVTDIVVG 207
Cdd:COG0492 3 VVIIGAGPAGLTAAIYAARAGLKTLVIEGG-EPGGQLAttkeienyPGFPEGISGPELAERLREQAERFGAEILLEEVTS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 208 AThtldelLAEEGF------------DAVFVGSGAGlPLFLGIPGENL---NGVYSAnefltrvnlmkayefPSYDTPVW 272
Cdd:COG0492 82 VD------KDDGPFrvttddgteyeaKAVIIATGAG-PRKLGLPGEEEfegRGVSYC---------------ATCDGFFF 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 273 RGRKVAVVGGGNVAMDAARTAKRLgAEEVFLVYRRseEEMPARREEVHHARQ-EGIEFKMLCSPQEIVGhDGWVTGMVAT 351
Cdd:COG0492 140 RGKDVVVVGGGDSALEEALYLTKF-ASKVTLIHRR--DELRASKILVERLRAnPKIEVLWNTEVTEIEG-DGRVEGVTLK 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 352 RMELGEpdasgrrapvcvmdsDFVIDCDTVIVALGTRSNP-LISQTtpDLEVTSRGYIATDENGATNKPGVFAGGDIVTG 430
Cdd:COG0492 216 NVKTGE---------------EKELEVDGVFVAIGLKPNTeLLKGL--GLELDEDGYIVVDEDMETSVPGVFAAGDVRDY 278
|
330 340
....*....|....*....|....*.
gi 1309180661 431 S-ATVILAMGAGKKAARAIDSWLGGA 455
Cdd:COG0492 279 KyRQAATAAGEGAIAALSAARYLEPL 304
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
134-441 |
6.34e-38 |
|
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: 139.76 E-value: 6.34e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 134 KRVAVVGSGPAGLACAGELRRFGHAVTIFES---LHAPGGVLTYGIPEFRLPKAIVQAEIEMLGVMGAEL---------- 200
Cdd:pfam07992 1 YDVVVIGGGPAGLAAALTLAQLGGKVTLIEDegtCPYGGCVLSKALLGAAEAPEIASLWADLYKRKEEVVkklnngievl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 201 ----VTDIVVGA-----THTLDELLAEEGFDAVFVGSGAGlPLFLGIPGENLNGVYSaNEFLTRVNLMKAyefpsydtpV 271
Cdd:pfam07992 81 lgteVVSIDPGAkkvvlEELVDGDGETITYDRLVIATGAR-PRLPPIPGVELNVGFL-VRTLDSAEALRL---------K 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 272 WRGRKVAVVGGGNVAMDAARTAKRLGAeEVFLVYRRSE----EEMPARREEVHHARQEGIEFKMLCSPQEIVGHDGWVTg 347
Cdd:pfam07992 150 LLPKRVVVVGGGYIGVELAAALAKLGK-EVTLIEALDRllraFDEEISAALEKALEKNGVEVRLGTSVKEIIGDGDGVE- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 348 mvatrMELGEPDasgrrapvcvmdsdfVIDCDTVIVALGTRSNPLISQTTpDLEVTSRGYIATDENGATNKPGVFAGGDI 427
Cdd:pfam07992 228 -----VILKDGT---------------EIDADLVVVAIGRRPNTELLEAA-GLELDERGGIVVDEYLRTSVPGIYAAGDC 286
|
330
....*....|....*
gi 1309180661 428 -VTGSATVILAMGAG 441
Cdd:pfam07992 287 rVGGPELAQNAVAQG 301
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
159-457 |
1.86e-15 |
|
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: 77.16 E-value: 1.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 159 VTIFE------------SLHAPGGVLTYGIPEFRLPKAIVQAEIEMLgvMGAElVTDI------VVGATHTldellaEEG 220
Cdd:COG0446 8 ITVIEkgphhsyqpcglPYYVGGGIKDPEDLLVRTPESFERKGIDVR--TGTE-VTAIdpeaktVTLRDGE------TLS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 221 FDAVFVGSGAgLPLFLGIPGENLNGVYS------ANEFLTRVNLMKayefpsydtpvwrGRKVAVVGGGNVAMDAARTAK 294
Cdd:COG0446 79 YDKLVLATGA-RPRPPPIPGLDLPGVFTlrtlddADALREALKEFK-------------GKRAVVIGGGPIGLELAEALR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 295 RLGAeEVFLVYR------RSEEEMPARREEVHhaRQEGIEFKMLCSPQEIVGHDGwvtgmvaTRMELgepdASGRRapvc 368
Cdd:COG0446 145 KRGL-KVTLVERaprllgVLDPEMAALLEEEL--REHGVELRLGETVVAIDGDDK-------VAVTL----TDGEE---- 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 369 vmdsdfvIDCDTVIVALGTRSNPLISQTTPdLEVTSRGYIATDENGATNKPGVFAGGD------IVTGSATVI----LAM 438
Cdd:COG0446 207 -------IPADLVVVAPGVRPNTELAKDAG-LALGERGWIKVDETLQTSDPDVYAAGDcaevphPVTGKTVYIplasAAN 278
|
330
....*....|....*....
gi 1309180661 439 GAGKKAARAIdswLGGAAR 457
Cdd:COG0446 279 KQGRVAAENI---LGGPAP 294
|
|
| PLN02852 |
PLN02852 |
ferredoxin-NADP+ reductase |
130-435 |
2.37e-15 |
|
ferredoxin-NADP+ reductase
Pssm-ID: 215457 Cd Length: 491 Bit Score: 78.20 E-value: 2.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 130 EPTGKRVAVVGSGPAGLACAGE-LRRFGHA-VTIFESLHAPGGVLTYGI----PEFRlpkaIVQAEIEmlGVMGAELVT- 202
Cdd:PLN02852 23 TSEPLHVCVVGSGPAGFYTADKlLKAHDGArVDIIERLPTPFGLVRSGVapdhPETK----NVTNQFS--RVATDDRVSf 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 203 --DIVVGATHTLDELlaEEGFDAVFVGSGAGLPLFLGIPGENLNGVYSANEFLTRVNLMKAYEFPSYDtpVWRGRKVAVV 280
Cdd:PLN02852 97 fgNVTLGRDVSLSEL--RDLYHVVVLAYGAESDRRLGIPGEDLPGVLSAREFVWWYNGHPDCVHLPPD--LKSSDTAVVL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 281 GGGNVAMDAARTAKRLGAE--------------------EVFLVYRR--------------------------------- 307
Cdd:PLN02852 173 GQGNVALDCARILLRPTDElastdiaehalealrgssvrKVYLVGRRgpvqaactakelrellglknvrvrikeadltls 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 308 --SEEEMPARR--EEVHHA--------------RQEGIEFKMLCSPQEIVGHD---GWVTGMVATRMELgEPDASGRRAp 366
Cdd:PLN02852 253 peDEEELKASRpkRRVYELlskaaaagkcapsgGQRELHFVFFRNPTRFLDSGdgnGHVAGVKLERTVL-EGAAGSGKQ- 330
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1309180661 367 VCVMDSDF-VIDCDTVIVALGTRSNPLISQT-------TPDLEvtsrGYIATDENGATNKPGVFAGGDIVTGSATVI 435
Cdd:PLN02852 331 VAVGTGEFeDLPCGLVLKSIGYKSLPVDGLPfdhkrgvVPNVH----GRVLSSASGADTEPGLYVVGWLKRGPTGII 403
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
134-457 |
5.03e-14 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 73.64 E-value: 5.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 134 KRVAVVGSGPAGLACAGELRRFGHA--VTIF--ESLHAPGGV-LTYGIPEFRLPKAIVQAEIEMLGVMGAELVTDI-VVG 207
Cdd:COG1251 2 MRIVIIGAGMAGVRAAEELRKLDPDgeITVIgaEPHPPYNRPpLSKVLAGETDEEDLLLRPADFYEENGIDLRLGTrVTA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 208 ---ATHTL-DELLAEEGFDAVFVGSGAGlPLFLGIPGENLNGVYSaneFLTR--VNLMKAYefpsydtpVWRGRKVAVVG 281
Cdd:COG1251 82 idrAARTVtLADGETLPYDKLVLATGSR-PRVPPIPGADLPGVFT---LRTLddADALRAA--------LAPGKRVVVIG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 282 GGNVAMDAARTAKRLGAEeVFLVYRRS-------EEEMPARREEVHhaRQEGIEFKMLCSPQEIVGHDGwvtgmvATRME 354
Cdd:COG1251 150 GGLIGLEAAAALRKRGLE-VTVVERAPrllprqlDEEAGALLQRLL--EALGVEVRLGTGVTEIEGDDR------VTGVR 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 355 LgepdASGRrapvcvmdsdfVIDCDTVIVALGTRSN-PLISQTtpDLEVtSRGyIATDENGATNKPGVFAGGDI------ 427
Cdd:COG1251 221 L----ADGE-----------ELPADLVVVAIGVRPNtELARAA--GLAV-DRG-IVVDDYLRTSDPDIYAAGDCaehpgp 281
|
330 340 350
....*....|....*....|....*....|...
gi 1309180661 428 VTGSATVIL---AMGAGKKAARAIdswLGGAAR 457
Cdd:COG1251 282 VYGRRVLELvapAYEQARVAAANL---AGGPAA 311
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
136-457 |
3.31e-13 |
|
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: 71.27 E-value: 3.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 136 VAVVGSGPAGLACAGELRRFGHAVTIFESlHAPGGVLT-------------------------YGI----PEFRLPKAI- 185
Cdd:COG1249 6 LVVIGAGPGGYVAAIRAAQLGLKVALVEK-GRLGGTCLnvgcipskallhaaevahearhaaeFGIsagaPSVDWAALMa 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 186 -VQAEIEML--GVMG-------------AELVTD--IVVGATHTLDellaeegFDAVFVGSGAgLPLFLGIPGENLNGVY 247
Cdd:COG1249 85 rKDKVVDRLrgGVEEllkkngvdvirgrARFVDPhtVEVTGGETLT-------ADHIVIATGS-RPRVPPIPGLDEVRVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 248 SANEFLTrvnlMKayEFPsydtpvwrgRKVAVVGGGNVAMDAARTAKRLGAEeVFLVYRRS------EEEMparREEVHH 321
Cdd:COG1249 157 TSDEALE----LE--ELP---------KSLVVIGGGYIGLEFAQIFARLGSE-VTLVERGDrllpgeDPEI---SEALEK 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 322 A-RQEGIEFKMLCSPQEIVGHDGwvtGMVATrmelgepdASGRRAPVcvmdsdfVIDCDTVIVALGTRSNplisqtTPDL 400
Cdd:COG1249 218 AlEKEGIDILTGAKVTSVEKTGD---GVTVT--------LEDGGGEE-------AVEADKVLVATGRRPN------TDGL 273
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1309180661 401 -------EVTSRGYIATDENGATNKPGVFAGGDIVTGSATVILAMGAGKKAARAIdswLGGAAR 457
Cdd:COG1249 274 gleaagvELDERGGIKVDEYLRTSVPGIYAIGDVTGGPQLAHVASAEGRVAAENI---LGKKPR 334
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
134-455 |
1.98e-11 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 65.83 E-value: 1.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 134 KRVAVVGSGPAGLACAGELRRF--GHAVTIFE-----SLHAPGgvLTYGIPEF---------RLPKAIVQAEI------E 191
Cdd:PRK09564 1 MKIIIIGGTAAGMSAAAKAKRLnkELEITVYEktdivSFGACG--LPYFVGGFfddpntmiaRTPEEFIKSGIdvktehE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 192 MLGVMGAElvTDIVVGATHTLDELlaEEGFDAVFVGSGAGlPLFLGIPGENLNGVYSANEFLTRVNLMKAYEFPSYdtpv 271
Cdd:PRK09564 79 VVKVDAKN--KTITVKNLKTGSIF--NDTYDKLMIATGAR-PIIPPIKNINLENVYTLKSMEDGLALKELLKDEEI---- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 272 wrgRKVAVVGGGNVAMDAARTAKRLGaEEVFLVYRRS-------EEEMPARREEvhHARQEGIEFKMLCSPQEIVGHDGw 344
Cdd:PRK09564 150 ---KNIVIIGAGFIGLEAVEAAKHLG-KNVRIIQLEDrilpdsfDKEITDVMEE--ELRENGVELHLNEFVKSLIGEDK- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 345 VTGMVATRMElgepdasgrrapvcvmdsdfvIDCDTVIVALGTRSNP-LISQTtpDLEVTSRGYIATDENGATNKPGVFA 423
Cdd:PRK09564 223 VEGVVTDKGE---------------------YEADVVIVATGVKPNTeFLEDT--GLKTLKNGAIIVDEYGETSIENIYA 279
|
330 340 350
....*....|....*....|....*....|....*....
gi 1309180661 424 GGD------IVTGSATVI-LAMGAgKKAARAIDSWLGGA 455
Cdd:PRK09564 280 AGDcatiynIVSNKNVYVpLATTA-NKLGRMVGENLAGR 317
|
|
| PRK15317 |
PRK15317 |
alkyl hydroperoxide reductase subunit F; Provisional |
236-445 |
2.28e-10 |
|
alkyl hydroperoxide reductase subunit F; Provisional
Pssm-ID: 237942 [Multi-domain] Cd Length: 517 Bit Score: 62.48 E-value: 2.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 236 LGIPGENlngvysanEFLTR-VnlmkAYeFPSYDTPVWRGRKVAVVGGGNVAMDAA-------------RTAKRLGAEEV 301
Cdd:PRK15317 325 MNVPGED--------EYRNKgV----AY-CPHCDGPLFKGKRVAVIGGGNSGVEAAidlagivkhvtvlEFAPELKADQV 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 302 FLvyrRSEEEMParreevhharqeGIEFKMLCSPQEIVGHDGWVTGMVATRMELGEpdasgrrapvcvmdsDFVIDCDTV 381
Cdd:PRK15317 392 LQ---DKLRSLP------------NVTIITNAQTTEVTGDGDKVTGLTYKDRTTGE---------------EHHLELEGV 441
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1309180661 382 IVALGtrsnpLISQTT---PDLEVTSRGYIATDENGATNKPGVFAGGDiVTGSA--TVILAMGAGKKAA 445
Cdd:PRK15317 442 FVQIG-----LVPNTEwlkGTVELNRRGEIIVDARGATSVPGVFAAGD-CTTVPykQIIIAMGEGAKAA 504
|
|
| PRK06116 |
PRK06116 |
glutathione reductase; Validated |
275-430 |
2.27e-08 |
|
glutathione reductase; Validated
Pssm-ID: 235701 [Multi-domain] Cd Length: 450 Bit Score: 55.93 E-value: 2.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 275 RKVAVVGGGNVAMDAARTAKRLGAEeVFLVYRRseeEMPAR------REEVHHA-RQEGIEFKMLCSPQEIVGHDgwvTG 347
Cdd:PRK06116 168 KRVAVVGAGYIAVEFAGVLNGLGSE-THLFVRG---DAPLRgfdpdiRETLVEEmEKKGIRLHTNAVPKAVEKNA---DG 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 348 MVATRMELGEpdasgrrapvcvmdsdfVIDCDTVIVALGTRSNplisqtTPDL-------EVTSRGYIATDENGATNKPG 420
Cdd:PRK06116 241 SLTLTLEDGE-----------------TLTVDCLIWAIGREPN------TDGLglenagvKLNEKGYIIVDEYQNTNVPG 297
|
170
....*....|
gi 1309180661 421 VFAGGDiVTG 430
Cdd:PRK06116 298 IYAVGD-VTG 306
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
134-428 |
5.47e-08 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 54.75 E-value: 5.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 134 KRVAVVGSGPAGLACAGELRRF---GHAVTIFE---------SLHapgGVLTyGipefRLPKAIVQAEI-EMLGVMGAEL 200
Cdd:COG1252 2 KRIVIVGGGFAGLEAARRLRKKlggDAEVTLIDpnpyhlfqpLLP---EVAA-G----TLSPDDIAIPLrELLRRAGVRF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 201 VTDIVVG---ATHTLdeLLA---EEGFDAVFVGSGAGLPLFlGIPG--ENLNGVYSANEFLTRVN-LMKAYEFPSYDTPV 271
Cdd:COG1252 74 IQGEVTGidpEARTV--TLAdgrTLSYDYLVIATGSVTNFF-GIPGlaEHALPLKTLEDALALRErLLAAFERAERRRLL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 272 wrgrKVAVVGGGN----VAMDAARTAKRLGAE--------EVFLVYRrSEEEMPARREEVHHA-----RQEGIEFkmlcs 334
Cdd:COG1252 151 ----TIVVVGGGPtgveLAGELAELLRKLLRYpgidpdkvRITLVEA-GPRILPGLGEKLSEAaekelEKRGVEV----- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 335 pqeIVGHDgwVTGMVATRMELgepdASGRRapvcvmdsdfvIDCDTVIVALGTRSNPLISQTtpDLEVTSRGYIATDENG 414
Cdd:COG1252 221 ---HTGTR--VTEVDADGVTL----EDGEE-----------IPADTVIWAAGVKAPPLLADL--GLPTDRRGRVLVDPTL 278
|
330
....*....|....*
gi 1309180661 415 -ATNKPGVFAGGDIV 428
Cdd:COG1252 279 qVPGHPNVFAIGDCA 293
|
|
| CzcO |
COG2072 |
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ... |
131-307 |
9.30e-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: 54.10 E-value: 9.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 131 PTGKRVAVVGSGPAGLACAGELRRFGHAVTIFESLHAPGGV---------------LTYGIPEFRLPKAI----VQAEI- 190
Cdd:COG2072 4 TEHVDVVVIGAGQAGLAAAYHLRRAGIDFVVLEKADDVGGTwrdnrypglrldtpsHLYSLPFFPNWSDDpdfpTGDEIl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 191 -------EMLGVM-----GAElVTDIVVGATHTLDELLAEEG----FDAVFVGSGA-GLPLFLGIPG-ENLNG--VYSAN 250
Cdd:COG2072 84 ayleayaDKFGLRrpirfGTE-VTSARWDEADGRWTVTTDDGetltARFVVVATGPlSRPKIPDIPGlEDFAGeqLHSAD 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1309180661 251 efltrvnlmkayefpsYDTPV-WRGRKVAVVGGGN----VAMDAARTakrlgAEEVFLVYRR 307
Cdd:COG2072 163 ----------------WRNPVdLAGKRVLVVGTGAsavqIAPELARV-----AAHVTVFQRT 203
|
|
| PRK12771 |
PRK12771 |
putative glutamate synthase (NADPH) small subunit; Provisional |
1-84 |
9.54e-08 |
|
putative glutamate synthase (NADPH) small subunit; Provisional
Pssm-ID: 237198 [Multi-domain] Cd Length: 564 Bit Score: 54.50 E-value: 9.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 1 MPERDALERARDFDEVSLGYSEEQALAEANRCIQCKN----PTCIEGCPVNIDIKSFIARIIDGDYA---GGvsvlkern 73
Cdd:PRK12771 475 RPELDADERVGDFDEVLGGLTEEEARQEAARCLSCGNcfecDNCYGACPQDAIIKLGPGRRYHFDYDkctGC-------- 546
|
90
....*....|.
gi 1309180661 74 alpAVCGRVCP 84
Cdd:PRK12771 547 ---HICADVCP 554
|
|
| YobN |
COG1231 |
Monoamine oxidase [Amino acid transport and metabolism]; |
131-182 |
1.31e-07 |
|
Monoamine oxidase [Amino acid transport and metabolism];
Pssm-ID: 440844 [Multi-domain] Cd Length: 440 Bit Score: 53.77 E-value: 1.31e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1309180661 131 PTGKRVAVVGSGPAGLACAGELRRFGHAVTIFESLHAPGG-VLTYGIPEFRLP 182
Cdd:COG1231 5 ARGKDVVIVGAGLAGLAAARELRKAGLDVTVLEARDRVGGrVWTLRFGDDGLY 57
|
|
| COG1233 |
COG1233 |
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ... |
134-170 |
1.43e-07 |
|
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440846 [Multi-domain] Cd Length: 491 Bit Score: 53.70 E-value: 1.43e-07
10 20 30
....*....|....*....|....*....|....*..
gi 1309180661 134 KRVAVVGSGPAGLACAGELRRFGHAVTIFESLHAPGG 170
Cdd:COG1233 4 YDVVVIGAGIGGLAAAALLARAGYRVTVLEKNDTPGG 40
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
276-343 |
1.68e-07 |
|
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: 48.35 E-value: 1.68e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1309180661 276 KVAVVGGGNVAMDAARTAKRLGAeEVFLVYRRSE----EEMPARREEVHHARQEGIEFKMLCSPQEIVGHDG 343
Cdd:pfam00070 1 RVVVVGGGYIGLELAGALARLGS-KVTVVERRDRllpgFDPEIAKILQEKLEKNGIEFLLNTTVEAIEGNGD 71
|
|
| HemY |
COG1232 |
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ... |
134-172 |
1.92e-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: 53.30 E-value: 1.92e-07
10 20 30
....*....|....*....|....*....|....*....
gi 1309180661 134 KRVAVVGSGPAGLACAGELRRFGHAVTIFESLHAPGGVL 172
Cdd:COG1232 2 KRVAVIGGGIAGLTAAYRLAKAGHEVTVLEASDRVGGLI 40
|
|
| NAD_binding_8 |
pfam13450 |
NAD(P)-binding Rossmann-like domain; |
138-182 |
1.96e-07 |
|
NAD(P)-binding Rossmann-like domain;
Pssm-ID: 433218 [Multi-domain] Cd Length: 67 Bit Score: 47.91 E-value: 1.96e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1309180661 138 VVGSGPAGLACAGELRRFGHAVTIFESLHAPGG-VLTYGIPEFRLP 182
Cdd:pfam13450 1 IVGAGLAGLVAAALLAKRGFRVLVLEKRDRLGGnAYSYRVPGYVFD 46
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
138-427 |
4.15e-07 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 52.13 E-value: 4.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 138 VVGSGPAGLACAGELRRFGHAVTIFESLHAPGGVLTYG-IPEfrlpKAIVQA---------------------EIEMLGV 195
Cdd:PRK06370 10 VIGAGQAGPPLAARAAGLGMKVALIERGLLGGTCVNTGcVPT----KTLIASaraahlarraaeygvsvggpvSVDFKAV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 196 MGA--ELVTDIVVGATHTLDELlaeEGFD-----AVF---------------------VGSGAGLPlflGIPGenLNGVy 247
Cdd:PRK06370 86 MARkrRIRARSRHGSEQWLRGL---EGVDvfrghARFespntvrvggetlrakrifinTGARAAIP---PIPG--LDEV- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 248 sanEFLTRVNLMKAYEFPsydtpvwrgRKVAVVGGGNVAMDAARTAKRLGAEeVFLVYR------RSEEEMPARREEVhh 321
Cdd:PRK06370 157 ---GYLTNETIFSLDELP---------EHLVIIGGGYIGLEFAQMFRRFGSE-VTVIERgprllpREDEDVAAAVREI-- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 322 ARQEGIEFKMLCSPQEIVGHDGWVTgmVATRMELGEPDasgrrapvcvmdsdfvIDCDTVIVALGTRSNplisqtTPDL- 400
Cdd:PRK06370 222 LEREGIDVRLNAECIRVERDGDGIA--VGLDCNGGAPE----------------ITGSHILVAVGRVPN------TDDLg 277
|
330 340 350
....*....|....*....|....*....|...
gi 1309180661 401 ------EVTSRGYIATDENGATNKPGVFAGGDI 427
Cdd:PRK06370 278 leaagvETDARGYIKVDDQLRTTNPGIYAAGDC 310
|
|
| COG3380 |
COG3380 |
Predicted NAD/FAD-dependent oxidoreductase [General function prediction only]; |
134-170 |
4.52e-07 |
|
Predicted NAD/FAD-dependent oxidoreductase [General function prediction only];
Pssm-ID: 442607 [Multi-domain] Cd Length: 331 Bit Score: 51.42 E-value: 4.52e-07
10 20 30
....*....|....*....|....*....|....*..
gi 1309180661 134 KRVAVVGSGPAGLACAGELRRFGHAVTIFESLHAPGG 170
Cdd:COG3380 4 PDIAIIGAGIAGLAAARALQDAGHEVTVFEKSRGVGG 40
|
|
| PRK07233 |
PRK07233 |
hypothetical protein; Provisional |
135-170 |
5.36e-07 |
|
hypothetical protein; Provisional
Pssm-ID: 235977 [Multi-domain] Cd Length: 434 Bit Score: 51.81 E-value: 5.36e-07
10 20 30
....*....|....*....|....*....|....*.
gi 1309180661 135 RVAVVGSGPAGLACAGELRRFGHAVTIFESLHAPGG 170
Cdd:PRK07233 1 KIAIVGGGIAGLAAAYRLAKRGHEVTVFEADDQLGG 36
|
|
| PRK12814 |
PRK12814 |
putative NADPH-dependent glutamate synthase small subunit; Provisional |
1-36 |
1.33e-06 |
|
putative NADPH-dependent glutamate synthase small subunit; Provisional
Pssm-ID: 139246 [Multi-domain] Cd Length: 652 Bit Score: 50.88 E-value: 1.33e-06
10 20 30
....*....|....*....|....*....|....*.
gi 1309180661 1 MPERDALERARDFDEVSLGYSEEQALAEANRCIQCK 36
Cdd:PRK12814 538 LPELPLEERTGGFEEVVTGYSPEQAREEALRCLRCR 573
|
|
| Ppro0129 |
COG2907 |
Predicted flavin-containing amine oxidase [General function prediction only]; |
132-170 |
2.52e-06 |
|
Predicted flavin-containing amine oxidase [General function prediction only];
Pssm-ID: 442151 [Multi-domain] Cd Length: 423 Bit Score: 49.73 E-value: 2.52e-06
10 20 30
....*....|....*....|....*....|....*....
gi 1309180661 132 TGKRVAVVGSGPAGLACAGELRRfGHAVTIFESLHAPGG 170
Cdd:COG2907 2 ARMRIAVIGSGISGLTAAWLLSR-RHDVTLFEANDRLGG 39
|
|
| PLN02172 |
PLN02172 |
flavin-containing monooxygenase FMO GS-OX |
125-174 |
2.75e-06 |
|
flavin-containing monooxygenase FMO GS-OX
Pssm-ID: 215116 [Multi-domain] Cd Length: 461 Bit Score: 49.47 E-value: 2.75e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1309180661 125 APEVGEPTGKRVAVVGSGPAGLACAGELRRFGHAVTIFESLHAPGGVLTY 174
Cdd:PLN02172 2 APAQNPINSQHVAVIGAGAAGLVAARELRREGHTVVVFEREKQVGGLWVY 51
|
|
| crtI_fam |
TIGR02734 |
phytoene desaturase; Phytoene is converted to lycopene by desaturation at four (two ... |
136-170 |
4.68e-06 |
|
phytoene desaturase; Phytoene is converted to lycopene by desaturation at four (two symmetrical pairs of) sites. This is achieved by two enzymes (crtP and crtQ) in cyanobacteria (Gloeobacter being an exception) and plants, but by a single enzyme in most other bacteria and in fungi. This single enzyme is called the bacterial-type phytoene desaturase, or CrtI. Most members of this family, part of the larger pfam01593, which also contains amino oxidases, are CrtI itself; it is likely that all members act on either phytoene or on related compounds such as dehydrosqualene, for carotenoid biosynthesis. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 274273 [Multi-domain] Cd Length: 495 Bit Score: 48.81 E-value: 4.68e-06
10 20 30
....*....|....*....|....*....|....*
gi 1309180661 136 VAVVGSGPAGLACAGELRRFGHAVTIFESLHAPGG 170
Cdd:TIGR02734 1 AVVIGAGFGGLALAIRLAAAGIPVTVVEQRDKPGG 35
|
|
| PRK07251 |
PRK07251 |
FAD-containing oxidoreductase; |
275-430 |
5.64e-06 |
|
FAD-containing oxidoreductase;
Pssm-ID: 180907 [Multi-domain] Cd Length: 438 Bit Score: 48.59 E-value: 5.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 275 RKVAVVGGGNVAMDAARTAKRLGAEEVFL-----VYRRSEEEMPARREEvhHARQEGIEFKMLCSPQEIVGHDGWVTgmv 349
Cdd:PRK07251 158 ERLGIIGGGNIGLEFAGLYNKLGSKVTVLdaastILPREEPSVAALAKQ--YMEEDGITFLLNAHTTEVKNDGDQVL--- 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 350 atrmelgepdasgrrapVCVMDSDFVIDCdtVIVALGTRSN--PLISQTTpDLEVTSRGYIATDENGATNKPGVFAGGDI 427
Cdd:PRK07251 233 -----------------VVTEDETYRFDA--LLYATGRKPNtePLGLENT-DIELTERGAIKVDDYCQTSVPGVFAVGDV 292
|
...
gi 1309180661 428 VTG 430
Cdd:PRK07251 293 NGG 295
|
|
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
375-448 |
1.43e-05 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 47.06 E-value: 1.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 375 VIDCDTVIVALGTRSNplisqtTPDL---EV---TSRGYIATDENGATNKPGVFAGGDIVTGSAtviLAMGA---GKKAA 445
Cdd:PRK06416 258 TLEADYVLVAVGRRPN------TENLgleELgvkTDRGFIEVDEQLRTNVPNIYAIGDIVGGPM---LAHKAsaeGIIAA 328
|
...
gi 1309180661 446 RAI 448
Cdd:PRK06416 329 EAI 331
|
|
| PRK06327 |
PRK06327 |
dihydrolipoamide dehydrogenase; Validated |
276-430 |
1.55e-05 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235779 [Multi-domain] Cd Length: 475 Bit Score: 47.23 E-value: 1.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 276 KVAVVGGGNVAMDAARTAKRLGAEEVFLvyrrseEEMP----ARREEVHHA-----RQEGIEFKmlcspqeivghdgwvt 346
Cdd:PRK06327 185 KLAVIGAGVIGLELGSVWRRLGAEVTIL------EALPaflaAADEQVAKEaakafTKQGLDIH---------------- 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 347 gmvaTRMELGEPDASGRRAPVCVMDSDF---VIDCDTVIVALGTRSNPL-ISQTTPDLEVTSRGYIATDENGATNKPGVF 422
Cdd:PRK06327 243 ----LGVKIGEIKTGGKGVSVAYTDADGeaqTLEVDKLIVSIGRVPNTDgLGLEAVGLKLDERGFIPVDDHCRTNVPNVY 318
|
....*...
gi 1309180661 423 AGGDIVTG 430
Cdd:PRK06327 319 AIGDVVRG 326
|
|
| COG3349 |
COG3349 |
Uncharacterized protein, contains NAD-binding domain and a Fe-S cluster [General function ... |
132-170 |
1.80e-05 |
|
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: 46.77 E-value: 1.80e-05
10 20 30
....*....|....*....|....*....|....*....
gi 1309180661 132 TGKRVAVVGSGPAGLACAGELRRFGHAVTIFESLHAPGG 170
Cdd:COG3349 2 MPPRVVVVGGGLAGLAAAVELAEAGFRVTLLEARPRLGG 40
|
|
| PLN03000 |
PLN03000 |
amine oxidase |
130-170 |
3.50e-05 |
|
amine oxidase
Pssm-ID: 178578 [Multi-domain] Cd Length: 881 Bit Score: 46.55 E-value: 3.50e-05
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1309180661 130 EPTGKRVAVVGSGPAGLACAGELRRFGHAVTIFESLHAPGG 170
Cdd:PLN03000 181 QSSKSSVVIVGAGLSGLAAARQLMRFGFKVTVLEGRKRPGG 221
|
|
| PRK07846 |
PRK07846 |
mycothione reductase; Reviewed |
275-427 |
3.85e-05 |
|
mycothione reductase; Reviewed
Pssm-ID: 181142 [Multi-domain] Cd Length: 451 Bit Score: 45.72 E-value: 3.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 275 RKVAVVGGGNVAMDAARTAKRLGAEeVFLVYR-----RSEEEMPARReevhharqegiefkmlcspqeivghdgwVTGMV 349
Cdd:PRK07846 167 ESLVIVGGGFIAAEFAHVFSALGVR-VTVVNRsgrllRHLDDDISER----------------------------FTELA 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 350 ATRME--LGEPDASGRRAP---VCVMDSDFVIDCDTVIVALGTRSNP-LISQTTPDLEVTSRGYIATDENGATNKPGVFA 423
Cdd:PRK07846 218 SKRWDvrLGRNVVGVSQDGsgvTLRLDDGSTVEADVLLVATGRVPNGdLLDAAAAGVDVDEDGRVVVDEYQRTSAEGVFA 297
|
....
gi 1309180661 424 GGDI 427
Cdd:PRK07846 298 LGDV 301
|
|
| UbiH |
COG0654 |
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ... |
135-163 |
7.99e-05 |
|
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: 44.54 E-value: 7.99e-05
10 20
....*....|....*....|....*....
gi 1309180661 135 RVAVVGSGPAGLACAGELRRFGHAVTIFE 163
Cdd:COG0654 5 DVLIVGGGPAGLALALALARAGIRVTVVE 33
|
|
| PLN02976 |
PLN02976 |
amine oxidase |
112-170 |
1.11e-04 |
|
amine oxidase
Pssm-ID: 215527 [Multi-domain] Cd Length: 1713 Bit Score: 44.86 E-value: 1.11e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1309180661 112 GDFDLACDLEHRcapevgeptgKRVAVVGSGPAGLACAGELRRFGHAVTIFESLHAPGG 170
Cdd:PLN02976 682 GNHCVLCDSVDR----------KKIIVVGAGPAGLTAARHLQRQGFSVTVLEARSRIGG 730
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
136-430 |
1.38e-04 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 44.01 E-value: 1.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 136 VAVVGSGPAGLACAGELRRFGHAVTIFESLHaPGGV-LTYG-IPEfrlpKA-IVQAEI-------EMLGVMGAELVTDI- 204
Cdd:PRK06292 6 VIVIGAGPAGYVAARRAAKLGKKVALIEKGP-LGGTcLNVGcIPS----KAlIAAAEAfheakhaEEFGIHADGPKIDFk 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 205 --------VVG--ATHTLDELLAEEG------------------------FDAVFVGSGAGLPlflGIPG-ENLNGVysa 249
Cdd:PRK06292 81 kvmarvrrERDrfVGGVVEGLEKKPKidkikgtarfvdpntvevngerieAKNIVIATGSRVP---PIPGvWLILGD--- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 250 nEFLTRVNLMKAYEFPsydtpvwrgRKVAVVGGGNVAMDAARTAKRLGAEEVFLVYRRS--EEEMPARREEVHHARQEgi 327
Cdd:PRK06292 155 -RLLTSDDAFELDKLP---------KSLAVIGGGVIGLELGQALSRLGVKVTVFERGDRilPLEDPEVSKQAQKILSK-- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 328 EFKMlcspqeIVGHDgwVTGMvatrmelgEPDASGRRAPVCVMDSDFVIDCDTVIVALGTRSN-PLISQTTPDLEVTSRG 406
Cdd:PRK06292 223 EFKI------KLGAK--VTSV--------EKSGDEKVEELEKGGKTETIEADYVLVATGRRPNtDGLGLENTGIELDERG 286
|
330 340
....*....|....*....|....
gi 1309180661 407 YIATDENGATNKPGVFAGGDIVTG 430
Cdd:PRK06292 287 RPVVDEHTQTSVPGIYAAGDVNGK 310
|
|
| AlaDh_PNT_C |
smart01002 |
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the ... |
276-319 |
1.67e-04 |
|
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the NAD-dependent reversible reductive amination of pyruvate into alanine.
Pssm-ID: 214966 [Multi-domain] Cd Length: 149 Bit Score: 41.72 E-value: 1.67e-04
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1309180661 276 KVAVVGGGNVAMDAARTAKRLGAeEVFLVYRRseeemPARREEV 319
Cdd:smart01002 22 KVVVIGAGVVGLGAAATAKGLGA-EVTVLDVR-----PARLRQL 59
|
|
| PRK04965 |
PRK04965 |
NADH:flavorubredoxin reductase NorW; |
263-426 |
3.95e-04 |
|
NADH:flavorubredoxin reductase NorW;
Pssm-ID: 179902 [Multi-domain] Cd Length: 377 Bit Score: 42.60 E-value: 3.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 263 EFPSYDTPVWRGRKVAVVGGG----NVAMDAARTAKRlgaeeVFLVYRRSE-------EEMPARREevHHARQEGIEFKM 331
Cdd:PRK04965 130 EYRAAETQLRDAQRVLVVGGGligtELAMDLCRAGKA-----VTLVDNAASllaslmpPEVSSRLQ--HRLTEMGVHLLL 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 332 LCSPQEIVGHDgwvTGMVATrmelgepdasgrrapvcvMDSDFVIDCDTVIVALGTRSNPLISQTTpDLEVtSRGyIATD 411
Cdd:PRK04965 203 KSQLQGLEKTD---SGIRAT------------------LDSGRSIEVDAVIAAAGLRPNTALARRA-GLAV-NRG-IVVD 258
|
170
....*....|....*
gi 1309180661 412 ENGATNKPGVFAGGD 426
Cdd:PRK04965 259 SYLQTSAPDIYALGD 273
|
|
| PRK07208 |
PRK07208 |
hypothetical protein; Provisional |
134-163 |
5.83e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 235967 [Multi-domain] Cd Length: 479 Bit Score: 42.18 E-value: 5.83e-04
10 20 30
....*....|....*....|....*....|
gi 1309180661 134 KRVAVVGSGPAGLACAGELRRFGHAVTIFE 163
Cdd:PRK07208 5 KSVVIIGAGPAGLTAAYELLKRGYPVTVLE 34
|
|
| Pyr_redox_3 |
pfam13738 |
Pyridine nucleotide-disulphide oxidoreductase; |
259-425 |
6.38e-04 |
|
Pyridine nucleotide-disulphide oxidoreductase;
Pssm-ID: 404603 [Multi-domain] Cd Length: 296 Bit Score: 41.44 E-value: 6.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 259 MKAYEFPSYDTPvwRGRKVAVVGGGNVAMDAARTAKRLGAeEVFLVYRRSE-EEMPAR---------REEVHHARQEGiE 328
Cdd:pfam13738 142 KHYSYVKDFHPY--AGQKVVVIGGYNSAVDAALELVRKGA-RVTVLYRGSEwEDRDSDpsyslspdtLNRLEELVKNG-K 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 329 FKML--CSPQEIVGHDGWVtgmvatrmELGEPDasGRRAPVcvmdsdfviDCDtVIVALGTRsnplisqttPDLEVTSRG 406
Cdd:pfam13738 218 IKAHfnAEVKEITEVDVSY--------KVHTED--GRKVTS---------NDD-PILATGYH---------PDLSFLKKG 268
|
170 180
....*....|....*....|....*...
gi 1309180661 407 YIATDENGA---------TNKPGVFAGG 425
Cdd:pfam13738 269 LFELDEDGRpvlteetesTNVPGLFLAG 296
|
|
| DadA |
COG0665 |
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism]; |
135-410 |
8.06e-04 |
|
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
Pssm-ID: 440429 [Multi-domain] Cd Length: 364 Bit Score: 41.43 E-value: 8.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 135 RVAVVGSGPAGLACAGELRRFGHAVTIFE-------SLHAPGGVLTYGipefrlpkaivqaeiemLGVMGAELVTDIVVG 207
Cdd:COG0665 4 DVVVIGGGIAGLSTAYHLARRGLDVTVLErgrpgsgASGRNAGQLRPG-----------------LAALADRALVRLARE 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 208 ATHTLDELLAEEGFDAVFVGSGAglpLFLGIPGENLngvysaNEFLTRVNLMKAYEFPSydtpvwrgrkvavvgggnVAM 287
Cdd:COG0665 67 ALDLWRELAAELGIDCDFRRTGV---LYLARTEAEL------AALRAEAEALRALGLPV------------------ELL 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 288 DAARTAKR---LGAEEVFLVYRRSEEEM--PAR--REEVHHARQEGIEFKMLCSPQEIVGHDGWVTGmVATrmelgepdA 360
Cdd:COG0665 120 DAAELRERepgLGSPDYAGGLYDPDDGHvdPAKlvRALARAARAAGVRIREGTPVTGLEREGGRVTG-VRT--------E 190
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1309180661 361 SGRrapvcvmdsdfvIDCDTVIVALGTRSNPLISQTTPDLEVTS-RGYIAT 410
Cdd:COG0665 191 RGT------------VRADAVVLAAGAWSARLLPMLGLRLPLRPvRGYVLV 229
|
|
| AlaDh_PNT_C |
pfam01262 |
Alanine dehydrogenase/PNT, C-terminal domain; This family now also contains the lysine ... |
276-328 |
8.30e-04 |
|
Alanine dehydrogenase/PNT, C-terminal domain; This family now also contains the lysine 2-oxoglutarate reductases.
Pssm-ID: 426165 [Multi-domain] Cd Length: 213 Bit Score: 40.56 E-value: 8.30e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1309180661 276 KVAVVGGGNVAMDAARTAKRLGAEEVFL-----VYRRSEEEMPARREEVHHARQEGIE 328
Cdd:pfam01262 30 KVLVIGGGVAGLNAAATAKGLGAIVTILdvrpaRLEQLESILGAKFVETLYSQAELIA 87
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
135-163 |
1.12e-03 |
|
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.
Pssm-ID: 425450 [Multi-domain] Cd Length: 80 Bit Score: 37.57 E-value: 1.12e-03
10 20
....*....|....*....|....*....
gi 1309180661 135 RVAVVGSGPAGLACAGELRRFGHAVTIFE 163
Cdd:pfam00070 1 RVVVVGGGYIGLELAGALARLGSKVTVVE 29
|
|
| PRK10262 |
PRK10262 |
thioredoxin reductase; Provisional |
272-456 |
2.01e-03 |
|
thioredoxin reductase; Provisional
Pssm-ID: 182343 [Multi-domain] Cd Length: 321 Bit Score: 40.04 E-value: 2.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 272 WRGRKVAVVGGGNVAMDAARTAKRLgAEEVFLVYRRS--EEEMPARREEVHHARQEGIEFKMLCSPQEIVGHDGWVTGMv 349
Cdd:PRK10262 144 YRNQKVAVIGGGNTAVEEALYLSNI-ASEVHLIHRRDgfRAEKILIKRLMDKVENGNIILHTNRTLEEVTGDQMGVTGV- 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 350 atrmelgepdasgRRAPVCVMDSDFVIDCDTVIVALGTRSNPLISQTTPDLEvtsRGYIATDEN-----GATNKPGVFAG 424
Cdd:PRK10262 222 -------------RLRDTQNSDNIESLDVAGLFVAIGHSPNTAIFEGQLELE---NGYIKVQSGihgnaTQTSIPGVFAA 285
|
170 180 190
....*....|....*....|....*....|...
gi 1309180661 425 GDIVTG-SATVILAMGAGKKAARAIDSWLGGAA 456
Cdd:PRK10262 286 GDVMDHiYRQAITSAGTGCMAALDAERYLDGLA 318
|
|
| HI0933_like |
pfam03486 |
HI0933-like protein; |
134-169 |
2.11e-03 |
|
HI0933-like protein;
Pssm-ID: 427330 [Multi-domain] Cd Length: 406 Bit Score: 40.26 E-value: 2.11e-03
10 20 30
....*....|....*....|....*....|....*.
gi 1309180661 134 KRVAVVGSGPAGLACAGELRRFGHAVTIFESLHAPG 169
Cdd:pfam03486 1 FDVIVIGGGAAGLMAAISAAKRGRRVLLIEKGKKLG 36
|
|
| PRK13512 |
PRK13512 |
coenzyme A disulfide reductase; Provisional |
377-445 |
2.65e-03 |
|
coenzyme A disulfide reductase; Provisional
Pssm-ID: 184103 [Multi-domain] Cd Length: 438 Bit Score: 40.15 E-value: 2.65e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1309180661 377 DCDTVIVALGTRSNPLISQTTpDLEVTSRGYIATDENGATNKPGVFAGGDIVTG-------SATVILAMGAGKKAA 445
Cdd:PRK13512 229 HYDMIIEGVGTHPNSKFIESS-NIKLDDKGFIPVNDKFETNVPNIYAIGDIITShyrhvdlPASVPLAWGAHRAAS 303
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
128-229 |
3.02e-03 |
|
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: 39.41 E-value: 3.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309180661 128 VGEPTGKRVAVVGSGPAGLACAGELRRFGHAVTIFEslHAPgGVLTYGIPEFrlpKAIVQAEIEMLGVmgaELVTDivvg 207
Cdd:COG0446 119 LKEFKGKRAVVIGGGPIGLELAEALRKRGLKVTLVE--RAP-RLLGVLDPEM---AALLEEELREHGV---ELRLG---- 185
|
90 100 110
....*....|....*....|....*....|....
gi 1309180661 208 atHTLDELLAEEG------------FDAVFVGSG 229
Cdd:COG0446 186 --ETVVAIDGDDKvavtltdgeeipADLVVVAPG 217
|
|
| ACS_1 |
cd01916 |
Acetyl-CoA synthase (ACS), also known as acetyl-CoA decarbonylase, is found in acetogenic and ... |
21-86 |
6.10e-03 |
|
Acetyl-CoA synthase (ACS), also known as acetyl-CoA decarbonylase, is found in acetogenic and methanogenic organisms and is responsible for the synthesis and breakdown of acetyl-CoA. ACS forms a heterotetramer with carbon monoxide dehydrogenase (CODH) consisting of two ACS and two CODH subunits. CODH reduces carbon dioxide to carbon monoxide and ACS then synthesizes acetyl-CoA from carbon monoxide, CoA, and a methyl group donated by another protein (CoFeSP). ACS has three structural domains, an N-terminal rossman fold domain with a helical region at its N-terminus which interacts with CODH, and two alpha + beta fold domains. A Ni-Fe-S center referred to as the A-cluster is located in the C-terminal domain. A large cavity exists between the three domains which may bind CoA.
Pssm-ID: 238897 [Multi-domain] Cd Length: 731 Bit Score: 38.93 E-value: 6.10e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1309180661 21 SEEQALAEANRCIQCKNptCIEGCPVNIDIKSFIARIIDGDYaGGVSVLKERNALPAVCGRVCPQE 86
Cdd:cd01916 356 TDEEFQELAAKCTDCGW--CTRACPNSLRIKEAMEAAKEGDF-SGLADLFDQCVGCGRCEQECPKE 418
|
|
| PRK11883 |
PRK11883 |
protoporphyrinogen oxidase; Reviewed |
134-172 |
6.40e-03 |
|
protoporphyrinogen oxidase; Reviewed
Pssm-ID: 237009 [Multi-domain] Cd Length: 451 Bit Score: 38.68 E-value: 6.40e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1309180661 134 KRVAVVGSGPAGLACAGELRRFG--HAVTIFESLHAPGGVL 172
Cdd:PRK11883 1 KKVAIIGGGITGLSAAYRLHKKGpdADITLLEASDRLGGKI 41
|
|
| PLN02529 |
PLN02529 |
lysine-specific histone demethylase 1 |
124-170 |
7.85e-03 |
|
lysine-specific histone demethylase 1
Pssm-ID: 178144 [Multi-domain] Cd Length: 738 Bit Score: 38.72 E-value: 7.85e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1309180661 124 CAPEVGE-PTGKRVAVVGSGPAGLACAGELRRFGHAVTIFESLHAPGG 170
Cdd:PLN02529 150 FASPIPEeGTEGSVIIVGAGLAGLAAARQLLSFGFKVVVLEGRNRPGG 197
|
|
| PLN02487 |
PLN02487 |
zeta-carotene desaturase |
126-170 |
9.20e-03 |
|
zeta-carotene desaturase
Pssm-ID: 215268 [Multi-domain] Cd Length: 569 Bit Score: 38.24 E-value: 9.20e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1309180661 126 PEVGEPTGKR--VAVVGSGPAGLACAGELRRFGHAVTIFESLHAPGG 170
Cdd:PLN02487 66 PEPEAYKGPKlkVAIIGAGLAGMSTAVELLDQGHEVDIYESRPFIGG 112
|
|
| COG4716 |
COG4716 |
Myosin-crossreactive antigen (function unknown) [Function unknown]; |
131-178 |
9.43e-03 |
|
Myosin-crossreactive antigen (function unknown) [Function unknown];
Pssm-ID: 443751 Cd Length: 578 Bit Score: 38.27 E-value: 9.43e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1309180661 131 PTGKRVAVVGSGPAGLACAGELRRFGH----AVTIFESLHAPGGVLT-YGIPE 178
Cdd:COG4716 20 VDDKSAYLVGSGLASLAAAAFLIRDGQmpgeNIHILEELDLPGGSLDgAGDPE 72
|
|
| PRK08132 |
PRK08132 |
FAD-dependent oxidoreductase; Provisional |
123-159 |
9.44e-03 |
|
FAD-dependent oxidoreductase; Provisional
Pssm-ID: 236158 [Multi-domain] Cd Length: 547 Bit Score: 38.31 E-value: 9.44e-03
10 20 30
....*....|....*....|....*....|....*....
gi 1309180661 123 RCAPEVGEPTGKR--VAVVGSGPAGLACAGELRRFGHAV 159
Cdd:PRK08132 11 RPHADQDADDPARhpVVVVGAGPVGLALAIDLAQQGVPV 49
|
|
| |
