|
Name |
Accession |
Description |
Interval |
E-value |
| gltD |
PRK12810 |
glutamate synthase subunit beta; Reviewed |
1-472 |
0e+00 |
|
glutamate synthase subunit beta; Reviewed
Pssm-ID: 237213 [Multi-domain] Cd Length: 471 Bit Score: 760.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 1 MADPFGFLKYERKDNPYRPVNERIKDFEELQTTLSVEERQKQAARCMNCGIPFCHegtfygggravSGCPNDNLIPEWND 80
Cdd:PRK12810 1 MGKPTGFLEYDRVDPKKRPVAERIKDFKEFYEPFSEEQAKIQAARCMDCGIPFCH-----------WGCPVHNYIPEWND 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 81 LIYKGDFRRAFERLTRTNPLPEMTGRVCPAPCEKACTEGLNGSGVTIHDNERFIIDNAFEEGWVADSgRPIERTGFKVAV 160
Cdd:PRK12810 70 LVYRGRWEEAAERLHQTNNFPEFTGRVCPAPCEGACTLNINFGPVTIKNIERYIIDKAFEEGWVKPD-PPVKRTGKKVAV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 161 VGSGPAGLSAAWRLNQLGHSVTVFERSDRFGGLLMYGIPNMKLDKKIVQRRIDTMASIGINFVANTEIGRDITAEELLEK 240
Cdd:PRK12810 149 VGSGPAGLAAADQLARAGHKVTVFERADRIGGLLRYGIPDFKLEKEVIDRRIELMEAEGIEFRTNVEVGKDITAEELLAE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 241 FDRVILATGASVPRDLDIPGRDLKGIRFAVDFLTETTKNLLDsDTHELPPLLEGKHVLVIGGGDTGNDCIGTAVRLGAAS 320
Cdd:PRK12810 229 YDAVFLGTGAYKPRDLGIPGRDLDGVHFAMDFLIQNTRRVLG-DETEPFISAKGKHVVVIGGGDTGMDCVGTAIRQGAKS 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 321 VRQLEITPQLPEKRLPTNPWPQYPMINRTGYGQEEAdfvqqtDLTDYITSTVEFLGENGQVTAVKTIKV---GPGFKAIE 397
Cdd:PRK12810 308 VTQRDIMPMPPSRRNKNNPWPYWPMKLEVSNAHEEG------VEREFNVQTKEFEGENGKVTGVKVVRTelgEGDFEPVE 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 398 GTEEVIKADLVLLAMGFTGAEKALFDQF--------RVECVYDDYSTRNEKVFVAGDARRGPSLVIWGIREGRKTAEKID 469
Cdd:PRK12810 382 GSEFVLPADLVLLAMGFTGPEAGLLAQFgveldergRVAAPDNAYQTSNPKVFAAGDMRRGQSLVVWAIAEGRQAARAID 461
|
...
gi 488191275 470 QNL 472
Cdd:PRK12810 462 AYL 464
|
|
| GOGAT_sm_gam |
TIGR01317 |
glutamate synthases, NADH/NADPH, small subunit; This model represents one of three built for ... |
3-472 |
0e+00 |
|
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: 592.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 3 DPFGFLKYERKDNPYRPVNERIKDFEELQTTLSVEERQKQAARCMNCGIPFCHegtfygggrAVSGCPNDNLIPEWNDLI 82
Cdd:TIGR01317 1 KPTGFLEYKRRKPTERDPRTRLKDWKEFTNPFDKESAKYQAARCMDCGTPFCH---------NDSGCPLNNLIPEFNDLV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 83 YKGDFRRAFERLTRTNPLPEMTGRVCPAPCEKACTEGLNGSGVTIHDNERFIIDNAFEEGWVADSgRPIERTGFKVAVVG 162
Cdd:TIGR01317 72 FRGRWKEALDRLHATNNFPEFTGRVCPAPCEGACTLGISEDPVGIKSIERIIIDKGFQEGWVQPR-PPSKRTGKKVAVVG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 163 SGPAGLSAAWRLNQLGHSVTVFERSDRFGGLLMYGIPNMKLDKKIVQRRIDTMASIGINFVANTEIGRDITAEELLEKFD 242
Cdd:TIGR01317 151 SGPAGLAAADQLNRAGHTVTVFEREDRCGGLLMYGIPNMKLDKAIVDRRIDLLSAEGIDFVTNTEIGVDISADELKEQFD 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 243 RVILATGASVPRDLDIPGRDLKGIRFAVDFLTETTKNLLDSDTHELPPL-LEGKHVLVIGGGDTGNDCIGTAVRLGAASV 321
Cdd:TIGR01317 231 AVVLAGGATKPRDLPIPGRELKGIHYAMEFLPSATKALLGKDFKDIIFIkAKGKKVVVIGGGDTGADCVGTSLRHGAASV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 322 RQLEITPQLPEKRLPTNPWPQYPMINRTGYGQEEADFVQQTDLTDYITSTVEFLG-ENGQVTAVKTIKV-----GPG--- 392
Cdd:TIGR01317 311 HQFEIMPKPPEARAKDNPWPEWPRVYRVDYAHEEAAAHYGRDPREYSILTKEFIGdDEGKVTALRTVRVewkksQDGkwq 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 393 FKAIEGTEEVIKADLVLLAMGFTGAEKALFDQFRVE--------CVYDDYSTRNEKVFVAGDARRGPSLVIWGIREGRKT 464
Cdd:TIGR01317 391 FVEIPGSEEVFEADLVLLAMGFVGPEQILLDDFGVKktrrgnisAGYDDYSTSIPGVFAAGDCRRGQSLIVWAINEGRKA 470
|
....*...
gi 488191275 465 AEKIDQNL 472
Cdd:TIGR01317 471 AAAVDRYL 478
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
23-470 |
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: 572.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 23 RIKDFEELQTTLSVEERQKQAARCMNCGIPFCHegtfygggravSGCPNDNLIPEWNDLIYKGDFRRAFERLTRTNPLPE 102
Cdd:COG0493 1 RIKDFREVYPGLSEEEAIEQAARCLDCGDPPCQ-----------TGCPVGNDIPEWIRLIAEGDYEEALELIHETNPFPE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 103 MTGRVCPAPCEKACTEGLNGSGVTIHDNERFIIDNAFEEGWVADSgRPIERTGFKVAVVGSGPAGLSAAWRLNQLGHSVT 182
Cdd:COG0493 70 VCGRVCPAPCEGACVRGIVDEPVAIGALERFIADKAFEEGWVKPP-PPAPRTGKKVAVVGSGPAGLAAAYQLARAGHEVT 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 183 VFERSDRFGGLLMYGIPNMKLDKKIVQRRIDTMASIGINFVANTEIGRDITAEELLEKFDRVILATGASVPRDLDIPGRD 262
Cdd:COG0493 149 VFEALDKPGGLLRYGIPEFRLPKDVLDREIELIEALGVEFRTNVEVGKDITLDELLEEFDAVFLATGAGKPRDLGIPGED 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 263 LKGIRFAVDFLTETTKNLLdsdthELPPLLEGKHVLVIGGGDTGNDCIGTAVRLGAASVRQLEItpqLPEKRLPTNPWpq 342
Cdd:COG0493 229 LKGVHSAMDFLTAVNLGEA-----PDTILAVGKRVVVIGGGNTAMDCARTALRLGAESVTIVYR---RTREEMPASKE-- 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 343 ypminRTGYGQEE-ADFVqqtdltdYITSTVEFLG-ENGQVTAVKTIKVGPG---------FKAIEGTEEVIKADLVLLA 411
Cdd:COG0493 299 -----EVEEALEEgVEFL-------FLVAPVEIIGdENGRVTGLECVRMELGepdesgrrrPVPIEGSEFTLPADLVILA 366
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488191275 412 MGFTGAEKALFDQF--------RVECVYDDYSTRNEKVFVAGDARRGPSLVIWGIREGRKTAEKIDQ 470
Cdd:COG0493 367 IGQTPDPSGLEEELgleldkrgTIVVDEETYQTSLPGVFAGGDAVRGPSLVVWAIAEGRKAARAIDR 433
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
6-473 |
3.09e-146 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 425.75 E-value: 3.09e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 6 GFLKYERKDNPYRPVNERIKDFEELQTTLSVEERQKQAARCMNCGIPFCHEGtfygggravsgCPNDNLIPEWNDLIYKG 85
Cdd:PRK11749 2 KFLTTPRIPMPRQDAEERAQNFDEVAPGYTPEEAIEEASRCLQCKDAPCVKA-----------CPVSIDIPEFIRLIAEG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 86 DFRRAFERLTRTNPLPEMTGRVCPAP--CEKACTEGLNGSGVTIHDNERFIIDNAFEEGWVADsgRPIERTGFKVAVVGS 163
Cdd:PRK11749 71 NLKGAAETILETNPLPAVCGRVCPQErlCEGACVRGKKGEPVAIGRLERYITDWAMETGWVLF--KRAPKTGKKVAVIGA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 164 GPAGLSAAWRLNQLGHSVTVFERSDRFGGLLMYGIPNMKLDKKIVQRRIDTMASIGINFVANTEIGRDITAEELLEKFDR 243
Cdd:PRK11749 149 GPAGLTAAHRLARKGYDVTIFEARDKAGGLLRYGIPEFRLPKDIVDREVERLLKLGVEIRTNTEVGRDITLDELRAGYDA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 244 VILATGASVPRDLDIPGRDLKGIRFAVDFLTETtkNLLDSDThelpPLLEGKHVLVIGGGDTGNDCIGTAVRLGAASV-- 321
Cdd:PRK11749 229 VFIGTGAGLPRFLGIPGENLGGVYSAVDFLTRV--NQAVADY----DLPVGKRVVVIGGGNTAMDAARTAKRLGAESVti 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 322 ---RQLEitpqlpekrlptnpwpqypmiNRTGYgQEEADFVQQTDLT-DYITSTVEFLGENGQVTAVKTIKV-------- 389
Cdd:PRK11749 303 vyrRGRE---------------------EMPAS-EEEVEHAKEEGVEfEWLAAPVEILGDEGRVTGVEFVRMelgepdas 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 390 GPGFKAIEGTEEVIKADLVLLAMGFTGAEKALFDQFRVEC--------VYDDYSTRNEKVFVAGDARRGPSLVIWGIREG 461
Cdd:PRK11749 361 GRRRVPIEGSEFTLPADLVIKAIGQTPNPLILSTTPGLELnrwgtiiaDDETGRTSLPGVFAGGDIVTGAATVVWAVGDG 440
|
490
....*....|..
gi 488191275 462 RKTAEKIDQNLR 473
Cdd:PRK11749 441 KDAAEAIHEYLE 452
|
|
| PRK12771 |
PRK12771 |
putative glutamate synthase (NADPH) small subunit; Provisional |
66-473 |
1.49e-93 |
|
putative glutamate synthase (NADPH) small subunit; Provisional
Pssm-ID: 237198 [Multi-domain] Cd Length: 564 Bit Score: 294.09 E-value: 1.49e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 66 VSGCPNDNLIPEWNDLIYKGDFRRAFERLTRTNPLPEMTGRVCPAPCEKACTEGLNGSGVTIHDNERFIIDNAFEEGWVA 145
Cdd:PRK12771 50 NAACPAGEDIRGWLALVRGGDYEYAWRRLTKDNPFPAVMGRVCYHPCESGCNRGQVDDAVGINAVERFLGDYAIANGWKF 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 146 DsgRPIERTGFKVAVVGSGPAGLSAAWRLNQLGHSVTVFERSDRFGGLLMYGIPNMKLDKKIVQRRIDTMASIGINFVAN 225
Cdd:PRK12771 130 P--APAPDTGKRVAVIGGGPAGLSAAYHLRRMGHAVTIFEAGPKLGGMMRYGIPAYRLPREVLDAEIQRILDLGVEVRLG 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 226 TEIGRDITAEELLEKFDRVILATGASVPRDLDIPGRDLKGIRFAVDFLTETTKNlldsdthELPPLleGKHVLVIGGGDT 305
Cdd:PRK12771 208 VRVGEDITLEQLEGEFDAVFVAIGAQLGKRLPIPGEDAAGVLDAVDFLRAVGEG-------EPPFL--GKRVVVIGGGNT 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 306 GNDCIGTAVRLGAASVRqleITPQLPEKRLPTNPwpqypminrtgygqEEADFVQQTDLT-DYITSTVEFLGENGQVTAV 384
Cdd:PRK12771 279 AMDAARTARRLGAEEVT---IVYRRTREDMPAHD--------------EEIEEALREGVEiNWLRTPVEIEGDENGATGL 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 385 KTIKVGPGFK-------AIEGTEEVIKADLVLLAMG----FTGAEKALFDQFRVECVYDDYSTR---NEKVFVAGDARRG 450
Cdd:PRK12771 342 RVITVEKMELdedgrpsPVTGEEETLEADLVVLAIGqdidSAGLESVPGVEVGRGVVQVDPNFMmtgRPGVFAGGDMVPG 421
|
410 420
....*....|....*....|...
gi 488191275 451 PSLVIWGIREGRKTAEKIDQNLR 473
Cdd:PRK12771 422 PRTVTTAIGHGKKAARNIDAFLG 444
|
|
| PRK12831 |
PRK12831 |
putative oxidoreductase; Provisional |
8-473 |
5.96e-86 |
|
putative oxidoreductase; Provisional
Pssm-ID: 183780 [Multi-domain] Cd Length: 464 Bit Score: 271.51 E-value: 5.96e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 8 LKYERKDNPYRPVNERIKDFEELQTTLSVEERQKQAARCMNCGIPFChegtfygggraVSGCPNDNLIPEWNDLIYKGDF 87
Cdd:PRK12831 4 DRKKRVPVREQDPEVRATNFEEVCLGYNEEEAVKEASRCLQCKKPKC-----------VKGCPVSINIPGFISKLKEGDF 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 88 RRAFERLTRTNPLPEMTGRVCP--APCEKACTEGLNGSGVTIHDNERFIIDNAFEEGwvADSGRPIERTGFKVAVVGSGP 165
Cdd:PRK12831 73 EEAAKIIAKYNALPAVCGRVCPqeSQCEGKCVLGIKGEPVAIGKLERFVADWARENG--IDLSETEEKKGKKVAVIGSGP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 166 AGLSAAWRLNQLGHSVTVFERSDRFGGLLMYGIPNMKLDK-KIVQRRIDTMASIGINFVANTEIGRDITAEELLE--KFD 242
Cdd:PRK12831 151 AGLTCAGDLAKMGYDVTIFEALHEPGGVLVYGIPEFRLPKeTVVKKEIENIKKLGVKIETNVVVGKTVTIDELLEeeGFD 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 243 RVILATGASVPRDLDIPGRDLKGIRFAVDFLTETtkNLL-----DSDThelpPLLEGKHVLVIGGGDTGNDCIGTAVRLG 317
Cdd:PRK12831 231 AVFIGSGAGLPKFMGIPGENLNGVFSANEFLTRV--NLMkaykpEYDT----PIKVGKKVAVVGGGNVAMDAARTALRLG 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 318 AasvrQLEITPQLPEKRLPTNpwpqypmINRTGYGQEEA-DFvqqtdltDYITSTVEFLG-ENGQVTAVKTIKVGPGFK- 394
Cdd:PRK12831 305 A----EVHIVYRRSEEELPAR-------VEEVHHAKEEGvIF-------DLLTNPVEILGdENGWVKGMKCIKMELGEPd 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 395 --------AIEGTEEVIKADLVLLAMG------FTGAEKALFDQFRVECVYDDYS--TRNEKVFVAGDARRGPSLVIWGI 458
Cdd:PRK12831 367 asgrrrpvEIEGSEFVLEVDTVIMSLGtspnplISSTTKGLKINKRGCIVADEETglTSKEGVFAGGDAVTGAATVILAM 446
|
490
....*....|....*
gi 488191275 459 REGRKTAEKIDQNLR 473
Cdd:PRK12831 447 GAGKKAAKAIDEYLS 461
|
|
| PRK12769 |
PRK12769 |
putative oxidoreductase Fe-S binding subunit; Reviewed |
11-468 |
3.20e-85 |
|
putative oxidoreductase Fe-S binding subunit; Reviewed
Pssm-ID: 183733 [Multi-domain] Cd Length: 654 Bit Score: 275.09 E-value: 3.20e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 11 ERKDNPYR------PVNERIKDFEELQTTLSVEERQKQAARCMNCGIPFCHEGTfygggravsgCPNDNLIPEWNDLIYK 84
Cdd:PRK12769 186 QMQATPPRgepdklAIEARKTGFDEIYLPFRADQAQREASRCLKCGEHSICEWT----------CPLHNHIPQWIELVKA 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 85 GDFRRAFERLTRTNPLPEMTGRVCPAP--CEKACTEGLNGSGVTIHDNERFIIDNAFEEGWVAD-SGrpIERTGFKVAVV 161
Cdd:PRK12769 256 GNIDAAVELSHQTNSLPEITGRVCPQDrlCEGACTLRDEYGAVTIGNIERYISDQALAKGWRPDlSQ--VTKSDKRVAII 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 162 GSGPAGLSAAWRLNQLGHSVTVFERSDRFGGLLMYGIPNMKLDKKIVQRRIDTMASIGINFVANTEIGRDITAEELLEKF 241
Cdd:PRK12769 334 GAGPAGLACADVLARNGVAVTVYDRHPEIGGLLTFGIPAFKLDKSLLARRREIFSAMGIEFELNCEVGKDISLESLLEDY 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 242 DRVILATGASVPRDLDIPGRDLKGIRFAVDFLTETTKNLLDSDTHELPPLLE--GKHVLVIGGGDTGNDCIGTAVRLGAA 319
Cdd:PRK12769 414 DAVFVGVGTYRSMKAGLPNEDAPGVYDALPFLIANTKQVMGLEELPEEPFINtaGLNVVVLGGGDTAMDCVRTALRHGAS 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 320 SV----RQLEitPQLP-EKRLPTNPwpqypminrtgyGQEEADF---VQQTDLTdyitstvefLGENGQVTAVKTIKVGP 391
Cdd:PRK12769 494 NVtcayRRDE--ANMPgSKKEVKNA------------REEGANFefnVQPVALE---------LNEQGHVCGIRFLRTRL 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 392 GF---------KAIEGTEEVIKADLVLLAMGFT--------GAEKALFDQFRVECVYDD---YSTRNEKVFVAGDARRGP 451
Cdd:PRK12769 551 GEpdaqgrrrpVPIPGSEFVMPADAVIMAFGFNphgmpwleSHGVTVDKWGRIIADVESqyrYQTSNPKIFAGGDAVRGA 630
|
490
....*....|....*..
gi 488191275 452 SLVIWGIREGRKTAEKI 468
Cdd:PRK12769 631 DLVVTAMAEGRHAAQGI 647
|
|
| gltA |
TIGR01316 |
glutamate synthase (NADPH), homotetrameric; This protein is homologous to the small subunit of ... |
19-472 |
2.87e-79 |
|
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: 253.64 E-value: 2.87e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 19 PVNERIKDFEELQTTLSVEERQKQAARCMNCGIPFchegtfyggGRAVSGCPNDNLIPEWNDLIYKGDFRRAFERLTRTN 98
Cdd:TIGR01316 1 PPEERSKLFQEAALGYTEQLALVEAQRCLNCKDAT---------KPCIKGCPVHVPIPEFIAKIQEGDFKGAVDIIKTTS 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 99 PLPEMTGRVCPAP--CEKACTEGLN----GSGVTIHDNERFIIDnafeegWVADSGRPIER-----TGFKVAVVGSGPAG 167
Cdd:TIGR01316 72 LLPAICGRVCPQErqCEGQCTVGKMfkdvGKPVSIGALERFVAD------WERQHGIETEPekapsTHKKVAVIGAGPAG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 168 LSAAWRLNQLGHSVTVFERSDRFGGLLMYGIPNMKLDKKIVQRRIDTMASIGINFVANTEIGRDITAEELLEKFDRVILA 247
Cdd:TIGR01316 146 LACASELAKAGHSVTVFEALHKPGGVVTYGIPEFRLPKEIVVTEIKTLKKLGVTFRMNFLVGKTATLEELFSQYDAVFIG 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 248 TGASVPRDLDIPGRDLKGIRFAVDFLTETTKNLLDSDTHELPPLLEGKHVLVIGGGDTGNDCIGTAVRLGAasvrqlEIT 327
Cdd:TIGR01316 226 TGAGLPKLMNIPGEELCGVYSANDFLTRANLMKAYEFPHADTPVYAGKSVVVIGGGNTAVDSARTALRLGA------EVH 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 328 PQLPEKRlptnpwpqYPMINRtgygQEEADFVQQTDLT-DYITSTVEFLG-ENGQVTAVKTIKVGPG---------FKAI 396
Cdd:TIGR01316 300 CLYRRTR--------EDMTAR----VEEIAHAEEEGVKfHFLCQPVEIIGdEEGNVRAVKFRKMDCQeqidsgerrFLPC 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 397 EGTEEVIKADLVLLAMGfTGAEKALFDQFRVEC-------VYDDYSTRNEKVFVAGDARRGPSLVIWGIREGRKTAEKID 469
Cdd:TIGR01316 368 GDAECKLEADAVIVAIG-NGSNPIMAETTRLKTsergtivVDEDQRTSIPGVFAGGDIILGAATVIRAMGQGKRAAKSIN 446
|
...
gi 488191275 470 QNL 472
Cdd:TIGR01316 447 EYL 449
|
|
| PRK12778 |
PRK12778 |
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ... |
19-473 |
2.29e-74 |
|
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;
Pssm-ID: 237200 [Multi-domain] Cd Length: 752 Bit Score: 248.50 E-value: 2.29e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 19 PVNERIKDFEELQTTLSVEERQKQAARCMNCGIPFChegtfygggraVSGCPNDNLIPEWNDLIYKGDFRRAFERLTRTN 98
Cdd:PRK12778 304 PEYRAHNRFEEVNLGLTKEQAMTEAKRCLDCKNPGC-----------VEGCPVGIDIPRFIKNIERGNFLEAAKILKETS 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 99 PLPEMTGRVCP--APCEKACTEGLNGS-GVTIHDNERFIIDnafeegWVADSGRP-----IERTGFKVAVVGSGPAGLSA 170
Cdd:PRK12778 373 ALPAVCGRVCPqeKQCESKCIHGKMGEeAVAIGYLERFVAD------YERESGNIsvpevAEKNGKKVAVIGSGPAGLSF 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 171 AWRLNQLGHSVTVFERSDRFGGLLMYGIPNMKLDKKIVQRRIDTMASIGINFVANTEIGRDITAEELL-EKFDRVILATG 249
Cdd:PRK12778 447 AGDLAKRGYDVTVFEALHEIGGVLKYGIPEFRLPKKIVDVEIENLKKLGVKFETDVIVGKTITIEELEeEGFKGIFIASG 526
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 250 ASVPRDLDIPGRDLKGIRFAVDFLTETtkNLLD-----SDThelpPLLEGKHVLVIGGGDTGNDCIGTAVRLGAASVRql 324
Cdd:PRK12778 527 AGLPNFMNIPGENSNGVMSSNEYLTRV--NLMDaaspdSDT----PIKFGKKVAVVGGGNTAMDSARTAKRLGAERVT-- 598
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 325 eITPQLPEKRLPTNpwpqypmINRTGYGQEEA-DFVqqtdltdYITSTVEFLG-ENGQVTAVKTIKVGPGFK-------- 394
Cdd:PRK12778 599 -IVYRRSEEEMPAR-------LEEVKHAKEEGiEFL-------TLHNPIEYLAdEKGWVKQVVLQKMELGEPdasgrrrp 663
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 395 -AIEGTEEVIKADLVLLAMG----------FTGAEKALFDQFRVEcvyDDYSTRNEKVFVAGDARRGPSLVIWGIREGRK 463
Cdd:PRK12778 664 vAIPGSTFTVDVDLVIVSVGvspnplvpssIPGLELNRKGTIVVD---EEMQSSIPGIYAGGDIVRGGATVILAMGDGKR 740
|
490
....*....|
gi 488191275 464 TAEKIDQNLR 473
Cdd:PRK12778 741 AAAAIDEYLS 750
|
|
| PRK12809 |
PRK12809 |
putative oxidoreductase Fe-S binding subunit; Reviewed |
21-468 |
6.40e-70 |
|
putative oxidoreductase Fe-S binding subunit; Reviewed
Pssm-ID: 183762 [Multi-domain] Cd Length: 639 Bit Score: 234.53 E-value: 6.40e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 21 NERIKDFEELQTTLSVEERQKQAARCMNCG-IPFCHegtfygggravSGCPNDNLIPEWNDLIYKGDFRRAFERLTRTNP 99
Cdd:PRK12809 185 SERKTHFGEIYCGLDPQQATYESDRCVYCAeKANCN-----------WHCPLHNAIPDYIRLVQEGKIIEAAELCHQTSS 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 100 LPEMTGRVCPAP--CEKACTEGLNGSGVTIHDNERFIIDNAFEEGWVADSGRPIERTGfKVAVVGSGPAGLSAAWRLNQL 177
Cdd:PRK12809 254 LPEICGRVCPQDrlCEGACTLKDHSGAVSIGNLERYITDTALAMGWRPDVSKVVPRSE-KVAVIGAGPAGLGCADILARA 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 178 GHSVTVFERSDRFGGLLMYGIPNMKLDKKIVQRRIDTMASIGINFVANTEIGRDITAEELLEKFDRVILATGASVPRDLD 257
Cdd:PRK12809 333 GVQVDVFDRHPEIGGMLTFGIPPFKLDKTVLSQRREIFTAMGIDFHLNCEIGRDITFSDLTSEYDAVFIGVGTYGMMRAD 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 258 IPGRDLKGIRFAVDFLTETTKNLLDSDTHELPPL--LEGKHVLVIGGGDTGNDCIGTAVRLGAASV----RQLEItpqlp 331
Cdd:PRK12809 413 LPHEDAPGVIQALPFLTAHTRQLMGLPESEEYPLtdVEGKRVVVLGGGDTTMDCLRTSIRLNAASVtcayRRDEV----- 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 332 ekrlpTNPWPQYPMINRTGYGQEEADFVQ-QTDLTDyitstveflgENGQVTAVKTIKVGPGF---------KAIEGTEE 401
Cdd:PRK12809 488 -----SMPGSRKEVVNAREEGVEFQFNVQpQYIACD----------EDGRLTAVGLIRTAMGEpgpdgrrrpRPVAGSEF 552
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488191275 402 VIKADLVLLAMGF----------TGAEKALFDQFRVECV-YDDYSTRNEKVFVAGDARRGPSLVIWGIREGRKTAEKI 468
Cdd:PRK12809 553 ELPADVLIMAFGFqahampwlqgSGIKLDKWGLIQTGDVgYLPTQTHLKKVFAGGDAVHGADLVVTAMAAGRQAARDM 630
|
|
| PRK13984 |
PRK13984 |
putative oxidoreductase; Provisional |
8-473 |
2.76e-67 |
|
putative oxidoreductase; Provisional
Pssm-ID: 172486 [Multi-domain] Cd Length: 604 Bit Score: 226.57 E-value: 2.76e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 8 LKYERKDNPYRPVNERIKDFEELQTTLSVEERQKQAARCMNCGIpfChegtfygggraVSGCPNDNLIPEWNDLIYKGDF 87
Cdd:PRK13984 149 LDLERVEMEEIPPEERVKSFIEIVKGYSKEQAMQEAARCVECGI--C-----------TDTCPAHMDIPQYIKAIYKDDL 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 88 RRAFERLTRTNPLPEMTGRVCPAPCEKACTEGLNGSGVTIHDNERFIIDNAFEEGWVADSGRPIERTGFKVAVVGSGPAG 167
Cdd:PRK13984 216 EEGLRWLYKTNPLSMVCGRVCTHKCETVCSIGHRGEPIAIRWLKRYIVDNVPVEKYSEILDDEPEKKNKKVAIVGSGPAG 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 168 LSAAWRLNQLGHSVTVFERSDRFGGLLMYGIPNMKLDKKIVQRRIDTMASIGINFVANTEIGRDITAEELLEKFDRVILA 247
Cdd:PRK13984 296 LSAAYFLATMGYEVTVYESLSKPGGVMRYGIPSYRLPDEALDKDIAFIEALGVKIHLNTRVGKDIPLEELREKHDAVFLS 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 248 TGASVPRDLDIPGRDLKGIRFAVDFLTETTKNLL-DSDTHELPpllegKHVLVIGGGDTGNDCIGTAVRLGAASVRQLEI 326
Cdd:PRK13984 376 TGFTLGRSTRIPGTDHPDVIQALPLLREIRDYLRgEGPKPKIP-----RSLVVIGGGNVAMDIARSMARLQKMEYGEVNV 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 327 TPQLPEK---RLPTNPwpqypminrtgygqEEADFVQQTDLTDYIT-STVEFLGENGQVTAVKTIKVGPGF--------K 394
Cdd:PRK13984 451 KVTSLERtfeEMPADM--------------EEIEEGLEEGVVIYPGwGPMEVVIENDKVKGVKFKKCVEVFdeegrfnpK 516
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 395 AIEGTEEVIKADLVLLAMG------FTGAE-KALFDQFRVECVYDDY-STRNEKVFVAGDARRGPSlVIWGIREGRKTAE 466
Cdd:PRK13984 517 FDESDQIIVEADMVVEAIGqapdysYLPEElKSKLEFVRGRILTNEYgQTSIPWLFAGGDIVHGPD-IIHGVADGYWAAE 595
|
....*..
gi 488191275 467 KIDQNLR 473
Cdd:PRK13984 596 GIDMYLR 602
|
|
| PRK12814 |
PRK12814 |
putative NADPH-dependent glutamate synthase small subunit; Provisional |
69-472 |
2.07e-62 |
|
putative NADPH-dependent glutamate synthase small subunit; Provisional
Pssm-ID: 139246 [Multi-domain] Cd Length: 652 Bit Score: 214.59 E-value: 2.07e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 69 CPNDNLIPEWNDLIYKGDFRRAFERLTRTNPLPEMTGRVCPAPCEKACTEGLNGSGVTIHDNERFIIDNAFEEgwvadSG 148
Cdd:PRK12814 108 CPAGCNIPGFIAAIARGDDREAIRIIKETIPLPGILGRICPAPCEEACRRHGVDEPVSICALKRYAADRDMES-----AE 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 149 RPI----ERTGFKVAVVGSGPAGLSAAWRLNQLGHSVTVFERSDRFGGLLMYGIPNMKLDKKIVQRRIDTMASIGINFVA 224
Cdd:PRK12814 183 RYIperaPKSGKKVAIIGAGPAGLTAAYYLLRKGHDVTIFDANEQAGGMMRYGIPRFRLPESVIDADIAPLRAMGAEFRF 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 225 NTEIGRDITAEELLEKFDRVILATGASVPRDLDIPGRDLKGIRFAVDFLtettKNLLDSDTHELpplleGKHVLVIGGGD 304
Cdd:PRK12814 263 NTVFGRDITLEELQKEFDAVLLAVGAQKASKMGIPGEELPGVISGIDFL----RNVALGTALHP-----GKKVVVIGGGN 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 305 TGNDCIGTAVRLGAASVRQLeitpqlpeKRLPTNPWPQypmiNRTGYGQEEADFVQQTDLTD--YITSTVEFLgengQVT 382
Cdd:PRK12814 334 TAIDAARTALRLGAESVTIL--------YRRTREEMPA----NRAEIEEALAEGVSLRELAApvSIERSEGGL----ELT 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 383 AVKTIKVGP---GFK---AIEGTEEVIKADLVLLAMG------------FTGAEKALFDQFRVECvyddySTRNEKVFVA 444
Cdd:PRK12814 398 AIKMQQGEPdesGRRrpvPVEGSEFTLQADTVISAIGqqvdppiaeaagIGTSRNGTVKVDPETL-----QTSVAGVFAG 472
|
410 420
....*....|....*....|....*...
gi 488191275 445 GDARRGPSLVIWGIREGRKTAEKIDQNL 472
Cdd:PRK12814 473 GDCVTGADIAINAVEQGKRAAHAIDLFL 500
|
|
| PRK12775 |
PRK12775 |
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin ... |
16-474 |
1.06e-54 |
|
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin domain-containing protein; Provisional
Pssm-ID: 183738 [Multi-domain] Cd Length: 1006 Bit Score: 197.09 E-value: 1.06e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 16 PYRPVNERIKDFEELQTTLSVEERQKQAARCMNCGIPFChegtfygggraVSGCPNDNLIPEWNDLIYKGDFRRAFERLT 95
Cdd:PRK12775 303 PERDAVERARNFKEVNLGYSLEDALQEAERCIQCAKPTC-----------IAGCPVQIDIPVFIRHVVVRDFDGALEVIY 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 96 RTNPLPEMTGRVCP--APCEKACTEGLNGSGVTIHDNERFIIDNAfeegwVADSGRPI---ERTGfKVAVVGSGPAGLSA 170
Cdd:PRK12775 372 EASIFPSICGRVCPqeTQCEAQCIIAKKHESVGIGRLERFVGDNA-----RAKPVKPPrfsKKLG-KVAICGSGPAGLAA 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 171 AWRLNQLGHSVTVFERSDRFGGLLMYGIPNMKLDKKIVQRRIDTMASIGINFVANTEIGRDITAEELLEK--FDRVILAT 248
Cdd:PRK12775 446 AADLVKYGVDVTVYEALHVVGGVLQYGIPSFRLPRDIIDREVQRLVDIGVKIETNKVIGKTFTVPQLMNDkgFDAVFLGV 525
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 249 GASVPRDLDIPGRDLKGIRFAVDFLTETtkNLLDSDTHEL--PPLLEGKHVLVIGGGDTGNDCIGTAVRLGAASVRQLEi 326
Cdd:PRK12775 526 GAGAPTFLGIPGEFAGQVYSANEFLTRV--NLMGGDKFPFldTPISLGKSVVVIGAGNTAMDCLRVAKRLGAPTVRCVY- 602
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 327 tpQLPEKRLPTNpwpqypmINRTGYGQEEA-DFVqqtdltdYITSTVEFL-GENGQVTAVKTIKVGPGFKAIEG------ 398
Cdd:PRK12775 603 --RRSEAEAPAR-------IEEIRHAKEEGiDFF-------FLHSPVEIYvDAEGSVRGMKVEEMELGEPDEKGrrkpmp 666
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 399 TEEVI--KADLVLLAMG------FTGAEKAL---------FDQFRVEcvyDDYSTRNEKVFVAGDARRGPSLVIWGIREG 461
Cdd:PRK12775 667 TGEFKdlECDTVIYALGtkanpiITQSTPGLalnkwgniaADDGKLE---STQSTNLPGVFAGGDIVTGGATVILAMGAG 743
|
490
....*....|...
gi 488191275 462 RKTAEKIDQNLRM 474
Cdd:PRK12775 744 RRAARSIATYLRL 756
|
|
| PRK12770 |
PRK12770 |
putative glutamate synthase subunit beta; Provisional |
150-473 |
5.37e-54 |
|
putative glutamate synthase subunit beta; Provisional
Pssm-ID: 237197 [Multi-domain] Cd Length: 352 Bit Score: 184.81 E-value: 5.37e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 150 PIERTGFKVAVVGSGPAGLSAAWRLNQLGHSVTVFERSDRFGGLLMYGIPNMKLDKKIVQRRIDTMASIGINFVANTEI- 228
Cdd:PRK12770 13 KPPPTGKKVAIIGAGPAGLAAAGYLACLGYEVHVYDKLPEPGGLMLFGIPEFRIPIERVREGVKELEEAGVVFHTRTKVc 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 229 --------------GRDITAEELLEKFDRVILATGASVPRDLDIPGRDLKGIRFAVDFLTETTKNLLDSDTHELPPLLEG 294
Cdd:PRK12770 93 cgeplheeegdefvERIVSLEELVKKYDAVLIATGTWKSRKLGIPGEDLPGVYSALEYLFRIRAAKLGYLPWEKVPPVEG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 295 KHVLVIGGGDTGNDCIGTAVRLGAASV-----RQLEITPQLPEkrlptnpwpqypMINRTgygqeEADFVQQTDLtdyiT 369
Cdd:PRK12770 173 KKVVVVGAGLTAVDAALEAVLLGAEKVylayrRTINEAPAGKY------------EIERL-----IARGVEFLEL----V 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 370 STVEFLGENGqVTAVKTIK--VGPGFKA-------IEGTEEVIKADLVLLAMG------FTGAEKALFDQFRVECVYD-D 433
Cdd:PRK12770 232 TPVRIIGEGR-VEGVELAKmrLGEPDESgrprpvpIPGSEFVLEADTVVFAIGeiptppFAKECLGIELNRKGEIVVDeK 310
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 488191275 434 YSTRNEKVFVAGDARRGPSLVIWGIREGRKTAEKIDQNLR 473
Cdd:PRK12770 311 HMTSREGVFAAGDVVTGPSKIGKAIKSGLRAAQSIHEWLD 350
|
|
| PRK12779 |
PRK12779 |
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; ... |
16-468 |
7.11e-49 |
|
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; Provisional
Pssm-ID: 183740 [Multi-domain] Cd Length: 944 Bit Score: 180.03 E-value: 7.11e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 16 PY-RPVNERIKDFEELQ------TTLSVEERQ------KQAARCMNCGIPFCHEGTF-YGGGRAVSGCPNDNLIPEWNDL 81
Cdd:PRK12779 147 PYiRPAEERAVDFDLVNqgylgyQSLGYSVREvelfvwLEVMRDKQCDDKPCELGVLvQGKAEPKGGCPVKIHIPEMLDL 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 82 IYKGDFRRAFERLTRTNPLPEMTGRVCPAP--CEKACTEglNGSGVTIHDNERFI----------IDNAFE---EGWVAD 146
Cdd:PRK12779 227 LGNGKHREALELIESCNPLPNVTGRVCPQElqCQGVCTH--TKRPIEIGQLEWYLpqheklvnpnANERFAgriSPWAAA 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 147 SGRPIertgfkvAVVGSGPAGLSAAWRLNQLGHSVTVFERSDRFGGLLMYGIPNMKLDKKIVQRRIDTMASIGINFVANT 226
Cdd:PRK12779 305 VKPPI-------AVVGSGPSGLINAYLLAVEGFPVTVFEAFHDLGGVLRYGIPEFRLPNQLIDDVVEKIKLLGGRFVKNF 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 227 EIGRDITAEEL-LEKFDRVILATGASVPRDLDIPGRDLKGIRFAVDFLTETtkNLLDS--DTHELP-PLLEGKHVLVIGG 302
Cdd:PRK12779 378 VVGKTATLEDLkAAGFWKIFVGTGAGLPTFMNVPGEHLLGVMSANEFLTRV--NLMRGldDDYETPlPEVKGKEVFVIGG 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 303 GDTGNDCIGTAVRLGA--------------ASVRQL----EITPQLPEKRLPtnpwpqypminRTGYGQEEADFVQQTDL 364
Cdd:PRK12779 456 GNTAMDAARTAKRLGGnvtivyrrtksempARVEELhhalEEGINLAVLRAP-----------REFIGDDHTHFVTHALL 524
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 365 tdyitsTVEFLGE---NGQVTAVKTikvgpgfkaieGTEEVIKADLVLLAMGFTG------AEKALFDQ--FRVECVYDD 433
Cdd:PRK12779 525 ------DVNELGEpdkSGRRSPKPT-----------GEIERVPVDLVIMALGNTAnpimkdAEPGLKTNkwGTIEVEKGS 587
|
490 500 510
....*....|....*....|....*....|....*
gi 488191275 434 YSTRNEKVFVAGDARRGPSLVIWGIREGRKTAEKI 468
Cdd:PRK12779 588 QRTSIKGVYSGGDAARGGSTAIRAAGDGQAAAKEI 622
|
|
| Fer4_20 |
pfam14691 |
Dihydroprymidine dehydrogenase domain II, 4Fe-4S cluster; Domain II of the enzyme ... |
23-143 |
3.04e-33 |
|
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: 121.49 E-value: 3.04e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 23 RIKDFEELQTTLSVEERQKQAARCMNCGIPFChegtfygggraVSGCPNDNLIPEWNDLIYKGDFRRAFERLTRTNPLPE 102
Cdd:pfam14691 1 RIKNFEEVALGYTEEEAIAEASRCLQCKDPPC-----------VKGCPVHIDIPEFIKLIAEGNFEGAARIILETNPLPA 69
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 488191275 103 MTGRVCPA--PCEKACTEGLNGSG-VTIHDNERFIIDNAFEEGW 143
Cdd:pfam14691 70 ICGRVCPQerQCEGACVLGKKGFEpVAIGRLERFAADWARENGI 113
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
156-461 |
8.95e-27 |
|
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: 109.72 E-value: 8.95e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 156 FKVAVVGSGPAGLSAAWRLNQLGHSVTVFERSDR---FGGLLMYGIPNMKLDKKIVQRRIDTMASI---------GINFV 223
Cdd:pfam07992 1 YDVVVIGGGPAGLAAALTLAQLGGKVTLIEDEGTcpyGGCVLSKALLGAAEAPEIASLWADLYKRKeevvkklnnGIEVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 224 ANTEI------GRDITAEELLE------KFDRVILATGASvPRDLDIPGRDLKGIrFAVDFLTETTKNLLDsdthelppl 291
Cdd:pfam07992 81 LGTEVvsidpgAKKVVLEELVDgdgetiTYDRLVIATGAR-PRLPPIPGVELNVG-FLVRTLDSAEALRLK--------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 292 LEGKHVLVIGGGDTGNDCIGTAVRLGaASVRQLEITPQLPEkrlptnpwpqypminrtGYGQEEADFVQqtdltdyitst 371
Cdd:pfam07992 150 LLPKRVVVVGGGYIGVELAAALAKLG-KEVTLIEALDRLLR-----------------AFDEEISAALE----------- 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 372 vEFLGENG-----QVTAVKTIKVGPGFKAIEGTEEVIKADLVLLAMGFTgAEKALFDQFRVEC------VYDDYS-TRNE 439
Cdd:pfam07992 201 -KALEKNGvevrlGTSVKEIIGDGDGVEVILKDGTEIDADLVVVAIGRR-PNTELLEAAGLELderggiVVDEYLrTSVP 278
|
330 340
....*....|....*....|...
gi 488191275 440 KVFVAGDAR-RGPSLVIWGIREG 461
Cdd:pfam07992 279 GIYAAGDCRvGGPELAQNAVAQG 301
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
156-468 |
1.37e-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: 97.08 E-value: 1.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 156 FKVAVVGSGPAGLSAAWRLNQLGHSVTVFERsDRFGG------------LL-------------MYGI--PNMKLD-KKI 207
Cdd:COG1249 4 YDLVVIGAGPGGYVAAIRAAQLGLKVALVEK-GRLGGtclnvgcipskaLLhaaevahearhaaEFGIsaGAPSVDwAAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 208 VQRR---IDTMASI--------GIN-------FVANTEIgrDITAEELLEkFDRVILATGaSVPRDLDIPGRDLKGIrfa 269
Cdd:COG1249 83 MARKdkvVDRLRGGveellkknGVDvirgrarFVDPHTV--EVTGGETLT-ADHIVIATG-SRPRVPPIPGLDEVRV--- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 270 vdfltettknlLDSDT----HELPpllegKHVLVIGGGDTGndC-IGTAV-RLGAAsVRQLEITPQLpekrLPTnpwpqy 343
Cdd:COG1249 156 -----------LTSDEalelEELP-----KSLVVIGGGYIG--LeFAQIFaRLGSE-VTLVERGDRL----LPG------ 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 344 pminrtgygqEEADFVQQtdLTDYITST-VEFLgENGQVTAVKtiKVGPGFKAI---EGTEEVIKADLVLLAMGFT---- 415
Cdd:COG1249 207 ----------EDPEISEA--LEKALEKEgIDIL-TGAKVTSVE--KTGDGVTVTledGGGEEAVEADKVLVATGRRpntd 271
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 488191275 416 --GAEKA---LFDQFRVEcVyDDYS-TRNEKVFVAGDARRGPSLVIWGIREGRKTAEKI 468
Cdd:COG1249 272 glGLEAAgveLDERGGIK-V-DEYLrTSVPGIYAIGDVTGGPQLAHVASAEGRVAAENI 328
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
156-465 |
3.48e-18 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 84.79 E-value: 3.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 156 FKVAVVGSGPAGLSAAWRLNQLGHSVTVFERsDRFGGLLM--------YGIP----------NM-----KLDKKIVQRRI 212
Cdd:COG0492 1 YDVVIIGAGPAGLTAAIYAARAGLKTLVIEG-GEPGGQLAttkeienyPGFPegisgpelaeRLreqaeRFGAEILLEEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 213 DTMASIGINFVANTEIGRDITAeellekfDRVILATGASvPRDLDIPGRDL---KGIRFAVdfltettknlldsdTHElP 289
Cdd:COG0492 80 TSVDKDDGPFRVTTDDGTEYEA-------KAVIIATGAG-PRKLGLPGEEEfegRGVSYCA--------------TCD-G 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 290 PLLEGKHVLVIGGGDTGndcIGTAVRLG--AASVRqleitpqlpekrlptnpwpqypMINRTGY---GQEEADFVQQTDL 364
Cdd:COG0492 137 FFFRGKDVVVVGGGDSA---LEEALYLTkfASKVT----------------------LIHRRDElraSKILVERLRANPK 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 365 TDYITSTV--EFLGENGqVTAVKTIKVGPgfkaieGTEEVIKADLVLLAMGFTgAEKALFDQFRVEC-------VYDDYS 435
Cdd:COG0492 192 IEVLWNTEvtEIEGDGR-VEGVTLKNVKT------GEEKELEVDGVFVAIGLK-PNTELLKGLGLELdedgyivVDEDME 263
|
330 340 350
....*....|....*....|....*....|.
gi 488191275 436 TRNEKVFVAGDARRGPS-LVIWGIREGRKTA 465
Cdd:COG0492 264 TSVPGVFAAGDVRDYKYrQAATAAGEGAIAA 294
|
|
| PLN02852 |
PLN02852 |
ferredoxin-NADP+ reductase |
151-309 |
1.12e-17 |
|
ferredoxin-NADP+ reductase
Pssm-ID: 215457 Cd Length: 491 Bit Score: 85.52 E-value: 1.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 151 IERTGFKVAVVGSGPAGLSAAWRL---NQLGHsVTVFERSDRFGGLLMYGIPNMKLDKKIVQRRID-TMASIGINFVANT 226
Cdd:PLN02852 22 STSEPLHVCVVGSGPAGFYTADKLlkaHDGAR-VDIIERLPTPFGLVRSGVAPDHPETKNVTNQFSrVATDDRVSFFGNV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 227 EIGRDITAEELLEKFDRVILATGASVPRDLDIPGRDLKGIRFAVDFLteTTKNLLDSDTHELPPLLEGKHVLVIGGGDTG 306
Cdd:PLN02852 101 TLGRDVSLSELRDLYHVVVLAYGAESDRRLGIPGEDLPGVLSAREFV--WWYNGHPDCVHLPPDLKSSDTAVVLGQGNVA 178
|
...
gi 488191275 307 NDC 309
Cdd:PLN02852 179 LDC 181
|
|
| CzcO |
COG2072 |
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ... |
156-306 |
2.85e-14 |
|
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: 74.51 E-value: 2.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 156 FKVAVVGSGPAGLSAAWRLNQLGHSVTVFERSDRFGG---------------LLMYGIPNMK------------------ 202
Cdd:COG2072 7 VDVVVIGAGQAGLAAAYHLRRAGIDFVVLEKADDVGGtwrdnrypglrldtpSHLYSLPFFPnwsddpdfptgdeilayl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 203 --------LDKKI-----VQR-RIDTMASIginFVANTEIGRDITAeellekfDRVILATGA-SVPRDLDIPGRDlkgiR 267
Cdd:COG2072 87 eayadkfgLRRPIrfgteVTSaRWDEADGR---WTVTTDDGETLTA-------RFVVVATGPlSRPKIPDIPGLE----D 152
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 488191275 268 FAVDFL-TETTKNLLDsdthelpplLEGKHVLVIGGGDTG 306
Cdd:COG2072 153 FAGEQLhSADWRNPVD---------LAGKRVLVVGTGASA 183
|
|
| HemY |
COG1232 |
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ... |
157-194 |
2.67e-13 |
|
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: 71.40 E-value: 2.67e-13
10 20 30
....*....|....*....|....*....|....*...
gi 488191275 157 KVAVVGSGPAGLSAAWRLNQLGHSVTVFERSDRFGGLL 194
Cdd:COG1232 3 RVAVIGGGIAGLTAAYRLAKAGHEVTVLEASDRVGGLI 40
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
181-447 |
7.94e-12 |
|
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: 65.99 E-value: 7.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 181 VTVFERSDRFGGL---LMYGIPNMKLD-KKIVQRRIDTMASIGINFVANTE---IGRD----ITAEELLEKFDRVILATG 249
Cdd:COG0446 8 ITVIEKGPHHSYQpcgLPYYVGGGIKDpEDLLVRTPESFERKGIDVRTGTEvtaIDPEaktvTLRDGETLSYDKLVLATG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 250 ASvPRDLDIPGRDLKGIrFAVDFL--TETTKNLLDSDthelppllEGKHVLVIGGGdtgndCIG-----TAVRLGaASVR 322
Cdd:COG0446 88 AR-PRPPPIPGLDLPGV-FTLRTLddADALREALKEF--------KGKRAVVIGGG-----PIGlelaeALRKRG-LKVT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 323 QLEITPQLpekrLPtnpwpqypminrtGYGQEEADFVQQTdLTDYitsTVEF-LGENgqvtaVKTIKVGPGFKAIEGTEE 401
Cdd:COG0446 152 LVERAPRL----LG-------------VLDPEMAALLEEE-LREH---GVELrLGET-----VVAIDGDDKVAVTLTDGE 205
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 488191275 402 VIKADLVLLAMGFtGAEKALFDQFRVEC-------VYDDYSTRNEKVFVAGDA 447
Cdd:COG0446 206 EIPADLVVVAPGV-RPNTELAKDAGLALgergwikVDETLQTSDPDVYAAGDC 257
|
|
| PRK07233 |
PRK07233 |
hypothetical protein; Provisional |
157-205 |
8.33e-12 |
|
hypothetical protein; Provisional
Pssm-ID: 235977 [Multi-domain] Cd Length: 434 Bit Score: 66.83 E-value: 8.33e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 488191275 157 KVAVVGSGPAGLSAAWRLNQLGHSVTVFERSDRFGGLL-MYGIPNMKLDK 205
Cdd:PRK07233 1 KIAIVGGGIAGLAAAYRLAKRGHEVTVFEADDQLGGLAaSFEFGGLPIER 50
|
|
| YobN |
COG1231 |
Monoamine oxidase [Amino acid transport and metabolism]; |
153-192 |
3.14e-11 |
|
Monoamine oxidase [Amino acid transport and metabolism];
Pssm-ID: 440844 [Multi-domain] Cd Length: 440 Bit Score: 64.94 E-value: 3.14e-11
10 20 30 40
....*....|....*....|....*....|....*....|
gi 488191275 153 RTGFKVAVVGSGPAGLSAAWRLNQLGHSVTVFERSDRFGG 192
Cdd:COG1231 5 ARGKDVVIVGAGLAGLAAARELRKAGLDVTVLEARDRVGG 44
|
|
| Ppro0129 |
COG2907 |
Predicted flavin-containing amine oxidase [General function prediction only]; |
157-192 |
6.05e-11 |
|
Predicted flavin-containing amine oxidase [General function prediction only];
Pssm-ID: 442151 [Multi-domain] Cd Length: 423 Bit Score: 63.98 E-value: 6.05e-11
10 20 30
....*....|....*....|....*....|....*.
gi 488191275 157 KVAVVGSGPAGLSAAWRLNQLgHSVTVFERSDRFGG 192
Cdd:COG2907 5 RIAVIGSGISGLTAAWLLSRR-HDVTLFEANDRLGG 39
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
157-413 |
1.67e-10 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 62.85 E-value: 1.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 157 KVAVVGSGPAGLSAAWRLNQLGH--SVTVF--ERS---DRFggLLMYGIPNMKLDKKIVQRRIDTMASIGINFVANTE-- 227
Cdd:COG1251 3 RIVIIGAGMAGVRAAEELRKLDPdgEITVIgaEPHppyNRP--PLSKVLAGETDEEDLLLRPADFYEENGIDLRLGTRvt 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 228 -IGRD----ITAEELLEKFDRVILATGASvPRDLDIPGRDLKGIrFAVdfltettKNLLDSDT-HELppLLEGKHVLVIG 301
Cdd:COG1251 81 aIDRAartvTLADGETLPYDKLVLATGSR-PRVPPIPGADLPGV-FTL-------RTLDDADAlRAA--LAPGKRVVVIG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 302 GGDTGNDCIGTAVRLGAAsVRQLEITPQLPEKRLPtnpwpqypminrtgygQEEADFVQQTdLTDY-I-----TSTVEFL 375
Cdd:COG1251 150 GGLIGLEAAAALRKRGLE-VTVVERAPRLLPRQLD----------------EEAGALLQRL-LEALgVevrlgTGVTEIE 211
|
250 260 270
....*....|....*....|....*....|....*...
gi 488191275 376 GEnGQVTAVKTikvgpgfkaieGTEEVIKADLVLLAMG 413
Cdd:COG1251 212 GD-DRVTGVRL-----------ADGEELPADLVVVAIG 237
|
|
| NAD_binding_8 |
pfam13450 |
NAD(P)-binding Rossmann-like domain; |
160-204 |
2.17e-10 |
|
NAD(P)-binding Rossmann-like domain;
Pssm-ID: 433218 [Multi-domain] Cd Length: 67 Bit Score: 56.39 E-value: 2.17e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 488191275 160 VVGSGPAGLSAAWRLNQLGHSVTVFERSDRFGGLLM-YGIPNMKLD 204
Cdd:pfam13450 1 IVGAGLAGLVAAALLAKRGFRVLVLEKRDRLGGNAYsYRVPGYVFD 46
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
156-447 |
3.45e-10 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 61.73 E-value: 3.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 156 FKVAVVGSGPAGLSAAWRLNQLGHSVTVFERsDRFGG-----------LLMY--------------GI--PNMKLD-KKI 207
Cdd:PRK06292 4 YDVIVIGAGPAGYVAARRAAKLGKKVALIEK-GPLGGtclnvgcipskALIAaaeafheakhaeefGIhaDGPKIDfKKV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 208 VQR------------RIDTMASIGIN-------FVANTEIgrDITAEELleKFDRVILATGASVPRdldIPGrdlkgirf 268
Cdd:PRK06292 83 MARvrrerdrfvggvVEGLEKKPKIDkikgtarFVDPNTV--EVNGERI--EAKNIVIATGSRVPP---IPG-------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 269 avdFLTETTKNLLDSDT-HELPPLleGKHVLVIGGGdtgndCIG--TAV---RLGAAsVRQLEITPQLpekrLPtnpwpq 342
Cdd:PRK06292 148 ---VWLILGDRLLTSDDaFELDKL--PKSLAVIGGG-----VIGleLGQalsRLGVK-VTVFERGDRI----LP------ 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 343 ypminrtgygQEEADFVQQtdLTDYITSTVEFLgENGQVTAVKTIKVGP-GFKAIEGTEEVIKADLVLLAMGFT------ 415
Cdd:PRK06292 207 ----------LEDPEVSKQ--AQKILSKEFKIK-LGAKVTSVEKSGDEKvEELEKGGKTETIEADYVLVATGRRpntdgl 273
|
330 340 350
....*....|....*....|....*....|....*.
gi 488191275 416 GAEKA---LFDQFRVecVYDDYSTRNEK-VFVAGDA 447
Cdd:PRK06292 274 GLENTgieLDERGRP--VVDEHTQTSVPgIYAAGDV 307
|
|
| PRK07208 |
PRK07208 |
hypothetical protein; Provisional |
157-193 |
7.95e-10 |
|
hypothetical protein; Provisional
Pssm-ID: 235967 [Multi-domain] Cd Length: 479 Bit Score: 60.67 E-value: 7.95e-10
10 20 30
....*....|....*....|....*....|....*..
gi 488191275 157 KVAVVGSGPAGLSAAWRLNQLGHSVTVFERSDRFGGL 193
Cdd:PRK07208 6 SVVIIGAGPAGLTAAYELLKRGYPVTVLEADPVVGGI 42
|
|
| COG3380 |
COG3380 |
Predicted NAD/FAD-dependent oxidoreductase [General function prediction only]; |
156-192 |
1.49e-09 |
|
Predicted NAD/FAD-dependent oxidoreductase [General function prediction only];
Pssm-ID: 442607 [Multi-domain] Cd Length: 331 Bit Score: 59.12 E-value: 1.49e-09
10 20 30
....*....|....*....|....*....|....*..
gi 488191275 156 FKVAVVGSGPAGLSAAWRLNQLGHSVTVFERSDRFGG 192
Cdd:COG3380 4 PDIAIIGAGIAGLAAARALQDAGHEVTVFEKSRGVGG 40
|
|
| PRK06567 |
PRK06567 |
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; Validated |
67-308 |
1.64e-09 |
|
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; Validated
Pssm-ID: 235832 [Multi-domain] Cd Length: 1028 Bit Score: 60.30 E-value: 1.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 67 SGCPNDNLIPEWNDLIYKGDFRRAFERLTRTNPLPEMTG-RVCpAPCEKACteglngsgvtIHD-----NERFIIDNAFE 140
Cdd:PRK06567 282 QGCPLKQKISEMNYVKAQGFNLSALAIIVIDNPMVAATGhRIC-NDCSKAC----------IYQkqdpvNIPLIESNILE 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 141 EGWVADSGR------------------PIERTGFKVAVVGSGPAGLSAAWRLNQLGHSVTVF------------------ 184
Cdd:PRK06567 351 ETLKLPYGLeiyllltrwnplniyaplPKEPTNYNILVTGLGPAGFSLSYYLLRSGHNVTAIdglkitllpfdvhkpikf 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 185 ---------ERSDR-FGGLLMYGIP------NMKLDKKIVQRRIDtmasigINFVANTEIGRDITAEELLE-KFDRVILA 247
Cdd:PRK06567 431 wheyknllsERMPRgFGGVAEYGITvrwdknNLDILRLILERNNN------FKYYDGVALDFNITKEQAFDlGFDHIAFC 504
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488191275 248 TGASVPRDLDIPGRDLKGIRFAVDFLTeTTKN----LLDSDTHelppLLEGKHVLVIGGGDTGND 308
Cdd:PRK06567 505 IGAGQPKVLDIENFEAKGVKTASDFLM-TLQSggafLKNSNTN----MVIRMPIAVIGGGLTSLD 564
|
|
| COG1233 |
COG1233 |
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ... |
156-192 |
2.44e-09 |
|
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440846 [Multi-domain] Cd Length: 491 Bit Score: 59.48 E-value: 2.44e-09
10 20 30
....*....|....*....|....*....|....*..
gi 488191275 156 FKVAVVGSGPAGLSAAWRLNQLGHSVTVFERSDRFGG 192
Cdd:COG1233 4 YDVVVIGAGIGGLAAAALLARAGYRVTVLEKNDTPGG 40
|
|
| COG3349 |
COG3349 |
Uncharacterized protein, contains NAD-binding domain and a Fe-S cluster [General function ... |
157-192 |
1.22e-08 |
|
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: 57.17 E-value: 1.22e-08
10 20 30
....*....|....*....|....*....|....*.
gi 488191275 157 KVAVVGSGPAGLSAAWRLNQLGHSVTVFERSDRFGG 192
Cdd:COG3349 5 RVVVVGGGLAGLAAAVELAEAGFRVTLLEARPRLGG 40
|
|
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
156-468 |
1.40e-07 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 53.61 E-value: 1.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 156 FKVAVVGSGPAGLSAAWRLNQLGHSVTVFERSDrFGGL-LMYG-IP-------------------------NMKLDKKIV 208
Cdd:PRK06416 5 YDVIVIGAGPGGYVAAIRAAQLGLKVAIVEKEK-LGGTcLNRGcIPskallhaaeradearhsedfgikaeNVGIDFKKV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 209 QRRID------------TMASIGIN-------FVANTEIG-RDITAEELLeKFDRVILATGaSVPRdlDIPGRDLKGirf 268
Cdd:PRK06416 84 QEWKNgvvnrltggvegLLKKNKVDiirgeakLVDPNTVRvMTEDGEQTY-TAKNIILATG-SRPR--ELPGIEIDG--- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 269 avdfltettKNLLDSDT----HELPpllegKHVLVIGGGDTGNDcIGTAVR-LGaASVRQLEITPQLpekrLPTnpwpqy 343
Cdd:PRK06416 157 ---------RVIWTSDEalnlDEVP-----KSLVVIGGGYIGVE-FASAYAsLG-AEVTIVEALPRI----LPG------ 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 344 pminrtgygqEEADFVQQTdLTDYITSTVEFlgengqVTAVKTIKVGPGFKAIE------GTEEVIKADLVLLAMGFTGA 417
Cdd:PRK06416 211 ----------EDKEISKLA-ERALKKRGIKI------KTGAKAKKVEQTDDGVTvtledgGKEETLEADYVLVAVGRRPN 273
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 488191275 418 EKAL-FDQFRVE-----CVYDDYS-TRNEKVFVAGDARRGPSLVIWGIREGRKTAEKI 468
Cdd:PRK06416 274 TENLgLEELGVKtdrgfIEVDEQLrTNVPNIYAIGDIVGGPMLAHKASAEGIIAAEAI 331
|
|
| PRK11883 |
PRK11883 |
protoporphyrinogen oxidase; Reviewed |
157-194 |
1.90e-07 |
|
protoporphyrinogen oxidase; Reviewed
Pssm-ID: 237009 [Multi-domain] Cd Length: 451 Bit Score: 53.31 E-value: 1.90e-07
10 20 30 40
....*....|....*....|....*....|....*....|
gi 488191275 157 KVAVVGSGPAGLSAAWRLNQLG--HSVTVFERSDRFGGLL 194
Cdd:PRK11883 2 KVAIIGGGITGLSAAYRLHKKGpdADITLLEASDRLGGKI 41
|
|
| UbiH |
COG0654 |
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ... |
156-191 |
2.19e-07 |
|
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: 52.63 E-value: 2.19e-07
10 20 30
....*....|....*....|....*....|....*.
gi 488191275 156 FKVAVVGSGPAGLSAAWRLNQLGHSVTVFERSDRFG 191
Cdd:COG0654 4 TDVLIVGGGPAGLALALALARAGIRVTVVERAPPPR 39
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
157-228 |
3.88e-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: 47.58 E-value: 3.88e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488191275 157 KVAVVGSGPAGLSAAWRLNQLGHSVTVFERSDRFGGllmygipnmKLDKKIVQRRIDTMASIGINFVANTEI 228
Cdd:pfam00070 1 RVVVVGGGYIGLELAGALARLGSKVTVVERRDRLLP---------GFDPEIAKILQEKLEKNGIEFLLNTTV 63
|
|
| DadA |
COG0665 |
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism]; |
157-201 |
4.44e-07 |
|
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
Pssm-ID: 440429 [Multi-domain] Cd Length: 364 Bit Score: 51.83 E-value: 4.44e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 488191275 157 KVAVVGSGPAGLSAAWRLNQLGHSVTVFER-------SDRFGGLLMYGIPNM 201
Cdd:COG0665 4 DVVVIGGGIAGLSTAYHLARRGLDVTVLERgrpgsgaSGRNAGQLRPGLAAL 55
|
|
| DAO |
pfam01266 |
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ... |
157-198 |
5.89e-07 |
|
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: Glycerol-3-phosphate dehydrogenase EC:1.1.99.5, Sarcosine oxidase beta subunit EC:1.5.3.1, D-alanine oxidase EC:1.4.99.1, D-aspartate oxidase EC:1.4.3.1.
Pssm-ID: 426168 [Multi-domain] Cd Length: 339 Bit Score: 51.24 E-value: 5.89e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 488191275 157 KVAVVGSGPAGLSAAWRLNQLGHSVTVFER--------SDRFGGLLMYGI 198
Cdd:pfam01266 1 DVVVIGGGIVGLSTAYELARRGLSVTLLERgddpgsgaSGRNAGLIHPGL 50
|
|
| HdrA |
COG1148 |
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion]; |
157-250 |
7.13e-07 |
|
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
Pssm-ID: 440762 [Multi-domain] Cd Length: 563 Bit Score: 51.78 E-value: 7.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 157 KVAVVGSGPAGLSAAWRLNQLGHSVTVFERSDRFGGL---LMYGIPNMK-----LDKKIVQ----RRID--TMA------ 216
Cdd:COG1148 142 RALVIGGGIAGMTAALELAEQGYEVYLVEKEPELGGRaaqLHKTFPGLDcpqciLEPLIAEveanPNITvyTGAeveevs 221
|
90 100 110
....*....|....*....|....*....|....*
gi 488191275 217 -SIGiNFVANTEIGrdiTAEELLEKFDRVILATGA 250
Cdd:COG1148 222 gYVG-NFTVTIKKG---PREEIEIEVGAIVLATGF 252
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
152-249 |
7.91e-07 |
|
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase [Lipid transport and metabolism];
Pssm-ID: 440215 [Multi-domain] Cd Length: 322 Bit Score: 50.97 E-value: 7.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 152 ERTGFKVAVVGSGPAGLSAAWRLNQLGHSVTVFERSDRfggllmygiPNMKLDKKIVQRRIDTMASIGINFVANTEIGRd 231
Cdd:COG0446 121 EFKGKRAVVIGGGPIGLELAEALRKRGLKVTLVERAPR---------LLGVLDPEMAALLEEELREHGVELRLGETVVA- 190
|
90 100
....*....|....*....|....*..
gi 488191275 232 ITAEELLE---------KFDRVILATG 249
Cdd:COG0446 191 IDGDDKVAvtltdgeeiPADLVVVAPG 217
|
|
| Amino_oxidase |
pfam01593 |
Flavin containing amine oxidoreductase; This family consists of various amine oxidases, ... |
166-192 |
1.19e-06 |
|
Flavin containing amine oxidoreductase; This family consists of various amine oxidases, including maze polyamine oxidase (PAO)and various flavin containing monoamine oxidases (MAO). The aligned region includes the flavin binding site of these enzymes. The family also contains phytoene dehydrogenases and related enzymes. In vertebrates MAO plays an important role regulating the intracellular levels of amines via there oxidation; these include various neurotransmitters, neurotoxins and trace amines. In lower eukaryotes such as aspergillus and in bacteria the main role of amine oxidases is to provide a source of ammonium. PAOs in plants, bacteria and protozoa oxidase spermidine and spermine to an aminobutyral, diaminopropane and hydrogen peroxide and are involved in the catabolism of polyamines. Other members of this family include tryptophan 2-monooxygenase, putrescine oxidase, corticosteroid binding proteins and antibacterial glycoproteins.
Pssm-ID: 396255 [Multi-domain] Cd Length: 446 Bit Score: 50.57 E-value: 1.19e-06
10 20
....*....|....*....|....*..
gi 488191275 166 AGLSAAWRLNQLGHSVTVFERSDRFGG 192
Cdd:pfam01593 2 AGLAAARELLRAGHDVTVLEARDRVGG 28
|
|
| YdhS |
COG4529 |
Uncharacterized NAD(P)/FAD-binding protein YdhS [General function prediction only]; |
157-341 |
1.74e-06 |
|
Uncharacterized NAD(P)/FAD-binding protein YdhS [General function prediction only];
Pssm-ID: 443597 [Multi-domain] Cd Length: 466 Bit Score: 50.34 E-value: 1.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 157 KVAVVGSGPAGLSAAWRLNQLGH---SVTVFERSDRFGGLLMYG---------IP--NM--------------------- 201
Cdd:COG4529 7 RIAIIGGGASGTALAIHLLRRAPeplRITLFEPRPELGRGVAYStdspehllnVPagRMsafpddpdhflrwlrengara 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 202 ----------------------------KLDKKIVQRRIDTMA----SIGINFVANTEIGRDITAeellekfDRVILATG 249
Cdd:COG4529 87 apaidpdafvprrlfgeylrerlaealaRAPAGVRLRHIRAEVvdleRDDGGYRVTLADGETLRA-------DAVVLATG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 250 ASVPRDLDIPGRDlkgirfavdfltetTKNLLDS--DTHELPPLLEGKHVLVIGGGDTGNDCIGTAVRLGaasvRQLEIT 327
Cdd:COG4529 160 HPPPAPPPGLAAG--------------SPRYIADpwPPGALARIPPDARVLIIGTGLTAIDVVLSLAARG----HRGPIT 221
|
250
....*....|....*....
gi 488191275 328 P-----QLPEKRLPTNPWP 341
Cdd:COG4529 222 AlsrrgLLPRAHPPGAPLP 240
|
|
| PLN02172 |
PLN02172 |
flavin-containing monooxygenase FMO GS-OX |
158-196 |
2.33e-06 |
|
flavin-containing monooxygenase FMO GS-OX
Pssm-ID: 215116 [Multi-domain] Cd Length: 461 Bit Score: 49.86 E-value: 2.33e-06
10 20 30
....*....|....*....|....*....|....*....
gi 488191275 158 VAVVGSGPAGLSAAWRLNQLGHSVTVFERSDRFGGLLMY 196
Cdd:PLN02172 13 VAVIGAGAAGLVAARELRREGHTVVVFEREKQVGGLWVY 51
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
157-276 |
2.43e-06 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 49.75 E-value: 2.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 157 KVAVVGSGPAGLSAAWRLNQLGHSVTVFERSDRfgglLMYGIpnmkLDK---KIVQRRIdtmASIGINFVANTEIgRDIT 233
Cdd:COG1251 144 RVVVIGGGLIGLEAAAALRKRGLEVTVVERAPR----LLPRQ----LDEeagALLQRLL---EALGVEVRLGTGV-TEIE 211
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 488191275 234 AEellEKFDRVILATGASVPRDLDIPGrdlKGIRFAVDFLTET 276
Cdd:COG1251 212 GD---DRVTGVRLADGEELPADLVVVA---IGVRPNTELARAA 248
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
157-306 |
2.47e-06 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 49.75 E-value: 2.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 157 KVAVVGSGPAGLSAAWRLNQL---GHSVTVFERSDR--FGGLLmYGIP--NMKLD------KKIVQR-----RIDTMasI 218
Cdd:COG1252 3 RIVIVGGGFAGLEAARRLRKKlggDAEVTLIDPNPYhlFQPLL-PEVAagTLSPDdiaiplRELLRRagvrfIQGEV--T 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 219 GINFVANT---EIGRDITaeellekFDRVILATGaSVPRDLDIPG-----RDLKGIRFAVDFLTETTKNLLDSDTHELPp 290
Cdd:COG1252 80 GIDPEARTvtlADGRTLS-------YDYLVIATG-SVTNFFGIPGlaehaLPLKTLEDALALRERLLAAFERAERRRLL- 150
|
170
....*....|....*.
gi 488191275 291 llegkHVLVIGGGDTG 306
Cdd:COG1252 151 -----TIVVVGGGPTG 161
|
|
| PLN02976 |
PLN02976 |
amine oxidase |
157-192 |
5.77e-06 |
|
amine oxidase
Pssm-ID: 215527 [Multi-domain] Cd Length: 1713 Bit Score: 49.10 E-value: 5.77e-06
10 20 30
....*....|....*....|....*....|....*.
gi 488191275 157 KVAVVGSGPAGLSAAWRLNQLGHSVTVFERSDRFGG 192
Cdd:PLN02976 695 KIIVVGAGPAGLTAARHLQRQGFSVTVLEARSRIGG 730
|
|
| FAD_binding_2 |
pfam00890 |
FAD binding domain; This family includes members that bind FAD. This family includes the ... |
158-219 |
9.20e-06 |
|
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: 47.67 E-value: 9.20e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 158 VAVVGSGPAGLSAAWRLNQLGHSVTVFERSDRF--------GGLLMYGIPNMKLDKKIVQRRIDTMASIG 219
Cdd:pfam00890 2 VLVIGGGLAGLAAALAAAEAGLKVAVVEKGQPFggatawssGGIDALGNPPQGGIDSPELHPTDTLKGLD 71
|
|
| HI0933_like |
pfam03486 |
HI0933-like protein; |
156-197 |
9.45e-06 |
|
HI0933-like protein;
Pssm-ID: 427330 [Multi-domain] Cd Length: 406 Bit Score: 47.96 E-value: 9.45e-06
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 488191275 156 FKVAVVGSGPAGLSAAWRLNQLGHSVTVFERSDRFG-GLLMYG 197
Cdd:pfam03486 1 FDVIVIGGGAAGLMAAISAAKRGRRVLLIEKGKKLGrKILISG 43
|
|
| PRK12771 |
PRK12771 |
putative glutamate synthase (NADPH) small subunit; Provisional |
7-53 |
1.19e-05 |
|
putative glutamate synthase (NADPH) small subunit; Provisional
Pssm-ID: 237198 [Multi-domain] Cd Length: 564 Bit Score: 47.56 E-value: 1.19e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 488191275 7 FLKYERKDNPYRPVNERIKDFEELQTTLSVEERQKQAARCMNCGIPF 53
Cdd:PRK12771 467 FTDAPRAQRPELDADERVGDFDEVLGGLTEEEARQEAARCLSCGNCF 513
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
156-446 |
1.24e-05 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 47.50 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 156 FKVAVVGSGPAGLSAAWRLNQLGHSVTVFERsDRFGG-LLMYG-IPNmkldKKIVQ--------RR-----IDTMASIGI 220
Cdd:PRK06370 6 YDAIVIGAGQAGPPLAARAAGLGMKVALIER-GLLGGtCVNTGcVPT----KTLIAsaraahlaRRaaeygVSVGGPVSV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 221 NFVANTEIGRDITA----------------------------------EELLEkFDRVILATG--ASVPrdlDIPGRDlk 264
Cdd:PRK06370 81 DFKAVMARKRRIRArsrhgseqwlrglegvdvfrgharfespntvrvgGETLR-AKRIFINTGarAAIP---PIPGLD-- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 265 girfAVDFLTETTknLLDSDthELPpllegKHVLVIGGGDTGNDCIGTAVRLGaASVRQLEITPQLpekrlptnpwpqyp 344
Cdd:PRK06370 155 ----EVGYLTNET--IFSLD--ELP-----EHLVIIGGGYIGLEFAQMFRRFG-SEVTVIERGPRL-------------- 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 345 mINRtgygqEEADF---VQQTDLTDYItsTVEFlgeNGQVTAVKTI--KVGPGFKAIEGTEEVIkADLVLLAMGFT---- 415
Cdd:PRK06370 207 -LPR-----EDEDVaaaVREILEREGI--DVRL---NAECIRVERDgdGIAVGLDCNGGAPEIT-GSHILVAVGRVpntd 274
|
330 340 350
....*....|....*....|....*....|....*.
gi 488191275 416 --GAEKA--LFDQFRVECVyDDY-STRNEKVFVAGD 446
Cdd:PRK06370 275 dlGLEAAgvETDARGYIKV-DDQlRTTNPGIYAAGD 309
|
|
| PTZ00188 |
PTZ00188 |
adrenodoxin reductase; Provisional |
152-251 |
2.78e-05 |
|
adrenodoxin reductase; Provisional
Pssm-ID: 240308 Cd Length: 506 Bit Score: 46.41 E-value: 2.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 152 ERTGFKVAVVGSGPAGLSAAWRLnqLGHS---VTVFERSDRFGGLLMYGIPNMKLDKKIVQRRID-TMASIGINFVANTE 227
Cdd:PTZ00188 36 EAKPFKVGIIGAGPSALYCCKHL--LKHErvkVDIFEKLPNPYGLIRYGVAPDHIHVKNTYKTFDpVFLSPNYRFFGNVH 113
|
90 100
....*....|....*....|....
gi 488191275 228 IGRDITAEELLEKFDRVILATGAS 251
Cdd:PTZ00188 114 VGVDLKMEELRNHYNCVIFCCGAS 137
|
|
| PRK00711 |
PRK00711 |
D-amino acid dehydrogenase; |
157-189 |
3.78e-05 |
|
D-amino acid dehydrogenase;
Pssm-ID: 234819 [Multi-domain] Cd Length: 416 Bit Score: 45.95 E-value: 3.78e-05
10 20 30
....*....|....*....|....*....|...
gi 488191275 157 KVAVVGSGPAGLSAAWRLNQLGHSVTVFERSDR 189
Cdd:PRK00711 2 RVVVLGSGVIGVTSAWYLAQAGHEVTVIDRQPG 34
|
|
| PLN02576 |
PLN02576 |
protoporphyrinogen oxidase |
145-192 |
5.74e-05 |
|
protoporphyrinogen oxidase
Pssm-ID: 215314 [Multi-domain] Cd Length: 496 Bit Score: 45.39 E-value: 5.74e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 488191275 145 ADSGRPIERTGFKVAVVGSGPAGLSAAWRL-NQLGHSVTVFERSDRFGG 192
Cdd:PLN02576 2 AIAEGSAAASSKDVAVVGAGVSGLAAAYALaSKHGVNVLVTEARDRVGG 50
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
157-446 |
6.82e-05 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 45.03 E-value: 6.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 157 KVAVVGSGPAGLSAAWRLNQLGHS--VTVFERSD--RFG--GLL-----MYGIPNMKLDK---KIVQRRIDTMAS---IG 219
Cdd:PRK09564 2 KIIIIGGTAAGMSAAAKAKRLNKEleITVYEKTDivSFGacGLPyfvggFFDDPNTMIARtpeEFIKSGIDVKTEhevVK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 220 INFVANTEIGRDI-TAEELLEKFDRVILATGAS--VPrdlDIPGRDLKGIrfavdfltETTKNLldSDTHELPPLL---E 293
Cdd:PRK09564 82 VDAKNKTITVKNLkTGSIFNDTYDKLMIATGARpiIP---PIKNINLENV--------YTLKSM--EDGLALKELLkdeE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 294 GKHVLVIGGGDTGNDCIGTAVRLGaASVRQLEItpqlpEKRLPTNPWpqypminrtgygQEEADFVQQTDLTD-----YI 368
Cdd:PRK09564 149 IKNIVIIGAGFIGLEAVEAAKHLG-KNVRIIQL-----EDRILPDSF------------DKEITDVMEEELREngvelHL 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 369 TSTVEFLGENGQVTAVKTIKvgpgfkaieGTeevIKADLVLLAMGFTGAEKALFDQfRVE------CVYDDY-STRNEKV 441
Cdd:PRK09564 211 NEFVKSLIGEDKVEGVVTDK---------GE---YEADVVIVATGVKPNTEFLEDT-GLKtlkngaIIVDEYgETSIENI 277
|
....*
gi 488191275 442 FVAGD 446
Cdd:PRK09564 278 YAAGD 282
|
|
| SdhA |
COG1053 |
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and ... |
156-192 |
7.60e-05 |
|
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and conversion]; Succinate dehydrogenase/fumarate reductase, flavoprotein subunit is part of the Pathway/BioSystem: TCA cycle
Pssm-ID: 440673 [Multi-domain] Cd Length: 443 Bit Score: 44.82 E-value: 7.60e-05
10 20 30
....*....|....*....|....*....|....*..
gi 488191275 156 FKVAVVGSGPAGLSAAWRLNQLGHSVTVFERSDRFGG 192
Cdd:COG1053 4 YDVVVVGSGGAGLRAALEAAEAGLKVLVLEKVPPRGG 40
|
|
| FixC |
COG0644 |
Dehydrogenase (flavoprotein) [Energy production and conversion]; |
164-191 |
7.69e-05 |
|
Dehydrogenase (flavoprotein) [Energy production and conversion];
Pssm-ID: 440409 [Multi-domain] Cd Length: 281 Bit Score: 44.57 E-value: 7.69e-05
10 20
....*....|....*....|....*...
gi 488191275 164 GPAGLSAAWRLNQLGHSVTVFERSDRFG 191
Cdd:COG0644 2 GPAGSAAARRLARAGLSVLLLEKGSFPG 29
|
|
| nitri_red_nirB |
TIGR02374 |
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ... |
226-413 |
2.68e-04 |
|
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen metabolism]
Pssm-ID: 162827 [Multi-domain] Cd Length: 785 Bit Score: 43.66 E-value: 2.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 226 TEIGRD----ITAEELLEKFDRVILATGaSVPRDLDIPGRDLKGIRFAVDFltETTKNLLDSDTHElppllegKHVLVIG 301
Cdd:TIGR02374 78 IQIDTDqkqvITDAGRTLSYDKLILATG-SYPFILPIPGADKKGVYVFRTI--EDLDAIMAMAQRF-------KKAAVIG 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 302 GGDTGNDCIGTAVRLGaASVRQLEITPQLPEKRLptnpwpqypmiNRTGyGQEEADFVQQTDLTDYI-TSTVEFLGEngq 380
Cdd:TIGR02374 148 GGLLGLEAAVGLQNLG-MDVSVIHHAPGLMAKQL-----------DQTA-GRLLQRELEQKGLTFLLeKDTVEIVGA--- 211
|
170 180 190
....*....|....*....|....*....|...
gi 488191275 381 vTAVKTIKVGPGfkaiegteEVIKADLVLLAMG 413
Cdd:TIGR02374 212 -TKADRIRFKDG--------SSLEADLIVMAAG 235
|
|
| PRK12409 |
PRK12409 |
D-amino acid dehydrogenase small subunit; Provisional |
157-186 |
3.95e-04 |
|
D-amino acid dehydrogenase small subunit; Provisional
Pssm-ID: 237093 [Multi-domain] Cd Length: 410 Bit Score: 42.70 E-value: 3.95e-04
10 20 30
....*....|....*....|....*....|
gi 488191275 157 KVAVVGSGPAGLSAAWRLNQLGHSVTVFER 186
Cdd:PRK12409 3 HIAVIGAGITGVTTAYALAQRGYQVTVFDR 32
|
|
| glucose_DH |
cd08230 |
Glucose dehydrogenase; Glucose dehydrogenase (GlcDH), a member of the medium chain ... |
157-251 |
5.03e-04 |
|
Glucose dehydrogenase; Glucose dehydrogenase (GlcDH), a member of the medium chain dehydrogenase/zinc-dependent alcohol dehydrogenase-like family, catalyzes the NADP(+)-dependent oxidation of glucose to gluconate, the first step in the Entner-Doudoroff pathway, an alternative to or substitute for glycolysis or the pentose phosphate pathway. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossman fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability.
Pssm-ID: 176192 [Multi-domain] Cd Length: 355 Bit Score: 42.21 E-value: 5.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 157 KVAVVGSGPAGLSAAWRLNQLGHSVTVFERSDRfggllmygiPNMKldkkivqrrIDTMASIGINFVaNTEIGrDITAEE 236
Cdd:cd08230 175 RALVLGAGPIGLLAALLLRLRGFEVYVLNRRDP---------PDPK---------ADIVEELGATYV-NSSKT-PVAEVK 234
|
90
....*....|....*
gi 488191275 237 LLEKFDRVILATGAS 251
Cdd:cd08230 235 LVGEFDLIIEATGVP 249
|
|
| PRK06753 |
PRK06753 |
hypothetical protein; Provisional |
157-186 |
5.75e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 168661 [Multi-domain] Cd Length: 373 Bit Score: 41.98 E-value: 5.75e-04
10 20 30
....*....|....*....|....*....|
gi 488191275 157 KVAVVGSGPAGLSAAWRLNQLGHSVTVFER 186
Cdd:PRK06753 2 KIAIIGAGIGGLTAAALLQEQGHEVKVFEK 31
|
|
| PRK07588 |
PRK07588 |
FAD-binding domain; |
157-194 |
6.49e-04 |
|
FAD-binding domain;
Pssm-ID: 169028 [Multi-domain] Cd Length: 391 Bit Score: 42.03 E-value: 6.49e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 488191275 157 KVAVVGSGPAGLSAAWRLNQLGHSVTVFERSDRF--GGLL 194
Cdd:PRK07588 2 KVAISGAGIAGPTLAYWLRRYGHEPTLIERAPELrtGGYM 41
|
|
| PRK09126 |
PRK09126 |
FAD-dependent hydroxylase; |
156-187 |
1.02e-03 |
|
FAD-dependent hydroxylase;
Pssm-ID: 236385 [Multi-domain] Cd Length: 392 Bit Score: 41.47 E-value: 1.02e-03
10 20 30
....*....|....*....|....*....|..
gi 488191275 156 FKVAVVGSGPAGLSAAWRLNQLGHSVTVFERS 187
Cdd:PRK09126 4 SDIVVVGAGPAGLSFARSLAGSGLKVTLIERQ 35
|
|
| PLN00093 |
PLN00093 |
geranylgeranyl diphosphate reductase; Provisional |
147-246 |
1.10e-03 |
|
geranylgeranyl diphosphate reductase; Provisional
Pssm-ID: 177713 [Multi-domain] Cd Length: 450 Bit Score: 41.28 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 147 SGRPIERTGFKVAVVGSGPAGLSAAWRLNQLGHSVTVFERS----DRFGG---LLMYGIPNMKLDkkIVQRRIDTMASIG 219
Cdd:PLN00093 31 ASKKLSGRKLRVAVIGGGPAGACAAETLAKGGIETFLIERKldnaKPCGGaipLCMVGEFDLPLD--IIDRKVTKMKMIS 108
|
90 100
....*....|....*....|....*..
gi 488191275 220 INFVAnTEIGRDITAEELLEKFDRVIL 246
Cdd:PLN00093 109 PSNVA-VDIGKTLKPHEYIGMVRREVL 134
|
|
| PRK05249 |
PRK05249 |
Si-specific NAD(P)(+) transhydrogenase; |
156-245 |
1.28e-03 |
|
Si-specific NAD(P)(+) transhydrogenase;
Pssm-ID: 235373 [Multi-domain] Cd Length: 461 Bit Score: 41.30 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 156 FKVAVVGSGPAGLSAAWRLNQLGHSVTVFERSDRFGGLLMY-G-IPNMKLdkkivqrRIDTMASIGIN---FVANTEIGR 230
Cdd:PRK05249 6 YDLVVIGSGPAGEGAAMQAAKLGKRVAVIERYRNVGGGCTHtGtIPSKAL-------REAVLRLIGFNqnpLYSSYRVKL 78
|
90
....*....|....*
gi 488191275 231 DITAEELLEKFDRVI 245
Cdd:PRK05249 79 RITFADLLARADHVI 93
|
|
| PRK06134 |
PRK06134 |
putative FAD-binding dehydrogenase; Reviewed |
158-192 |
1.77e-03 |
|
putative FAD-binding dehydrogenase; Reviewed
Pssm-ID: 180419 [Multi-domain] Cd Length: 581 Bit Score: 40.86 E-value: 1.77e-03
10 20 30
....*....|....*....|....*....|....*
gi 488191275 158 VAVVGSGPAGLSAAWRLNQLGHSVTVFERSDRFGG 192
Cdd:PRK06134 15 VLVIGSGAAGLSAAVTAAWHGLKVIVVEKDPVFGG 49
|
|
| Pyr_redox_3 |
pfam13738 |
Pyridine nucleotide-disulphide oxidoreductase; |
157-287 |
1.77e-03 |
|
Pyridine nucleotide-disulphide oxidoreductase;
Pssm-ID: 404603 [Multi-domain] Cd Length: 296 Bit Score: 40.28 E-value: 1.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 157 KVAVVGSGPAGLSAAWRLNQLGHSVTVFERSDrfggllmyGIPNMKLDKKI-----VQRRIDT---MASIGINFVAN-TE 227
Cdd:pfam13738 157 KVVVIGGYNSAVDAALELVRKGARVTVLYRGS--------EWEDRDSDPSYslspdTLNRLEElvkNGKIKAHFNAEvKE 228
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488191275 228 IGRD-----ITAEE--LLEKFDRVILATGASVPRDLdipgrdLKGIRFAVDfltETTKNLLDSDTHE 287
Cdd:pfam13738 229 ITEVdvsykVHTEDgrKVTSNDDPILATGYHPDLSF------LKKGLFELD---EDGRPVLTEETES 286
|
|
| PRK12843 |
PRK12843 |
FAD-dependent oxidoreductase; |
155-202 |
2.86e-03 |
|
FAD-dependent oxidoreductase;
Pssm-ID: 237225 [Multi-domain] Cd Length: 578 Bit Score: 40.10 E-value: 2.86e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 488191275 155 GFKVAVVGSGPAGLSAAWRLNQLGHSVTVFERSDRFGGLLMYG-----IPNMK 202
Cdd:PRK12843 16 EFDVIVIGAGAAGMSAALFAAIAGLKVLLVERTEYVGGTTATSagttwIPGTR 68
|
|
| PRK07251 |
PRK07251 |
FAD-containing oxidoreductase; |
157-249 |
3.18e-03 |
|
FAD-containing oxidoreductase;
Pssm-ID: 180907 [Multi-domain] Cd Length: 438 Bit Score: 39.73 E-value: 3.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 157 KVAVVGSGPAGLSAAWRLNQLGHSVTVFERSDRFGGllmygipnmKLDKKIVQRRIDTMASIGINFVAN---TEIGRD-- 231
Cdd:PRK07251 159 RLGIIGGGNIGLEFAGLYNKLGSKVTVLDAASTILP---------REEPSVAALAKQYMEEDGITFLLNahtTEVKNDgd 229
|
90 100
....*....|....*....|.
gi 488191275 232 ---ITAEELLEKFDRVILATG 249
Cdd:PRK07251 230 qvlVVTEDETYRFDALLYATG 250
|
|
| proto_IX_ox |
TIGR00562 |
protoporphyrinogen oxidase; This enzyme oxidizes protoporphyrinogen IX to protoporphyrin IX, a ... |
157-192 |
3.68e-03 |
|
protoporphyrinogen oxidase; This enzyme oxidizes protoporphyrinogen IX to protoporphyrin IX, a precursor of heme and chlorophyll. Bacillus subtilis HemY also has coproporphyrinogen III to coproporphyrin III oxidase activity in a heterologous expression system, although the role for this activity in vivo is unclear. This protein is a flavoprotein and has a beta-alpha-beta dinucleotide binding motif near the amino end. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]
Pssm-ID: 213540 [Multi-domain] Cd Length: 462 Bit Score: 39.82 E-value: 3.68e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 488191275 157 KVAVVGSGPAGLSAAWRLN----QLGHSVTVFERSDRFGG 192
Cdd:TIGR00562 4 HVVIIGGGISGLCAAYYLEkeipELPVELTLVEASDRVGG 43
|
|
| GG-red-SF |
TIGR02032 |
geranylgeranyl reductase family; This model represents a subfamily which includes ... |
156-188 |
5.00e-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: 38.84 E-value: 5.00e-03
10 20 30
....*....|....*....|....*....|...
gi 488191275 156 FKVAVVGSGPAGLSAAWRLNQLGHSVTVFERSD 188
Cdd:TIGR02032 1 YDVVVVGAGPAGASAAYRLADKGLRVLLLEKKS 33
|
|
| mhpA |
PRK06183 |
bifunctional 3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic acid hydroxylase; |
156-189 |
5.11e-03 |
|
bifunctional 3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic acid hydroxylase;
Pssm-ID: 235727 [Multi-domain] Cd Length: 500 Bit Score: 39.12 E-value: 5.11e-03
10 20 30
....*....|....*....|....*....|....
gi 488191275 156 FKVAVVGSGPAGLSAAWRLNQLGHSVTVFERSDR 189
Cdd:PRK06183 11 TDVVIVGAGPVGLTLANLLGQYGVRVLVLERWPT 44
|
|
| PRK07236 |
PRK07236 |
hypothetical protein; Provisional |
152-193 |
6.19e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 235980 [Multi-domain] Cd Length: 386 Bit Score: 38.75 E-value: 6.19e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 488191275 152 ERTGFKVAVVGSGPAGLSAAWRLNQLGHSVTVFERS-----DRFGGL 193
Cdd:PRK07236 3 HMSGPRAVVIGGSLGGLFAALLLRRAGWDVDVFERSpteldGRGAGI 49
|
|
| Thi4 |
pfam01946 |
Thi4 family; This family includes Swiss:P32318 a putative thiamine biosynthetic enzyme. |
158-192 |
6.41e-03 |
|
Thi4 family; This family includes Swiss:P32318 a putative thiamine biosynthetic enzyme.
Pssm-ID: 460393 Cd Length: 232 Bit Score: 38.22 E-value: 6.41e-03
10 20 30
....*....|....*....|....*....|....*.
gi 488191275 158 VAVVGSGPAGLSAAWRL-NQLGHSVTVFERSDRFGG 192
Cdd:pfam01946 20 VVIVGAGSSGLTAAYYLaKNRGLKVAIIERSVSPGG 55
|
|
| PLN02268 |
PLN02268 |
probable polyamine oxidase |
158-192 |
6.75e-03 |
|
probable polyamine oxidase
Pssm-ID: 177909 [Multi-domain] Cd Length: 435 Bit Score: 38.90 E-value: 6.75e-03
10 20 30
....*....|....*....|....*....|....*
gi 488191275 158 VAVVGSGPAGLSAAWRLNQLGHSVTVFERSDRFGG 192
Cdd:PLN02268 3 VIVIGGGIAGIAAARALHDASFKVTLLESRDRIGG 37
|
|
| AlaDh_PNT_C |
smart01002 |
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the ... |
157-254 |
7.07e-03 |
|
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: 37.10 E-value: 7.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191275 157 KVAVVGSGPAGLSAAWRLNQLGHSVTVFERSdrfggllmygIPNMKLDKKIVQRRIDTMASIGINFvanteigrditaEE 236
Cdd:smart01002 22 KVVVIGAGVVGLGAAATAKGLGAEVTVLDVR----------PARLRQLESLLGARFTTLYSQAELL------------EE 79
|
90 100
....*....|....*....|.
gi 488191275 237 LLEKFDRVI---LATGASVPR 254
Cdd:smart01002 80 AVKEADLVIgavLIPGAKAPK 100
|
|
| FAD_oxidored |
pfam12831 |
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases ... |
158-194 |
7.60e-03 |
|
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases and related proteins.
Pssm-ID: 432816 [Multi-domain] Cd Length: 420 Bit Score: 38.74 E-value: 7.60e-03
10 20 30
....*....|....*....|....*....|....*..
gi 488191275 158 VAVVGSGPAGLSAAWRLNQLGHSVTVFERSDRFGGLL 194
Cdd:pfam12831 2 VVVVGGGPAGVAAAIAAARAGAKVLLVERRGFLGGML 38
|
|
| mnmC |
PRK01747 |
bifunctional tRNA (5-methylaminomethyl-2-thiouridine)(34)-methyltransferase MnmD/FAD-dependent ... |
143-189 |
8.38e-03 |
|
bifunctional tRNA (5-methylaminomethyl-2-thiouridine)(34)-methyltransferase MnmD/FAD-dependent 5-carboxymethylaminomethyl-2-thiouridine(34) oxidoreductase MnmC;
Pssm-ID: 234978 [Multi-domain] Cd Length: 662 Bit Score: 38.67 E-value: 8.38e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 488191275 143 WVADSGRPIERtgfKVAVVGSGPAGLSAAWRLNQLGHSVTVFERSDR 189
Cdd:PRK01747 251 WFARPGSPKAR---DAAIIGGGIAGAALALALARRGWQVTLYEADEA 294
|
|
| |
