|
Name |
Accession |
Description |
Interval |
E-value |
| gltD |
PRK12810 |
glutamate synthase subunit beta; Reviewed |
1-477 |
0e+00 |
|
glutamate synthase subunit beta; Reviewed
Pssm-ID: 237213 [Multi-domain] Cd Length: 471 Bit Score: 685.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 1 MADPFGFLEYPKKENPLREIKERIYDWHELQIPLSEEERRKQAARCMVCGIPFCHTGsffggqravsgCPNDNLIPEWND 80
Cdd:PRK12810 1 MGKPTGFLEYDRVDPKKRPVAERIKDFKEFYEPFSEEQAKIQAARCMDCGIPFCHWG-----------CPVHNYIPEWND 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 81 LVFQGRYKEAFERLAKTNPLPEMTGRVCPAPCEDGCTEALNGQGVTIHDNERFIIDTAFENNWVKASgTPQRQTDFKIAV 160
Cdd:PRK12810 70 LVYRGRWEEAAERLHQTNNFPEFTGRVCPAPCEGACTLNINFGPVTIKNIERYIIDKAFEEGWVKPD-PPVKRTGKKVAV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 161 VGSGPAGLSAAWRLNQLGHHVTVFEREDRFGGLLMYGIPSMKLDKAIVQRRVDLMEELGVTFIANTEVSSDVMAKQLQKD 240
Cdd:PRK12810 149 VGSGPAGLAAADQLARAGHKVTVFERADRIGGLLRYGIPDFKLEKEVIDRRIELMEAEGIEFRTNVEVGKDITAEELLAE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 241 FDRVILTTGAGVPRDLSIPGRQLTGIRFAVDYLTEVTKDVLKYGKKTTSRkLEGKHVVVIGGGDTGNDCIGSAIRQGAAS 320
Cdd:PRK12810 229 YDAVFLGTGAYKPRDLGIPGRDLDGVHFAMDFLIQNTRRVLGDETEPFIS-AKGKHVVVIGGGDTGMDCVGTAIRQGAKS 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 321 VKQLEITAEPPVYRSKKNPWPEYPITRHLGYGQEEAyaiykeELTAYQTTITAFVGAQrGQLIAVETMKV---DEAFQPV 397
Cdd:PRK12810 308 VTQRDIMPMPPSRRNKNNPWPYWPMKLEVSNAHEEG------VEREFNVQTKEFEGEN-GKVTGVKVVRTelgEGDFEPV 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 398 EGTKEILEADLVLLAMGFLGTEKHLLDLFDVN--------EIYDDYTTDNEHVMVAGDARRGPSLVIWGIREGRLAAEQV 469
Cdd:PRK12810 381 EGSEFVLPADLVLLAMGFTGPEAGLLAQFGVEldergrvaAPDNAYQTSNPKVFAAGDMRRGQSLVVWAIAEGRQAARAI 460
|
....*...
gi 1341813615 470 NDSLLALS 477
Cdd:PRK12810 461 DAYLMGST 468
|
|
| GOGAT_sm_gam |
TIGR01317 |
glutamate synthases, NADH/NADPH, small subunit; This model represents one of three built for ... |
3-478 |
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: 564.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 3 DPFGFLEYPKKENPLREIKERIYDWHELQIPLSEEERRKQAARCMVCGIPFCHTGSffggqravsGCPNDNLIPEWNDLV 82
Cdd:TIGR01317 1 KPTGFLEYKRRKPTERDPRTRLKDWKEFTNPFDKESAKYQAARCMDCGTPFCHNDS---------GCPLNNLIPEFNDLV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 83 FQGRYKEAFERLAKTNPLPEMTGRVCPAPCEDGCTEALNGQGVTIHDNERFIIDTAFENNWVKASgTPQRQTDFKIAVVG 162
Cdd:TIGR01317 72 FRGRWKEALDRLHATNNFPEFTGRVCPAPCEGACTLGISEDPVGIKSIERIIIDKGFQEGWVQPR-PPSKRTGKKVAVVG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 163 SGPAGLSAAWRLNQLGHHVTVFEREDRFGGLLMYGIPSMKLDKAIVQRRVDLMEELGVTFIANTEVSSDVMAKQLQKDFD 242
Cdd:TIGR01317 151 SGPAGLAAADQLNRAGHTVTVFEREDRCGGLLMYGIPNMKLDKAIVDRRIDLLSAEGIDFVTNTEIGVDISADELKEQFD 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 243 RVILTTGAGVPRDLSIPGRQLTGIRFAVDYLTEVTKDVLKYGKKTTSR-KLEGKHVVVIGGGDTGNDCIGSAIRQGAASV 321
Cdd:TIGR01317 231 AVVLAGGATKPRDLPIPGRELKGIHYAMEFLPSATKALLGKDFKDIIFiKAKGKKVVVIGGGDTGADCVGTSLRHGAASV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 322 KQLEITAEPPVYRSKKNPWPEYPITRHLGYGQEEAYAIYKEELTAYQTTITAFVGAQRGQLIAVETMKVD--------EA 393
Cdd:TIGR01317 311 HQFEIMPKPPEARAKDNPWPEWPRVYRVDYAHEEAAAHYGRDPREYSILTKEFIGDDEGKVTALRTVRVEwkksqdgkWQ 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 394 FQPVEGTKEILEADLVLLAMGFLGTEKHLLDLFDVNEI--------YDDYTTDNEHVMVAGDARRGPSLVIWGIREGRLA 465
Cdd:TIGR01317 391 FVEIPGSEEVFEADLVLLAMGFVGPEQILLDDFGVKKTrrgnisagYDDYSTSIPGVFAAGDCRRGQSLIVWAINEGRKA 470
|
490
....*....|...
gi 1341813615 466 AEQVNDSLLALSY 478
Cdd:TIGR01317 471 AAAVDRYLMGSSV 483
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
23-471 |
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: 517.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 23 RIYDWHELQIPLSEEERRKQAARCMVCGIPFCHTGsffggqravsgCPNDNLIPEWNDLVFQGRYKEAFERLAKTNPLPE 102
Cdd:COG0493 1 RIKDFREVYPGLSEEEAIEQAARCLDCGDPPCQTG-----------CPVGNDIPEWIRLIAEGDYEEALELIHETNPFPE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 103 MTGRVCPAPCEDGCTEALNGQGVTIHDNERFIIDTAFENNWVKASgTPQRQTDFKIAVVGSGPAGLSAAWRLNQLGHHVT 182
Cdd:COG0493 70 VCGRVCPAPCEGACVRGIVDEPVAIGALERFIADKAFEEGWVKPP-PPAPRTGKKVAVVGSGPAGLAAAYQLARAGHEVT 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 183 VFEREDRFGGLLMYGIPSMKLDKAIVQRRVDLMEELGVTFIANTEVSSDVMAKQLQKDFDRVILTTGAGVPRDLSIPGRQ 262
Cdd:COG0493 149 VFEALDKPGGLLRYGIPEFRLPKDVLDREIELIEALGVEFRTNVEVGKDITLDELLEEFDAVFLATGAGKPRDLGIPGED 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 263 LTGIRFAVDYLTEVTKDVLkygKKTTSRKleGKHVVVIGGGDTGNDCIGSAIRQGAASVKQLEItaeppvyRSKKNPwPE 342
Cdd:COG0493 229 LKGVHSAMDFLTAVNLGEA---PDTILAV--GKRVVVIGGGNTAMDCARTALRLGAESVTIVYR-------RTREEM-PA 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 343 YPITRHlgYGQEEAyAIYKeeltaYQTTITAFVGAQRGQLIAVETMKV-----DE----AFQPVEGTKEILEADLVLLAM 413
Cdd:COG0493 296 SKEEVE--EALEEG-VEFL-----FLVAPVEIIGDENGRVTGLECVRMelgepDEsgrrRPVPIEGSEFTLPADLVILAI 367
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1341813615 414 GFLGTEKHLLDLFDV-----NEI---YDDYTTDNEHVMVAGDARRGPSLVIWGIREGRLAAEQVND 471
Cdd:COG0493 368 GQTPDPSGLEEELGLeldkrGTIvvdEETYQTSLPGVFAGGDAVRGPSLVVWAIAEGRKAARAIDR 433
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
6-473 |
2.92e-126 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 374.90 E-value: 2.92e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 6 GFLEYPKKENPLREIKERIYDWHELQIPLSEEERRKQAARCMVCGIPFCHTGsffggqravsgCPNDNLIPEWNDLVFQG 85
Cdd:PRK11749 2 KFLTTPRIPMPRQDAEERAQNFDEVAPGYTPEEAIEEASRCLQCKDAPCVKA-----------CPVSIDIPEFIRLIAEG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 86 RYKEAFERLAKTNPLPEMTGRVCPAP--CEDGCTEALNGQGVTIHDNERFIIDTAFENNWVKAsgTPQRQTDFKIAVVGS 163
Cdd:PRK11749 71 NLKGAAETILETNPLPAVCGRVCPQErlCEGACVRGKKGEPVAIGRLERYITDWAMETGWVLF--KRAPKTGKKVAVIGA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 164 GPAGLSAAWRLNQLGHHVTVFEREDRFGGLLMYGIPSMKLDKAIVQRRVDLMEELGVTFIANTEVSSDVMAKQLQKDFDR 243
Cdd:PRK11749 149 GPAGLTAAHRLARKGYDVTIFEARDKAGGLLRYGIPEFRLPKDIVDREVERLLKLGVEIRTNTEVGRDITLDELRAGYDA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 244 VILTTGAGVPRDLSIPGRQLTGIRFAVDYLTEVTKdvlkygKKTTSRKLEGKHVVVIGGGDTGNDCIGSAIRQGAASVKQ 323
Cdd:PRK11749 229 VFIGTGAGLPRFLGIPGENLGGVYSAVDFLTRVNQ------AVADYDLPVGKRVVVIGGGNTAMDAARTAKRLGAESVTI 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 324 leitaeppVYRSKKNPWPeypitrhlGYGQEEAYAiyKEE------LTAyqttITAFVGAQRGQL-IAVETMKVDEA--- 393
Cdd:PRK11749 303 --------VYRRGREEMP--------ASEEEVEHA--KEEgvefewLAA----PVEILGDEGRVTgVEFVRMELGEPdas 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 394 ---FQPVEGTKEILEADLVLLAmgfLGTEKHLLDLFDVNE---------IYDDYT--TDNEHVMVAGDARRGPSLVIWGI 459
Cdd:PRK11749 361 grrRVPIEGSEFTLPADLVIKA---IGQTPNPLILSTTPGlelnrwgtiIADDETgrTSLPGVFAGGDIVTGAATVVWAV 437
|
490
....*....|....
gi 1341813615 460 REGRLAAEQVNDSL 473
Cdd:PRK11749 438 GDGKDAAEAIHEYL 451
|
|
| PRK12771 |
PRK12771 |
putative glutamate synthase (NADPH) small subunit; Provisional |
66-479 |
2.12e-84 |
|
putative glutamate synthase (NADPH) small subunit; Provisional
Pssm-ID: 237198 [Multi-domain] Cd Length: 564 Bit Score: 270.59 E-value: 2.12e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 66 VSGCPNDNLIPEWNDLVFQGRYKEAFERLAKTNPLPEMTGRVCPAPCEDGCTEALNGQGVTIHDNERFIIDTAFENNWvk 145
Cdd:PRK12771 50 NAACPAGEDIRGWLALVRGGDYEYAWRRLTKDNPFPAVMGRVCYHPCESGCNRGQVDDAVGINAVERFLGDYAIANGW-- 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 146 ASGTPQRQTDFKIAVVGSGPAGLSAAWRLNQLGHHVTVFEREDRFGGLLMYGIPSMKLDKAIVQRRVDLMEELGVTFIAN 225
Cdd:PRK12771 128 KFPAPAPDTGKRVAVIGGGPAGLSAAYHLRRMGHAVTIFEAGPKLGGMMRYGIPAYRLPREVLDAEIQRILDLGVEVRLG 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 226 TEVSSDVMAKQLQKDFDRVILTTGAGVPRDLSIPGRQLTGIRFAVDYLTEVTKDvlkyGKKTTsrkleGKHVVVIGGGDT 305
Cdd:PRK12771 208 VRVGEDITLEQLEGEFDAVFVAIGAQLGKRLPIPGEDAAGVLDAVDFLRAVGEG----EPPFL-----GKRVVVIGGGNT 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 306 GNDCIGSAIRQGAASVKQleitaeppVYRSKKNpwpeypitrHLGYGQEEAyaiykEELTA------YQTTITAFVGAQR 379
Cdd:PRK12771 279 AMDAARTARRLGAEEVTI--------VYRRTRE---------DMPAHDEEI-----EEALRegveinWLRTPVEIEGDEN 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 380 GQ----LIAVETMKVDEA--FQPVEGTKEILEADLVLLAMGfLGTEKHLLDLFDVNEI------YDDYT--TDNEHVMVA 445
Cdd:PRK12771 337 GAtglrVITVEKMELDEDgrPSPVTGEEETLEADLVVLAIG-QDIDSAGLESVPGVEVgrgvvqVDPNFmmTGRPGVFAG 415
|
410 420 430
....*....|....*....|....*....|....
gi 1341813615 446 GDARRGPSLVIWGIREGRLAAEQVNDSLLALSYH 479
Cdd:PRK12771 416 GDMVPGPRTVTTAIGHGKKAARNIDAFLGGEPYE 449
|
|
| PRK12831 |
PRK12831 |
putative oxidoreductase; Provisional |
11-473 |
2.16e-71 |
|
putative oxidoreductase; Provisional
Pssm-ID: 183780 [Multi-domain] Cd Length: 464 Bit Score: 233.76 E-value: 2.16e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 11 PKKENPLRE--IKERIYDWHELQIPLSEEERRKQAARCMVCGIPFChtgsffggqraVSGCPNDNLIPEWNDLVFQGRYK 88
Cdd:PRK12831 5 RKKRVPVREqdPEVRATNFEEVCLGYNEEEAVKEASRCLQCKKPKC-----------VKGCPVSINIPGFISKLKEGDFE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 89 EAFERLAKTNPLPEMTGRVCP--APCEDGCTEALNGQGVTIHDNERFIIDTAFENNwVKASGTPQRQtDFKIAVVGSGPA 166
Cdd:PRK12831 74 EAAKIIAKYNALPAVCGRVCPqeSQCEGKCVLGIKGEPVAIGKLERFVADWARENG-IDLSETEEKK-GKKVAVIGSGPA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 167 GLSAAWRLNQLGHHVTVFEREDRFGGLLMYGIPSMKLDK-AIVQRRVDLMEELGVTFIANTEVSSDVMAKQLQKD--FDR 243
Cdd:PRK12831 152 GLTCAGDLAKMGYDVTIFEALHEPGGVLVYGIPEFRLPKeTVVKKEIENIKKLGVKIETNVVVGKTVTIDELLEEegFDA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 244 VILTTGAGVPRDLSIPGRQLTGIRFAVDYLTEVtkDVLK-YGKKTTSRKLEGKHVVVIGGGDTGNDCIGSAIRQGAasvk 322
Cdd:PRK12831 232 VFIGSGAGLPKFMGIPGENLNGVFSANEFLTRV--NLMKaYKPEYDTPIKVGKKVAVVGGGNVAMDAARTALRLGA---- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 323 qlEITAeppVYRSKKNPWPeypitrhlgyGQEEAYAIYKEELTAYQ--TTITAFVGAQRGQLIAV--ETMKVDEAFQ--- 395
Cdd:PRK12831 306 --EVHI---VYRRSEEELP----------ARVEEVHHAKEEGVIFDllTNPVEILGDENGWVKGMkcIKMELGEPDAsgr 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 396 ----PVEGTKEILEADLVLLAMG------FLGTEKHLldlfDVNE----IYDDYT--TDNEHVMVAGDARRGPSLVIWGI 459
Cdd:PRK12831 371 rrpvEIEGSEFVLEVDTVIMSLGtspnplISSTTKGL----KINKrgciVADEETglTSKEGVFAGGDAVTGAATVILAM 446
|
490
....*....|....
gi 1341813615 460 REGRLAAEQVNDSL 473
Cdd:PRK12831 447 GAGKKAAKAIDEYL 460
|
|
| PRK12769 |
PRK12769 |
putative oxidoreductase Fe-S binding subunit; Reviewed |
11-473 |
1.07e-67 |
|
putative oxidoreductase Fe-S binding subunit; Reviewed
Pssm-ID: 183733 [Multi-domain] Cd Length: 654 Bit Score: 228.86 E-value: 1.07e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 11 PKKENPLREIKERIYDWHELQIPLSEEERRKQAARCMVCGipfchtgsffggQRAVS--GCPNDNLIPEWNDLVFQGRYK 88
Cdd:PRK12769 192 PRGEPDKLAIEARKTGFDEIYLPFRADQAQREASRCLKCG------------EHSICewTCPLHNHIPQWIELVKAGNID 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 89 EAFERLAKTNPLPEMTGRVCPAP--CEDGCTEALNGQGVTIHDNERFIIDTAFENNWvKASGTPQRQTDFKIAVVGSGPA 166
Cdd:PRK12769 260 AAVELSHQTNSLPEITGRVCPQDrlCEGACTLRDEYGAVTIGNIERYISDQALAKGW-RPDLSQVTKSDKRVAIIGAGPA 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 167 GLSAAWRLNQLGHHVTVFEREDRFGGLLMYGIPSMKLDKAIVQRRVDLMEELGVTFIANTEVSSDVMAKQLQKDFDRVIL 246
Cdd:PRK12769 339 GLACADVLARNGVAVTVYDRHPEIGGLLTFGIPAFKLDKSLLARRREIFSAMGIEFELNCEVGKDISLESLLEDYDAVFV 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 247 ttGAGVPRDL--SIPGRQLTGIRFAVDYLTEVTKDVLKYGKKTTSR--KLEGKHVVVIGGGDTGNDCIGSAIRQGAASVK 322
Cdd:PRK12769 419 --GVGTYRSMkaGLPNEDAPGVYDALPFLIANTKQVMGLEELPEEPfiNTAGLNVVVLGGGDTAMDCVRTALRHGASNVT 496
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 323 QLEITAEPPVYRSKKnpwpEYPITRHLGYGQEEAYAIYKEEL-TAYQTTITAFVGAQRGQLIAVETMKVdeafQPVEGTK 401
Cdd:PRK12769 497 CAYRRDEANMPGSKK----EVKNAREEGANFEFNVQPVALELnEQGHVCGIRFLRTRLGEPDAQGRRRP----VPIPGSE 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 402 EILEADLVLLAMGF-----LGTEKHLLDLFDVNEIYDD------YTTDNEHVMVAGDARRGPSLVIWGIREGRLAAEQVN 470
Cdd:PRK12769 569 FVMPADAVIMAFGFnphgmPWLESHGVTVDKWGRIIADvesqyrYQTSNPKIFAGGDAVRGADLVVTAMAEGRHAAQGII 648
|
...
gi 1341813615 471 DSL 473
Cdd:PRK12769 649 DWL 651
|
|
| gltA |
TIGR01316 |
glutamate synthase (NADPH), homotetrameric; This protein is homologous to the small subunit of ... |
21-473 |
1.94e-62 |
|
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: 209.73 E-value: 1.94e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 21 KERIYDWHELQIPLSEEERRKQAARCMVCGIPFchtgsffggQRAVSGCPNDNLIPEWNDLVFQGRYKEAFERLAKTNPL 100
Cdd:TIGR01316 3 EERSKLFQEAALGYTEQLALVEAQRCLNCKDAT---------KPCIKGCPVHVPIPEFIAKIQEGDFKGAVDIIKTTSLL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 101 PEMTGRVCPAP--CEDGCTEALN----GQGVTIHDNERFIIDtafennWVKASGTPQRQ-----TDFKIAVVGSGPAGLS 169
Cdd:TIGR01316 74 PAICGRVCPQErqCEGQCTVGKMfkdvGKPVSIGALERFVAD------WERQHGIETEPekapsTHKKVAVIGAGPAGLA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 170 AAWRLNQLGHHVTVFEREDRFGGLLMYGIPSMKLDKAIVQRRVDLMEELGVTFIANTEVSSDVMAKQLQKDFDRVILTTG 249
Cdd:TIGR01316 148 CASELAKAGHSVTVFEALHKPGGVVTYGIPEFRLPKEIVVTEIKTLKKLGVTFRMNFLVGKTATLEELFSQYDAVFIGTG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 250 AGVPRDLSIPGRQLTGIRFAVDYLTEVT-KDVLKYGKKTTSRKLeGKHVVVIGGGDTGNDCIGSAIRQGAasvkqlEITA 328
Cdd:TIGR01316 228 AGLPKLMNIPGEELCGVYSANDFLTRANlMKAYEFPHADTPVYA-GKSVVVIGGGNTAVDSARTALRLGA------EVHC 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 329 eppVYRSkknpwpeypiTRHLGYGQEEAYAIYKEELTAYQ--TTITAFVGAQRGQLIAVETMKVD---------EAFQPV 397
Cdd:TIGR01316 301 ---LYRR----------TREDMTARVEEIAHAEEEGVKFHflCQPVEIIGDEEGNVRAVKFRKMDcqeqidsgeRRFLPC 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 398 EGTKEILEADLVLLAMGF----LGTEKHLLDL-----FDVNEiydDYTTDNEHVMVAGDARRGPSLVIWGIREGRLAAEQ 468
Cdd:TIGR01316 368 GDAECKLEADAVIVAIGNgsnpIMAETTRLKTsergtIVVDE---DQRTSIPGVFAGGDIILGAATVIRAMGQGKRAAKS 444
|
....*
gi 1341813615 469 VNDSL 473
Cdd:TIGR01316 445 INEYL 449
|
|
| PRK12814 |
PRK12814 |
putative NADPH-dependent glutamate synthase small subunit; Provisional |
69-470 |
1.38e-59 |
|
putative NADPH-dependent glutamate synthase small subunit; Provisional
Pssm-ID: 139246 [Multi-domain] Cd Length: 652 Bit Score: 206.89 E-value: 1.38e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 69 CPNDNLIPEWNDLVFQGRYKEAFERLAKTNPLPEMTGRVCPAPCEDGCTEALNGQGVTI---------HDN---ERFIID 136
Cdd:PRK12814 108 CPAGCNIPGFIAAIARGDDREAIRIIKETIPLPGILGRICPAPCEEACRRHGVDEPVSIcalkryaadRDMesaERYIPE 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 137 TAfennwvKASGTpqrqtdfKIAVVGSGPAGLSAAWRLNQLGHHVTVFEREDRFGGLLMYGIPSMKLDKAIVQRRVDLME 216
Cdd:PRK12814 188 RA------PKSGK-------KVAIIGAGPAGLTAAYYLLRKGHDVTIFDANEQAGGMMRYGIPRFRLPESVIDADIAPLR 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 217 ELGVTFIANTEVSSDVMAKQLQKDFDRVILTTGAGVPRDLSIPGRQLTGIRFAVDYLTEVTKdvlkyGKKTTSrkleGKH 296
Cdd:PRK12814 255 AMGAEFRFNTVFGRDITLEELQKEFDAVLLAVGAQKASKMGIPGEELPGVISGIDFLRNVAL-----GTALHP----GKK 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 297 VVVIGGGDTGNDCIGSAIRQGAASVKQLeitaeppvYRSKKNpwpEYPITRHlgyGQEEAYA--IYKEELTAyQTTITAF 374
Cdd:PRK12814 326 VVVIGGGNTAIDAARTALRLGAESVTIL--------YRRTRE---EMPANRA---EIEEALAegVSLRELAA-PVSIERS 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 375 VGAQRGQLIAVETMKVDEAFQ----PVEGTKEILEADLVLLAMG-----------FLGTEKHLldLFDVNEiyDDYTTDN 439
Cdd:PRK12814 391 EGGLELTAIKMQQGEPDESGRrrpvPVEGSEFTLQADTVISAIGqqvdppiaeaaGIGTSRNG--TVKVDP--ETLQTSV 466
|
410 420 430
....*....|....*....|....*....|.
gi 1341813615 440 EHVMVAGDARRGPSLVIWGIREGRLAAEQVN 470
Cdd:PRK12814 467 AGVFAGGDCVTGADIAINAVEQGKRAAHAID 497
|
|
| PRK12809 |
PRK12809 |
putative oxidoreductase Fe-S binding subunit; Reviewed |
21-469 |
1.21e-58 |
|
putative oxidoreductase Fe-S binding subunit; Reviewed
Pssm-ID: 183762 [Multi-domain] Cd Length: 639 Bit Score: 204.10 E-value: 1.21e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 21 KERIYDWHELQIPLSEEERRKQAARCMVCGipfchtgsffggQRAVSG--CPNDNLIPEWNDLVFQGRYKEAFERLAKTN 98
Cdd:PRK12809 185 SERKTHFGEIYCGLDPQQATYESDRCVYCA------------EKANCNwhCPLHNAIPDYIRLVQEGKIIEAAELCHQTS 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 99 PLPEMTGRVCPAP--CEDGCTEALNGQGVTIHDNERFIIDTAFENNWVKASG--TPQRQtdfKIAVVGSGPAGLSAAWRL 174
Cdd:PRK12809 253 SLPEICGRVCPQDrlCEGACTLKDHSGAVSIGNLERYITDTALAMGWRPDVSkvVPRSE---KVAVIGAGPAGLGCADIL 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 175 NQLGHHVTVFEREDRFGGLLMYGIPSMKLDKAIVQRRVDLMEELGVTFIANTEVSSDVMAKQLQKDFDRVILTTGAGVPR 254
Cdd:PRK12809 330 ARAGVQVDVFDRHPEIGGMLTFGIPPFKLDKTVLSQRREIFTAMGIDFHLNCEIGRDITFSDLTSEYDAVFIGVGTYGMM 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 255 DLSIPGRQLTGIRFAVDYLTEVTKDV--LKYGKKTTSRKLEGKHVVVIGGGDTGNDCIGSAIRQGAASVKqleitaepPV 332
Cdd:PRK12809 410 RADLPHEDAPGVIQALPFLTAHTRQLmgLPESEEYPLTDVEGKRVVVLGGGDTTMDCLRTSIRLNAASVT--------CA 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 333 YRSKKNPWPeypitrhlgyGQEEAYAIYKEELTAYQTTI--TAFVGAQRGQLIAVETMKVDEAF---------QPVEGTK 401
Cdd:PRK12809 482 YRRDEVSMP----------GSRKEVVNAREEGVEFQFNVqpQYIACDEDGRLTAVGLIRTAMGEpgpdgrrrpRPVAGSE 551
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1341813615 402 EILEADLVLLAMGF----------LGTEKHLLDLFDVNEI-YDDYTTDNEHVMVAGDARRGPSLVIWGIREGRLAAEQV 469
Cdd:PRK12809 552 FELPADVLIMAFGFqahampwlqgSGIKLDKWGLIQTGDVgYLPTQTHLKKVFAGGDAVHGADLVVTAMAAGRQAARDM 630
|
|
| PRK12778 |
PRK12778 |
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ... |
11-475 |
4.30e-58 |
|
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;
Pssm-ID: 237200 [Multi-domain] Cd Length: 752 Bit Score: 204.59 E-value: 4.30e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 11 PKKENPLREIKERIYD-WHELQIPLSEEERRKQAARCMVCGIPFChtgsffggqraVSGCPNDNLIPEWNDLVFQGRYKE 89
Cdd:PRK12778 295 ERVPMPELDPEYRAHNrFEEVNLGLTKEQAMTEAKRCLDCKNPGC-----------VEGCPVGIDIPRFIKNIERGNFLE 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 90 AFERLAKTNPLPEMTGRVCP--APCEDGCTEA-LNGQGVTIHDNERFIIDTAFENNWVKASGTPQRqTDFKIAVVGSGPA 166
Cdd:PRK12778 364 AAKILKETSALPAVCGRVCPqeKQCESKCIHGkMGEEAVAIGYLERFVADYERESGNISVPEVAEK-NGKKVAVIGSGPA 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 167 GLSAAWRLNQLGHHVTVFEREDRFGGLLMYGIPSMKLDKAIVQRRVDLMEELGVTFIANTEVSSDVMAKQLQK-DFDRVI 245
Cdd:PRK12778 443 GLSFAGDLAKRGYDVTVFEALHEIGGVLKYGIPEFRLPKKIVDVEIENLKKLGVKFETDVIVGKTITIEELEEeGFKGIF 522
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 246 LTTGAGVPRDLSIPGRQLTGIRFAVDYLTEVtkDVLK-YGKKTTSRKLEGKHVVVIGGGDTGNDCIGSAIRQGAASVKQl 324
Cdd:PRK12778 523 IASGAGLPNFMNIPGENSNGVMSSNEYLTRV--NLMDaASPDSDTPIKFGKKVAVVGGGNTAMDSARTAKRLGAERVTI- 599
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 325 eitaeppVYRSKKNPWPeypitrhlgyGQEEAYAIYKEELTAYQTTIT--AFVGAQRGQLIAV--ETMKVDEAFQ----- 395
Cdd:PRK12778 600 -------VYRRSEEEMP----------ARLEEVKHAKEEGIEFLTLHNpiEYLADEKGWVKQVvlQKMELGEPDAsgrrr 662
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 396 --PVEGTKEILEADLVLLAMG------FLGTEKHL-LDLFDVNEIYDDYTTDNEHVMVAGDARRGPSLVIWGIREGRLAA 466
Cdd:PRK12778 663 pvAIPGSTFTVDVDLVIVSVGvspnplVPSSIPGLeLNRKGTIVVDEEMQSSIPGIYAGGDIVRGGATVILAMGDGKRAA 742
|
....*....
gi 1341813615 467 EQVNDSLLA 475
Cdd:PRK12778 743 AAIDEYLSS 751
|
|
| PRK13984 |
PRK13984 |
putative oxidoreductase; Provisional |
8-473 |
4.24e-53 |
|
putative oxidoreductase; Provisional
Pssm-ID: 172486 [Multi-domain] Cd Length: 604 Bit Score: 188.44 E-value: 4.24e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 8 LEYPKKENPLREIKERIYDWHELQIPLSEEERRKQAARCMVCGIpfChtgsffggqraVSGCPNDNLIPEWNDLVFQGRY 87
Cdd:PRK13984 149 LDLERVEMEEIPPEERVKSFIEIVKGYSKEQAMQEAARCVECGI--C-----------TDTCPAHMDIPQYIKAIYKDDL 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 88 KEAFERLAKTNPLPEMTGRVCPAPCEDGCTEALNGQGVTIHDNERFIIDTAFENNWVKASGTPQRQTDFKIAVVGSGPAG 167
Cdd:PRK13984 216 EEGLRWLYKTNPLSMVCGRVCTHKCETVCSIGHRGEPIAIRWLKRYIVDNVPVEKYSEILDDEPEKKNKKVAIVGSGPAG 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 168 LSAAWRLNQLGHHVTVFEREDRFGGLLMYGIPSMKLDKAIVQRRVDLMEELGVTFIANTEVSSDVMAKQLQKDFDRVILT 247
Cdd:PRK13984 296 LSAAYFLATMGYEVTVYESLSKPGGVMRYGIPSYRLPDEALDKDIAFIEALGVKIHLNTRVGKDIPLEELREKHDAVFLS 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 248 TGAGVPRDLSIPGRQLTGIRFAVDYLTEVTKDVLKYGKKTTSrkleGKHVVVIGGGDTGNDCIGSAIRQGAASVKQLEIT 327
Cdd:PRK13984 376 TGFTLGRSTRIPGTDHPDVIQALPLLREIRDYLRGEGPKPKI----PRSLVVIGGGNVAMDIARSMARLQKMEYGEVNVK 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 328 AEppvyrSKKNPWPEYPI-TRHLGYGQEEAYAIYKEEltayqttitafvGAQR-----GQLIAVETMKVDEA------FQ 395
Cdd:PRK13984 452 VT-----SLERTFEEMPAdMEEIEEGLEEGVVIYPGW------------GPMEvvienDKVKGVKFKKCVEVfdeegrFN 514
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 396 PV--EGTKEILEADLVLLAMG------FLGTE-KHLLDLFDVNEIYDDY-TTDNEHVMVAGDARRGPSlVIWGIREGRLA 465
Cdd:PRK13984 515 PKfdESDQIIVEADMVVEAIGqapdysYLPEElKSKLEFVRGRILTNEYgQTSIPWLFAGGDIVHGPD-IIHGVADGYWA 593
|
....*...
gi 1341813615 466 AEQVNDSL 473
Cdd:PRK13984 594 AEGIDMYL 601
|
|
| PRK12770 |
PRK12770 |
putative glutamate synthase subunit beta; Provisional |
148-475 |
1.53e-46 |
|
putative glutamate synthase subunit beta; Provisional
Pssm-ID: 237197 [Multi-domain] Cd Length: 352 Bit Score: 164.78 E-value: 1.53e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 148 GTPQRQTDFKIAVVGSGPAGLSAAWRLNQLGHHVTVFEREDRFGGLLMYGIPSMKLDKAIVQRRVDLMEELGVTFIANTE 227
Cdd:PRK12770 11 KEKPPPTGKKVAIIGAGPAGLAAAGYLACLGYEVHVYDKLPEPGGLMLFGIPEFRIPIERVREGVKELEEAGVVFHTRTK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 228 V---------SSDVMAKQ------LQKDFDRVILTTGAGVPRDLSIPGRQLTGIRFAVDYLTEVTKDVLKYGKKTTSRKL 292
Cdd:PRK12770 91 VccgeplheeEGDEFVERivsleeLVKKYDAVLIATGTWKSRKLGIPGEDLPGVYSALEYLFRIRAAKLGYLPWEKVPPV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 293 EGKHVVVIGGGDTGNDCIGSAIRQGAASVKQleitaeppVYRSKKNpwpeypitrhlgygqeEAYAIYKE---------- 362
Cdd:PRK12770 171 EGKKVVVVGAGLTAVDAALEAVLLGAEKVYL--------AYRRTIN----------------EAPAGKYEierliargve 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 363 --ELtayqTTITAFVGAQRGQLIAVETMKVDEAFQ-------PVEGTKEILEADLVLLAMGFLGT-----EKHLLDLFDV 428
Cdd:PRK12770 227 flEL----VTPVRIIGEGRVEGVELAKMRLGEPDEsgrprpvPIPGSEFVLEADTVVFAIGEIPTppfakECLGIELNRK 302
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1341813615 429 NEIYDD--YTTDNEHVMVAGDARRGPSLVIWGIREGRLAAEQVNDSLLA 475
Cdd:PRK12770 303 GEIVVDekHMTSREGVFAAGDVVTGPSKIGKAIKSGLRAAQSIHEWLDL 351
|
|
| PRK12775 |
PRK12775 |
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin ... |
16-469 |
2.25e-46 |
|
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin domain-containing protein; Provisional
Pssm-ID: 183738 [Multi-domain] Cd Length: 1006 Bit Score: 172.82 E-value: 2.25e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 16 PLREIKERIYDWHELQIPLSEEERRKQAARCMVCGIPFChtgsffggqraVSGCPNDNLIPEWNDLVFQGRYKEAFERLA 95
Cdd:PRK12775 303 PERDAVERARNFKEVNLGYSLEDALQEAERCIQCAKPTC-----------IAGCPVQIDIPVFIRHVVVRDFDGALEVIY 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 96 KTNPLPEMTGRVCP--APCEDGCTEALNGQGVTIHDNERFIIDTAfennwvkaSGTPQRQTDF-----KIAVVGSGPAGL 168
Cdd:PRK12775 372 EASIFPSICGRVCPqeTQCEAQCIIAKKHESVGIGRLERFVGDNA--------RAKPVKPPRFskklgKVAICGSGPAGL 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 169 SAAWRLNQLGHHVTVFEREDRFGGLLMYGIPSMKLDKAIVQRRVDLMEELGVTFIANTEVSSDVMAKQLQKD--FDRVIL 246
Cdd:PRK12775 444 AAAADLVKYGVDVTVYEALHVVGGVLQYGIPSFRLPRDIIDREVQRLVDIGVKIETNKVIGKTFTVPQLMNDkgFDAVFL 523
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 247 TTGAGVPRDLSIPGRQLTGIRFAVDYLTEVT---KDVLKYGKKTTSRkleGKHVVVIGGGDTGNDCIGSAIRQGAASVKq 323
Cdd:PRK12775 524 GVGAGAPTFLGIPGEFAGQVYSANEFLTRVNlmgGDKFPFLDTPISL---GKSVVVIGAGNTAMDCLRVAKRLGAPTVR- 599
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 324 leitaepPVYRSKKNPWPEYpiTRHLGYGQEEAYAIYKeeLTAYQTTITAFVGAQRGqlIAVETMKVDEA-----FQPVE 398
Cdd:PRK12775 600 -------CVYRRSEAEAPAR--IEEIRHAKEEGIDFFF--LHSPVEIYVDAEGSVRG--MKVEEMELGEPdekgrRKPMP 666
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 399 GTKEI-LEADLVLLAMGF------------LGTEKHLLDLFDVNEIYDDYTTDNEHVMVAGDARRGPSLVIWGIREGRLA 465
Cdd:PRK12775 667 TGEFKdLECDTVIYALGTkanpiitqstpgLALNKWGNIAADDGKLESTQSTNLPGVFAGGDIVTGGATVILAMGAGRRA 746
|
....
gi 1341813615 466 AEQV 469
Cdd:PRK12775 747 ARSI 750
|
|
| PRK12779 |
PRK12779 |
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; ... |
6-473 |
2.05e-45 |
|
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; Provisional
Pssm-ID: 183740 [Multi-domain] Cd Length: 944 Bit Score: 170.01 E-value: 2.05e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 6 GFLEYPKKENPLREIKerIYDWHELQiplseeeRRKQaarcmvCGIPFCHTGSFFGGQR-AVSGCPNDNLIPEWNDLVFQ 84
Cdd:PRK12779 165 GYLGYQSLGYSVREVE--LFVWLEVM-------RDKQ------CDDKPCELGVLVQGKAePKGGCPVKIHIPEMLDLLGN 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 85 GRYKEAFERLAKTNPLPEMTGRVCPapcedgctEALNGQGVTIHdNERFI-------------------IDTAFE---NN 142
Cdd:PRK12779 230 GKHREALELIESCNPLPNVTGRVCP--------QELQCQGVCTH-TKRPIeigqlewylpqheklvnpnANERFAgriSP 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 143 WVKASGTPqrqtdfkIAVVGSGPAGLSAAWRLNQLGHHVTVFEREDRFGGLLMYGIPSMKLDKAIVQRRVDLMEELGVTF 222
Cdd:PRK12779 301 WAAAVKPP-------IAVVGSGPSGLINAYLLAVEGFPVTVFEAFHDLGGVLRYGIPEFRLPNQLIDDVVEKIKLLGGRF 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 223 IANTEVSSDVMAKQLQKD-FDRVILTTGAGVPRDLSIPGRQLTGIRFAVDYLTEVTkdvLKYGKK----TTSRKLEGKHV 297
Cdd:PRK12779 374 VKNFVVGKTATLEDLKAAgFWKIFVGTGAGLPTFMNVPGEHLLGVMSANEFLTRVN---LMRGLDddyeTPLPEVKGKEV 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 298 VVIGGGDTGNDCIGSAIRQGAasvkqlEITAeppVYRSKKNPWPEYpiTRHLGYGQEEayAIYKEELTAyqttITAFVGA 377
Cdd:PRK12779 451 FVIGGGNTAMDAARTAKRLGG------NVTI---VYRRTKSEMPAR--VEELHHALEE--GINLAVLRA----PREFIGD 513
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 378 QRGQLIAVETMKVDEAFQPVE---------GTKEILEADLVLLAMGF------------LGTEKhlLDLFDVNEiyDDYT 436
Cdd:PRK12779 514 DHTHFVTHALLDVNELGEPDKsgrrspkptGEIERVPVDLVIMALGNtanpimkdaepgLKTNK--WGTIEVEK--GSQR 589
|
490 500 510
....*....|....*....|....*....|....*..
gi 1341813615 437 TDNEHVMVAGDARRGPSLVIWGIREGRLAAEQVNDSL 473
Cdd:PRK12779 590 TSIKGVYSGGDAARGGSTAIRAAGDGQAAAKEIVGEI 626
|
|
| Fer4_20 |
pfam14691 |
Dihydroprymidine dehydrogenase domain II, 4Fe-4S cluster; Domain II of the enzyme ... |
23-143 |
2.09e-28 |
|
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: 108.40 E-value: 2.09e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 23 RIYDWHELQIPLSEEERRKQAARCMVCGIPFChtgsffggqraVSGCPNDNLIPEWNDLVFQGRYKEAFERLAKTNPLPE 102
Cdd:pfam14691 1 RIKNFEEVALGYTEEEAIAEASRCLQCKDPPC-----------VKGCPVHIDIPEFIKLIAEGNFEGAARIILETNPLPA 69
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1341813615 103 MTGRVCPA--PCEDGCTeaLNGQG---VTIHDNERFIIDTAFENNW 143
Cdd:pfam14691 70 ICGRVCPQerQCEGACV--LGKKGfepVAIGRLERFAADWARENGI 113
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
156-462 |
7.61e-23 |
|
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: 98.54 E-value: 7.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 156 FKIAVVGSGPAGLSAAWRLNQLGHHVTVFEREDR---FGGLLMYGIPSMKLDKAIVQRRVDLMEEL---------GVTFI 223
Cdd:pfam07992 1 YDVVVIGGGPAGLAAALTLAQLGGKVTLIEDEGTcpyGGCVLSKALLGAAEAPEIASLWADLYKRKeevvkklnnGIEVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 224 ANTEVSS-DVMAKQLQK-----------DFDRVILTTGAGvPRDLSIPGRQLTGIrFAVDYLTEVtkDVLKYGKKttsrk 291
Cdd:pfam07992 81 LGTEVVSiDPGAKKVVLeelvdgdgetiTYDRLVIATGAR-PRLPPIPGVELNVG-FLVRTLDSA--EALRLKLL----- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 292 leGKHVVVIGGGDTGNDCIGSAIRQGAasvkqlEITaepPVYRSKKnpwpeypITRHLGygqEEAYAIYKEELTAY---- 367
Cdd:pfam07992 152 --PKRVVVVGGGYIGVELAAALAKLGK------EVT---LIEALDR-------LLRAFD---EEISAALEKALEKNgvev 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 368 --QTTITAFVGaqRGQLIAVETmkvdeafqpveGTKEILEADLVLLAMGF----LGTEKHLLDLFDVNEIY-DDYT-TDN 439
Cdd:pfam07992 211 rlGTSVKEIIG--DGDGVEVIL-----------KDGTEIDADLVVVAIGRrpntELLEAAGLELDERGGIVvDEYLrTSV 277
|
330 340
....*....|....*....|....
gi 1341813615 440 EHVMVAGDAR-RGPSLVIWGIREG 462
Cdd:pfam07992 278 PGIYAAGDCRvGGPELAQNAVAQG 301
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
156-466 |
3.88e-13 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 69.76 E-value: 3.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 156 FKIAVVGSGPAGLSAAWRLNQLGHHVTVFEReDRFGGLLM--------YGIPSMKLDKAIVQRRVDLMEELGVTFIaNTE 227
Cdd:COG0492 1 YDVVIIGAGPAGLTAAIYAARAGLKTLVIEG-GEPGGQLAttkeienyPGFPEGISGPELAERLREQAERFGAEIL-LEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 228 VSSdvmAKQLQKDF------------DRVILTTGAGvPRDLSIPGRQL---TGIRFAvdylteVTKDVLKYgkkttsrkl 292
Cdd:COG0492 79 VTS---VDKDDGPFrvttddgteyeaKAVIIATGAG-PRKLGLPGEEEfegRGVSYC------ATCDGFFF--------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 293 EGKHVVVIGGGDTGndcIGSAI--RQGAASVkqleitaeppvyrskknpwpeYPITRhlgYGQEEAYAIYKEELTA---- 366
Cdd:COG0492 140 RGKDVVVVGGGDSA---LEEALylTKFASKV---------------------TLIHR---RDELRASKILVERLRAnpki 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 367 ---YQTTITAFVGAQRgqliaVETMKVDeafQPVEGTKEILEADLVLLAMGFLGT----EKHLLDLFDVNEIY--DDYTT 437
Cdd:COG0492 193 evlWNTEVTEIEGDGR-----VEGVTLK---NVKTGEEKELEVDGVFVAIGLKPNtellKGLGLELDEDGYIVvdEDMET 264
|
330 340 350
....*....|....*....|....*....|
gi 1341813615 438 DNEHVMVAGDARRGPS-LVIWGIREGRLAA 466
Cdd:COG0492 265 SVPGVFAAGDVRDYKYrQAATAAGEGAIAA 294
|
|
| HemY |
COG1232 |
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ... |
157-194 |
3.90e-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: 71.02 E-value: 3.90e-13
10 20 30
....*....|....*....|....*....|....*...
gi 1341813615 157 KIAVVGSGPAGLSAAWRLNQLGHHVTVFEREDRFGGLL 194
Cdd:COG1232 3 RVAVIGGGIAGLTAAYRLAKAGHEVTVLEASDRVGGLI 40
|
|
| PLN02852 |
PLN02852 |
ferredoxin-NADP+ reductase |
146-309 |
1.79e-12 |
|
ferredoxin-NADP+ reductase
Pssm-ID: 215457 Cd Length: 491 Bit Score: 69.34 E-value: 1.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 146 ASGTPQRQTDFKIAVVGSGPAGLSAAWRLnqLGHH----VTVFEREDRFGGLLMYGI----PSMKldkaIVQRRVD-LME 216
Cdd:PLN02852 17 SNSSSSTSEPLHVCVVGSGPAGFYTADKL--LKAHdgarVDIIERLPTPFGLVRSGVapdhPETK----NVTNQFSrVAT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 217 ELGVTFIANTEVSSDVMAKQLQKDFDRVILTTGAGVPRDLSIPGRQLTGIRFAVDYltevtkdVLKY-----GKKTTSRK 291
Cdd:PLN02852 91 DDRVSFFGNVTLGRDVSLSELRDLYHVVVLAYGAESDRRLGIPGEDLPGVLSAREF-------VWWYnghpdCVHLPPDL 163
|
170
....*....|....*...
gi 1341813615 292 LEGKHVVVIGGGDTGNDC 309
Cdd:PLN02852 164 KSSDTAVVLGQGNVALDC 181
|
|
| PRK07233 |
PRK07233 |
hypothetical protein; Provisional |
157-219 |
2.47e-12 |
|
hypothetical protein; Provisional
Pssm-ID: 235977 [Multi-domain] Cd Length: 434 Bit Score: 68.37 E-value: 2.47e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1341813615 157 KIAVVGSGPAGLSAAWRLNQLGHHVTVFEREDRFGGLL-MYGIPSMKL----------DKAIvqrrVDLMEELG 219
Cdd:PRK07233 1 KIAIVGGGIAGLAAAYRLAKRGHEVTVFEADDQLGGLAaSFEFGGLPIerfyhhifksDEAL----LELLDELG 70
|
|
| Ppro0129 |
COG2907 |
Predicted flavin-containing amine oxidase [General function prediction only]; |
157-192 |
3.89e-12 |
|
Predicted flavin-containing amine oxidase [General function prediction only];
Pssm-ID: 442151 [Multi-domain] Cd Length: 423 Bit Score: 67.83 E-value: 3.89e-12
10 20 30
....*....|....*....|....*....|....*.
gi 1341813615 157 KIAVVGSGPAGLSAAWRLNQLgHHVTVFEREDRFGG 192
Cdd:COG2907 5 RIAVIGSGISGLTAAWLLSRR-HDVTLFEANDRLGG 39
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
157-414 |
1.36e-11 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 65.93 E-value: 1.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 157 KIAVVGSGPAGLSAAWRLNQLGHH--VTVFERE-----DRFggLLMYGIPSMKLDKAIVQRRVDLMEELGVTFIANTEVS 229
Cdd:COG1251 3 RIVIIGAGMAGVRAAEELRKLDPDgeITVIGAEphppyNRP--PLSKVLAGETDEEDLLLRPADFYEENGIDLRLGTRVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 230 S-DVMAKQLQKD------FDRVILTTGAgVPRDLSIPGRQLTGIrFA------VDYLTEVTKdvlkygkkttsrklEGKH 296
Cdd:COG1251 81 AiDRAARTVTLAdgetlpYDKLVLATGS-RPRVPPIPGADLPGV-FTlrtlddADALRAALA--------------PGKR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 297 VVVIGGGdtgndCIG----SAIRQGAASVKQLEITaeppvyrskknpwpEYPITRHLGygqEEAYAIYKEELTA------ 366
Cdd:COG1251 145 VVVIGGG-----LIGleaaAALRKRGLEVTVVERA--------------PRLLPRQLD---EEAGALLQRLLEAlgvevr 202
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1341813615 367 YQTTITAFVGAQRgqliaVETMKVDeafqpvegTKEILEADLVLLAMG 414
Cdd:COG1251 203 LGTGVTEIEGDDR-----VTGVRLA--------DGEELPADLVVVAIG 237
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
154-469 |
2.64e-11 |
|
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: 65.49 E-value: 2.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 154 TDFKIAVVGSGPAGLSAAWRLNQLGHHVTVFEReDRFGGL-LMYG-IPS-------------------------MKLD-K 205
Cdd:COG1249 2 KDYDLVVIGAGPGGYVAAIRAAQLGLKVALVEK-GRLGGTcLNVGcIPSkallhaaevahearhaaefgisagaPSVDwA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 206 AIVQRR-----------VDLMEELGVTFI--------ANT-EVSSDvmaKQLQkdFDRVILTTGAgVPRDLSIPGrqLTG 265
Cdd:COG1249 81 ALMARKdkvvdrlrggvEELLKKNGVDVIrgrarfvdPHTvEVTGG---ETLT--ADHIVIATGS-RPRVPPIPG--LDE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 266 IRfavdYLTevTKDVLkygkkttsrKLE--GKHVVVIGGGDTGndC-IGSAIRQ-GAasvkqlEITAeppVYRSKknpwp 341
Cdd:COG1249 153 VR----VLT--SDEAL---------ELEelPKSLVVIGGGYIG--LeFAQIFARlGS------EVTL---VERGD----- 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 342 eypitrHLGYGQEEAYAiykEELTAY----------QTTITAFVGAQRGQLIAVETmkvdeafqpvEGTKEILEADLVLL 411
Cdd:COG1249 202 ------RLLPGEDPEIS---EALEKAlekegidiltGAKVTSVEKTGDGVTVTLED----------GGGEEAVEADKVLV 262
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1341813615 412 AMGF------LGTEKHLLDLFDVNEIY-DDY-TTDNEHVMVAGDARRGPSLVIWGIREGRLAAEQV 469
Cdd:COG1249 263 ATGRrpntdgLGLEAAGVELDERGGIKvDEYlRTSVPGIYAIGDVTGGPQLAHVASAEGRVAAENI 328
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
157-228 |
1.90e-10 |
|
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: 56.83 E-value: 1.90e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1341813615 157 KIAVVGSGPAGLSAAWRLNQLGHHVTVFEREDRFGGllmygipsmKLDKAIVQRRVDLMEELGVTFIANTEV 228
Cdd:pfam00070 1 RVVVVGGGYIGLELAGALARLGSKVTVVERRDRLLP---------GFDPEIAKILQEKLEKNGIEFLLNTTV 63
|
|
| NAD_binding_8 |
pfam13450 |
NAD(P)-binding Rossmann-like domain; |
160-192 |
2.64e-10 |
|
NAD(P)-binding Rossmann-like domain;
Pssm-ID: 433218 [Multi-domain] Cd Length: 67 Bit Score: 56.00 E-value: 2.64e-10
10 20 30
....*....|....*....|....*....|...
gi 1341813615 160 VVGSGPAGLSAAWRLNQLGHHVTVFEREDRFGG 192
Cdd:pfam13450 1 IVGAGLAGLVAAALLAKRGFRVLVLEKRDRLGG 33
|
|
| CzcO |
COG2072 |
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ... |
150-321 |
6.08e-10 |
|
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: 61.03 E-value: 6.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 150 PQRQTDFKIAVVGSGPAGLSAAWRLNQLGHHVTVFEREDRFGG---------------LLMYGIPSMKLDKA-------- 206
Cdd:COG2072 1 TAATEHVDVVVIGAGQAGLAAAYHLRRAGIDFVVLEKADDVGGtwrdnrypglrldtpSHLYSLPFFPNWSDdpdfptgd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 207 -IVQ------RRVDLMEElgVTFiaNTEVSS----------DV-MAKQLQKDFDRVILTTGA-GVPRDLSIPGRQltgiR 267
Cdd:COG2072 81 eILAyleayaDKFGLRRP--IRF--GTEVTSarwdeadgrwTVtTDDGETLTARFVVVATGPlSRPKIPDIPGLE----D 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1341813615 268 FAVDYLtevtkdvlkygkkTTSR-----KLEGKHVVVIGGGDTGNDCIgSAIRQGAASV 321
Cdd:COG2072 153 FAGEQL-------------HSADwrnpvDLAGKRVLVVGTGASAVQIA-PELARVAAHV 197
|
|
| PRK07208 |
PRK07208 |
hypothetical protein; Provisional |
157-193 |
7.37e-10 |
|
hypothetical protein; Provisional
Pssm-ID: 235967 [Multi-domain] Cd Length: 479 Bit Score: 61.06 E-value: 7.37e-10
10 20 30
....*....|....*....|....*....|....*..
gi 1341813615 157 KIAVVGSGPAGLSAAWRLNQLGHHVTVFEREDRFGGL 193
Cdd:PRK07208 6 SVVIIGAGPAGLTAAYELLKRGYPVTVLEADPVVGGI 42
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
181-467 |
9.98e-10 |
|
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: 59.82 E-value: 9.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 181 VTVFEREDRF-----GGLLMYGIPSMKLDKAIVqRRVDLMEELGVTFIANTEVSS-DVMAKQLQ-KD-----FDRVILTT 248
Cdd:COG0446 8 ITVIEKGPHHsyqpcGLPYYVGGGIKDPEDLLV-RTPESFERKGIDVRTGTEVTAiDPEAKTVTlRDgetlsYDKLVLAT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 249 GAgVPRDLSIPGRQLTGIRFAVDY-LTEVTKDVLKYGKkttsrkleGKHVVVIGGGdtgndCIG-----SAIRQGaasvk 322
Cdd:COG0446 87 GA-RPRPPPIPGLDLPGVFTLRTLdDADALREALKEFK--------GKRAVVIGGG-----PIGlelaeALRKRG----- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 323 qLEITAeppVYRSKKnPWPEYPitrhlgygqEEAYAIYKEELTAY------QTTITAFVGAQRGQLIAVEtmkvdeafqp 396
Cdd:COG0446 148 -LKVTL---VERAPR-LLGVLD---------PEMAALLEEELREHgvelrlGETVVAIDGDDKVAVTLTD---------- 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 397 vegtKEILEADLVLLAMGF---------LGTEKHLLDLFDVNEiydDYTTDNEHVMVAGDARRGPSLVI--------WG- 458
Cdd:COG0446 204 ----GEEIPADLVVVAPGVrpntelakdAGLALGERGWIKVDE---TLQTSDPDVYAAGDCAEVPHPVTgktvyiplASa 276
|
330
....*....|
gi 1341813615 459 -IREGRLAAE 467
Cdd:COG0446 277 aNKQGRVAAE 286
|
|
| YobN |
COG1231 |
Monoamine oxidase [Amino acid transport and metabolism]; |
152-192 |
2.22e-09 |
|
Monoamine oxidase [Amino acid transport and metabolism];
Pssm-ID: 440844 [Multi-domain] Cd Length: 440 Bit Score: 59.16 E-value: 2.22e-09
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1341813615 152 RQTDFKIAVVGSGPAGLSAAWRLNQLGHHVTVFEREDRFGG 192
Cdd:COG1231 4 RARGKDVVIVGAGLAGLAAARELRKAGLDVTVLEARDRVGG 44
|
|
| COG1233 |
COG1233 |
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ... |
154-192 |
1.22e-08 |
|
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440846 [Multi-domain] Cd Length: 491 Bit Score: 57.17 E-value: 1.22e-08
10 20 30
....*....|....*....|....*....|....*....
gi 1341813615 154 TDFKIAVVGSGPAGLSAAWRLNQLGHHVTVFEREDRFGG 192
Cdd:COG1233 2 MMYDVVVIGAGIGGLAAAALLARAGYRVTVLEKNDTPGG 40
|
|
| UbiH |
COG0654 |
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ... |
153-220 |
3.14e-08 |
|
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: 55.33 E-value: 3.14e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1341813615 153 QTDFKIAVVGSGPAGLSAAWRLNQLGHHVTVFEREDRFGGLLmYGIpsmkldkAIVQRRVDLMEELGV 220
Cdd:COG0654 1 MMRTDVLIVGGGPAGLALALALARAGIRVTVVERAPPPRPDG-RGI-------ALSPRSLELLRRLGL 60
|
|
| COG3380 |
COG3380 |
Predicted NAD/FAD-dependent oxidoreductase [General function prediction only]; |
156-192 |
3.57e-08 |
|
Predicted NAD/FAD-dependent oxidoreductase [General function prediction only];
Pssm-ID: 442607 [Multi-domain] Cd Length: 331 Bit Score: 54.88 E-value: 3.57e-08
10 20 30
....*....|....*....|....*....|....*..
gi 1341813615 156 FKIAVVGSGPAGLSAAWRLNQLGHHVTVFEREDRFGG 192
Cdd:COG3380 4 PDIAIIGAGIAGLAAARALQDAGHEVTVFEKSRGVGG 40
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
155-467 |
5.26e-08 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 55.18 E-value: 5.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 155 DFKIAVVGSGPAGLSAAWRLNQLGHHVTVFEREDrFGG-----------LLMY--------------GIPSMKLD---KA 206
Cdd:PRK06292 3 KYDVIVIGAGPAGYVAARRAAKLGKKVALIEKGP-LGGtclnvgcipskALIAaaeafheakhaeefGIHADGPKidfKK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 207 IVQRR---VD---------LMEELGVT-------FIANTEVssDVMAKQLQkdFDRVILTTGAGVPRdlsIPGRQLtgiR 267
Cdd:PRK06292 82 VMARVrreRDrfvggvvegLEKKPKIDkikgtarFVDPNTV--EVNGERIE--AKNIVIATGSRVPP---IPGVWL---I 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 268 FAVDYLTevTKDVLKYgkkttsRKLeGKHVVVIGGGDTGNDcIGSAIRQGAASVKQLEitaeppvyrskknpwpeypITR 347
Cdd:PRK06292 152 LGDRLLT--SDDAFEL------DKL-PKSLAVIGGGVIGLE-LGQALSRLGVKVTVFE-------------------RGD 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 348 HLGYG-----QEEAYAIYKEEL---TAYQTTITAFVGAQRgqliavetmkvdEAFQPVEGTKEILEADLVLLAMG----- 414
Cdd:PRK06292 203 RILPLedpevSKQAQKILSKEFkikLGAKVTSVEKSGDEK------------VEELEKGGKTETIEADYVLVATGrrpnt 270
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1341813615 415 -FLGTEKHLLDLFDVNEI-YDDYT-TDNEHVMVAGDARRGPSLVIWGIREGRLAAE 467
Cdd:PRK06292 271 dGLGLENTGIELDERGRPvVDEHTqTSVPGIYAAGDVNGKPPLLHEAADEGRIAAE 326
|
|
| COG3349 |
COG3349 |
Uncharacterized protein, contains NAD-binding domain and a Fe-S cluster [General function ... |
157-192 |
1.60e-07 |
|
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: 53.32 E-value: 1.60e-07
10 20 30
....*....|....*....|....*....|....*.
gi 1341813615 157 KIAVVGSGPAGLSAAWRLNQLGHHVTVFEREDRFGG 192
Cdd:COG3349 5 RVVVVGGGLAGLAAAVELAEAGFRVTLLEARPRLGG 40
|
|
| PRK11883 |
PRK11883 |
protoporphyrinogen oxidase; Reviewed |
157-194 |
1.64e-07 |
|
protoporphyrinogen oxidase; Reviewed
Pssm-ID: 237009 [Multi-domain] Cd Length: 451 Bit Score: 53.31 E-value: 1.64e-07
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1341813615 157 KIAVVGSGPAGLSAAWRLNQLG--HHVTVFEREDRFGGLL 194
Cdd:PRK11883 2 KVAIIGGGITGLSAAYRLHKKGpdADITLLEASDRLGGKI 41
|
|
| PRK12771 |
PRK12771 |
putative glutamate synthase (NADPH) small subunit; Provisional |
7-53 |
3.05e-07 |
|
putative glutamate synthase (NADPH) small subunit; Provisional
Pssm-ID: 237198 [Multi-domain] Cd Length: 564 Bit Score: 52.96 E-value: 3.05e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1341813615 7 FLEYPKKENPLREIKERIYDWHELQIPLSEEERRKQAARCMVCGIPF 53
Cdd:PRK12771 467 FTDAPRAQRPELDADERVGDFDEVLGGLTEEEARQEAARCLSCGNCF 513
|
|
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
154-303 |
3.49e-07 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 52.46 E-value: 3.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 154 TDFKIAVVGSGPAGLSAAWRLNQLGHHVTVFEREDrFGGL-LMYG-IPS-------------------------MKLDKA 206
Cdd:PRK06416 3 FEYDVIVIGAGPGGYVAAIRAAQLGLKVAIVEKEK-LGGTcLNRGcIPSkallhaaeradearhsedfgikaenVGIDFK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 207 IVQRRVD------------LMEELGVTFI--------ANT-EVSSDVMAKQLQkdFDRVILTTGAgVPRdlSIPGrqltg 265
Cdd:PRK06416 82 KVQEWKNgvvnrltggvegLLKKNKVDIIrgeaklvdPNTvRVMTEDGEQTYT--AKNIILATGS-RPR--ELPG----- 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1341813615 266 irfavdyltevtkdvLKYGKKT--TSR---KLEG--KHVVVIGGG 303
Cdd:PRK06416 152 ---------------IEIDGRViwTSDealNLDEvpKSLVVIGGG 181
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
157-249 |
4.10e-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: 51.74 E-value: 4.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 157 KIAVVGSGPAGLSAAWRLNQLGHHVTVFEREDRfgglLMygipsMKLDKAIVQRRVDLMEELGVTFIANTEVSS-----D 231
Cdd:COG0446 126 RAVVIGGGPIGLELAEALRKRGLKVTLVERAPR----LL-----GVLDPEMAALLEEELREHGVELRLGETVVAidgddK 196
|
90 100
....*....|....*....|.
gi 1341813615 232 VMAKQLQK---DFDRVILTTG 249
Cdd:COG0446 197 VAVTLTDGeeiPADLVVVAPG 217
|
|
| HdrA |
COG1148 |
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion]; |
157-230 |
5.51e-07 |
|
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
Pssm-ID: 440762 [Multi-domain] Cd Length: 563 Bit Score: 52.17 E-value: 5.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 157 KIAVVGSGPAGLSAAWRLNQLGHHVTVFEREDRFGGL---LMYGIPSMKLDKAIVQrrvDLMEEL----GVTFIANTEVS 229
Cdd:COG1148 142 RALVIGGGIAGMTAALELAEQGYEVYLVEKEPELGGRaaqLHKTFPGLDCPQCILE---PLIAEVeanpNITVYTGAEVE 218
|
.
gi 1341813615 230 S 230
Cdd:COG1148 219 E 219
|
|
| DAO |
pfam01266 |
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ... |
157-218 |
7.59e-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: 50.86 E-value: 7.59e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1341813615 157 KIAVVGSGPAGLSAAWRLNQLGHHVTVFEREDRFG--------GLLMYGIPSMKLD--KAIVQRRVDLMEEL 218
Cdd:pfam01266 1 DVVVIGGGIVGLSTAYELARRGLSVTLLERGDDPGsgasgrnaGLIHPGLRYLEPSelARLALEALDLWEEL 72
|
|
| DadA |
COG0665 |
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism]; |
154-238 |
1.15e-06 |
|
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
Pssm-ID: 440429 [Multi-domain] Cd Length: 364 Bit Score: 50.67 E-value: 1.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 154 TDFKIAVVGSGPAGLSAAWRLNQLGHHVTVFERED-------RFGGLLMYGIPSMKLDK--AIVQRRVDLMEEL------ 218
Cdd:COG0665 1 ATADVVVIGGGIAGLSTAYHLARRGLDVTVLERGRpgsgasgRNAGQLRPGLAALADRAlvRLAREALDLWRELaaelgi 80
|
90 100
....*....|....*....|....*..
gi 1341813615 219 -------GVTFIANTEVSSDVMAKQLQ 238
Cdd:COG0665 81 dcdfrrtGVLYLARTEAELAALRAEAE 107
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
157-273 |
1.59e-06 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 50.14 E-value: 1.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 157 KIAVVGSGPAGLSAAWRLNQLGHHVTVFEREDRfgglLMygiPSMkLDKAIVQRRVDLMEELGVTFIANTEVSSdvmakq 236
Cdd:COG1251 144 RVVVIGGGLIGLEAAAALRKRGLEVTVVERAPR----LL---PRQ-LDEEAGALLQRLLEALGVEVRLGTGVTE------ 209
|
90 100 110
....*....|....*....|....*....|....*....
gi 1341813615 237 LQKD--FDRVILTTGAGVPRDLSIPGrqlTGIRFAVDYL 273
Cdd:COG1251 210 IEGDdrVTGVRLADGEELPADLVVVA---IGVRPNTELA 245
|
|
| PLN02172 |
PLN02172 |
flavin-containing monooxygenase FMO GS-OX |
149-196 |
2.34e-06 |
|
flavin-containing monooxygenase FMO GS-OX
Pssm-ID: 215116 [Multi-domain] Cd Length: 461 Bit Score: 49.86 E-value: 2.34e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1341813615 149 TPQRQTDFKIAVVGSGPAGLSAAWRLNQLGHHVTVFEREDRFGGLLMY 196
Cdd:PLN02172 4 AQNPINSQHVAVIGAGAAGLVAARELRREGHTVVVFEREKQVGGLWVY 51
|
|
| Amino_oxidase |
pfam01593 |
Flavin containing amine oxidoreductase; This family consists of various amine oxidases, ... |
166-192 |
1.12e-05 |
|
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: 47.49 E-value: 1.12e-05
10 20
....*....|....*....|....*..
gi 1341813615 166 AGLSAAWRLNQLGHHVTVFEREDRFGG 192
Cdd:pfam01593 2 AGLAAARELLRAGHDVTVLEARDRVGG 28
|
|
| PRK00711 |
PRK00711 |
D-amino acid dehydrogenase; |
157-189 |
1.34e-05 |
|
D-amino acid dehydrogenase;
Pssm-ID: 234819 [Multi-domain] Cd Length: 416 Bit Score: 47.49 E-value: 1.34e-05
10 20 30
....*....|....*....|....*....|...
gi 1341813615 157 KIAVVGSGPAGLSAAWRLNQLGHHVTVFEREDR 189
Cdd:PRK00711 2 RVVVLGSGVIGVTSAWYLAQAGHEVTVIDRQPG 34
|
|
| PLN02976 |
PLN02976 |
amine oxidase |
157-192 |
1.80e-05 |
|
amine oxidase
Pssm-ID: 215527 [Multi-domain] Cd Length: 1713 Bit Score: 47.55 E-value: 1.80e-05
10 20 30
....*....|....*....|....*....|....*.
gi 1341813615 157 KIAVVGSGPAGLSAAWRLNQLGHHVTVFEREDRFGG 192
Cdd:PLN02976 695 KIIVVGAGPAGLTAARHLQRQGFSVTVLEARSRIGG 730
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
157-306 |
2.06e-05 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 46.66 E-value: 2.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 157 KIAVVGSGPAGLSAAWRLNQL---GHHVTVFEREDR--FGGLLmYGIPSMKLDKAIVQRRV-DLMEELGVTFIaNTEVSS 230
Cdd:COG1252 3 RIVIVGGGFAGLEAARRLRKKlggDAEVTLIDPNPYhlFQPLL-PEVAAGTLSPDDIAIPLrELLRRAGVRFI-QGEVTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 231 -DVMAKQLQKD------FDRVILTTGAgVPRDLSIPGRQltgiRFA-----VDYLTEVTKDVLKYGKKTTSRKLegKHVV 298
Cdd:COG1252 81 iDPEARTVTLAdgrtlsYDYLVIATGS-VTNFFGIPGLA----EHAlplktLEDALALRERLLAAFERAERRRL--LTIV 153
|
....*...
gi 1341813615 299 VIGGGDTG 306
Cdd:COG1252 154 VVGGGPTG 161
|
|
| YdhS |
COG4529 |
Uncharacterized NAD(P)/FAD-binding protein YdhS [General function prediction only]; |
157-347 |
2.47e-05 |
|
Uncharacterized NAD(P)/FAD-binding protein YdhS [General function prediction only];
Pssm-ID: 443597 [Multi-domain] Cd Length: 466 Bit Score: 46.49 E-value: 2.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 157 KIAVVGSGPAGLSAAWRLNQLGH---HVTVFEREDRFGGLLMYGIPS-----------MKLDK----------------- 205
Cdd:COG4529 7 RIAIIGGGASGTALAIHLLRRAPeplRITLFEPRPELGRGVAYSTDSpehllnvpagrMSAFPddpdhflrwlrengara 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 206 -------AIVQRRV------DLMEEL---GVTFIANTEVSSDVMAKQLQKD-------------FDRVILTTGAGVPRDL 256
Cdd:COG4529 87 apaidpdAFVPRRLfgeylrERLAEAlarAPAGVRLRHIRAEVVDLERDDGgyrvtladgetlrADAVVLATGHPPPAPP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 257 siPGRQLTGIRFAVDY-----LTEVTKDvlkygkkttsrklegKHVVVIGGGDTGNDCIGSAIRQGaasvKQLEITA--- 328
Cdd:COG4529 167 --PGLAAGSPRYIADPwppgaLARIPPD---------------ARVLIIGTGLTAIDVVLSLAARG----HRGPITAlsr 225
|
250 260
....*....|....*....|.
gi 1341813615 329 --EPPVYRSKKNPWPEYPITR 347
Cdd:COG4529 226 rgLLPRAHPPGAPLPLKFLTP 246
|
|
| glucose_DH |
cd08230 |
Glucose dehydrogenase; Glucose dehydrogenase (GlcDH), a member of the medium chain ... |
159-251 |
6.77e-05 |
|
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: 44.90 E-value: 6.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 159 AVVGSGPAGLSAAWRLNQLGHHVTVFEREDRfggllmygiPSMKLdkaivqrrvDLMEELGVTFIANTEVssDVMAKQLQ 238
Cdd:cd08230 177 LVLGAGPIGLLAALLLRLRGFEVYVLNRRDP---------PDPKA---------DIVEELGATYVNSSKT--PVAEVKLV 236
|
90
....*....|...
gi 1341813615 239 KDFDRVILTTGAG 251
Cdd:cd08230 237 GEFDLIIEATGVP 249
|
|
| PRK07251 |
PRK07251 |
FAD-containing oxidoreductase; |
157-248 |
6.94e-05 |
|
FAD-containing oxidoreductase;
Pssm-ID: 180907 [Multi-domain] Cd Length: 438 Bit Score: 45.13 E-value: 6.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 157 KIAVVGSGPAGLSAAWRLNQLGHHVTVFEREDRFGGllmygipsmKLDKAIVQRRVDLMEELGVTFIANTEVssdvmaKQ 236
Cdd:PRK07251 159 RLGIIGGGNIGLEFAGLYNKLGSKVTVLDAASTILP---------REEPSVAALAKQYMEEDGITFLLNAHT------TE 223
|
90
....*....|..
gi 1341813615 237 LQKDFDRVILTT 248
Cdd:PRK07251 224 VKNDGDQVLVVT 235
|
|
| HI0933_like |
pfam03486 |
HI0933-like protein; |
156-197 |
7.18e-05 |
|
HI0933-like protein;
Pssm-ID: 427330 [Multi-domain] Cd Length: 406 Bit Score: 44.88 E-value: 7.18e-05
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1341813615 156 FKIAVVGSGPAGLSAAWRLNQLGHHVTVFEREDRFG-GLLMYG 197
Cdd:pfam03486 1 FDVIVIGGGAAGLMAAISAAKRGRRVLLIEKGKKLGrKILISG 43
|
|
| PRK12409 |
PRK12409 |
D-amino acid dehydrogenase small subunit; Provisional |
157-186 |
1.46e-04 |
|
D-amino acid dehydrogenase small subunit; Provisional
Pssm-ID: 237093 [Multi-domain] Cd Length: 410 Bit Score: 43.86 E-value: 1.46e-04
10 20 30
....*....|....*....|....*....|
gi 1341813615 157 KIAVVGSGPAGLSAAWRLNQLGHHVTVFER 186
Cdd:PRK12409 3 HIAVIGAGITGVTTAYALAQRGYQVTVFDR 32
|
|
| PLN02576 |
PLN02576 |
protoporphyrinogen oxidase |
144-192 |
1.59e-04 |
|
protoporphyrinogen oxidase
Pssm-ID: 215314 [Multi-domain] Cd Length: 496 Bit Score: 44.23 E-value: 1.59e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1341813615 144 VKASGTPQRQTDfkIAVVGSGPAGLSAAWRL-NQLGHHVTVFEREDRFGG 192
Cdd:PLN02576 3 IAEGSAAASSKD--VAVVGAGVSGLAAAYALaSKHGVNVLVTEARDRVGG 50
|
|
| Thi4 |
pfam01946 |
Thi4 family; This family includes Swiss:P32318 a putative thiamine biosynthetic enzyme. |
158-238 |
1.70e-04 |
|
Thi4 family; This family includes Swiss:P32318 a putative thiamine biosynthetic enzyme.
Pssm-ID: 460393 Cd Length: 232 Bit Score: 42.84 E-value: 1.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 158 IAVVGSGPAGLSAAWRL-NQLGHHVTVFEREDRFGGLLMYGipSMKLDKAIVQRRVDL-MEELGVTFIA---------NT 226
Cdd:pfam01946 20 VVIVGAGSSGLTAAYYLaKNRGLKVAIIERSVSPGGGAWLG--GQLFSAMVVRKPAHLfLDEFGIPYEDegdyvvvkhAA 97
|
90
....*....|..
gi 1341813615 227 EVSSDVMAKQLQ 238
Cdd:pfam01946 98 LFTSTLMSKALQ 109
|
|
| FAD_binding_2 |
pfam00890 |
FAD binding domain; This family includes members that bind FAD. This family includes the ... |
158-219 |
2.41e-04 |
|
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: 43.43 E-value: 2.41e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 158 IAVVGSGPAGLSAAWRLNQLGHHVTVFEREDRF--------GGLLMYGIPSMKLDKAIVQRRVDLMEELG 219
Cdd:pfam00890 2 VLVIGGGLAGLAAALAAAEAGLKVAVVEKGQPFggatawssGGIDALGNPPQGGIDSPELHPTDTLKGLD 71
|
|
| PRK07236 |
PRK07236 |
hypothetical protein; Provisional |
157-221 |
3.43e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 235980 [Multi-domain] Cd Length: 386 Bit Score: 42.99 E-value: 3.43e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 157 KIAVVGSGPAGLSAAWRLNQLGHHVTVFER-----EDRFGGLLMYgiPSMKldKAIVQRRVDLMEELGVT 221
Cdd:PRK07236 8 RAVVIGGSLGGLFAALLLRRAGWDVDVFERsptelDGRGAGIVLQ--PELL--RALAEAGVALPADIGVP 73
|
|
| PRK06753 |
PRK06753 |
hypothetical protein; Provisional |
157-316 |
5.77e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 168661 [Multi-domain] Cd Length: 373 Bit Score: 41.98 E-value: 5.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 157 KIAVVGSGPAGLSAAWRLNQLGHHVTVFEREdrfggllmygiPSMKLDKAIVQRRVDLMEELGVTFIA----NTEVSSDV 232
Cdd:PRK06753 2 KIAIIGAGIGGLTAAALLQEQGHEVKVFEKN-----------ESVKEVGAGIGIGDNVIKKLGNHDLAkgikNAGQILST 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 233 MAKQLQKD--FDRVILTTGagvPRDLSIPGRQLTGIrfavdYLTEVTKDVLKYGKKTTSRKLEGKHVVVI---GGGDTGN 307
Cdd:PRK06753 71 MNLLDDKGtlLNKVKLKSN---TLNVTLHRQTLIDI-----IKSYVKEDAIFTGKEVTKIENETDKVTIHfadGESEAFD 142
|
170
....*....|....
gi 1341813615 308 DCIG-----SAIRQ 316
Cdd:PRK06753 143 LCIGadgihSKVRQ 156
|
|
| FixC |
COG0644 |
Dehydrogenase (flavoprotein) [Energy production and conversion]; |
164-191 |
6.43e-04 |
|
Dehydrogenase (flavoprotein) [Energy production and conversion];
Pssm-ID: 440409 [Multi-domain] Cd Length: 281 Bit Score: 41.49 E-value: 6.43e-04
10 20
....*....|....*....|....*...
gi 1341813615 164 GPAGLSAAWRLNQLGHHVTVFEREDRFG 191
Cdd:COG0644 2 GPAGSAAARRLARAGLSVLLLEKGSFPG 29
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
124-249 |
6.54e-04 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 42.09 E-value: 6.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 124 GVTIHDNERFII-DTAFENNWVkasgtPQRqtdfkIAVVGSGPAGLSAAWRLNQLGHHVTVFEREDRFGGLlmygipsmk 202
Cdd:PRK06292 147 GVWLILGDRLLTsDDAFELDKL-----PKS-----LAVIGGGVIGLELGQALSRLGVKVTVFERGDRILPL--------- 207
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1341813615 203 LDKAIVQRRVDLMEElGVTFIANTEVSS-----DVMAKQLQKD-------FDRVILTTG 249
Cdd:PRK06292 208 EDPEVSKQAQKILSK-EFKIKLGAKVTSveksgDEKVEELEKGgktetieADYVLVATG 265
|
|
| PRK05249 |
PRK05249 |
Si-specific NAD(P)(+) transhydrogenase; |
155-192 |
6.64e-04 |
|
Si-specific NAD(P)(+) transhydrogenase;
Pssm-ID: 235373 [Multi-domain] Cd Length: 461 Bit Score: 42.07 E-value: 6.64e-04
10 20 30
....*....|....*....|....*....|....*...
gi 1341813615 155 DFKIAVVGSGPAGLSAAWRLNQLGHHVTVFEREDRFGG 192
Cdd:PRK05249 5 DYDLVVIGSGPAGEGAAMQAAKLGKRVAVIERYRNVGG 42
|
|
| SdhA |
COG1053 |
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and ... |
155-192 |
7.29e-04 |
|
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: 41.74 E-value: 7.29e-04
10 20 30
....*....|....*....|....*....|....*...
gi 1341813615 155 DFKIAVVGSGPAGLSAAWRLNQLGHHVTVFEREDRFGG 192
Cdd:COG1053 3 EYDVVVVGSGGAGLRAALEAAEAGLKVLVLEKVPPRGG 40
|
|
| PRK06134 |
PRK06134 |
putative FAD-binding dehydrogenase; Reviewed |
144-219 |
8.79e-04 |
|
putative FAD-binding dehydrogenase; Reviewed
Pssm-ID: 180419 [Multi-domain] Cd Length: 581 Bit Score: 41.63 E-value: 8.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 144 VKASGTPQRQTDfkIAVVGSGPAGLSAAWRLNQLGHHVTVFEREDRFGGLL-----MYGIPSMKL------DKAIVQRRV 212
Cdd:PRK06134 3 SAAAYPPDLECD--VLVIGSGAAGLSAAVTAAWHGLKVIVVEKDPVFGGTTawsggWMWIPRNPLarragiVEDIEQPRT 80
|
....*..
gi 1341813615 213 DLMEELG 219
Cdd:PRK06134 81 YLRHELG 87
|
|
| PRK07845 |
PRK07845 |
flavoprotein disulfide reductase; Reviewed |
157-232 |
1.09e-03 |
|
flavoprotein disulfide reductase; Reviewed
Pssm-ID: 236112 [Multi-domain] Cd Length: 466 Bit Score: 41.38 E-value: 1.09e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1341813615 157 KIAVVGSGPAGLSAAWRLNQLGHHVTVFEReDRFGG--LLMYGIPSMKL-DKAIVQRRVDLMEELGVTFIANTEVSSDV 232
Cdd:PRK07845 3 RIVIIGGGPGGYEAALVAAQLGADVTVIER-DGLGGaaVLTDCVPSKTLiATAEVRTELRRAAELGIRFIDDGEARVDL 80
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
153-303 |
1.14e-03 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 41.34 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 153 QTDFKIAVVGSGPAGLSAAWRLNQLGHHVTVFEReDRFGG-LLMYG-IPSmkldKAIVQ--RRVDLM---EELGVTFIAN 225
Cdd:PRK06370 3 AQRYDAIVIGAGQAGPPLAARAAGLGMKVALIER-GLLGGtCVNTGcVPT----KTLIAsaRAAHLArraAEYGVSVGGP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 226 TEVS-SDVMAKQLQ-------------KDFDRVILTTGAGV---PRDLSIPGRQLTGIRF-----------------AVD 271
Cdd:PRK06370 78 VSVDfKAVMARKRRirarsrhgseqwlRGLEGVDVFRGHARfesPNTVRVGGETLRAKRIfintgaraaippipgldEVG 157
|
170 180 190
....*....|....*....|....*....|..
gi 1341813615 272 YLTEVTkdVLKYGKKTtsrklegKHVVVIGGG 303
Cdd:PRK06370 158 YLTNET--IFSLDELP-------EHLVIIGGG 180
|
|
| mhpA |
PRK06183 |
bifunctional 3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic acid hydroxylase; |
147-189 |
1.21e-03 |
|
bifunctional 3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic acid hydroxylase;
Pssm-ID: 235727 [Multi-domain] Cd Length: 500 Bit Score: 41.43 E-value: 1.21e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1341813615 147 SGTPQRQTDFKIAVVGSGPAGLSAAWRLNQLGHHVTVFEREDR 189
Cdd:PRK06183 2 AAQHPDAHDTDVVIVGAGPVGLTLANLLGQYGVRVLVLERWPT 44
|
|
| PRK07588 |
PRK07588 |
FAD-binding domain; |
157-194 |
1.53e-03 |
|
FAD-binding domain;
Pssm-ID: 169028 [Multi-domain] Cd Length: 391 Bit Score: 40.87 E-value: 1.53e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1341813615 157 KIAVVGSGPAGLSAAWRLNQLGHHVTVFEREDRF--GGLL 194
Cdd:PRK07588 2 KVAISGAGIAGPTLAYWLRRYGHEPTLIERAPELrtGGYM 41
|
|
| PRK12834 |
PRK12834 |
putative FAD-binding dehydrogenase; Reviewed |
152-211 |
3.68e-03 |
|
putative FAD-binding dehydrogenase; Reviewed
Pssm-ID: 183782 [Multi-domain] Cd Length: 549 Bit Score: 39.88 E-value: 3.68e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 152 RQTDFKIAVVGSGPAGLSAAWRLNQLGHHVTVFEREDR----------FGGLLMYGIPSmkldkaivQRR 211
Cdd:PRK12834 1 MAMDADVIVVGAGLAGLVAAAELADAGKRVLLLDQENEanlggqafwsLGGLFLVDSPE--------QRR 62
|
|
| PRK09126 |
PRK09126 |
FAD-dependent hydroxylase; |
156-186 |
3.85e-03 |
|
FAD-dependent hydroxylase;
Pssm-ID: 236385 [Multi-domain] Cd Length: 392 Bit Score: 39.54 E-value: 3.85e-03
10 20 30
....*....|....*....|....*....|.
gi 1341813615 156 FKIAVVGSGPAGLSAAWRLNQLGHHVTVFER 186
Cdd:PRK09126 4 SDIVVVGAGPAGLSFARSLAGSGLKVTLIER 34
|
|
| COG3573 |
COG3573 |
Predicted oxidoreductase [General function prediction only]; |
160-211 |
4.06e-03 |
|
Predicted oxidoreductase [General function prediction only];
Pssm-ID: 442794 [Multi-domain] Cd Length: 551 Bit Score: 39.78 E-value: 4.06e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1341813615 160 VVGSGPAGLSAAWRLNQLGHHVTVFEREDR----------FGGLLMYGIPsmkldkaiVQRR 211
Cdd:COG3573 10 VVGAGLAGLVAAAELADAGRRVLLLDQEPEanlggqafwsFGGLFLVDSP--------EQRR 63
|
|
| PRK08255 |
PRK08255 |
bifunctional salicylyl-CoA 5-hydroxylase/oxidoreductase; |
157-191 |
4.74e-03 |
|
bifunctional salicylyl-CoA 5-hydroxylase/oxidoreductase;
Pssm-ID: 236203 [Multi-domain] Cd Length: 765 Bit Score: 39.54 E-value: 4.74e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1341813615 157 KIAVVGSGPAGLSAAWRLNQL--GHHVTVFER---EDRFG 191
Cdd:PRK08255 2 RIVCIGGGPAGLYFALLMKLLdpAHEVTVVERnrpYDTFG 41
|
|
| GG-red-SF |
TIGR02032 |
geranylgeranyl reductase family; This model represents a subfamily which includes ... |
156-188 |
6.48e-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: 38.45 E-value: 6.48e-03
10 20 30
....*....|....*....|....*....|...
gi 1341813615 156 FKIAVVGSGPAGLSAAWRLNQLGHHVTVFERED 188
Cdd:TIGR02032 1 YDVVVVGAGPAGASAAYRLADKGLRVLLLEKKS 33
|
|
| PLN02529 |
PLN02529 |
lysine-specific histone demethylase 1 |
146-286 |
6.52e-03 |
|
lysine-specific histone demethylase 1
Pssm-ID: 178144 [Multi-domain] Cd Length: 738 Bit Score: 39.10 E-value: 6.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 146 ASGTPQRQTDFKIAVVGSGPAGLSAAWRLNQLGHHVTVFEREDRFGGLLMYGIPSMKLDKAIVqrrvdlmeELGVTFIAN 225
Cdd:PLN02529 151 ASPIPEEGTEGSVIIVGAGLAGLAAARQLLSFGFKVVVLEGRNRPGGRVYTQKMGRKGQFAAV--------DLGGSVITG 222
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1341813615 226 TEVSS-DVMAKQ----LQKDFDRVILTTGAGVPRDLSIPGRQLTGIRFAVDYLTEVTKDVLKYGKK 286
Cdd:PLN02529 223 IHANPlGVLARQlsipLHKVRDNCPLYKPDGALVDKEIDSNIEFIFNKLLDKVTELRQIMGGFAND 288
|
|
| sdhA |
PRK07573 |
fumarate reductase/succinate dehydrogenase flavoprotein subunit; |
150-184 |
6.97e-03 |
|
fumarate reductase/succinate dehydrogenase flavoprotein subunit;
Pssm-ID: 236054 [Multi-domain] Cd Length: 640 Bit Score: 39.03 E-value: 6.97e-03
10 20 30
....*....|....*....|....*....|....*
gi 1341813615 150 PQRQTDFKIAVVGSGPAGLSAAWRLNQLGHHVTVF 184
Cdd:PRK07573 30 PANKRKFDVIVVGTGLAGASAAATLGELGYNVKVF 64
|
|
| FAD_binding_3 |
pfam01494 |
FAD binding domain; This domain is involved in FAD binding in a number of enzymes. |
155-274 |
7.04e-03 |
|
FAD binding domain; This domain is involved in FAD binding in a number of enzymes.
Pssm-ID: 396193 [Multi-domain] Cd Length: 348 Bit Score: 38.46 E-value: 7.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341813615 155 DFKIAVVGSGPAGLSAAWRLNQLGHHVTVFEREDRFGGLLMYGIpsmkldkaIVQRRVDLMEELGV--TFIAnTEVSSDV 232
Cdd:pfam01494 1 ETDVLIVGGGPAGLMLALLLARAGVRVVLVERHATTSVLPRAHG--------LNQRTMELLRQAGLedRILA-EGVPHEG 71
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1341813615 233 MAKQLQKDFDRVILTTGAGVPRDLSIP----------GRQLTG--IRFAVDYLT 274
Cdd:pfam01494 72 MGLAFYNTRRRADLDFLTSPPRVTVYPqtelepilveHAEARGaqVRFGTEVLS 125
|
|
| PRK07494 |
PRK07494 |
UbiH/UbiF family hydroxylase; |
155-220 |
7.26e-03 |
|
UbiH/UbiF family hydroxylase;
Pssm-ID: 181001 [Multi-domain] Cd Length: 388 Bit Score: 38.73 E-value: 7.26e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1341813615 155 DFKIAVVGSGPAGLSAAWRLNQLGHHVTVFER-----EDRFGGLLMygiPSmkldkaivqrrVDLMEELGV 220
Cdd:PRK07494 7 HTDIAVIGGGPAGLAAAIALARAGASVALVAPeppyaDLRTTALLG---PS-----------IRFLERLGL 63
|
|
| PRK12842 |
PRK12842 |
putative succinate dehydrogenase; Reviewed |
160-192 |
8.03e-03 |
|
putative succinate dehydrogenase; Reviewed
Pssm-ID: 237224 [Multi-domain] Cd Length: 574 Bit Score: 38.52 E-value: 8.03e-03
10 20 30
....*....|....*....|....*....|...
gi 1341813615 160 VVGSGPAGLSAAWRLNQLGHHVTVFEREDRFGG 192
Cdd:PRK12842 14 VIGSGAGGLSAAITARKLGLDVVVLEKEPVFGG 46
|
|
| PRK08132 |
PRK08132 |
FAD-dependent oxidoreductase; Provisional |
146-189 |
8.76e-03 |
|
FAD-dependent oxidoreductase; Provisional
Pssm-ID: 236158 [Multi-domain] Cd Length: 547 Bit Score: 38.70 E-value: 8.76e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1341813615 146 ASGTPQRQtdfKIAVVGSGPAGLSAAWRLNQLGHHVTVFEREDR 189
Cdd:PRK08132 17 DADDPARH---PVVVVGAGPVGLALAIDLAQQGVPVVLLDDDDT 57
|
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