|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
3-412 |
2.76e-171 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 486.99 E-value: 2.76e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447059109 3 QQNYlDELTPAFTPLLAIKEASRCLLCHDAPCSQACPAQTDPGKFIRSIYFRNFKGAAETIRENNALGAVCARVCPTEKL 82
Cdd:PRK11749 20 AQNF-DEVAPGYTPEEAIEEASRCLQCKDAPCVKACPVSIDIPEFIRLIAEGNLKGAAETILETNPLPAVCGRVCPQERL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447059109 83 CQSGCTRAGVDTPIDIGRLQRFVTDFEQQTGMEIYQPGTKTLGKVAIIGAGPAGLQASVTLTNQGYDVTIYEKEAHPGGW 162
Cdd:PRK11749 99 CEGACVRGKKGEPVAIGRLERYITDWAMETGWVLFKRAPKTGKKVAVIGAGPAGLTAAHRLARKGYDVTIFEARDKAGGL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447059109 163 LRNGIPQFRLPQSVLDAEIARIEKMGVTIKCNNEVGNTLTLEQLKAENRAVLVTVGLSSGSGLSLF--EHSDVEIAVDFL 240
Cdd:PRK11749 179 LRYGIPEFRLPKDIVDREVERLLKLGVEIRTNTEVGRDITLDELRAGYDAVFIGTGAGLPRFLGIPgeNLGGVYSAVDFL 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447059109 241 QRARQA--QGDISIPQSALIIGGGDVAMDVASTLKVLGCQAVTCVAREELDEFPASEKEFASARELGVSIIDGFTPVAVE 318
Cdd:PRK11749 259 TRVNQAvaDYDLPVGKRVVVIGGGNTAMDAARTAKRLGAESVTIVYRRGREEMPASEEEVEHAKEEGVEFEWLAAPVEIL 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447059109 319 GNK-----VTFKHVRL-------------PG-ELTMAADKIILAVGQHARLDAFA-----ELEPQRNTIKTQ-NYQTRDP 373
Cdd:PRK11749 339 GDEgrvtgVEFVRMELgepdasgrrrvpiEGsEFTLPADLVIKAIGQTPNPLILSttpglELNRWGTIIADDeTGRTSLP 418
|
410 420 430
....*....|....*....|....*....|....*....
gi 447059109 374 QVFAAGDIVEGDKTVVYAVKTGKEAAEAIHHYLEGACSC 412
Cdd:PRK11749 419 GVFAGGDIVTGAATVVWAVGDGKDAAEAIHEYLEGAASA 457
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
8-405 |
7.14e-134 |
|
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: 391.04 E-value: 7.14e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447059109 8 DELTPAFTPLLAIKEASRCLLCHDAPCSQACPAQTDPGKFIRSIYFRNFKGAAETIRENNALGAVCARVCPteKLCQSGC 87
Cdd:COG0493 6 REVYPGLSEEEAIEQAARCLDCGDPPCQTGCPVGNDIPEWIRLIAEGDYEEALELIHETNPFPEVCGRVCP--APCEGAC 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447059109 88 TRAGVDTPIDIGRLQRFVTDFEQQTG-MEIYQPGTKTLGKVAIIGAGPAGLQASVTLTNQGYDVTIYEKEAHPGGWLRNG 166
Cdd:COG0493 84 VRGIVDEPVAIGALERFIADKAFEEGwVKPPPPAPRTGKKVAVVGSGPAGLAAAYQLARAGHEVTVFEALDKPGGLLRYG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447059109 167 IPQFRLPQSVLDAEIARIEKMGVTIKCNNEVGNTLTLEQLKAENRAVLVTVgLSSGSGLSLFEHSD---VEIAVDFLQRA 243
Cdd:COG0493 164 IPEFRLPKDVLDREIELIEALGVEFRTNVEVGKDITLDELLEEFDAVFLAT-GAGKPRDLGIPGEDlkgVHSAMDFLTAV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447059109 244 RQAQGDISIPQ---SALIIGGGDVAMDVASTLKVLGCQAVTCVAREELDEFPASEKEFASARELGVSIIDGFTPVAVEGN 320
Cdd:COG0493 243 NLGEAPDTILAvgkRVVVIGGGNTAMDCARTALRLGAESVTIVYRRTREEMPASKEEVEEALEEGVEFLFLVAPVEIIGD 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447059109 321 K------VTFKHVRL--------------PG-ELTMAADKIILAVGQHARLDAFAELEP----QRNTIKT--QNYQTRDP 373
Cdd:COG0493 323 EngrvtgLECVRMELgepdesgrrrpvpiEGsEFTLPADLVILAIGQTPDPSGLEEELGleldKRGTIVVdeETYQTSLP 402
|
410 420 430
....*....|....*....|....*....|..
gi 447059109 374 QVFAAGDIVEGDKTVVYAVKTGKEAAEAIHHY 405
Cdd:COG0493 403 GVFAGGDAVRGPSLVVWAIAEGRKAARAIDRY 434
|
|
| PRK12831 |
PRK12831 |
putative oxidoreductase; Provisional |
8-408 |
2.53e-86 |
|
putative oxidoreductase; Provisional
Pssm-ID: 183780 [Multi-domain] Cd Length: 464 Bit Score: 270.35 E-value: 2.53e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447059109 8 DELTPAFTPLLAIKEASRCLLCHDAPCSQACPAQTDPGKFIRSIYFRNFKGAAETIRENNALGAVCARVCPTEKLCQSGC 87
Cdd:PRK12831 24 EEVCLGYNEEEAVKEASRCLQCKKPKCVKGCPVSINIPGFISKLKEGDFEEAAKIIAKYNALPAVCGRVCPQESQCEGKC 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447059109 88 TRAGVDTPIDIGRLQRFVTDFEQQTGMEIYQPGTKTLGKVAIIGAGPAGLQASVTLTNQGYDVTIYEKEAHPGGWLRNGI 167
Cdd:PRK12831 104 VLGIKGEPVAIGKLERFVADWARENGIDLSETEEKKGKKVAVIGSGPAGLTCAGDLAKMGYDVTIFEALHEPGGVLVYGI 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447059109 168 PQFRLPQS-VLDAEIARIEKMGVTIKCNNEVGNTLTLEQLKAEN--RAVLVTVglssGSGLSLF-----EHSD-VEIAVD 238
Cdd:PRK12831 184 PEFRLPKEtVVKKEIENIKKLGVKIETNVVVGKTVTIDELLEEEgfDAVFIGS----GAGLPKFmgipgENLNgVFSANE 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447059109 239 FLQRAR--QAQGD-----ISIPQSALIIGGGDVAMDVASTLKVLGCQaVTCVAREELDEFPASEKEFASARELGVsIIDG 311
Cdd:PRK12831 260 FLTRVNlmKAYKPeydtpIKVGKKVAVVGGGNVAMDAARTALRLGAE-VHIVYRRSEEELPARVEEVHHAKEEGV-IFDL 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447059109 312 FT-PVAVEGNK------VTF--------------KHVRLPG-ELTMAADKIILAVGQHAR---LDAFAELEPQRN-TIKT 365
Cdd:PRK12831 338 LTnPVEILGDEngwvkgMKCikmelgepdasgrrRPVEIEGsEFVLEVDTVIMSLGTSPNpliSSTTKGLKINKRgCIVA 417
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 447059109 366 --QNYQTRDPQVFAAGDIVEGDKTVVYAVKTGKEAAEAIHHYLEG 408
Cdd:PRK12831 418 deETGLTSKEGVFAGGDAVTGAATVILAMGAGKKAAKAIDEYLSK 462
|
|
| PRK12778 |
PRK12778 |
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ... |
5-409 |
1.18e-83 |
|
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;
Pssm-ID: 237200 [Multi-domain] Cd Length: 752 Bit Score: 270.84 E-value: 1.18e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447059109 5 NYLDELTPAFTPLLAIKEASRCLLCHDAPCSQACPAQTDPGKFIRSIYFRNFKGAAETIRENNALGAVCARVCPTEKLCQ 84
Cdd:PRK12778 310 NRFEEVNLGLTKEQAMTEAKRCLDCKNPGCVEGCPVGIDIPRFIKNIERGNFLEAAKILKETSALPAVCGRVCPQEKQCE 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447059109 85 SGCTR--AGVDtPIDIGRLQRFVTDFEQQTG-MEIYQPGTKTLGKVAIIGAGPAGLQASVTLTNQGYDVTIYEKEAHPGG 161
Cdd:PRK12778 390 SKCIHgkMGEE-AVAIGYLERFVADYERESGnISVPEVAEKNGKKVAVIGSGPAGLSFAGDLAKRGYDVTVFEALHEIGG 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447059109 162 WLRNGIPQFRLPQSVLDAEIARIEKMGVTIKCNNEVGNTLTLEQLKAEN-RAVLVtvglSSGSGLSLFEH------SDVE 234
Cdd:PRK12778 469 VLKYGIPEFRLPKKIVDVEIENLKKLGVKFETDVIVGKTITIEELEEEGfKGIFI----ASGAGLPNFMNipgensNGVM 544
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447059109 235 IAVDFLQRA---RQAQGDISIP----QSALIIGGGDVAMDVASTLKVLGCQAVTCVAREELDEFPASEKEFASARELGVS 307
Cdd:PRK12778 545 SSNEYLTRVnlmDAASPDSDTPikfgKKVAVVGGGNTAMDSARTAKRLGAERVTIVYRRSEEEMPARLEEVKHAKEEGIE 624
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447059109 308 IIDGFTPVAVEGN-KVTFKHVRL-------------------PG-ELTMAADKIILAVGQHAR---LDAFAELEPQR--N 361
Cdd:PRK12778 625 FLTLHNPIEYLADeKGWVKQVVLqkmelgepdasgrrrpvaiPGsTFTVDVDLVIVSVGVSPNplvPSSIPGLELNRkgT 704
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 447059109 362 TIKTQNYQTRDPQVFAAGDIVEGDKTVVYAVKTGKEAAEAIHHYLEGA 409
Cdd:PRK12778 705 IVVDEEMQSSIPGIYAGGDIVRGGATVILAMGDGKRAAAAIDEYLSSK 752
|
|
| PRK12771 |
PRK12771 |
putative glutamate synthase (NADPH) small subunit; Provisional |
33-409 |
4.12e-83 |
|
putative glutamate synthase (NADPH) small subunit; Provisional
Pssm-ID: 237198 [Multi-domain] Cd Length: 564 Bit Score: 264.81 E-value: 4.12e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447059109 33 PCSQACPAQTD-PG--KFIRSIyfrNFKGAAETIRENNALGAVCARVCPTEklCQSGCTRAGVDTPIDIGRLQRFVTDFE 109
Cdd:PRK12771 48 PCNAACPAGEDiRGwlALVRGG---DYEYAWRRLTKDNPFPAVMGRVCYHP--CESGCNRGQVDDAVGINAVERFLGDYA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447059109 110 QQTGMEIYQPGTKTLGKVAIIGAGPAGLQASVTLTNQGYDVTIYEKEAHPGGWLRNGIPQFRLPQSVLDAEIARIEKMGV 189
Cdd:PRK12771 123 IANGWKFPAPAPDTGKRVAVIGGGPAGLSAAYHLRRMGHAVTIFEAGPKLGGMMRYGIPAYRLPREVLDAEIQRILDLGV 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447059109 190 TIKCNNEVGNTLTLEQLKAENRAVLVTVGLssgsglslfeHSD--VEI----------AVDFLqRARQAQGDISIPQSAL 257
Cdd:PRK12771 203 EVRLGVRVGEDITLEQLEGEFDAVFVAIGA----------QLGkrLPIpgedaagvldAVDFL-RAVGEGEPPFLGKRVV 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447059109 258 IIGGGDVAMDVASTLKVLGCQAVTCVAREELDEFPASEKEFASARELGVSIIDGFTPVAVEGNKVTFKHVRL-------- 329
Cdd:PRK12771 272 VIGGGNTAMDAARTARRLGAEEVTIVYRRTREDMPAHDEEIEEALREGVEINWLRTPVEIEGDENGATGLRVitvekmel 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447059109 330 -------PG---ELTMAADKIILAVGQH---ARLDAFAELEPQRNTIKT-QNYQ-TRDPQVFAAGDIVEGDKTVVYAVKT 394
Cdd:PRK12771 352 dedgrpsPVtgeEETLEADLVVLAIGQDidsAGLESVPGVEVGRGVVQVdPNFMmTGRPGVFAGGDMVPGPRTVTTAIGH 431
|
410
....*....|....*
gi 447059109 395 GKEAAEAIHHYLEGA 409
Cdd:PRK12771 432 GKKAARNIDAFLGGE 446
|
|
| gltA |
TIGR01316 |
glutamate synthase (NADPH), homotetrameric; This protein is homologous to the small subunit of ... |
9-406 |
2.86e-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: 251.71 E-value: 2.86e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447059109 9 ELTPAFTPLLAIKEASRCLLCHDA--PCSQACPAQTDPGKFIRSIYFRNFKGAAETIRENNALGAVCARVCPTEKLCQSG 86
Cdd:TIGR01316 11 EAALGYTEQLALVEAQRCLNCKDAtkPCIKGCPVHVPIPEFIAKIQEGDFKGAVDIIKTTSLLPAICGRVCPQERQCEGQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447059109 87 CT----RAGVDTPIDIGRLQRFVTDFEQQTGMEIYQ---PGTKtlGKVAIIGAGPAGLQASVTLTNQGYDVTIYEKEAHP 159
Cdd:TIGR01316 91 CTvgkmFKDVGKPVSIGALERFVADWERQHGIETEPekaPSTH--KKVAVIGAGPAGLACASELAKAGHSVTVFEALHKP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447059109 160 GGWLRNGIPQFRLPQSVLDAEIARIEKMGVTIKCNNEVGNTLTLEQLKAENRAVLVTV-GLSSGSGLSLFEHSD-VEIAV 237
Cdd:TIGR01316 169 GGVVTYGIPEFRLPKEIVVTEIKTLKKLGVTFRMNFLVGKTATLEELFSQYDAVFIGTgAGLPKLMNIPGEELCgVYSAN 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447059109 238 DFLQRAR--------QAQGDISIPQSALIIGGGDVAMDVASTLKVLGCQaVTCVAREELDEFPASEKEFASARELGVSII 309
Cdd:TIGR01316 249 DFLTRANlmkayefpHADTPVYAGKSVVVIGGGNTAVDSARTALRLGAE-VHCLYRRTREDMTARVEEIAHAEEEGVKFH 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447059109 310 DGFTPVAVEGNK------VTFKH------------VRLPG---ELTMAADKIILAVGQHAR----LDAFAELEPQRNTIK 364
Cdd:TIGR01316 328 FLCQPVEIIGDEegnvraVKFRKmdcqeqidsgerRFLPCgdaECKLEADAVIVAIGNGSNpimaETTRLKTSERGTIVV 407
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 447059109 365 TQNYQTRDPQVFAAGDIVEGDKTVVYAVKTGKEAAEAIHHYL 406
Cdd:TIGR01316 408 DEDQRTSIPGVFAGGDIILGAATVIRAMGQGKRAAKSINEYL 449
|
|
| gltD |
PRK12810 |
glutamate synthase subunit beta; Reviewed |
9-409 |
2.46e-78 |
|
glutamate synthase subunit beta; Reviewed
Pssm-ID: 237213 [Multi-domain] Cd Length: 471 Bit Score: 249.70 E-value: 2.46e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447059109 9 ELTPAFTPLLAIKEASRCLLCHDAPCSQACPAQTDPGKFIRSIYFRNFKGAAETIRENNALGAVCARVCPTEklCQSGCT 88
Cdd:PRK12810 29 EFYEPFSEEQAKIQAARCMDCGIPFCHWGCPVHNYIPEWNDLVYRGRWEEAAERLHQTNNFPEFTGRVCPAP--CEGACT 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447059109 89 RAGVDTPIDIGRLQRFVTDfeqqTGMEI-----YQPGTKTLGKVAIIGAGPAGLQASVTLTNQGYDVTIYEKEAHPGGWL 163
Cdd:PRK12810 107 LNINFGPVTIKNIERYIID----KAFEEgwvkpDPPVKRTGKKVAVVGSGPAGLAAADQLARAGHKVTVFERADRIGGLL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447059109 164 RNGIPQFRLPQSVLDAEIARIEKMGVTIKCNNEVGNTLTLEQLKAENRAVLVTVgLSSGSGLSLFEHSD---VEIAVDFL 240
Cdd:PRK12810 183 RYGIPDFKLEKEVIDRRIELMEAEGIEFRTNVEVGKDITAEELLAEYDAVFLGT-GAYKPRDLGIPGRDldgVHFAMDFL 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447059109 241 -QRARQAQGDISIPQ-SA-----LIIGGGDVAMDVASTLKVLGCQAVTcvAREELDEfPASEK-------------EFAS 300
Cdd:PRK12810 262 iQNTRRVLGDETEPFiSAkgkhvVVIGGGDTGMDCVGTAIRQGAKSVT--QRDIMPM-PPSRRnknnpwpywpmklEVSN 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447059109 301 ARELGVSIIDGFTPVAVEG--NKVTFKHV-----------RLPG-ELTMAADKIILAVG-QHARLDAFAELE---PQRNT 362
Cdd:PRK12810 339 AHEEGVEREFNVQTKEFEGenGKVTGVKVvrtelgegdfePVEGsEFVLPADLVLLAMGfTGPEAGLLAQFGvelDERGR 418
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 447059109 363 IK--TQNYQTRDPQVFAAGDIVEGDKTVVYAVKTGKEAAEAIHHYLEGA 409
Cdd:PRK12810 419 VAapDNAYQTSNPKVFAAGDMRRGQSLVVWAIAEGRQAARAIDAYLMGS 467
|
|
| PRK13984 |
PRK13984 |
putative oxidoreductase; Provisional |
9-409 |
1.86e-75 |
|
putative oxidoreductase; Provisional
Pssm-ID: 172486 [Multi-domain] Cd Length: 604 Bit Score: 245.83 E-value: 1.86e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447059109 9 ELTPAFTPLLAIKEASRCLLChdAPCSQACPAQTDPGKFIRSIYFRNFKGAAETIRENNALGAVCARVCpTEKlCQSGCT 88
Cdd:PRK13984 170 EIVKGYSKEQAMQEAARCVEC--GICTDTCPAHMDIPQYIKAIYKDDLEEGLRWLYKTNPLSMVCGRVC-THK-CETVCS 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447059109 89 RAGVDTPIDIGRLQRFVTDfeqQTGMEIY-----QPGTKTLGKVAIIGAGPAGLQASVTLTNQGYDVTIYEKEAHPGGWL 163
Cdd:PRK13984 246 IGHRGEPIAIRWLKRYIVD---NVPVEKYseildDEPEKKNKKVAIVGSGPAGLSAAYFLATMGYEVTVYESLSKPGGVM 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447059109 164 RNGIPQFRLPQSVLDAEIARIEKMGVTIKCNNEVGNTLTLEQLKAENRAVLVTV--GLSSGSGLSLFEHSDVEIAVDFLQ 241
Cdd:PRK13984 323 RYGIPSYRLPDEALDKDIAFIEALGVKIHLNTRVGKDIPLEELREKHDAVFLSTgfTLGRSTRIPGTDHPDVIQALPLLR 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447059109 242 RARQ-AQGD---ISIPQSALIIGGGDVAMDVASTLKVLGCQA-------VTCVAReELDEFPASEKEFASARELGVSIID 310
Cdd:PRK13984 403 EIRDyLRGEgpkPKIPRSLVVIGGGNVAMDIARSMARLQKMEygevnvkVTSLER-TFEEMPADMEEIEEGLEEGVVIYP 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447059109 311 GFTP--VAVEGNKVtfKHVRL-------------------PGELTMAADKIILAVGQHARLDAFAE-----LEPQRNTIK 364
Cdd:PRK13984 482 GWGPmeVVIENDKV--KGVKFkkcvevfdeegrfnpkfdeSDQIIVEADMVVEAIGQAPDYSYLPEelkskLEFVRGRIL 559
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 447059109 365 TQNY-QTRDPQVFAAGDIVEGdKTVVYAVKTGKEAAEAIHHYLEGA 409
Cdd:PRK13984 560 TNEYgQTSIPWLFAGGDIVHG-PDIIHGVADGYWAAEGIDMYLRKQ 604
|
|
| PRK12814 |
PRK12814 |
putative NADPH-dependent glutamate synthase small subunit; Provisional |
31-408 |
4.74e-75 |
|
putative NADPH-dependent glutamate synthase small subunit; Provisional
Pssm-ID: 139246 [Multi-domain] Cd Length: 652 Bit Score: 246.18 E-value: 4.74e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447059109 31 DAPCSQACPAQTDPGKFIRSIYFRNFKGAAETIRENNALGAVCARVCPTEklCQSGCTRAGVDTPIDIGRLQRFVTDFEQ 110
Cdd:PRK12814 101 LGPCELACPAGCNIPGFIAAIARGDDREAIRIIKETIPLPGILGRICPAP--CEEACRRHGVDEPVSICALKRYAADRDM 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447059109 111 QTGME-IYQPGTKTLGKVAIIGAGPAGLQASVTLTNQGYDVTIYEKEAHPGGWLRNGIPQFRLPQSVLDAEIARIEKMGV 189
Cdd:PRK12814 179 ESAERyIPERAPKSGKKVAIIGAGPAGLTAAYYLLRKGHDVTIFDANEQAGGMMRYGIPRFRLPESVIDADIAPLRAMGA 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447059109 190 TIKCNNEVGNTLTLEQLKAENRAVLVTV-GLSSGSGLSLFEHSD-VEIAVDFLQRArqAQGDISIP-QSALIIGGGDVAM 266
Cdd:PRK12814 259 EFRFNTVFGRDITLEELQKEFDAVLLAVgAQKASKMGIPGEELPgVISGIDFLRNV--ALGTALHPgKKVVVIGGGNTAI 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447059109 267 DVASTLKVLGCQAVTCVAREELDEFPASEKEFASARELGVSIIDGFTPVAVE----GNKVTF--------------KHVR 328
Cdd:PRK12814 337 DAARTALRLGAESVTILYRRTREEMPANRAEIEEALAEGVSLRELAAPVSIErsegGLELTAikmqqgepdesgrrRPVP 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447059109 329 LPG-ELTMAADKIILAVGQHA--RLDAFAELEPQRN-TIKT--QNYQTRDPQVFAAGDIVEGDKTVVYAVKTGKEAAEAI 402
Cdd:PRK12814 417 VEGsEFTLQADTVISAIGQQVdpPIAEAAGIGTSRNgTVKVdpETLQTSVAGVFAGGDCVTGADIAINAVEQGKRAAHAI 496
|
....*.
gi 447059109 403 HHYLEG 408
Cdd:PRK12814 497 DLFLNG 502
|
|
| PRK12775 |
PRK12775 |
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin ... |
1-406 |
6.28e-68 |
|
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin domain-containing protein; Provisional
Pssm-ID: 183738 [Multi-domain] Cd Length: 1006 Bit Score: 232.52 E-value: 6.28e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447059109 1 MPQQNYLD------ELTPAFTPLLAIKEASRCLLCHDAPCSQACPAQTDPGKFIRSIYFRNFKGAAETIRENNALGAVCA 74
Cdd:PRK12775 302 MPERDAVErarnfkEVNLGYSLEDALQEAERCIQCAKPTCIAGCPVQIDIPVFIRHVVVRDFDGALEVIYEASIFPSICG 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447059109 75 RVCPTEKLCQSGCTRAGVDTPIDIGRLQRFVTDFEQQtgmeiyQPG-----TKTLGKVAIIGAGPAGLQASVTLTNQGYD 149
Cdd:PRK12775 382 RVCPQETQCEAQCIIAKKHESVGIGRLERFVGDNARA------KPVkpprfSKKLGKVAICGSGPAGLAAAADLVKYGVD 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447059109 150 VTIYEKEAHPGGWLRNGIPQFRLPQSVLDAEIARIEKMGVTIKCNNEVGNTLTLEQLKAEN--RAVLVTVGLSSGSGLSL 227
Cdd:PRK12775 456 VTVYEALHVVGGVLQYGIPSFRLPRDIIDREVQRLVDIGVKIETNKVIGKTFTVPQLMNDKgfDAVFLGVGAGAPTFLGI 535
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447059109 228 FEH--SDVEIAVDFLQRARQAQGD--------ISIPQSALIIGGGDVAMDVASTLKVLGCQAVTCVAREELDEFPASEKE 297
Cdd:PRK12775 536 PGEfaGQVYSANEFLTRVNLMGGDkfpfldtpISLGKSVVVIGAGNTAMDCLRVAKRLGAPTVRCVYRRSEAEAPARIEE 615
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447059109 298 FASARELGVSIIDGFTPV--------AVEGNKVTFKHVRLPGE------------LTMAADKIILAVGQHA--------- 348
Cdd:PRK12775 616 IRHAKEEGIDFFFLHSPVeiyvdaegSVRGMKVEEMELGEPDEkgrrkpmptgefKDLECDTVIYALGTKAnpiitqstp 695
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447059109 349 -----RLDAFAELEPQRNTIKTQNYqtrdPQVFAAGDIVEGDKTVVYAVKTGKEAAEAIHHYL 406
Cdd:PRK12775 696 glalnKWGNIAADDGKLESTQSTNL----PGVFAGGDIVTGGATVILAMGAGRRAARSIATYL 754
|
|
| PRK12769 |
PRK12769 |
putative oxidoreductase Fe-S binding subunit; Reviewed |
8-406 |
8.53e-53 |
|
putative oxidoreductase Fe-S binding subunit; Reviewed
Pssm-ID: 183733 [Multi-domain] Cd Length: 654 Bit Score: 186.49 E-value: 8.53e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447059109 8 DELTPAFTPLLAIKEASRCLLCHD-APCSQACPAQTDPGKFIRSIYFRNFKGAAETIRENNALGAVCARVCPTEKLCQSG 86
Cdd:PRK12769 209 DEIYLPFRADQAQREASRCLKCGEhSICEWTCPLHNHIPQWIELVKAGNIDAAVELSHQTNSLPEITGRVCPQDRLCEGA 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447059109 87 CTRAGVDTPIDIGRLQRFVTDFEQQTGMEIYQPGTKTLGK-VAIIGAGPAGLQASVTLTNQGYDVTIYEKEAHPGGWLRN 165
Cdd:PRK12769 289 CTLRDEYGAVTIGNIERYISDQALAKGWRPDLSQVTKSDKrVAIIGAGPAGLACADVLARNGVAVTVYDRHPEIGGLLTF 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447059109 166 GIPQFRLPQSVLDAEIARIEKMGVTIKCNNEVGNTLTLEQLKAENRAVLVTVgLSSGSGLSLFEHSD---VEIAVDFL-Q 241
Cdd:PRK12769 369 GIPAFKLDKSLLARRREIFSAMGIEFELNCEVGKDISLESLLEDYDAVFVGV-GTYRSMKAGLPNEDapgVYDALPFLiA 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447059109 242 RARQAQGDISIPQ---------SALIIGGGDVAMDVASTLKVLGCQAVTCVAREELDEFPASEKEFASARELGVSIIDGF 312
Cdd:PRK12769 448 NTKQVMGLEELPEepfintaglNVVVLGGGDTAMDCVRTALRHGASNVTCAYRRDEANMPGSKKEVKNAREEGANFEFNV 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447059109 313 TPVAVEGNK------VTFKHVRL--------------PG-ELTMAADKIILAVG-----------QHARLDAFAELEPqr 360
Cdd:PRK12769 528 QPVALELNEqghvcgIRFLRTRLgepdaqgrrrpvpiPGsEFVMPADAVIMAFGfnphgmpwlesHGVTVDKWGRIIA-- 605
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 447059109 361 NTIKTQNYQTRDPQVFAAGDIVEGDKTVVYAVKTGKEAAEAIHHYL 406
Cdd:PRK12769 606 DVESQYRYQTSNPKIFAGGDAVRGADLVVTAMAEGRHAAQGIIDWL 651
|
|
| PRK12809 |
PRK12809 |
putative oxidoreductase Fe-S binding subunit; Reviewed |
3-399 |
5.04e-47 |
|
putative oxidoreductase Fe-S binding subunit; Reviewed
Pssm-ID: 183762 [Multi-domain] Cd Length: 639 Bit Score: 170.59 E-value: 5.04e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447059109 3 QQNYLDELTPAFTPLLAIKEASRCLLC-HDAPCSQACPAQTDPGKFIRSIYFRNFKGAAETIRENNALGAVCARVCPTEK 81
Cdd:PRK12809 187 RKTHFGEIYCGLDPQQATYESDRCVYCaEKANCNWHCPLHNAIPDYIRLVQEGKIIEAAELCHQTSSLPEICGRVCPQDR 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447059109 82 LCQSGCTRAGVDTPIDIGRLQRFVTDFEQQTGmeiYQPG----TKTLGKVAIIGAGPAGLQASVTLTNQGYDVTIYEKEA 157
Cdd:PRK12809 267 LCEGACTLKDHSGAVSIGNLERYITDTALAMG---WRPDvskvVPRSEKVAVIGAGPAGLGCADILARAGVQVDVFDRHP 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447059109 158 HPGGWLRNGIPQFRLPQSVLDAEIARIEKMGVTIKCNNEVGNTLTLEQLKAENRAVLVTVgLSSGSGLSLFEHSD---VE 234
Cdd:PRK12809 344 EIGGMLTFGIPPFKLDKTVLSQRREIFTAMGIDFHLNCEIGRDITFSDLTSEYDAVFIGV-GTYGMMRADLPHEDapgVI 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447059109 235 IAVDFL-QRARQAQGdisIPQSA------------LIIGGGDVAMDVASTLKVLGCQAVTCVAREELDEFPASEKEFASA 301
Cdd:PRK12809 423 QALPFLtAHTRQLMG---LPESEeypltdvegkrvVVLGGGDTTMDCLRTSIRLNAASVTCAYRRDEVSMPGSRKEVVNA 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447059109 302 RELGVSIIDGFTPVAV----EGNKVTFKHVRL----PG-------------ELTMAADKIILAVGQHA-----------R 349
Cdd:PRK12809 500 REEGVEFQFNVQPQYIacdeDGRLTAVGLIRTamgePGpdgrrrprpvagsEFELPADVLIMAFGFQAhampwlqgsgiK 579
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 447059109 350 LDAFAELepQRNTIKTQNYQTRDPQVFAAGDIVEGDKTVVYAVKTGKEAA 399
Cdd:PRK12809 580 LDKWGLI--QTGDVGYLPTQTHLKKVFAGGDAVHGADLVVTAMAAGRQAA 627
|
|
| Fer4_20 |
pfam14691 |
Dihydroprymidine dehydrogenase domain II, 4Fe-4S cluster; Domain II of the enzyme ... |
8-113 |
6.68e-47 |
|
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: 156.55 E-value: 6.68e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447059109 8 DELTPAFTPLLAIKEASRCLLCHDAPCSQACPAQTDPGKFIRSIYFRNFKGAAETIRENNALGAVCARVCPTEKLCQSGC 87
Cdd:pfam14691 6 EEVALGYTEEEAIAEASRCLQCKDPPCVKGCPVHIDIPEFIKLIAEGNFEGAARIILETNPLPAICGRVCPQERQCEGAC 85
|
90 100
....*....|....*....|....*..
gi 447059109 88 TRAGV-DTPIDIGRLQRFVTDFEQQTG 113
Cdd:pfam14691 86 VLGKKgFEPVAIGRLERFAADWARENG 112
|
|
| PRK12779 |
PRK12779 |
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; ... |
4-402 |
1.34e-41 |
|
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; Provisional
Pssm-ID: 183740 [Multi-domain] Cd Length: 944 Bit Score: 156.92 E-value: 1.34e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447059109 4 QNYLDELTPAFT----PLLAIKEASRCLLCHDAPCS------------QACPAQTDPGKFIRSIYFRNFKGAAETIRENN 67
Cdd:PRK12779 164 QGYLGYQSLGYSvrevELFVWLEVMRDKQCDDKPCElgvlvqgkaepkGGCPVKIHIPEMLDLLGNGKHREALELIESCN 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447059109 68 ALGAVCARVCPTEKLCQSGCTRAgvDTPIDIGRLQRFVTDFEQQTGMEIYQP--------GTKTLGKVAIIGAGPAGLQA 139
Cdd:PRK12779 244 PLPNVTGRVCPQELQCQGVCTHT--KRPIEIGQLEWYLPQHEKLVNPNANERfagrispwAAAVKPPIAVVGSGPSGLIN 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447059109 140 SVTLTNQGYDVTIYEKEAHPGGWLRNGIPQFRLPQSVLDAEIARIEKMGVTIKCNNEVGNTLTLEQLKAEN--RAVLVTV 217
Cdd:PRK12779 322 AYLLAVEGFPVTVFEAFHDLGGVLRYGIPEFRLPNQLIDDVVEKIKLLGGRFVKNFVVGKTATLEDLKAAGfwKIFVGTG 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447059109 218 GLSSGSGLSLFEH-SDVEIAVDFLQRARQAQG-----DISIPQSA----LIIGGGDVAMDVASTLKVLGCQaVTCVAREE 287
Cdd:PRK12779 402 AGLPTFMNVPGEHlLGVMSANEFLTRVNLMRGldddyETPLPEVKgkevFVIGGGNTAMDAARTAKRLGGN-VTIVYRRT 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447059109 288 LDEFPASEKEFASARELGVSIIDGFTPVAVEGNKVTfKHV------------------RLP---GE-LTMAADKIILAVG 345
Cdd:PRK12779 481 KSEMPARVEELHHALEEGINLAVLRAPREFIGDDHT-HFVthalldvnelgepdksgrRSPkptGEiERVPVDLVIMALG 559
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447059109 346 QHAR---LDAFAELEPQR-NTIKTQ--NYQTRDPQVFAAGDIVEGDKTVVYAVKTGKEAAEAI 402
Cdd:PRK12779 560 NTANpimKDAEPGLKTNKwGTIEVEkgSQRTSIKGVYSGGDAARGGSTAIRAAGDGQAAAKEI 622
|
|
| PRK12770 |
PRK12770 |
putative glutamate synthase subunit beta; Provisional |
118-408 |
3.34e-40 |
|
putative glutamate synthase subunit beta; Provisional
Pssm-ID: 237197 [Multi-domain] Cd Length: 352 Bit Score: 146.29 E-value: 3.34e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447059109 118 QPGTKTLGKVAIIGAGPAGLQASVTLTNQGYDVTIYEKEAHPGGWLRNGIPQFRLPQSVLDAEIARIEKMGVT------I 191
Cdd:PRK12770 12 EKPPPTGKKVAIIGAGPAGLAAAGYLACLGYEVHVYDKLPEPGGLMLFGIPEFRIPIERVREGVKELEEAGVVfhtrtkV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447059109 192 KCNNE---------VGNTLTLEQLKAENRAVLVTVGL--SSGSGLSLFEHSDVEIAVDFLQRARQAQ-GDIS---IPQSA 256
Cdd:PRK12770 92 CCGEPlheeegdefVERIVSLEELVKKYDAVLIATGTwkSRKLGIPGEDLPGVYSALEYLFRIRAAKlGYLPwekVPPVE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447059109 257 ----LIIGGGDVAMDVASTLKVLGCQAVTCVAREELDEFPASEKEFASARELGVSIIDGFTPVAVEGN----KVTFKHVR 328
Cdd:PRK12770 172 gkkvVVVGAGLTAVDAALEAVLLGAEKVYLAYRRTINEAPAGKYEIERLIARGVEFLELVTPVRIIGEgrveGVELAKMR 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447059109 329 L--------------PG-ELTMAADKIILAVGQH-----ARLDAFAELEPqRNTIKTQN-YQTRDPQVFAAGDIVEGDKT 387
Cdd:PRK12770 252 LgepdesgrprpvpiPGsEFVLEADTVVFAIGEIptppfAKECLGIELNR-KGEIVVDEkHMTSREGVFAAGDVVTGPSK 330
|
330 340
....*....|....*....|.
gi 447059109 388 VVYAVKTGKEAAEAIHHYLEG 408
Cdd:PRK12770 331 IGKAIKSGLRAAQSIHEWLDL 351
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
126-395 |
1.25e-20 |
|
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: 91.61 E-value: 1.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447059109 126 KVAIIGAGPAGLQASVTLTNQGYDVTIYEKEahpGGWLRNG-IPQFRLPQSVLDAEIARIE------KMGVTIKCNNEVG 198
Cdd:pfam07992 2 DVVVIGGGPAGLAAALTLAQLGGKVTLIEDE---GTCPYGGcVLSKALLGAAEAPEIASLWadlykrKEEVVKKLNNGIE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447059109 199 NTLTLEQLKAENRAVLVTVGLSSGSGLSLFEHSDVEIA----------------VDFLQRA-RQAQGDIS--IPQSALII 259
Cdd:pfam07992 79 VLLGTEVVSIDPGAKKVVLEELVDGDGETITYDRLVIAtgarprlppipgvelnVGFLVRTlDSAEALRLklLPKRVVVV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447059109 260 GGGDVAMDVASTLKVLGCQAVTCVAREELdeFPASEKEFASA-----RELGVSIIDGFTPVAVEGNKVTFKhVRLPGELT 334
Cdd:pfam07992 159 GGGYIGVELAAALAKLGKEVTLIEALDRL--LRAFDEEISAAlekalEKNGVEVRLGTSVKEIIGDGDGVE-VILKDGTE 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447059109 335 MAADKIILAVGQHARLDAFAEL---EPQRNTIKTQNY-QTRDPQVFAAGDI-VEGDKTVVYAVKTG 395
Cdd:pfam07992 236 IDADLVVVAIGRRPNTELLEAAgleLDERGGIVVDEYlRTSVPGIYAAGDCrVGGPELAQNAVAQG 301
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
126-409 |
1.43e-20 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 91.33 E-value: 1.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447059109 126 KVAIIGAGPAGLQASVTLTNQGYDVTIYEKEAhPGGWLRN--------GIPQFRLPQSVLDAEIARIEKMGVTIKcNNEV 197
Cdd:COG0492 2 DVVIIGAGPAGLTAAIYAARAGLKTLVIEGGE-PGGQLATtkeienypGFPEGISGPELAERLREQAERFGAEIL-LEEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447059109 198 gNTLTLEQ----LKAEN------RAVLVTVGLssgsglslfehSDVEIAVDFLQRAR--------QAQGDISIPQSALII 259
Cdd:COG0492 80 -TSVDKDDgpfrVTTDDgteyeaKAVIIATGA-----------GPRKLGLPGEEEFEgrgvsycaTCDGFFFRGKDVVVV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447059109 260 GGGDVAMDVASTLKVLGCQaVTCVAREelDEFPASEKEFASAREL-GVSIIDGFTPVAVEGN----KVTFKHVRLPGELT 334
Cdd:COG0492 148 GGGDSALEEALYLTKFASK-VTLIHRR--DELRASKILVERLRANpKIEVLWNTEVTEIEGDgrveGVTLKNVKTGEEKE 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447059109 335 MAADKIILAVGQHARLDAFAELE---PQRNTIKT-QNYQTRDPQVFAAGDIVEGD-KTVVYAVKTGKEAAEAIHHYLEGA 409
Cdd:COG0492 225 LEVDGVFVAIGLKPNTELLKGLGlelDEDGYIVVdEDMETSVPGVFAAGDVRDYKyRQAATAAGEGAIAALSAARYLEPL 304
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
253-402 |
1.89e-11 |
|
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: 64.83 E-value: 1.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447059109 253 PQSALIIGGGDVAMDVASTLKVLGCQaVTCVAREE-LdeFPASEKEFASA-----RELGVSIIDGFTPVAVEG-NKVTfk 325
Cdd:COG0446 124 GKRAVVIGGGPIGLELAEALRKRGLK-VTLVERAPrL--LGVLDPEMAALleeelREHGVELRLGETVVAIDGdDKVA-- 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447059109 326 hVRLPGELTMAADKIILAVGQHARLDaFAELEP----QRNTIKT-QNYQTRDPQVFAAGDIVE-----GDKTVVY----- 390
Cdd:COG0446 199 -VTLTDGEEIPADLVVVAPGVRPNTE-LAKDAGlalgERGWIKVdETLQTSDPDVYAAGDCAEvphpvTGKTVYIplasa 276
|
170
....*....|..
gi 447059109 391 AVKTGKEAAEAI 402
Cdd:COG0446 277 ANKQGRVAAENI 288
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
255-325 |
3.14e-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: 56.06 E-value: 3.14e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447059109 255 SALIIGGGDVAMDVASTLKVLGCQaVTCVAReeLDEF-PASEKEFASA-----RELGVSIIDGFTPVAVEGNKVTFK 325
Cdd:pfam00070 1 RVVVVGGGYIGLELAGALARLGSK-VTVVER--RDRLlPGFDPEIAKIlqeklEKNGIEFLLNTTVEAIEGNGDGVV 74
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
252-382 |
5.51e-10 |
|
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: 60.87 E-value: 5.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447059109 252 IPQSALIIGGGDVAMDVASTLKVLGCQaVTCVAReeLDEF-PASEKEFASA-----RELGVSIIDGFTPVAVE----GNK 321
Cdd:COG1249 167 LPKSLVVIGGGYIGLEFAQIFARLGSE-VTLVER--GDRLlPGEDPEISEAlekalEKEGIDILTGAKVTSVEktgdGVT 243
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447059109 322 VTFKHVRlpGELTMAADKIILAVGQHARLDAF----AELEP-QRNTIKT-QNYQTRDPQVFAAGDIV 382
Cdd:COG1249 244 VTLEDGG--GEEAVEADKVLVATGRRPNTDGLgleaAGVELdERGGIKVdEYLRTSVPGIYAIGDVT 308
|
|
| COG1233 |
COG1233 |
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ... |
126-173 |
1.28e-09 |
|
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440846 [Multi-domain] Cd Length: 491 Bit Score: 59.86 E-value: 1.28e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 447059109 126 KVAIIGAGPAGLQASVTLTNQGYDVTIYEKEAHPGGWLRngipQFRLP 173
Cdd:COG1233 5 DVVVIGAGIGGLAAAALLARAGYRVTVLEKNDTPGGRAR----TFERP 48
|
|
| PRK07208 |
PRK07208 |
hypothetical protein; Provisional |
126-161 |
1.81e-09 |
|
hypothetical protein; Provisional
Pssm-ID: 235967 [Multi-domain] Cd Length: 479 Bit Score: 59.13 E-value: 1.81e-09
10 20 30
....*....|....*....|....*....|....*.
gi 447059109 126 KVAIIGAGPAGLQASVTLTNQGYDVTIYEKEAHPGG 161
Cdd:PRK07208 6 SVVIIGAGPAGLTAAYELLKRGYPVTVLEADPVVGG 41
|
|
| HemY |
COG1232 |
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ... |
126-164 |
2.30e-09 |
|
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: 58.69 E-value: 2.30e-09
10 20 30
....*....|....*....|....*....|....*....
gi 447059109 126 KVAIIGAGPAGLQASVTLTNQGYDVTIYEKEAHPGGWLR 164
Cdd:COG1232 3 RVAVIGGGIAGLTAAYRLAKAGHEVTVLEASDRVGGLIR 41
|
|
| TRX_reduct |
TIGR01292 |
thioredoxin-disulfide reductase; This model describes thioredoxin-disulfide reductase, a ... |
126-406 |
2.39e-09 |
|
thioredoxin-disulfide reductase; This model describes thioredoxin-disulfide reductase, a member of the pyridine nucleotide-disulphide oxidoreductases (pfam00070). [Energy metabolism, Electron transport]
Pssm-ID: 273540 [Multi-domain] Cd Length: 299 Bit Score: 58.02 E-value: 2.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447059109 126 KVAIIGAGPAGLQASVTLTNQGYDVTIYEKEAhPGGWL------------RNGIPQFRLPQS-----------VLDAEIA 182
Cdd:TIGR01292 1 DVIIIGAGPAGLTAAIYAARANLKPLLIEGME-PGGQLttttevenypgfPEGISGPELMEKmkeqavkfgaeIIYEEVI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447059109 183 RIEKMGVTIKCNNEVGNTLTleqlkaeNRAVLVTVGLssgsglslfEHSDVEIAV--DFLQRARQA----QGDISIPQSA 256
Cdd:TIGR01292 80 KVDKSDRPFKVYTGDGKEYT-------AKAVIIATGA---------SARKLGIPGedEFWGRGVSYcatcDGPFFKNKEV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447059109 257 LIIGGGDVAMDVASTLKVLGCQaVTCVAREelDEFPASEKEFASAREL-GVSIIDGFTPVAVEG----NKVTFKHVRLPG 331
Cdd:TIGR01292 144 AVVGGGDSAIEEALYLTRIAKK-VTLVHRR--DKFRAEKILLDRLKKNpKIEFLWNSTVEEIVGdnkvEGVKIKNTVTGE 220
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447059109 332 ELTMAADKIILAVGQHARLDAFAELE--PQRNTIKTQNY-QTRDPQVFAAGDIVE-GDKTVVYAVKTGKEAAEAIHHYL 406
Cdd:TIGR01292 221 EEELEVDGVFIAIGHEPNTELLKGLLelDENGYIVTDEGmRTSVPGVFAAGDVRDkGYRQAVTAAGDGCIAALSAERYL 299
|
|
| HdrA |
COG1148 |
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion]; |
126-197 |
3.43e-09 |
|
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
Pssm-ID: 440762 [Multi-domain] Cd Length: 563 Bit Score: 58.72 E-value: 3.43e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447059109 126 KVAIIGAGPAGLQASVTLTNQGYDVTIYEKEAHPGGWLRN---GIPQFRLPQSVLDAEIARIEKM-GVTIKCNNEV 197
Cdd:COG1148 142 RALVIGGGIAGMTAALELAEQGYEVYLVEKEPELGGRAAQlhkTFPGLDCPQCILEPLIAEVEANpNITVYTGAEV 217
|
|
| NAD_binding_8 |
pfam13450 |
NAD(P)-binding Rossmann-like domain; |
129-178 |
4.00e-09 |
|
NAD(P)-binding Rossmann-like domain;
Pssm-ID: 433218 [Multi-domain] Cd Length: 67 Bit Score: 52.53 E-value: 4.00e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 447059109 129 IIGAGPAGLQASVTLTNQGYDVTIYEKEAHPGGWLRNgipqFRLPQSVLD 178
Cdd:pfam13450 1 IVGAGLAGLVAAALLAKRGFRVLVLEKRDRLGGNAYS----YRVPGYVFD 46
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
126-383 |
3.61e-08 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 55.15 E-value: 3.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447059109 126 KVAIIGAGPAGLQASVTLTNQGYD--VTIYEKEAHP-----------GG--------------WLRNGIpQFRLPQSV-- 176
Cdd:COG1251 3 RIVIIGAGMAGVRAAEELRKLDPDgeITVIGAEPHPpynrpplskvlAGetdeedlllrpadfYEENGI-DLRLGTRVta 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447059109 177 LDAEiARIekmgVTIKCNNEVG------------NTLTLEQLKAENRAVLVTVglssgsglslfehSDVEiavDFLQRAR 244
Cdd:COG1251 82 IDRA-ART----VTLADGETLPydklvlatgsrpRVPPIPGADLPGVFTLRTL-------------DDAD---ALRAALA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447059109 245 QAQgdisipqSALIIGGGDVAMDVASTLKVLGCQaVTCVAREE------LDEfPASEkEFASA-RELGVSIIDGFTPVAV 317
Cdd:COG1251 141 PGK-------RVVVIGGGLIGLEAAAALRKRGLE-VTVVERAPrllprqLDE-EAGA-LLQRLlEALGVEVRLGTGVTEI 210
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447059109 318 EG-NKVTfkHVRLPGELTMAADKIILAVGQHARlDAFAE---LEPQRNtIKTQNY-QTRDPQVFAAGDIVE 383
Cdd:COG1251 211 EGdDRVT--GVRLADGEELPADLVVVAIGVRPN-TELARaagLAVDRG-IVVDDYlRTSDPDIYAAGDCAE 277
|
|
| CzcO |
COG2072 |
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ... |
127-172 |
7.80e-08 |
|
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ion transport and metabolism];
Pssm-ID: 441675 [Multi-domain] Cd Length: 414 Bit Score: 54.10 E-value: 7.80e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 447059109 127 VAIIGAGPAGLQASVTLTNQGYDVTIYEKEAHPGG-WLRNGIPQFRL 172
Cdd:COG2072 9 VVVIGAGQAGLAAAYHLRRAGIDFVVLEKADDVGGtWRDNRYPGLRL 55
|
|
| PRK09754 |
PRK09754 |
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional |
129-381 |
2.13e-07 |
|
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional
Pssm-ID: 170080 [Multi-domain] Cd Length: 396 Bit Score: 52.62 E-value: 2.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447059109 129 IIGAGPAGLQASVTLTNQGYDVTI----------YEKEAHPGGWLRNGIPQfrlPQSVLDAEI---ARIE-KMGVTIK-- 192
Cdd:PRK09754 8 IVGGGQAAAMAAASLRQQGFTGELhlfsderhlpYERPPLSKSMLLEDSPQ---LQQVLPANWwqeNNVHlHSGVTIKtl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447059109 193 --CNNEV----GNTLTLEQL--KAENRAVLVTVGLSSGSGLSLFEHSDVEiavdflQRARQAqgdISIPQSALIIGGGDV 264
Cdd:PRK09754 85 grDTRELvltnGESWHWDQLfiATGAAARPLPLLDALGERCFTLRHAGDA------ARLREV---LQPERSVVIVGAGTI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447059109 265 AMDVASTLKVLGC------QAVTCVAREEldefPASEKEFASAR--ELGVSI-IDGFTPVAVEGNKVTFKhvrLPGELTM 335
Cdd:PRK09754 156 GLELAASATQRRCkvtvieLAATVMGRNA----PPPVQRYLLQRhqQAGVRIlLNNAIEHVVDGEKVELT---LQSGETL 228
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 447059109 336 AADKIILAVGQHAR--LDAFAELEPQRNTIKTQNYQTRDPQVFAAGDI 381
Cdd:PRK09754 229 QADVVIYGIGISANdqLAREANLDTANGIVIDEACRTCDPAIFAGGDV 276
|
|
| COG3349 |
COG3349 |
Uncharacterized protein, contains NAD-binding domain and a Fe-S cluster [General function ... |
125-161 |
2.63e-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: 52.55 E-value: 2.63e-07
10 20 30
....*....|....*....|....*....|....*..
gi 447059109 125 GKVAIIGAGPAGLQASVTLTNQGYDVTIYEKEAHPGG 161
Cdd:COG3349 4 PRVVVVGGGLAGLAAAVELAEAGFRVTLLEARPRLGG 40
|
|
| PRK07233 |
PRK07233 |
hypothetical protein; Provisional |
126-161 |
2.90e-07 |
|
hypothetical protein; Provisional
Pssm-ID: 235977 [Multi-domain] Cd Length: 434 Bit Score: 52.20 E-value: 2.90e-07
10 20 30
....*....|....*....|....*....|....*.
gi 447059109 126 KVAIIGAGPAGLQASVTLTNQGYDVTIYEKEAHPGG 161
Cdd:PRK07233 1 KIAIVGGGIAGLAAAYRLAKRGHEVTVFEADDQLGG 36
|
|
| COG3380 |
COG3380 |
Predicted NAD/FAD-dependent oxidoreductase [General function prediction only]; |
126-161 |
6.66e-07 |
|
Predicted NAD/FAD-dependent oxidoreductase [General function prediction only];
Pssm-ID: 442607 [Multi-domain] Cd Length: 331 Bit Score: 50.65 E-value: 6.66e-07
10 20 30
....*....|....*....|....*....|....*.
gi 447059109 126 KVAIIGAGPAGLQASVTLTNQGYDVTIYEKEAHPGG 161
Cdd:COG3380 5 DIAIIGAGIAGLAAARALQDAGHEVTVFEKSRGVGG 40
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
239-408 |
7.33e-07 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 50.90 E-value: 7.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447059109 239 FLQRARQAQGDIsipqsaLIIGGG----DVAMDVASTLKVLGCQA--------VTCVAREE--LDEFPASEKEFASA--R 302
Cdd:COG1252 141 FERAERRRLLTI------VVVGGGptgvELAGELAELLRKLLRYPgidpdkvrITLVEAGPriLPGLGEKLSEAAEKelE 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447059109 303 ELGVSIIDGFTPVAVEGNKVTFKHvrlpGElTMAADKIILAVGQHARlDAFAELE---PQRNTIKTQNYQ--TRDPQVFA 377
Cdd:COG1252 215 KRGVEVHTGTRVTEVDADGVTLED----GE-EIPADTVIWAAGVKAP-PLLADLGlptDRRGRVLVDPTLqvPGHPNVFA 288
|
170 180 190
....*....|....*....|....*....|....*....
gi 447059109 378 AGDI--VEGD------KTVVYAVKTGKEAAEAIHHYLEG 408
Cdd:COG1252 289 IGDCaaVPDPdgkpvpKTAQAAVQQAKVLAKNIAALLRG 327
|
|
| PRK05249 |
PRK05249 |
Si-specific NAD(P)(+) transhydrogenase; |
252-382 |
4.07e-06 |
|
Si-specific NAD(P)(+) transhydrogenase;
Pssm-ID: 235373 [Multi-domain] Cd Length: 461 Bit Score: 48.61 E-value: 4.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447059109 252 IPQSALIIGGGDVAMDVASTLKVLGCQaVTCV-AREELDEFpaSEKEFASA-----RELGVSIIDGFTPVAVEG--NKVT 323
Cdd:PRK05249 174 LPRSLIIYGAGVIGCEYASIFAALGVK-VTLInTRDRLLSF--LDDEISDAlsyhlRDSGVTIRHNEEVEKVEGgdDGVI 250
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447059109 324 fkhVRLPGELTMAADKIILAVGQHARLDAF----AELEP-QRNTIK-TQNYQTRDPQVFAAGDIV 382
Cdd:PRK05249 251 ---VHLKSGKKIKADCLLYANGRTGNTDGLnlenAGLEAdSRGQLKvNENYQTAVPHIYAVGDVI 312
|
|
| YobN |
COG1231 |
Monoamine oxidase [Amino acid transport and metabolism]; |
126-161 |
5.20e-06 |
|
Monoamine oxidase [Amino acid transport and metabolism];
Pssm-ID: 440844 [Multi-domain] Cd Length: 440 Bit Score: 48.38 E-value: 5.20e-06
10 20 30
....*....|....*....|....*....|....*.
gi 447059109 126 KVAIIGAGPAGLQASVTLTNQGYDVTIYEKEAHPGG 161
Cdd:COG1231 9 DVVIVGAGLAGLAAARELRKAGLDVTVLEARDRVGG 44
|
|
| mhpA |
PRK06183 |
bifunctional 3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic acid hydroxylase; |
127-184 |
7.31e-06 |
|
bifunctional 3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic acid hydroxylase;
Pssm-ID: 235727 [Multi-domain] Cd Length: 500 Bit Score: 47.98 E-value: 7.31e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 447059109 127 VAIIGAGPAGLQASVTLTNQGYDVTIYEKEAHPggwlrngipqFRLPQSV-LDAEIARI 184
Cdd:PRK06183 13 VVIVGAGPVGLTLANLLGQYGVRVLVLERWPTL----------YDLPRAVgIDDEALRV 61
|
|
| PLN02487 |
PLN02487 |
zeta-carotene desaturase |
126-161 |
1.06e-05 |
|
zeta-carotene desaturase
Pssm-ID: 215268 [Multi-domain] Cd Length: 569 Bit Score: 47.49 E-value: 1.06e-05
10 20 30
....*....|....*....|....*....|....*.
gi 447059109 126 KVAIIGAGPAGLQASVTLTNQGYDVTIYEKEAHPGG 161
Cdd:PLN02487 77 KVAIIGAGLAGMSTAVELLDQGHEVDIYESRPFIGG 112
|
|
| PRK13748 |
PRK13748 |
putative mercuric reductase; Provisional |
251-399 |
1.41e-05 |
|
putative mercuric reductase; Provisional
Pssm-ID: 184298 [Multi-domain] Cd Length: 561 Bit Score: 47.07 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447059109 251 SIPQSALIIGGGDVAMDVASTLKVLGCQaVTCVAREEL--DEFPA-SEKEFASARELGVSIID--GFTPVAVEGNKVTFK 325
Cdd:PRK13748 268 TIPERLAVIGSSVVALELAQAFARLGSK-VTILARSTLffREDPAiGEAVTAAFRAEGIEVLEhtQASQVAHVDGEFVLT 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447059109 326 HVRlpGELTmaADKIILAVGQHAR-----LDAFA-ELEPQRNTIKTQNYQTRDPQVFAAGDIVEGDKTVVYAVKTGKEAA 399
Cdd:PRK13748 347 TGH--GELR--ADKLLVATGRAPNtrslaLDAAGvTVNAQGAIVIDQGMRTSVPHIYAAGDCTDQPQFVYVAAAAGTRAA 422
|
|
| PRK04965 |
PRK04965 |
NADH:flavorubredoxin reductase NorW; |
240-383 |
2.02e-05 |
|
NADH:flavorubredoxin reductase NorW;
Pssm-ID: 179902 [Multi-domain] Cd Length: 377 Bit Score: 46.45 E-value: 2.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447059109 240 LQRARQAQGDISIPQSALIIGGG----DVAMDVASTLKvlgcqAVTCVAREE------LDEFPASEKEFAsARELGVSII 309
Cdd:PRK04965 128 QQEYRAAETQLRDAQRVLVVGGGligtELAMDLCRAGK-----AVTLVDNAAsllaslMPPEVSSRLQHR-LTEMGVHLL 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447059109 310 DGFTPVAVE----GNKVTFKHVRlpgelTMAADKIILAVGQHA--RLDAFAELEPQRNTIKTQNYQTRDPQVFAAGDIVE 383
Cdd:PRK04965 202 LKSQLQGLEktdsGIRATLDSGR-----SIEVDAVIAAAGLRPntALARRAGLAVNRGIVVDSYLQTSAPDIYALGDCAE 276
|
|
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
252-402 |
2.07e-05 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 46.68 E-value: 2.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447059109 252 IPQSALIIGGGDVAMDVASTLKVLGCQaVTCVarEELDE-FPASEKEFASA-----RELGVSIIDG--FTPVAVEGNKVT 323
Cdd:PRK06416 171 VPKSLVVIGGGYIGVEFASAYASLGAE-VTIV--EALPRiLPGEDKEISKLaeralKKRGIKIKTGakAKKVEQTDDGVT 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447059109 324 FKHVRLPGELTMAADKIILAVGQHARLDAF----AELEPQRNTIKTQNY-QTRDPQVFAAGDIVEGDKTVVYAVKTGKEA 398
Cdd:PRK06416 248 VTLEDGGKEETLEADYVLVAVGRRPNTENLgleeLGVKTDRGFIEVDEQlRTNVPNIYAIGDIVGGPMLAHKASAEGIIA 327
|
....
gi 447059109 399 AEAI 402
Cdd:PRK06416 328 AEAI 331
|
|
| UbiH |
COG0654 |
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ... |
126-164 |
2.89e-05 |
|
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme transport and metabolism, Energy production and conversion]; 2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases is part of the Pathway/BioSystem: Ubiquinone biosynthesis
Pssm-ID: 440419 [Multi-domain] Cd Length: 326 Bit Score: 45.70 E-value: 2.89e-05
10 20 30
....*....|....*....|....*....|....*....
gi 447059109 126 KVAIIGAGPAGLQASVTLTNQGYDVTIYEKEAHPGGWLR 164
Cdd:COG0654 5 DVLIVGGGPAGLALALALARAGIRVTVVERAPPPRPDGR 43
|
|
| YhiN |
COG2081 |
Predicted flavoprotein YhiN [General function prediction only]; |
128-160 |
4.20e-05 |
|
Predicted flavoprotein YhiN [General function prediction only];
Pssm-ID: 441684 [Multi-domain] Cd Length: 402 Bit Score: 45.43 E-value: 4.20e-05
10 20 30
....*....|....*....|....*....|...
gi 447059109 128 AIIGAGPAGLQASVTLTNQGYDVTIYEKEAHPG 160
Cdd:COG2081 1 IVIGAGAAGLMAAITAAERGARVLLLEKNPKVG 33
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
126-217 |
4.64e-05 |
|
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.
Pssm-ID: 425450 [Multi-domain] Cd Length: 80 Bit Score: 41.42 E-value: 4.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447059109 126 KVAIIGAGPAGLQASVTLTNQGYDVTIYEKEAHPGgwlrngipqfrlpqSVLDAEIARI-----EKMGVTIKCNNEVgnt 200
Cdd:pfam00070 1 RVVVVGGGYIGLELAGALARLGSKVTVVERRDRLL--------------PGFDPEIAKIlqeklEKNGIEFLLNTTV--- 63
|
90
....*....|....*..
gi 447059109 201 ltlEQLKAENRAVLVTV 217
Cdd:pfam00070 64 ---EAIEGNGDGVVVVL 77
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
253-382 |
4.98e-05 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 45.17 E-value: 4.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447059109 253 PQSALIIGGGDVAMDVASTLKVLGCQaVTCVAReeLDEF-PASEKEFASA--RELG--VSIIDGFTPVAVEGNKVTFKHV 327
Cdd:PRK06292 169 PKSLAVIGGGVIGLELGQALSRLGVK-VTVFER--GDRIlPLEDPEVSKQaqKILSkeFKIKLGAKVTSVEKSGDEKVEE 245
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447059109 328 RLPG--ELTMAADKIILAVGQHARLDAFA------ELEPqRNTIKTQNY-QTRDPQVFAAGDIV 382
Cdd:PRK06292 246 LEKGgkTETIEADYVLVATGRRPNTDGLGlentgiELDE-RGRPVVDEHtQTSVPGIYAAGDVN 308
|
|
| Ppro0129 |
COG2907 |
Predicted flavin-containing amine oxidase [General function prediction only]; |
126-161 |
5.17e-05 |
|
Predicted flavin-containing amine oxidase [General function prediction only];
Pssm-ID: 442151 [Multi-domain] Cd Length: 423 Bit Score: 45.11 E-value: 5.17e-05
10 20 30
....*....|....*....|....*....|....*.
gi 447059109 126 KVAIIGAGPAGLQASVTLtNQGYDVTIYEKEAHPGG 161
Cdd:COG2907 5 RIAVIGSGISGLTAAWLL-SRRHDVTLFEANDRLGG 39
|
|
| PRK06753 |
PRK06753 |
hypothetical protein; Provisional |
126-155 |
6.01e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 168661 [Multi-domain] Cd Length: 373 Bit Score: 44.68 E-value: 6.01e-05
10 20 30
....*....|....*....|....*....|
gi 447059109 126 KVAIIGAGPAGLQASVTLTNQGYDVTIYEK 155
Cdd:PRK06753 2 KIAIIGAGIGGLTAAALLQEQGHEVKVFEK 31
|
|
| HI0933_like |
pfam03486 |
HI0933-like protein; |
126-160 |
8.06e-05 |
|
HI0933-like protein;
Pssm-ID: 427330 [Multi-domain] Cd Length: 406 Bit Score: 44.49 E-value: 8.06e-05
10 20 30
....*....|....*....|....*....|....*
gi 447059109 126 KVAIIGAGPAGLQASVTLTNQGYDVTIYEKEAHPG 160
Cdd:pfam03486 2 DVIVIGGGAAGLMAAISAAKRGRRVLLIEKGKKLG 36
|
|
| Ala_dh_like |
cd01620 |
Alanine dehydrogenase and related dehydrogenases; Alanine dehydrogenase/Transhydrogenase, such ... |
69-175 |
1.46e-04 |
|
Alanine dehydrogenase and related dehydrogenases; Alanine dehydrogenase/Transhydrogenase, such as the hexameric L-alanine dehydrogenase of Phormidium lapideum, contain 2 Rossmann fold-like domains linked by an alpha helical region. Related proteins include Saccharopine Dehydrogenase (SDH), bifunctional lysine ketoglutarate reductase /saccharopine dehydrogenase enzyme, N(5)-(carboxyethyl)ornithine synthase, and Rubrum transdehydrogenase. Alanine dehydrogenase (L-AlaDH) catalyzes the NAD-dependent conversion of pyrucate to L-alanine via reductive amination. Transhydrogenases found in bacterial and inner mitochondrial membranes link NAD(P)(H)-dependent redox reactions to proton translocation. The energy of the proton electrochemical gradient (delta-p), generated by the respiratory electron transport chain, is consumed by transhydrogenase in NAD(P)+ reduction. Transhydrogenase is likely involved in the regulation of the citric acid cycle. Rubrum transhydrogenase has 3 components, dI, dII, and dIII. dII spans the membrane while dI and dIII protrude on the cytoplasmic/matirx side. DI contains 2 domains with Rossmann folds, linked by a long alpha helix, and contains a NAD binding site. Two dI polypeptides (represented in this sub-family) spontaneously form a heterotrimer with one dIII in the absence of dII. In the heterotrimer, both dI chains may bind NAD, but only one is well-ordered. dIII also binds a well-ordered NADP, but in a different orientation than classical Rossmann domains.
Pssm-ID: 240621 [Multi-domain] Cd Length: 317 Bit Score: 43.55 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447059109 69 LGAVCARVCpTEKLCQSGCTRAGVDT--PIDIGRLQRF------------VTDFE-QQTGMEIYQPGTKTlGKVAIIGAG 133
Cdd:cd01620 94 LHAATNRGV-VEVLMRKKLTAYALEDleNDFRPRLAPNsniagyagvqlgAYELArIQGGRMGGAGGVPP-AKVLIIGAG 171
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 447059109 134 PAGLQASVTLTNQGYDVTIYE-KEAHPGGWLRNGIPQFRLPQS 175
Cdd:cd01620 172 VVGLGAAKIAKKLGANVLVYDiKEEKLKGVETLGGSRLRYSQK 214
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
122-197 |
1.68e-04 |
|
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.
Pssm-ID: 400379 [Multi-domain] Cd Length: 301 Bit Score: 43.08 E-value: 1.68e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447059109 122 KTLGKVAIIGAGPAGLQASVTLTNQGYDVTIYEkeahpggwlRNGIPQFRLPQSVLDAEIARIEKMGVTIKCNNEV 197
Cdd:pfam07992 150 LLPKRVVVVGGGYIGVELAAALAKLGKEVTLIE---------ALDRLLRAFDEEISAALEKALEKNGVEVRLGTSV 216
|
|
| DAO |
pfam01266 |
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ... |
126-392 |
1.95e-04 |
|
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: 43.16 E-value: 1.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447059109 126 KVAIIGAGPAGLQASVTLTNQGYDVTIYEKEAHPG--------GWLRNGI---PQFRLPQSVLDA--EIARIEKmgvtik 192
Cdd:pfam01266 1 DVVVIGGGIVGLSTAYELARRGLSVTLLERGDDPGsgasgrnaGLIHPGLrylEPSELARLALEAldLWEELEE------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447059109 193 cnnEVGNTLTLEQlkaeNRAVLVTVGLSSGSGLSLFE-HSDVEIAVDFLQRARQAQGDisiPQSALIIGG----GDVAMD 267
Cdd:pfam01266 75 ---ELGIDCGFRR----CGVLVLARDEEEEALEKLLAaLRRLGVPAELLDAEELRELE---PLLPGLRGGlfypDGGHVD 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447059109 268 VAstlkvlgcQAVTCVAREeldefpasekefasARELGVSIIDGfTPV--AVEGNKVTfkHVRLPGEltmaADKIILAVG 345
Cdd:pfam01266 145 PA--------RLLRALARA--------------AEALGVRIIEG-TEVtgIEEEGGVW--GVVTTGE----ADAVVNAAG 195
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 447059109 346 QHARLDAFAELEPQRNTIKTQNYQTR---DPQVFAAGDIVEGDKTVVYAV 392
Cdd:pfam01266 196 AWADLLALPGLRLPVRPVRGQVLVLEplpEALLILPVPITVDPGRGVYLR 245
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
252-381 |
2.06e-04 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 43.27 E-value: 2.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447059109 252 IPQSALIIGGGDVAMDVASTLKVLGCQaVTCV-------AREELDefpASEKEFASARELGVSIIDGFTPVAVE--GNKV 322
Cdd:PRK06370 170 LPEHLVIIGGGYIGLEFAQMFRRFGSE-VTVIergprllPREDED---VAAAVREILEREGIDVRLNAECIRVErdGDGI 245
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447059109 323 TFKHVRLPGELTMAADKIILAVGQHARLDAFAeLEP------QRNTIKTQNY-QTRDPQVFAAGDI 381
Cdd:PRK06370 246 AVGLDCNGGAPEITGSHILVAVGRVPNTDDLG-LEAagvetdARGYIKVDDQlRTTNPGIYAAGDC 310
|
|
| crtI_fam |
TIGR02734 |
phytoene desaturase; Phytoene is converted to lycopene by desaturation at four (two ... |
127-161 |
2.30e-04 |
|
phytoene desaturase; Phytoene is converted to lycopene by desaturation at four (two symmetrical pairs of) sites. This is achieved by two enzymes (crtP and crtQ) in cyanobacteria (Gloeobacter being an exception) and plants, but by a single enzyme in most other bacteria and in fungi. This single enzyme is called the bacterial-type phytoene desaturase, or CrtI. Most members of this family, part of the larger pfam01593, which also contains amino oxidases, are CrtI itself; it is likely that all members act on either phytoene or on related compounds such as dehydrosqualene, for carotenoid biosynthesis. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 274273 [Multi-domain] Cd Length: 495 Bit Score: 43.42 E-value: 2.30e-04
10 20 30
....*....|....*....|....*....|....*
gi 447059109 127 VAIIGAGPAGLQASVTLTNQGYDVTIYEKEAHPGG 161
Cdd:TIGR02734 1 AVVIGAGFGGLALAIRLAAAGIPVTVVEQRDKPGG 35
|
|
| TGR |
TIGR01438 |
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ... |
251-400 |
2.76e-04 |
|
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member of the pyridine nucleotide disulfide oxidoreductase family contains a C-terminal motif Cys-SeCys-Gly, where SeCys is selenocysteine encoded by TGA (in some sequence reports interpreted as a stop codon). In some members of this subfamily, Cys-SeCys-Gly is replaced by Cys-Cys-Gly. The reach of the selenium atom at the C-term arm of the protein is proposed to allow broad substrate specificity.
Pssm-ID: 273624 [Multi-domain] Cd Length: 484 Bit Score: 42.92 E-value: 2.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447059109 251 SIPQSALIIGGGDVAMDVASTLKVLGcQAVTCVAREEL----DEFPASeKEFASARELGVSIIDGFTPVAVE--GNKVTF 324
Cdd:TIGR01438 178 YCPGKTLVVGASYVALECAGFLAGIG-LDVTVMVRSILlrgfDQDCAN-KVGEHMEEHGVKFKRQFVPIKVEqiEAKVLV 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447059109 325 KHVRLPGELTMAADKIILAVGQHARLDAF----AELEPQRNTIK---TQNYQTRDPQVFAAGDIVEGDKTVV-YAVKTGK 396
Cdd:TIGR01438 256 EFTDSTNGIEEEYDTVLLAIGRDACTRKLnlenVGVKINKKTGKipaDEEEQTNVPYIYAVGDILEDKPELTpVAIQAGR 335
|
....
gi 447059109 397 EAAE 400
Cdd:TIGR01438 336 LLAQ 339
|
|
| PLN02976 |
PLN02976 |
amine oxidase |
126-161 |
2.84e-04 |
|
amine oxidase
Pssm-ID: 215527 [Multi-domain] Cd Length: 1713 Bit Score: 43.32 E-value: 2.84e-04
10 20 30
....*....|....*....|....*....|....*.
gi 447059109 126 KVAIIGAGPAGLQASVTLTNQGYDVTIYEKEAHPGG 161
Cdd:PLN02976 695 KIIVVGAGPAGLTAARHLQRQGFSVTVLEARSRIGG 730
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
125-197 |
3.25e-04 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 42.44 E-value: 3.25e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447059109 125 GKVAIIGAGPAGLQASVTLTNQGYDVTIyekeAHPGGWLrngipqfrLPQsVLDAEIARI-----EKMGVTIKCNNEV 197
Cdd:COG1251 143 KRVVVIGGGLIGLEAAAALRKRGLEVTV----VERAPRL--------LPR-QLDEEAGALlqrllEALGVEVRLGTGV 207
|
|
| PRK07846 |
PRK07846 |
mycothione reductase; Reviewed |
253-381 |
4.00e-04 |
|
mycothione reductase; Reviewed
Pssm-ID: 181142 [Multi-domain] Cd Length: 451 Bit Score: 42.25 E-value: 4.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447059109 253 PQSALIIGGGDVAMDVASTLKVLGCQaVTCVAREEL------DEFPASEKEFASARelgVSIIDGFTPVAVE--GNKVTf 324
Cdd:PRK07846 166 PESLVIVGGGFIAAEFAHVFSALGVR-VTVVNRSGRllrhldDDISERFTELASKR---WDVRLGRNVVGVSqdGSGVT- 240
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447059109 325 khVRLPGELTMAADKIILAVGQHA---RLDAFA---ELEPQRNtIKTQNYQ-TRDPQVFAAGDI 381
Cdd:PRK07846 241 --LRLDDGSTVEADVLLVATGRVPngdLLDAAAagvDVDEDGR-VVVDEYQrTSAEGVFALGDV 301
|
|
| DadA |
COG0665 |
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism]; |
126-174 |
6.58e-04 |
|
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
Pssm-ID: 440429 [Multi-domain] Cd Length: 364 Bit Score: 41.43 E-value: 6.58e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 447059109 126 KVAIIGAGPAGLQASVTLTNQGYDVTIYEKEA-------HPGGWLRNGIPQFRLPQ 174
Cdd:COG0665 4 DVVVIGGGIAGLSTAYHLARRGLDVTVLERGRpgsgasgRNAGQLRPGLAALADRA 59
|
|
| FixC |
COG0644 |
Dehydrogenase (flavoprotein) [Energy production and conversion]; |
132-160 |
9.79e-04 |
|
Dehydrogenase (flavoprotein) [Energy production and conversion];
Pssm-ID: 440409 [Multi-domain] Cd Length: 281 Bit Score: 40.72 E-value: 9.79e-04
10 20
....*....|....*....|....*....
gi 447059109 132 AGPAGLQASVTLTNQGYDVTIYEKEAHPG 160
Cdd:COG0644 1 AGPAGSAAARRLARAGLSVLLLEKGSFPG 29
|
|
| PLN02172 |
PLN02172 |
flavin-containing monooxygenase FMO GS-OX |
127-163 |
1.02e-03 |
|
flavin-containing monooxygenase FMO GS-OX
Pssm-ID: 215116 [Multi-domain] Cd Length: 461 Bit Score: 41.00 E-value: 1.02e-03
10 20 30
....*....|....*....|....*....|....*...
gi 447059109 127 VAIIGAGPAGLQASVTLTNQGYDVTIYEKEAHPGG-WL 163
Cdd:PLN02172 13 VAVIGAGAAGLVAARELRREGHTVVVFEREKQVGGlWV 50
|
|
| TIGR00275 |
TIGR00275 |
flavoprotein, HI0933 family; The model when searched with a partial length search brings in ... |
128-160 |
1.03e-03 |
|
flavoprotein, HI0933 family; The model when searched with a partial length search brings in proteins with a dinucleotide-binding motif (Rossman fold) over the initial 40 residues of the model, including oxidoreductases and dehydrogenases. Partially characterized members include an FAD-binding protein from Bacillus cereus and flavoprotein HI0933 from Haemophilus influenzae. [Unknown function, Enzymes of unknown specificity]
Pssm-ID: 272992 [Multi-domain] Cd Length: 400 Bit Score: 41.04 E-value: 1.03e-03
10 20 30
....*....|....*....|....*....|...
gi 447059109 128 AIIGAGPAGLQASVTLTNQGYDVTIYEKEAHPG 160
Cdd:TIGR00275 1 IIIGGGAAGLMAAITAARAGLSVLLLEKNKKIG 33
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
126-216 |
1.17e-03 |
|
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase [Lipid transport and metabolism];
Pssm-ID: 440215 [Multi-domain] Cd Length: 322 Bit Score: 40.56 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447059109 126 KVAIIGAGPAGLQASVTLTNQGYDVTIYEKEAHPggwlrngipqfrLPqsVLDAEIARI-----EKMGVTIKCNNEVgnt 200
Cdd:COG0446 126 RAVVIGGGPIGLELAEALRKRGLKVTLVERAPRL------------LG--VLDPEMAALleeelREHGVELRLGETV--- 188
|
90
....*....|....*.
gi 447059109 201 ltlEQLKAENRAVLVT 216
Cdd:COG0446 189 ---VAIDGDDKVAVTL 201
|
|
| PLN00093 |
PLN00093 |
geranylgeranyl diphosphate reductase; Provisional |
126-201 |
1.76e-03 |
|
geranylgeranyl diphosphate reductase; Provisional
Pssm-ID: 177713 [Multi-domain] Cd Length: 450 Bit Score: 40.51 E-value: 1.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447059109 126 KVAIIGAGPAGLQASVTLTNQGYDVTIYEKE---AHPGGwlrNGIP-----QFRLPQSVLDaeiARIEKMGVTIKCNNEV 197
Cdd:PLN00093 41 RVAVIGGGPAGACAAETLAKGGIETFLIERKldnAKPCG---GAIPlcmvgEFDLPLDIID---RKVTKMKMISPSNVAV 114
|
....*.
gi 447059109 198 --GNTL 201
Cdd:PLN00093 115 diGKTL 120
|
|
| GG-red-SF |
TIGR02032 |
geranylgeranyl reductase family; This model represents a subfamily which includes ... |
127-160 |
2.32e-03 |
|
geranylgeranyl reductase family; This model represents a subfamily which includes geranylgeranyl reductases involved in chlorophyll and bacteriochlorophyll biosynthesis as well as other related enzymes which may also act on geranylgeranyl groups or related substrates. [Biosynthesis of cofactors, prosthetic groups, and carriers, Chlorophyll and bacteriochlorphyll]
Pssm-ID: 273936 [Multi-domain] Cd Length: 295 Bit Score: 39.61 E-value: 2.32e-03
10 20 30
....*....|....*....|....*....|....
gi 447059109 127 VAIIGAGPAGLQASVTLTNQGYDVTIYEKEAHPG 160
Cdd:TIGR02032 3 VVVVGAGPAGASAAYRLADKGLRVLLLEKKSFPR 36
|
|
| PTZ00058 |
PTZ00058 |
glutathione reductase; Provisional |
253-382 |
2.43e-03 |
|
glutathione reductase; Provisional
Pssm-ID: 185420 [Multi-domain] Cd Length: 561 Bit Score: 39.98 E-value: 2.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447059109 253 PQSALIIGGGDVAMDVASTLKVLGCQAVTCVAREEL----DEFPASEKEfASARELGVSIIDGFTPVAVEGNKVTFKHVR 328
Cdd:PTZ00058 237 AKRIGIAGSGYIAVELINVVNRLGAESYIFARGNRLlrkfDETIINELE-NDMKKNNINIITHANVEEIEKVKEKNLTIY 315
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 447059109 329 LP-GELTMAADKIILAVGQHARLDAFA----ELEPQRNTIKTQNYQ-TRDPQVFAAGDIV 382
Cdd:PTZ00058 316 LSdGRKYEHFDYVIYCVGRSPNTEDLNlkalNIKTPKGYIKVDDNQrTSVKHIYAVGDCC 375
|
|
| PRK08243 |
PRK08243 |
4-hydroxybenzoate 3-monooxygenase; Validated |
126-155 |
3.42e-03 |
|
4-hydroxybenzoate 3-monooxygenase; Validated
Pssm-ID: 236198 [Multi-domain] Cd Length: 392 Bit Score: 39.40 E-value: 3.42e-03
10 20 30
....*....|....*....|....*....|
gi 447059109 126 KVAIIGAGPAGLQASVTLTNQGYDVTIYEK 155
Cdd:PRK08243 4 QVAIIGAGPAGLLLGQLLHLAGIDSVVLER 33
|
|
| COG2509 |
COG2509 |
FAD-dependent dehydrogenase [General function prediction only]; |
126-155 |
4.22e-03 |
|
FAD-dependent dehydrogenase [General function prediction only];
Pssm-ID: 441999 [Multi-domain] Cd Length: 466 Bit Score: 39.33 E-value: 4.22e-03
10 20 30
....*....|....*....|....*....|
gi 447059109 126 KVAIIGAGPAGLQASVTLTNQGYDVTIYEK 155
Cdd:COG2509 32 DVVIVGAGPAGLFAALELAEAGLKPLVLER 61
|
|
| FAD_binding_2 |
pfam00890 |
FAD binding domain; This family includes members that bind FAD. This family includes the ... |
127-161 |
4.28e-03 |
|
FAD binding domain; This family includes members that bind FAD. This family includes the flavoprotein subunits from succinate and fumarate dehydrogenase, aspartate oxidase and the alpha subunit of adenylylsulphate reductase.
Pssm-ID: 395718 [Multi-domain] Cd Length: 398 Bit Score: 39.19 E-value: 4.28e-03
10 20 30
....*....|....*....|....*....|....*
gi 447059109 127 VAIIGAGPAGLQASVTLTNQGYDVTIYEKEAHPGG 161
Cdd:pfam00890 2 VLVIGGGLAGLAAALAAAEAGLKVAVVEKGQPFGG 36
|
|
| SdhA |
COG1053 |
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and ... |
127-161 |
4.38e-03 |
|
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: 39.05 E-value: 4.38e-03
10 20 30
....*....|....*....|....*....|....*
gi 447059109 127 VAIIGAGPAGLQASVTLTNQGYDVTIYEKEAHPGG 161
Cdd:COG1053 6 VVVVGSGGAGLRAALEAAEAGLKVLVLEKVPPRGG 40
|
|
| mnmC |
PRK01747 |
bifunctional tRNA (5-methylaminomethyl-2-thiouridine)(34)-methyltransferase MnmD/FAD-dependent ... |
126-160 |
4.65e-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: 39.06 E-value: 4.65e-03
10 20 30
....*....|....*....|....*....|....*
gi 447059109 126 KVAIIGAGPAGLQASVTLTNQGYDVTIYEKEAHPG 160
Cdd:PRK01747 262 DAAIIGGGIAGAALALALARRGWQVTLYEADEAPA 296
|
|
| FAD_binding_3 |
pfam01494 |
FAD binding domain; This domain is involved in FAD binding in a number of enzymes. |
126-155 |
5.89e-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: 5.89e-03
10 20 30
....*....|....*....|....*....|
gi 447059109 126 KVAIIGAGPAGLQASVTLTNQGYDVTIYEK 155
Cdd:pfam01494 3 DVLIVGGGPAGLMLALLLARAGVRVVLVER 32
|
|
| PRK12842 |
PRK12842 |
putative succinate dehydrogenase; Reviewed |
127-161 |
6.51e-03 |
|
putative succinate dehydrogenase; Reviewed
Pssm-ID: 237224 [Multi-domain] Cd Length: 574 Bit Score: 38.52 E-value: 6.51e-03
10 20 30
....*....|....*....|....*....|....*
gi 447059109 127 VAIIGAGPAGLQASVTLTNQGYDVTIYEKEAHPGG 161
Cdd:PRK12842 12 VLVIGSGAGGLSAAITARKLGLDVVVLEKEPVFGG 46
|
|
| Amino_oxidase |
pfam01593 |
Flavin containing amine oxidoreductase; This family consists of various amine oxidases, ... |
135-164 |
6.75e-03 |
|
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: 38.63 E-value: 6.75e-03
10 20 30
....*....|....*....|....*....|
gi 447059109 135 AGLQASVTLTNQGYDVTIYEKEAHPGGWLR 164
Cdd:pfam01593 2 AGLAAARELLRAGHDVTVLEARDRVGGRIR 31
|
|
| PRK11883 |
PRK11883 |
protoporphyrinogen oxidase; Reviewed |
126-164 |
7.98e-03 |
|
protoporphyrinogen oxidase; Reviewed
Pssm-ID: 237009 [Multi-domain] Cd Length: 451 Bit Score: 38.29 E-value: 7.98e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 447059109 126 KVAIIGAGPAGLQASVTLTNQG--YDVTIYEKEAHPGGWLR 164
Cdd:PRK11883 2 KVAIIGGGITGLSAAYRLHKKGpdADITLLEASDRLGGKIQ 42
|
|
| PLN02529 |
PLN02529 |
lysine-specific histone demethylase 1 |
117-161 |
9.41e-03 |
|
lysine-specific histone demethylase 1
Pssm-ID: 178144 [Multi-domain] Cd Length: 738 Bit Score: 38.33 E-value: 9.41e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 447059109 117 YQPGTKTLGKVAIIGAGPAGLQASVTLTNQGYDVTIYEKEAHPGG 161
Cdd:PLN02529 153 PIPEEGTEGSVIIVGAGLAGLAAARQLLSFGFKVVVLEGRNRPGG 197
|
|
| |
