|
Name |
Accession |
Description |
Interval |
E-value |
| gltD_gamma_fam |
TIGR01318 |
glutamate synthase small subunit family protein, proteobacterial; This model represents one of ... |
9-473 |
0e+00 |
|
glutamate synthase small subunit family protein, proteobacterial; This model represents one of three built for the NADPH-dependent or NADH-dependent glutamate synthase (EC 1.4.1.13 and 1.4.1.14, respectively) small subunit and homologs. TIGR01317 describes the small subunit (or equivalent region from longer forms) in eukaryotes, Gram-positive bacteria, and some other lineages, both NADH and NADPH-dependent. TIGR01316 describes a protein of similar length, from Archaea and a number of bacterial lineages, that forms glutamate synthase homotetramers without a large subunit. This model describes both glutatate synthase small subunit and closely related paralogs of unknown function from a number of gamma and alpha subdivision Proteobacteria, including E. coli.
Pssm-ID: 273553 [Multi-domain] Cd Length: 467 Bit Score: 804.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 9 FQFLDVPRQDPEKKDITVRKAEFVEIYKPFTSETVTNQTHRCLGCGNPYCEWKCPVHNYIPNWLKLIAEGQIFQAAELCH 88
Cdd:TIGR01318 1 FQFIDLPRQDPDKIPVEERKTDFREIYGPFDKGQAQYQADRCLDCGNPYCEWKCPVHNAIPQWLQLVQEGRIDEAAELSH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 89 QTNTLPEVCGRVCPQDRLCEGACTLNDGFGAVTIGNAEKYINDTAFALGWRPDMSHVKWTGKKVAIIGAGPAGLGCADIL 168
Cdd:TIGR01318 81 QTNTLPEICGRVCPQDRLCEGACTLNDEGGAVTIGNLERYITDTALAMGWRPDLSHVQPTGKRVAVIGAGPAGLACADIL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 169 ARGGVKPVVFDKRPEIGGLLTFGIPEFKMEKDVMKRRREIFTGMGIEFRLNTEIGKDVTIDELLAEYDAVFMGMGTYTYM 248
Cdd:TIGR01318 161 ARAGVQVVVFDRHPEIGGLLTFGIPSFKLDKAVLSRRREIFTAMGIEFRLNCEVGRDISLDDLLEDYDAVFLGVGTYRSM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 249 KGGFPGEDLDGVYDALDFLISNVNRCQGWEKDPSE-YISMDGKKVIVLGGGDTAMDCNRTSLRQGAHDVTCAYRRDESNM 327
Cdd:TIGR01318 241 RGGLPGEDAPGVLPALPFLIANTRQLMGLPEEPEEpLIDVEGKRVVVLGGGDTAMDCVRTAIRLGATKVTCAYRRDEANM 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 328 PGSAREVKNAYEEGIKFLFNRQPIEIV-GENGKVTGVKVVTTQMGEPDSRGRRSPEPIPGSEEVLPADAVLLAFGFRPSP 406
Cdd:TIGR01318 321 PGSRREVANAREEGVEFLFNVQPVSIEsDEDGQVIGVTVVRTKLGEPDANGRRRPVPVAGSEFVLPADVVIMAFGFSPHL 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 523535166 407 ADWFGSVNINLDGSGRVVAPEQQEFKFQTSNPKIFAGGDMVRGSDLVVTAIWEGRQAAEGILDYLGV 473
Cdd:TIGR01318 401 MPWLAAHGITLDSWGRIITALSSGLTYQTTNPKIFAGGDAVRGADLVVTAVAEGRDAAQGILDWLGV 467
|
|
| gltD |
PRK12810 |
glutamate synthase subunit beta; Reviewed |
7-473 |
0e+00 |
|
glutamate synthase subunit beta; Reviewed
Pssm-ID: 237213 [Multi-domain] Cd Length: 471 Bit Score: 803.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 7 NDFQFLDVPRQDPEKKDITVRKAEFVEIYKPFTSETVTNQTHRCLGCGNPYCEWKCPVHNYIPNWLKLIAEGQIFQAAEL 86
Cdd:PRK12810 3 KPTGFLEYDRVDPKKRPVAERIKDFKEFYEPFSEEQAKIQAARCMDCGIPFCHWGCPVHNYIPEWNDLVYRGRWEEAAER 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 87 CHQTNTLPEVCGRVCPQDrlCEGACTLNDGFGAVTIGNAEKYINDTAFALGW-RPDmSHVKWTGKKVAIIGAGPAGLGCA 165
Cdd:PRK12810 83 LHQTNNFPEFTGRVCPAP--CEGACTLNINFGPVTIKNIERYIIDKAFEEGWvKPD-PPVKRTGKKVAVVGSGPAGLAAA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 166 DILARGGVKPVVFDKRPEIGGLLTFGIPEFKMEKDVMKRRREIFTGMGIEFRLNTEIGKDVTIDELLAEYDAVFMGMGTY 245
Cdd:PRK12810 160 DQLARAGHKVTVFERADRIGGLLRYGIPDFKLEKEVIDRRIELMEAEGIEFRTNVEVGKDITAEELLAEYDAVFLGTGAY 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 246 TYMKGGFPGEDLDGVYDALDFLISNVNRCQGWEKDPseYISMDGKKVIVLGGGDTAMDCNRTSLRQGAHDVTcayRRDES 325
Cdd:PRK12810 240 KPRDLGIPGRDLDGVHFAMDFLIQNTRRVLGDETEP--FISAKGKHVVVIGGGDTGMDCVGTAIRQGAKSVT---QRDIM 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 326 NMPGSAR-------------EVKNAYEEGIKFLFNRQPIEIVGENGKVTGVKVVTTQMGEPDsrgrrsPEPIPGSEEVLP 392
Cdd:PRK12810 315 PMPPSRRnknnpwpywpmklEVSNAHEEGVEREFNVQTKEFEGENGKVTGVKVVRTELGEGD------FEPVEGSEFVLP 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 393 ADAVLLAFGFRPSPADWFGSVNINLDGSGRVVAPeqqEFKFQTSNPKIFAGGDMVRGSDLVVTAIWEGRQAAEGILDYLG 472
Cdd:PRK12810 389 ADLVLLAMGFTGPEAGLLAQFGVELDERGRVAAP---DNAYQTSNPKVFAAGDMRRGQSLVVWAIAEGRQAARAIDAYLM 465
|
.
gi 523535166 473 V 473
Cdd:PRK12810 466 G 466
|
|
| PRK12769 |
PRK12769 |
putative oxidoreductase Fe-S binding subunit; Reviewed |
15-473 |
0e+00 |
|
putative oxidoreductase Fe-S binding subunit; Reviewed
Pssm-ID: 183733 [Multi-domain] Cd Length: 654 Bit Score: 745.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 15 PRQDPEKKDITVRKAEFVEIYKPFTSETVTNQTHRCLGCG-NPYCEWKCPVHNYIPNWLKLIAEGQIFQAAELCHQTNTL 93
Cdd:PRK12769 192 PRGEPDKLAIEARKTGFDEIYLPFRADQAQREASRCLKCGeHSICEWTCPLHNHIPQWIELVKAGNIDAAVELSHQTNSL 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 94 PEVCGRVCPQDRLCEGACTLNDGFGAVTIGNAEKYINDTAFALGWRPDMSHVKWTGKKVAIIGAGPAGLGCADILARGGV 173
Cdd:PRK12769 272 PEITGRVCPQDRLCEGACTLRDEYGAVTIGNIERYISDQALAKGWRPDLSQVTKSDKRVAIIGAGPAGLACADVLARNGV 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 174 KPVVFDKRPEIGGLLTFGIPEFKMEKDVMKRRREIFTGMGIEFRLNTEIGKDVTIDELLAEYDAVFMGMGTYTYMKGGFP 253
Cdd:PRK12769 352 AVTVYDRHPEIGGLLTFGIPAFKLDKSLLARRREIFSAMGIEFELNCEVGKDISLESLLEDYDAVFVGVGTYRSMKAGLP 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 254 GEDLDGVYDALDFLISNVNRCQGWEKDPSE-YISMDGKKVIVLGGGDTAMDCNRTSLRQGAHDVTCAYRRDESNMPGSAR 332
Cdd:PRK12769 432 NEDAPGVYDALPFLIANTKQVMGLEELPEEpFINTAGLNVVVLGGGDTAMDCVRTALRHGASNVTCAYRRDEANMPGSKK 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 333 EVKNAYEEGIKFLFNRQPIEIV-GENGKVTGVKVVTTQMGEPDSRGRRSPEPIPGSEEVLPADAVLLAFGFRPSPADWFG 411
Cdd:PRK12769 512 EVKNAREEGANFEFNVQPVALElNEQGHVCGIRFLRTRLGEPDAQGRRRPVPIPGSEFVMPADAVIMAFGFNPHGMPWLE 591
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 523535166 412 SVNINLDGSGRVVAPEQQEFKFQTSNPKIFAGGDMVRGSDLVVTAIWEGRQAAEGILDYLGV 473
Cdd:PRK12769 592 SHGVTVDKWGRIIADVESQYRYQTSNPKIFAGGDAVRGADLVVTAMAEGRHAAQGIIDWLGV 653
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
27-470 |
0e+00 |
|
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport and metabolism, General function prediction only]; NADPH-dependent glutamate synthase beta chain or related oxidoreductase is part of the Pathway/BioSystem: Glutamine biosynthesis
Pssm-ID: 440259 [Multi-domain] Cd Length: 434 Bit Score: 659.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 27 RKAEFVEIYKPFTSETVTNQTHRCLGCGNPYCEWKCPVHNYIPNWLKLIAEGQIFQAAELCHQTNTLPEVCGRVCPqdRL 106
Cdd:COG0493 1 RIKDFREVYPGLSEEEAIEQAARCLDCGDPPCQTGCPVGNDIPEWIRLIAEGDYEEALELIHETNPFPEVCGRVCP--AP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 107 CEGACTLNDGFGAVTIGNAEKYINDTAFALGWRPDMSHVKWTGKKVAIIGAGPAGLGCADILARGGVKPVVFDKRPEIGG 186
Cdd:COG0493 79 CEGACVRGIVDEPVAIGALERFIADKAFEEGWVKPPPPAPRTGKKVAVVGSGPAGLAAAYQLARAGHEVTVFEALDKPGG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 187 LLTFGIPEFKMEKDVMKRRREIFTGMGIEFRLNTEIGKDVTIDELLAEYDAVFMGMGTYTYMKGGFPGEDLDGVYDALDF 266
Cdd:COG0493 159 LLRYGIPEFRLPKDVLDREIELIEALGVEFRTNVEVGKDITLDELLEEFDAVFLATGAGKPRDLGIPGEDLKGVHSAMDF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 267 LIsNVNRcqgweKDPSEYISMDGKKVIVLGGGDTAMDCNRTSLRQGAHDVTCAYRRDESNMPGSAREVKNAYEEGIKFLF 346
Cdd:COG0493 239 LT-AVNL-----GEAPDTILAVGKRVVVIGGGNTAMDCARTALRLGAESVTIVYRRTREEMPASKEEVEEALEEGVEFLF 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 347 NRQPIEIVG-ENGKVTGVKVVTTQMGEPDSRGRRSPEPIPGSEEVLPADAVLLAFGFRPSPADWFGSVNINLDGSGRVVA 425
Cdd:COG0493 313 LVAPVEIIGdENGRVTGLECVRMELGEPDESGRRRPVPIEGSEFTLPADLVILAIGQTPDPSGLEEELGLELDKRGTIVV 392
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 523535166 426 PEQqefKFQTSNPKIFAGGDMVRGSDLVVTAIWEGRQAAEGILDY 470
Cdd:COG0493 393 DEE---TYQTSLPGVFAGGDAVRGPSLVVWAIAEGRKAARAIDRY 434
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
10-471 |
0e+00 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 578.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 10 QFLDVPRQDPEKKDITVRKAEFVEIYKPFTSETVTNQTHRCLGCGNPYCEWKCPVHNYIPNWLKLIAEGQIFQAAELCHQ 89
Cdd:PRK11749 2 KFLTTPRIPMPRQDAEERAQNFDEVAPGYTPEEAIEEASRCLQCKDAPCVKACPVSIDIPEFIRLIAEGNLKGAAETILE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 90 TNTLPEVCGRVCPQDRLCEGACTLNDGFGAVTIGNAEKYINDTAFALGWRPDMSHVKwTGKKVAIIGAGPAGLGCADILA 169
Cdd:PRK11749 82 TNPLPAVCGRVCPQERLCEGACVRGKKGEPVAIGRLERYITDWAMETGWVLFKRAPK-TGKKVAVIGAGPAGLTAAHRLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 170 RGGVKPVVFDKRPEIGGLLTFGIPEFKMEKDVMKRRREIFTGMGIEFRLNTEIGKDVTIDELLAEYDAVFMGMGTYTYMK 249
Cdd:PRK11749 161 RKGYDVTIFEARDKAGGLLRYGIPEFRLPKDIVDREVERLLKLGVEIRTNTEVGRDITLDELRAGYDAVFIGTGAGLPRF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 250 GGFPGEDLDGVYDALDFLIsNVNRCQGWEKDPSeyismdGKKVIVLGGGDTAMDCNRTSLRQGAHDVTCAYRRDESNMPG 329
Cdd:PRK11749 241 LGIPGENLGGVYSAVDFLT-RVNQAVADYDLPV------GKRVVVIGGGNTAMDAARTAKRLGAESVTIVYRRGREEMPA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 330 SAREVKNAYEEGIKFLFNRQPIEIVGENGKVTGVKVVTTQMGEPDSRGRRSpEPIPGSEEVLPADAVLLAFGFRPSPADW 409
Cdd:PRK11749 314 SEEEVEHAKEEGVEFEWLAAPVEILGDEGRVTGVEFVRMELGEPDASGRRR-VPIEGSEFTLPADLVIKAIGQTPNPLIL 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 523535166 410 FGSVNINLDGSGRVVAPEQQefkFQTSNPKIFAGGDMVRGSDLVVTAIWEGRQAAEGILDYL 471
Cdd:PRK11749 393 STTPGLELNRWGTIIADDET---GRTSLPGVFAGGDIVTGAATVVWAVGDGKDAAEAIHEYL 451
|
|
| PRK12809 |
PRK12809 |
putative oxidoreductase Fe-S binding subunit; Reviewed |
12-468 |
0e+00 |
|
putative oxidoreductase Fe-S binding subunit; Reviewed
Pssm-ID: 183762 [Multi-domain] Cd Length: 639 Bit Score: 576.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 12 LDV-PRQDPEKKDITVRKAEFVEIYKPFTSETVTNQTHRCLGCGN-PYCEWKCPVHNYIPNWLKLIAEGQIFQAAELCHQ 89
Cdd:PRK12809 171 LPVnSRKGADKISASERKTHFGEIYCGLDPQQATYESDRCVYCAEkANCNWHCPLHNAIPDYIRLVQEGKIIEAAELCHQ 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 90 TNTLPEVCGRVCPQDRLCEGACTLNDGFGAVTIGNAEKYINDTAFALGWRPDMSHVKWTGKKVAIIGAGPAGLGCADILA 169
Cdd:PRK12809 251 TSSLPEICGRVCPQDRLCEGACTLKDHSGAVSIGNLERYITDTALAMGWRPDVSKVVPRSEKVAVIGAGPAGLGCADILA 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 170 RGGVKPVVFDKRPEIGGLLTFGIPEFKMEKDVMKRRREIFTGMGIEFRLNTEIGKDVTIDELLAEYDAVFMGMGTYTYMK 249
Cdd:PRK12809 331 RAGVQVDVFDRHPEIGGMLTFGIPPFKLDKTVLSQRREIFTAMGIDFHLNCEIGRDITFSDLTSEYDAVFIGVGTYGMMR 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 250 GGFPGEDLDGVYDALDFLISNVNRCQGWEkDPSEY--ISMDGKKVIVLGGGDTAMDCNRTSLRQGAHDVTCAYRRDESNM 327
Cdd:PRK12809 411 ADLPHEDAPGVIQALPFLTAHTRQLMGLP-ESEEYplTDVEGKRVVVLGGGDTTMDCLRTSIRLNAASVTCAYRRDEVSM 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 328 PGSAREVKNAYEEGIKFLFNRQPIEIV-GENGKVTGVKVVTTQMGEPDSRGRRSPEPIPGSEEVLPADAVLLAFGFRPSP 406
Cdd:PRK12809 490 PGSRKEVVNAREEGVEFQFNVQPQYIAcDEDGRLTAVGLIRTAMGEPGPDGRRRPRPVAGSEFELPADVLIMAFGFQAHA 569
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 523535166 407 ADWFGSVNINLDGSGRVVAPEQQEFKFQTSNPKIFAGGDMVRGSDLVVTAIWEGRQAAEGIL 468
Cdd:PRK12809 570 MPWLQGSGIKLDKWGLIQTGDVGYLPTQTHLKKVFAGGDAVHGADLVVTAMAAGRQAARDML 631
|
|
| PRK12831 |
PRK12831 |
putative oxidoreductase; Provisional |
14-471 |
1.69e-136 |
|
putative oxidoreductase; Provisional
Pssm-ID: 183780 [Multi-domain] Cd Length: 464 Bit Score: 400.93 E-value: 1.69e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 14 VPRQDPEkkditVRKAEFVEIYKPFTSETVTNQTHRCLGCGNPYCEWKCPVHNYIPNWLKLIAEGQIFQAAELCHQTNTL 93
Cdd:PRK12831 11 VREQDPE-----VRATNFEEVCLGYNEEEAVKEASRCLQCKKPKCVKGCPVSINIPGFISKLKEGDFEEAAKIIAKYNAL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 94 PEVCGRVCPQDRLCEGACTLNDGFGAVTIGNAEKYINDTAFALGWRPDMSHVKwTGKKVAIIGAGPAGLGCADILARGGV 173
Cdd:PRK12831 86 PAVCGRVCPQESQCEGKCVLGIKGEPVAIGKLERFVADWARENGIDLSETEEK-KGKKVAVIGSGPAGLTCAGDLAKMGY 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 174 KPVVFDKRPEIGGLLTFGIPEFKMEKD-VMKRRREIFTGMGIEFRLNTEIGKDVTIDELLAE--YDAVFMGMGTYTYMKG 250
Cdd:PRK12831 165 DVTIFEALHEPGGVLVYGIPEFRLPKEtVVKKEIENIKKLGVKIETNVVVGKTVTIDELLEEegFDAVFIGSGAGLPKFM 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 251 GFPGEDLDGVYDALDFLiSNVNRCQGWEKDPSEYISMdGKKVIVLGGGDTAMDCNRTSLRQGAhDVTCAYRRDESNMPGS 330
Cdd:PRK12831 245 GIPGENLNGVFSANEFL-TRVNLMKAYKPEYDTPIKV-GKKVAVVGGGNVAMDAARTALRLGA-EVHIVYRRSEEELPAR 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 331 AREVKNAYEEGIKFLFNRQPIEIVG-ENGKVTGVKVVTTQMGEPDSRGRRSPEPIPGSEEVLPADAVLLAFGFRPSPADW 409
Cdd:PRK12831 322 VEEVHHAKEEGVIFDLLTNPVEILGdENGWVKGMKCIKMELGEPDASGRRRPVEIEGSEFVLEVDTVIMSLGTSPNPLIS 401
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 523535166 410 FGSVNINLDGSGRVVAPEQQefkFQTSNPKIFAGGDMVRGSDLVVTAIWEGRQAAEGILDYL 471
Cdd:PRK12831 402 STTKGLKINKRGCIVADEET---GLTSKEGVFAGGDAVTGAATVILAMGAGKKAAKAIDEYL 460
|
|
| PRK12778 |
PRK12778 |
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ... |
14-471 |
4.28e-121 |
|
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;
Pssm-ID: 237200 [Multi-domain] Cd Length: 752 Bit Score: 371.00 E-value: 4.28e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 14 VPRQDPEKKditvRKAEFVEIYKPFTSETVTNQTHRCLGCGNPYCEWKCPVHNYIPNWLKLIAEGQIFQAAELCHQTNTL 93
Cdd:PRK12778 299 MPELDPEYR----AHNRFEEVNLGLTKEQAMTEAKRCLDCKNPGCVEGCPVGIDIPRFIKNIERGNFLEAAKILKETSAL 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 94 PEVCGRVCPQDRLCEGACT-LNDGFGAVTIGNAEKYINDTAFALGwRPDMSHVK-WTGKKVAIIGAGPAGLGCADILARG 171
Cdd:PRK12778 375 PAVCGRVCPQEKQCESKCIhGKMGEEAVAIGYLERFVADYERESG-NISVPEVAeKNGKKVAVIGSGPAGLSFAGDLAKR 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 172 GVKPVVFDKRPEIGGLLTFGIPEFKMEKDVMKRRREIFTGMGIEFRLNTEIGKDVTIDELLAE-YDAVFM--GMGTYTYM 248
Cdd:PRK12778 454 GYDVTVFEALHEIGGVLKYGIPEFRLPKKIVDVEIENLKKLGVKFETDVIVGKTITIEELEEEgFKGIFIasGAGLPNFM 533
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 249 kgGFPGEDLDGVYDALDFLiSNVNRCQGWEKDPSEYISMdGKKVIVLGGGDTAMDCNRTSLRQGAHDVTCAYRRDESNMP 328
Cdd:PRK12778 534 --NIPGENSNGVMSSNEYL-TRVNLMDAASPDSDTPIKF-GKKVAVVGGGNTAMDSARTAKRLGAERVTIVYRRSEEEMP 609
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 329 GSAREVKNAYEEGIKFLFNRQPIEIVG-ENGKVTGVKVVTTQMGEPDSRGRRSPEPIPGSEEVLPADAVLLAFGFRPSPA 407
Cdd:PRK12778 610 ARLEEVKHAKEEGIEFLTLHNPIEYLAdEKGWVKQVVLQKMELGEPDASGRRRPVAIPGSTFTVDVDLVIVSVGVSPNPL 689
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 523535166 408 DWFGSVNINLDGSGRVVAPEQQefkfQTSNPKIFAGGDMVRGSDLVVTAIWEGRQAAEGILDYL 471
Cdd:PRK12778 690 VPSSIPGLELNRKGTIVVDEEM----QSSIPGIYAGGDIVRGGATVILAMGDGKRAAAAIDEYL 749
|
|
| GOGAT_sm_gam |
TIGR01317 |
glutamate synthases, NADH/NADPH, small subunit; This model represents one of three built for ... |
11-471 |
1.80e-119 |
|
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: 358.37 E-value: 1.80e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 11 FLDVPRQDPEKKDITVRKAEFVEIYKPFTSETVTNQTHRCLGCGNPYC--EWKCPVHNYIPNWLKLIAEGQIFQAAELCH 88
Cdd:TIGR01317 5 FLEYKRRKPTERDPRTRLKDWKEFTNPFDKESAKYQAARCMDCGTPFChnDSGCPLNNLIPEFNDLVFRGRWKEALDRLH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 89 QTNTLPEVCGRVCPQDrlCEGACTLNDGFGAVTIGNAEKYINDTAFALGW-RPDMSHVKwTGKKVAIIGAGPAGLGCADI 167
Cdd:TIGR01317 85 ATNNFPEFTGRVCPAP--CEGACTLGISEDPVGIKSIERIIIDKGFQEGWvQPRPPSKR-TGKKVAVVGSGPAGLAAADQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 168 LARGGVKPVVFDKRPEIGGLLTFGIPEFKMEKDVMKRRREIFTGMGIEFRLNTEIGKDVTIDELLAEYDAVFMGMGTYTY 247
Cdd:TIGR01317 162 LNRAGHTVTVFEREDRCGGLLMYGIPNMKLDKAIVDRRIDLLSAEGIDFVTNTEIGVDISADELKEQFDAVVLAGGATKP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 248 MKGGFPGEDLDGVYDALDFLISNvNRCQgWEKDPSE--YISMDGKKVIVLGGGDTAMDCNRTSLRQGAHDVT-------C 318
Cdd:TIGR01317 242 RDLPIPGRELKGIHYAMEFLPSA-TKAL-LGKDFKDiiFIKAKGKKVVVIGGGDTGADCVGTSLRHGAASVHqfeimpkP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 319 AYRRDESNM----PGSAReVKNAYEEGiKFLFNRQP-------IEIVG-ENGKVTGVKVVTTQMgEPDSRGRRSPEPIPG 386
Cdd:TIGR01317 320 PEARAKDNPwpewPRVYR-VDYAHEEA-AAHYGRDPreysiltKEFIGdDEGKVTALRTVRVEW-KKSQDGKWQFVEIPG 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 387 SEEVLPADAVLLAFGFRPSPADWFGSVNINLDGSGRVVAPEQQefkFQTSNPKIFAGGDMVRGSDLVVTAIWEGRQAAEG 466
Cdd:TIGR01317 397 SEEVFEADLVLLAMGFVGPEQILLDDFGVKKTRRGNISAGYDD---YSTSIPGVFAAGDCRRGQSLIVWAINEGRKAAAA 473
|
....*
gi 523535166 467 ILDYL 471
Cdd:TIGR01317 474 VDRYL 478
|
|
| gltA |
TIGR01316 |
glutamate synthase (NADPH), homotetrameric; This protein is homologous to the small subunit of ... |
19-471 |
1.99e-115 |
|
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: 346.86 E-value: 1.99e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 19 PEKKDITVRKAEFveiykPFTSETVTNQTHRCLGCGNPY--CEWKCPVHNYIPNWLKLIAEGQIFQAAELCHQTNTLPEV 96
Cdd:TIGR01316 2 PEERSKLFQEAAL-----GYTEQLALVEAQRCLNCKDATkpCIKGCPVHVPIPEFIAKIQEGDFKGAVDIIKTTSLLPAI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 97 CGRVCPQDRLCEGACTLNDGFG----AVTIGNAEKYINDTAFALGWRPDMSHVKWTGKKVAIIGAGPAGLGCADILARGG 172
Cdd:TIGR01316 77 CGRVCPQERQCEGQCTVGKMFKdvgkPVSIGALERFVADWERQHGIETEPEKAPSTHKKVAVIGAGPAGLACASELAKAG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 173 VKPVVFDKRPEIGGLLTFGIPEFKMEKDVMKRRREIFTGMGIEFRLNTEIGKDVTIDELLAEYDAVFMGMGTYTYMKGGF 252
Cdd:TIGR01316 157 HSVTVFEALHKPGGVVTYGIPEFRLPKEIVVTEIKTLKKLGVTFRMNFLVGKTATLEELFSQYDAVFIGTGAGLPKLMNI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 253 PGEDLDGVYDALDFLiSNVNRCQGWEKDPSEYISMDGKKVIVLGGGDTAMDCNRTSLRQGAhDVTCAYRRDESNMPGSAR 332
Cdd:TIGR01316 237 PGEELCGVYSANDFL-TRANLMKAYEFPHADTPVYAGKSVVVIGGGNTAVDSARTALRLGA-EVHCLYRRTREDMTARVE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 333 EVKNAYEEGIKFLFNRQPIEIVG-ENGKVTGVKVVTTQMGEPDSRGRRSPEPIPGSEEVLPADAVLLAFGFRPSPADWFG 411
Cdd:TIGR01316 315 EIAHAEEEGVKFHFLCQPVEIIGdEEGNVRAVKFRKMDCQEQIDSGERRFLPCGDAECKLEADAVIVAIGNGSNPIMAET 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 412 SvNINLDGSGRVVAPEQQEfkfqTSNPKIFAGGDMVRGSDLVVTAIWEGRQAAEGILDYL 471
Cdd:TIGR01316 395 T-RLKTSERGTIVVDEDQR----TSIPGVFAGGDIILGAATVIRAMGQGKRAAKSINEYL 449
|
|
| PRK12771 |
PRK12771 |
putative glutamate synthase (NADPH) small subunit; Provisional |
56-472 |
6.59e-106 |
|
putative glutamate synthase (NADPH) small subunit; Provisional
Pssm-ID: 237198 [Multi-domain] Cd Length: 564 Bit Score: 326.06 E-value: 6.59e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 56 PYCEWKCPVHNYIPNWLKLIAEGQIFQAAELCHQTNTLPEVCGRVCPQDrlCEGACTLNDGFGAVTIGNAEKYINDTAFA 135
Cdd:PRK12771 47 PPCNAACPAGEDIRGWLALVRGGDYEYAWRRLTKDNPFPAVMGRVCYHP--CESGCNRGQVDDAVGINAVERFLGDYAIA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 136 LGWRPDMSHVKwTGKKVAIIGAGPAGLGCADILARGGVKPVVFDKRPEIGGLLTFGIPEFKMEKDVMKRrrEI--FTGMG 213
Cdd:PRK12771 125 NGWKFPAPAPD-TGKRVAVIGGGPAGLSAAYHLRRMGHAVTIFEAGPKLGGMMRYGIPAYRLPREVLDA--EIqrILDLG 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 214 IEFRLNTEIGKDVTIDELLAEYDAVFMGMGTYTYMKGGFPGEDLDGVYDALDFLisnvnRCQGWEKDPseyisMDGKKVI 293
Cdd:PRK12771 202 VEVRLGVRVGEDITLEQLEGEFDAVFVAIGAQLGKRLPIPGEDAAGVLDAVDFL-----RAVGEGEPP-----FLGKRVV 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 294 VLGGGDTAMDCNRTSLRQGAHDVTCAYRRDESNMPGSAREVKNAYEEGIKFLFNRQPIEIVGENGKVTGVKVVTTQMGEP 373
Cdd:PRK12771 272 VIGGGNTAMDAARTARRLGAEEVTIVYRRTREDMPAHDEEIEEALREGVEINWLRTPVEIEGDENGATGLRVITVEKMEL 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 374 DSRGRrsPEPIPGSEEVLPADAVLLAFG----FRPspadwFGSVNINLDGSGRVVAPEQQEFkfqTSNPKIFAGGDMVRG 449
Cdd:PRK12771 352 DEDGR--PSPVTGEEETLEADLVVLAIGqdidSAG-----LESVPGVEVGRGVVQVDPNFMM---TGRPGVFAGGDMVPG 421
|
410 420
....*....|....*....|...
gi 523535166 450 SDLVVTAIWEGRQAAEGILDYLG 472
Cdd:PRK12771 422 PRTVTTAIGHGKKAARNIDAFLG 444
|
|
| PRK12775 |
PRK12775 |
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin ... |
14-471 |
1.57e-93 |
|
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin domain-containing protein; Provisional
Pssm-ID: 183738 [Multi-domain] Cd Length: 1006 Bit Score: 304.56 E-value: 1.57e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 14 VPRQDP-EKKDITVRKAEFVEIYKPFTSETVTNQTHRCLGCGNPYCEWKCPVHNYIPNWLKLIAEGQIFQAAELCHQTNT 92
Cdd:PRK12775 296 VPHQTPmPERDAVERARNFKEVNLGYSLEDALQEAERCIQCAKPTCIAGCPVQIDIPVFIRHVVVRDFDGALEVIYEASI 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 93 LPEVCGRVCPQDRLCEGACTLNDGFGAVTIGNAEKYINDTAFAlgwrPDMSHVKWTGK--KVAIIGAGPAGLGCADILAR 170
Cdd:PRK12775 376 FPSICGRVCPQETQCEAQCIIAKKHESVGIGRLERFVGDNARA----KPVKPPRFSKKlgKVAICGSGPAGLAAAADLVK 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 171 GGVKPVVFDKRPEIGGLLTFGIPEFKMEKDVMKRRREIFTGMGIEFRLNTEIGKDVTIDELLAE--YDAVFMGMGTYTYM 248
Cdd:PRK12775 452 YGVDVTVYEALHVVGGVLQYGIPSFRLPRDIIDREVQRLVDIGVKIETNKVIGKTFTVPQLMNDkgFDAVFLGVGAGAPT 531
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 249 KGGFPGEDLDGVYDALDFLiSNVNrCQGWEKDP--SEYISMdGKKVIVLGGGDTAMDCNRTSLRQGAHDVTCAYRRDESN 326
Cdd:PRK12775 532 FLGIPGEFAGQVYSANEFL-TRVN-LMGGDKFPflDTPISL-GKSVVVIGAGNTAMDCLRVAKRLGAPTVRCVYRRSEAE 608
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 327 MPGSAREVKNAYEEGIKFLFNRQPIEI-VGENGKVTGVKVVTTQMGEPDSRGRRSPEPIpGSEEVLPADAVLLAFGFRPS 405
Cdd:PRK12775 609 APARIEEIRHAKEEGIDFFFLHSPVEIyVDAEGSVRGMKVEEMELGEPDEKGRRKPMPT-GEFKDLECDTVIYALGTKAN 687
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 523535166 406 PADWFGSVNINLDGSGRVVAPEQQEFKFQTSN-PKIFAGGDMVRGSDLVVTAIWEGRQAAEGILDYL 471
Cdd:PRK12775 688 PIITQSTPGLALNKWGNIAADDGKLESTQSTNlPGVFAGGDIVTGGATVILAMGAGRRAARSIATYL 754
|
|
| PRK12814 |
PRK12814 |
putative NADPH-dependent glutamate synthase small subunit; Provisional |
50-472 |
2.38e-91 |
|
putative NADPH-dependent glutamate synthase small subunit; Provisional
Pssm-ID: 139246 [Multi-domain] Cd Length: 652 Bit Score: 290.86 E-value: 2.38e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 50 CLGCGNPyCEWKCPVHNYIPNWLKLIAEGQIFQAAELCHQTNTLPEVCGRVCPQDrlCEGACTLNDGFGAVTIGNAEKYI 129
Cdd:PRK12814 97 CGDCLGP-CELACPAGCNIPGFIAAIARGDDREAIRIIKETIPLPGILGRICPAP--CEEACRRHGVDEPVSICALKRYA 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 130 --NDTAFALGWRPDMShvKWTGKKVAIIGAGPAGLGCADILARGGVKPVVFDKRPEIGGLLTFGIPEFKMEKDVMKRRRE 207
Cdd:PRK12814 174 adRDMESAERYIPERA--PKSGKKVAIIGAGPAGLTAAYYLLRKGHDVTIFDANEQAGGMMRYGIPRFRLPESVIDADIA 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 208 IFTGMGIEFRLNTEIGKDVTIDELLAEYDAVFMGMGTYTYMKGGFPGEDLDGVYDALDFLiSNVNrcQGWEKDPseyism 287
Cdd:PRK12814 252 PLRAMGAEFRFNTVFGRDITLEELQKEFDAVLLAVGAQKASKMGIPGEELPGVISGIDFL-RNVA--LGTALHP------ 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 288 dGKKVIVLGGGDTAMDCNRTSLRQGAHDVTCAYRRDESNMPGSAREVKNAYEEGIKFLFNRQPIEIVGENGKVTgVKVVT 367
Cdd:PRK12814 323 -GKKVVVIGGGNTAIDAARTALRLGAESVTILYRRTREEMPANRAEIEEALAEGVSLRELAAPVSIERSEGGLE-LTAIK 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 368 TQMGEPDSRGRRSPEPIPGSEEVLPADAVLLAFG--FRPSPADWFGsvnINLDGSGRVVAPEQQefkFQTSNPKIFAGGD 445
Cdd:PRK12814 401 MQQGEPDESGRRRPVPVEGSEFTLQADTVISAIGqqVDPPIAEAAG---IGTSRNGTVKVDPET---LQTSVAGVFAGGD 474
|
410 420
....*....|....*....|....*..
gi 523535166 446 MVRGSDLVVTAIWEGRQAAEGILDYLG 472
Cdd:PRK12814 475 CVTGADIAINAVEQGKRAAHAIDLFLN 501
|
|
| PRK12770 |
PRK12770 |
putative glutamate synthase subunit beta; Provisional |
148-471 |
1.77e-84 |
|
putative glutamate synthase subunit beta; Provisional
Pssm-ID: 237197 [Multi-domain] Cd Length: 352 Bit Score: 263.77 E-value: 1.77e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 148 TGKKVAIIGAGPAGLGCADILARGGVKPVVFDKRPEIGGLLTFGIPEFKMEKDVMKRRREIFTGMGIEFRLNTEI----- 222
Cdd:PRK12770 17 TGKKVAIIGAGPAGLAAAGYLACLGYEVHVYDKLPEPGGLMLFGIPEFRIPIERVREGVKELEEAGVVFHTRTKVccgep 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 223 ----------GKDVTIDELLAEYDAVFMGMGTYTYMKGGFPGEDLDGVYDALDFLIS-NVNR--CQGWEKDPseyiSMDG 289
Cdd:PRK12770 97 lheeegdefvERIVSLEELVKKYDAVLIATGTWKSRKLGIPGEDLPGVYSALEYLFRiRAAKlgYLPWEKVP----PVEG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 290 KKVIVLGGGDTAMDCNRTSLRQGAHDVTCAYRRDESNMPGSAREVKNAYEEGIKFLFNRQPIEIVGEnGKVTGVKVVTTQ 369
Cdd:PRK12770 173 KKVVVVGAGLTAVDAALEAVLLGAEKVYLAYRRTINEAPAGKYEIERLIARGVEFLELVTPVRIIGE-GRVEGVELAKMR 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 370 MGEPDSRGRRSPEPIPGSEEVLPADAVLLAFGFRPSPADWFGSVNINLDGSGRVVAPEqqefKFQTSNPKIFAGGDMVRG 449
Cdd:PRK12770 252 LGEPDESGRPRPVPIPGSEFVLEADTVVFAIGEIPTPPFAKECLGIELNRKGEIVVDE----KHMTSREGVFAAGDVVTG 327
|
330 340
....*....|....*....|..
gi 523535166 450 SDLVVTAIWEGRQAAEGILDYL 471
Cdd:PRK12770 328 PSKIGKAIKSGLRAAQSIHEWL 349
|
|
| PRK13984 |
PRK13984 |
putative oxidoreductase; Provisional |
8-471 |
1.32e-80 |
|
putative oxidoreductase; Provisional
Pssm-ID: 172486 [Multi-domain] Cd Length: 604 Bit Score: 261.63 E-value: 1.32e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 8 DFQFLDVPRQDPEKKDITVRKAEFVEIYKPFTSETVTNQTHRCLGCGnpYCEWKCPVHNYIPNWLKLIAEGQIFQAAELC 87
Cdd:PRK13984 145 NSELLDLERVEMEEIPPEERVKSFIEIVKGYSKEQAMQEAARCVECG--ICTDTCPAHMDIPQYIKAIYKDDLEEGLRWL 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 88 HQTNTLPEVCGRVCPQDrlCEGACTLNDGFGAVTIGNAEKYINDTAFALGWRP--DMSHVKwTGKKVAIIGAGPAGLGCA 165
Cdd:PRK13984 223 YKTNPLSMVCGRVCTHK--CETVCSIGHRGEPIAIRWLKRYIVDNVPVEKYSEilDDEPEK-KNKKVAIVGSGPAGLSAA 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 166 DILARGGVKPVVFDKRPEIGGLLTFGIPEFKMEKDVMKRRREIFTGMGIEFRLNTEIGKDVTIDELLAEYDAVFMGMGTY 245
Cdd:PRK13984 300 YFLATMGYEVTVYESLSKPGGVMRYGIPSYRLPDEALDKDIAFIEALGVKIHLNTRVGKDIPLEELREKHDAVFLSTGFT 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 246 TYMKGGFPGEDLDGVYDALDFL--ISNVNRCQGwekdPSEYISmdgKKVIVLGGGDTAMDCNRTSLR-----QGAHDVTC 318
Cdd:PRK13984 380 LGRSTRIPGTDHPDVIQALPLLreIRDYLRGEG----PKPKIP---RSLVVIGGGNVAMDIARSMARlqkmeYGEVNVKV 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 319 -AYRRDESNMPGSAREVKNAYEEGIKFLFNRQPIEIVGENGKVTGVKVVTTqMGEPDSRGRRSPEPIPGSEEVLPADAVL 397
Cdd:PRK13984 453 tSLERTFEEMPADMEEIEEGLEEGVVIYPGWGPMEVVIENDKVKGVKFKKC-VEVFDEEGRFNPKFDESDQIIVEADMVV 531
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 523535166 398 LAFGFRPS----PADWFGSVNINldgSGRVVAPEQQefkfQTSNPKIFAGGDMVRGSDlVVTAIWEGRQAAEGILDYL 471
Cdd:PRK13984 532 EAIGQAPDysylPEELKSKLEFV---RGRILTNEYG----QTSIPWLFAGGDIVHGPD-IIHGVADGYWAAEGIDMYL 601
|
|
| PRK12779 |
PRK12779 |
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; ... |
62-469 |
2.40e-67 |
|
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; Provisional
Pssm-ID: 183740 [Multi-domain] Cd Length: 944 Bit Score: 232.42 E-value: 2.40e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 62 CPVHNYIPNWLKLIAEGQIFQAAELCHQTNTLPEVCGRVCPQDRLCEGACTLNDgfGAVTIGNAEKYI--------NDTA 133
Cdd:PRK12779 214 CPVKIHIPEMLDLLGNGKHREALELIESCNPLPNVTGRVCPQELQCQGVCTHTK--RPIEIGQLEWYLpqheklvnPNAN 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 134 FALGWRPDmSHVKWTGKKVAIIGAGPAGLGCADILARGGVKPVVFDKRPEIGGLLTFGIPEFKMEKDVMKRRREIFTGMG 213
Cdd:PRK12779 292 ERFAGRIS-PWAAAVKPPIAVVGSGPSGLINAYLLAVEGFPVTVFEAFHDLGGVLRYGIPEFRLPNQLIDDVVEKIKLLG 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 214 IEFRLNTEIGKDVTIDELLAE-YDAVFMGMGT--YTYMKggFPGEDLDGVYDALDFLiSNVNRCQGWEKD-PSEYISMDG 289
Cdd:PRK12779 371 GRFVKNFVVGKTATLEDLKAAgFWKIFVGTGAglPTFMN--VPGEHLLGVMSANEFL-TRVNLMRGLDDDyETPLPEVKG 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 290 KKVIVLGGGDTAMDCNRTSLRQGAHdVTCAYRRDESNMPGSAREVKNAYEEGIKFLFNRQPIEIVG--ENGKVTGVKVVT 367
Cdd:PRK12779 448 KEVFVIGGGNTAMDAARTAKRLGGN-VTIVYRRTKSEMPARVEELHHALEEGINLAVLRAPREFIGddHTHFVTHALLDV 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 368 TQMGEPDSRGRRSPEPIpGSEEVLPADAVLLAFGFRPSP--ADWFGSVNINLDGSGRVVAPEQqefkfQTSNPKIFAGGD 445
Cdd:PRK12779 527 NELGEPDKSGRRSPKPT-GEIERVPVDLVIMALGNTANPimKDAEPGLKTNKWGTIEVEKGSQ-----RTSIKGVYSGGD 600
|
410 420
....*....|....*....|....
gi 523535166 446 MVRGSDLVVTAIWEGRQAAEGILD 469
Cdd:PRK12779 601 AARGGSTAIRAAGDGQAAAKEIVG 624
|
|
| Fer4_20 |
pfam14691 |
Dihydroprymidine dehydrogenase domain II, 4Fe-4S cluster; Domain II of the enzyme ... |
27-138 |
9.88e-55 |
|
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: 178.50 E-value: 9.88e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 27 RKAEFVEIYKPFTSETVTNQTHRCLGCGNPYCEWKCPVHNYIPNWLKLIAEGQIFQAAELCHQTNTLPEVCGRVCPQDRL 106
Cdd:pfam14691 1 RIKNFEEVALGYTEEEAIAEASRCLQCKDPPCVKGCPVHIDIPEFIKLIAEGNFEGAARIILETNPLPAICGRVCPQERQ 80
|
90 100 110
....*....|....*....|....*....|...
gi 523535166 107 CEGACTLN-DGFGAVTIGNAEKYINDTAFALGW 138
Cdd:pfam14691 81 CEGACVLGkKGFEPVAIGRLERFAADWARENGI 113
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
151-471 |
1.00e-39 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 145.26 E-value: 1.00e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 151 KVAIIGAGPAGLGCADILARGGVKPVVFDkRPEIGGLLT--------FGIPEFKMEKDVMKRRREIFTGMGIEFRLN--T 220
Cdd:COG0492 2 DVVIIGAGPAGLTAAIYAARAGLKTLVIE-GGEPGGQLAttkeienyPGFPEGISGPELAERLREQAERFGAEILLEevT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 221 EIGKD-----VTIDElLAEY--DAVFMGMGTYtYMKGGFPGEDldgvydalDFLISNVN---RCQGWEkdpseyisMDGK 290
Cdd:COG0492 81 SVDKDdgpfrVTTDD-GTEYeaKAVIIATGAG-PRKLGLPGEE--------EFEGRGVSycaTCDGFF--------FRGK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 291 KVIVLGGGDTAMDcNRTSLRQGAHDVTCAYRRDESN-MPGSAREVKNAyeEGIKFLFNRQPIEIVGEnGKVTGVKVVTTQ 369
Cdd:COG0492 143 DVVVVGGGDSALE-EALYLTKFASKVTLIHRRDELRaSKILVERLRAN--PKIEVLWNTEVTEIEGD-GRVEGVTLKNVK 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 370 MGEpdsrgrrspepipgsEEVLPADAVLLAFGFRPSpADWFGSVNINLDGSGRVVAPEQQEfkfqTSNPKIFAGGDMVRG 449
Cdd:COG0492 219 TGE---------------EKELEVDGVFVAIGLKPN-TELLKGLGLELDEDGYIVVDEDME----TSVPGVFAAGDVRDY 278
|
330 340
....*....|....*....|...
gi 523535166 450 S-DLVVTAIWEGRQAAEGILDYL 471
Cdd:COG0492 279 KyRQAATAAGEGAIAALSAARYL 301
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
150-460 |
2.49e-30 |
|
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: 119.35 E-value: 2.49e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 150 KKVAIIGAGPAGLGCADILARGGVKPVVFDKRPEI---GGLLTFGI-------PEFKMEKDVMKRRREIFTGM--GIEFR 217
Cdd:pfam07992 1 YDVVVIGGGPAGLAAALTLAQLGGKVTLIEDEGTCpygGCVLSKALlgaaeapEIASLWADLYKRKEEVVKKLnnGIEVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 218 LNTEI------------GKDVTIDELLAEYDAVFMGMGTYTYMkggfPGedLDGVYDALDFLISNVNRCQGWEKDPSEyi 285
Cdd:pfam07992 81 LGTEVvsidpgakkvvlEELVDGDGETITYDRLVIATGARPRL----PP--IPGVELNVGFLVRTLDSAEALRLKLLP-- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 286 smdgKKVIVLGGGDTAMDCNRTSLRQGAHdVTCAYRRDESnMPGSAREVKNAYEE-----GIKFLFNRQPIEIVGENGkv 360
Cdd:pfam07992 153 ----KRVVVVGGGYIGVELAAALAKLGKE-VTLIEALDRL-LRAFDEEISAALEKaleknGVEVRLGTSVKEIIGDGD-- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 361 tGVKVVTtqmgepdsrgrrspepipGSEEVLPADAVLLAFGFRPSPaDWFGSVNINLDGSGRVVAPEQQefkfQTSNPKI 440
Cdd:pfam07992 225 -GVEVIL------------------KDGTEIDADLVVVAIGRRPNT-ELLEAAGLELDERGGIVVDEYL----RTSVPGI 280
|
330 340
....*....|....*....|.
gi 523535166 441 FAGGDM-VRGSDLVVTAIWEG 460
Cdd:pfam07992 281 YAAGDCrVGGPELAQNAVAQG 301
|
|
| TRX_reduct |
TIGR01292 |
thioredoxin-disulfide reductase; This model describes thioredoxin-disulfide reductase, a ... |
151-471 |
4.19e-24 |
|
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: 101.93 E-value: 4.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 151 KVAIIGAGPAGLGCADILARGGVKPVVFDkRPEIGGLLTF--------GIPEF--------KMEKDVMKRRREIFTGMGI 214
Cdd:TIGR01292 1 DVIIIGAGPAGLTAAIYAARANLKPLLIE-GMEPGGQLTTttevenypGFPEGisgpelmeKMKEQAVKFGAEIIYEEVI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 215 EFRLNTEIGKDVTIDELLAEYDAVFMGMGTyTYMKGGFPGEDldgvydalDFL---ISNVNRCqgwekDPSEYismDGKK 291
Cdd:TIGR01292 80 KVDKSDRPFKVYTGDGKEYTAKAVIIATGA-SARKLGIPGED--------EFWgrgVSYCATC-----DGPFF---KNKE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 292 VIVLGGGDTAMDcNRTSLRQGAHDVTCAYRRD----ESNMPGSAREVKNayeegIKFLFNRQPIEIVGENgKVTGVKVVT 367
Cdd:TIGR01292 143 VAVVGGGDSAIE-EALYLTRIAKKVTLVHRRDkfraEKILLDRLKKNPK-----IEFLWNSTVEEIVGDN-KVEGVKIKN 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 368 TQMGEpdsrgrrspepipgsEEVLPADAVLLAFGFRPSPADWFGSvnINLDGSGRVVAPEQQefkfQTSNPKIFAGGDmV 447
Cdd:TIGR01292 216 TVTGE---------------EEELEVDGVFIAIGHEPNTELLKGL--LELDENGYIVTDEGM----RTSVPGVFAAGD-V 273
|
330 340
....*....|....*....|....*.
gi 523535166 448 RGSDL--VVTAIWEGRQAAEGILDYL 471
Cdd:TIGR01292 274 RDKGYrqAVTAAGDGCIAALSAERYL 299
|
|
| PLN02852 |
PLN02852 |
ferredoxin-NADP+ reductase |
152-424 |
5.70e-18 |
|
ferredoxin-NADP+ reductase
Pssm-ID: 215457 Cd Length: 491 Bit Score: 86.29 E-value: 5.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 152 VAIIGAGPAGLGCADILARG--GVKPVVFDKRPEIGGLLTFGI-PEFKMEKDVMKRRREIFTGMGIEFRLNTEIGKDVTI 228
Cdd:PLN02852 29 VCVVGSGPAGFYTADKLLKAhdGARVDIIERLPTPFGLVRSGVaPDHPETKNVTNQFSRVATDDRVSFFGNVTLGRDVSL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 229 DELLAEYDAVFMGMGTYTYMKGGFPGEDLDGVYDALDFLisnvnrcqGWEKDPSEYISM-----DGKKVIVLGGGDTAMD 303
Cdd:PLN02852 109 SELRDLYHVVVLAYGAESDRRLGIPGEDLPGVLSAREFV--------WWYNGHPDCVHLppdlkSSDTAVVLGQGNVALD 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 304 CNRTSLRQGAH----DVTC-------------AY---RR-------------------------DESNM---PGSAREVK 335
Cdd:PLN02852 181 CARILLRPTDElastDIAEhalealrgssvrkVYlvgRRgpvqaactakelrellglknvrvriKEADLtlsPEDEEELK 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 336 N------AYEEGIK-----------------FLFNRQPIEIV---GENGKVTGVKVVTTQMgEPDSRGRRSPEPIPGSEE 389
Cdd:PLN02852 261 AsrpkrrVYELLSKaaaagkcapsggqrelhFVFFRNPTRFLdsgDGNGHVAGVKLERTVL-EGAAGSGKQVAVGTGEFE 339
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 523535166 390 VLPADAVLLAFGFRPSPAD--WFGS---VNINLdgSGRVV 424
Cdd:PLN02852 340 DLPCGLVLKSIGYKSLPVDglPFDHkrgVVPNV--HGRVL 377
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
152-468 |
1.37e-14 |
|
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: 75.51 E-value: 1.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 152 VAIIGAGPAGLGCADILARGGVKPVVFDKRPeIGG------------LL-------------TFGI----PEFKMEKdVM 202
Cdd:COG1249 6 LVVIGAGPGGYVAAIRAAQLGLKVALVEKGR-LGGtclnvgcipskaLLhaaevahearhaaEFGIsagaPSVDWAA-LM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 203 KRRREIFTGM--GIEFRL-----------------NT-EIGKDVTIdellaEYDAVFMGMGTYTYMkggFPGEDLDGVY- 261
Cdd:COG1249 84 ARKDKVVDRLrgGVEELLkkngvdvirgrarfvdpHTvEVTGGETL-----TADHIVIATGSRPRV---PPIPGLDEVRv 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 262 ----DALDflisnvnrcqgWEKDPseyismdgKKVIVLGGGDTAMdcnrtSLRQ-----GAhDVTCAYRRDE--SNM-PG 329
Cdd:COG1249 156 ltsdEALE-----------LEELP--------KSLVVIGGGYIGL-----EFAQifarlGS-EVTLVERGDRllPGEdPE 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 330 SAREVKNAYE-EGIKFLFNRQPIEIVGENGKVTgvkvVTTQMGepdsrgrrspepipGSEEVLPADAVLLAFGFRPSPAD 408
Cdd:COG1249 211 ISEALEKALEkEGIDILTGAKVTSVEKTGDGVT----VTLEDG--------------GGEEAVEADKVLVATGRRPNTDG 272
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 523535166 409 W-FGSVNINLDGSGRVVAPEQqefkFQTSNPKIFAGGDMVRGSDLVVTAIWEGRQAAEGIL 468
Cdd:COG1249 273 LgLEAAGVELDERGGIKVDEY----LRTSVPGIYAIGDVTGGPQLAHVASAEGRVAAENIL 329
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
173-468 |
2.49e-14 |
|
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: 73.69 E-value: 2.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 173 VKPVVFDKRPEIG----GLLTFGIPEFKMEKDVMKRRREIFTGMGIEFRLNTEI------GKDVTID--ELLAeYDAVFM 240
Cdd:COG0446 6 AEITVIEKGPHHSyqpcGLPYYVGGGIKDPEDLLVRTPESFERKGIDVRTGTEVtaidpeAKTVTLRdgETLS-YDKLVL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 241 GMGTyTYMKGGFPGEDLDGVY-----DALDFLISNVNrcqgwekdpseyiSMDGKKVIVLGGGDTA--MDCNrtsLRQGA 313
Cdd:COG0446 85 ATGA-RPRPPPIPGLDLPGVFtlrtlDDADALREALK-------------EFKGKRAVVIGGGPIGleLAEA---LRKRG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 314 HDVTCAYRRDESnMPGSAREVKNAYEE-----GIKFLFNRQPIEIVGENGkvtgVKVVTTqmgepdsrgrrspepipgSE 388
Cdd:COG0446 148 LKVTLVERAPRL-LGVLDPEMAALLEEelrehGVELRLGETVVAIDGDDK----VAVTLT------------------DG 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 389 EVLPADAVLLAFGFRPSpADWFGSVNINLDGSGRVVAPEQQefkfQTSNPKIFAGGDMVRGSDLVV----------TAIW 458
Cdd:COG0446 205 EEIPADLVVVAPGVRPN-TELAKDAGLALGERGWIKVDETL----QTSDPDVYAAGDCAEVPHPVTgktvyiplasAANK 279
|
330
....*....|
gi 523535166 459 EGRQAAEGIL 468
Cdd:COG0446 280 QGRVAAENIL 289
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
150-468 |
2.01e-13 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 71.71 E-value: 2.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 150 KKVAIIGAGPAGLGCAD-ILARGGVKPV-VFDK-------RPeiggLLTFGIPEFKMEKDVMKRRREIFTGMGIEFRLNT 220
Cdd:COG1251 2 MRIVIIGAGMAGVRAAEeLRKLDPDGEItVIGAephppynRP----PLSKVLAGETDEEDLLLRPADFYEENGIDLRLGT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 221 EI------GKDVTID--ELLAeYDAVFMGMGTYTYMkGGFPGEDLDGVY------DALDFLisnvnrcqgwekdpsEYIS 286
Cdd:COG1251 78 RVtaidraARTVTLAdgETLP-YDKLVLATGSRPRV-PPIPGADLPGVFtlrtldDADALR---------------AALA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 287 mDGKKVIVLGGG----DTAMDcnrtsLRQGAHDVTCAYRRD---ESNM-PGSAREVKNAYEE-GIKFLFNRQPIEIVGEn 357
Cdd:COG1251 141 -PGKRVVVIGGGliglEAAAA-----LRKRGLEVTVVERAPrllPRQLdEEAGALLQRLLEAlGVEVRLGTGVTEIEGD- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 358 GKVTGVKVvttqmgepdsrgrrspepipGSEEVLPADAVLLAFGFRPSpADWFGSVNINLDGsGrVVAPEQqefkFQTSN 437
Cdd:COG1251 214 DRVTGVRL--------------------ADGEELPADLVVVAIGVRPN-TELARAAGLAVDR-G-IVVDDY----LRTSD 266
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 523535166 438 PKIFAGGD------MVRGSDLV--VTAIWE-GRQAAEGIL 468
Cdd:COG1251 267 PDIYAAGDcaehpgPVYGRRVLelVAPAYEqARVAAANLA 306
|
|
| PRK07233 |
PRK07233 |
hypothetical protein; Provisional |
151-199 |
5.62e-09 |
|
hypothetical protein; Provisional
Pssm-ID: 235977 [Multi-domain] Cd Length: 434 Bit Score: 57.97 E-value: 5.62e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 523535166 151 KVAIIGAGPAGLGCADILARGGVKPVVFDKRPEIGGLL-TFGIPEFKMEK 199
Cdd:PRK07233 1 KIAIVGGGIAGLAAAYRLAKRGHEVTVFEADDQLGGLAaSFEFGGLPIER 50
|
|
| CzcO |
COG2072 |
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ... |
152-322 |
2.20e-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: 56.02 E-value: 2.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 152 VAIIGAGPAGLGCADILARGGVKPVVFDKRPEIGG---------------LLTFGIPEFKME--------KDVMKR---- 204
Cdd:COG2072 9 VVVIGAGQAGLAAAYHLRRAGIDFVVLEKADDVGGtwrdnrypglrldtpSHLYSLPFFPNWsddpdfptGDEILAylea 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 205 -------RREIFTGMGIE----------FRLNTEIGKDVTidellaeYDAVFMGMGTYTymKG---GFPGEDldgvydal 264
Cdd:COG2072 89 yadkfglRRPIRFGTEVTsarwdeadgrWTVTTDDGETLT-------ARFVVVATGPLS--RPkipDIPGLE-------- 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 523535166 265 DFlisnvnrcQG-------WeKDPSEYismDGKKVIVLGGGDTAMDCNRTSLRQGAHdVTCAYRR 322
Cdd:COG2072 152 DF--------AGeqlhsadW-RNPVDL---AGKRVLVVGTGASAVQIAPELARVAAH-VTVFQRT 203
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
152-470 |
2.29e-08 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 56.34 E-value: 2.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 152 VAIIGAGPAGLGCADILARGGVKPVVFDKRP------------------------EIGGLLTFGI--PEFKME-KDVMKR 204
Cdd:PRK06292 6 VIVIGAGPAGYVAARRAAKLGKKVALIEKGPlggtclnvgcipskaliaaaeafhEAKHAEEFGIhaDGPKIDfKKVMAR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 205 RREI---FTGmGIEFRLNTEIGKD-------------VTIDELLAEYDAVFMGMG-TYTYMKGGFPGEDlDGVYDALDFL 267
Cdd:PRK06292 86 VRRErdrFVG-GVVEGLEKKPKIDkikgtarfvdpntVEVNGERIEAKNIVIATGsRVPPIPGVWLILG-DRLLTSDDAF 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 268 IsnvnrcqgWEKDPseyismdgKKVIVLGGGDTAMDcnrtsL-----RQGAhDVTCAYRRDE--SNM-PGSAREVKNAYE 339
Cdd:PRK06292 164 E--------LDKLP--------KSLAVIGGGVIGLE-----LgqalsRLGV-KVTVFERGDRilPLEdPEVSKQAQKILS 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 340 EGIKFLFNRQPIEIVGENGkvtgVKVVTTQMGepdsrgrrspepipGSEEVLPADAVLLAFGFRP-SPADWFGSVNINLD 418
Cdd:PRK06292 222 KEFKIKLGAKVTSVEKSGD----EKVEELEKG--------------GKTETIEADYVLVATGRRPnTDGLGLENTGIELD 283
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 523535166 419 GSGRVVAPEqqefKFQTSNPKIFAGGDMVRGSDLVVTAIWEGRQAAEGILDY 470
Cdd:PRK06292 284 ERGRPVVDE----HTQTSVPGIYAAGDVNGKPPLLHEAADEGRIAAENAAGD 331
|
|
| COG3380 |
COG3380 |
Predicted NAD/FAD-dependent oxidoreductase [General function prediction only]; |
150-186 |
3.03e-08 |
|
Predicted NAD/FAD-dependent oxidoreductase [General function prediction only];
Pssm-ID: 442607 [Multi-domain] Cd Length: 331 Bit Score: 55.27 E-value: 3.03e-08
10 20 30
....*....|....*....|....*....|....*..
gi 523535166 150 KKVAIIGAGPAGLGCADILARGGVKPVVFDKRPEIGG 186
Cdd:COG3380 4 PDIAIIGAGIAGLAAARALQDAGHEVTVFEKSRGVGG 40
|
|
| HemY |
COG1232 |
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ... |
150-188 |
3.06e-08 |
|
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: 55.61 E-value: 3.06e-08
10 20 30
....*....|....*....|....*....|....*....
gi 523535166 150 KKVAIIGAGPAGLGCADILARGGVKPVVFDKRPEIGGLL 188
Cdd:COG1232 2 KRVAVIGGGIAGLTAAYRLAKAGHEVTVLEASDRVGGLI 40
|
|
| COG2509 |
COG2509 |
FAD-dependent dehydrogenase [General function prediction only]; |
144-221 |
1.04e-07 |
|
FAD-dependent dehydrogenase [General function prediction only];
Pssm-ID: 441999 [Multi-domain] Cd Length: 466 Bit Score: 53.96 E-value: 1.04e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 523535166 144 HVKWTGKKVAIIGAGPAGLGCADILARGGVKPVVFDKrpeiGglltfgipefkmeKDVMKRRREIFTGMGiEFRLNTE 221
Cdd:COG2509 25 GIPSLKYDVVIVGAGPAGLFAALELAEAGLKPLVLER----G-------------KDVEERTCPVAEFWR-KGKCNPE 84
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
150-471 |
1.19e-07 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 53.60 E-value: 1.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 150 KKVAIIGAGPAGLGCADILAR---GGVKPVVFDKRPE----------IGGLLTFGipefkmekDVMKRRREIFTGMGIEF 216
Cdd:COG1252 2 KRIVIVGGGFAGLEAARRLRKklgGDAEVTLIDPNPYhlfqpllpevAAGTLSPD--------DIAIPLRELLRRAGVRF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 217 RLN--TEI---GKDVTID---ELlaEYDAVFMGMGTyTYMKGGFPGED-----LDGVYDALDF---LISNVNRcqgwekd 280
Cdd:COG1252 74 IQGevTGIdpeARTVTLAdgrTL--SYDYLVIATGS-VTNFFGIPGLAehalpLKTLEDALALrerLLAAFER------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 281 pseYISMDGKKVIVLGGGDT------AMD------CNRTSLRQGAHDVTCAYRRDE--SNMPGSARE-VKNAYEE-GIKF 344
Cdd:COG1252 144 ---AERRRLLTIVVVGGGPTgvelagELAellrklLRYPGIDPDKVRITLVEAGPRilPGLGEKLSEaAEKELEKrGVEV 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 345 LFNRQPIEIVGEngkvtgvKVVTTqmgepdsrgrrspepipgSEEVLPADAVLLAFGFRPSPadWFGSVNINLDGSGRVV 424
Cdd:COG1252 221 HTGTRVTEVDAD-------GVTLE------------------DGEEIPADTVIWAAGVKAPP--LLADLGLPTDRRGRVL 273
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 523535166 425 APEQqefkFQT-SNPKIFAGGDMVRGSD--------LVVTAIWEGRQAAEGILDYL 471
Cdd:COG1252 274 VDPT----LQVpGHPNVFAIGDCAAVPDpdgkpvpkTAQAAVQQAKVLAKNIAALL 325
|
|
| PRK07208 |
PRK07208 |
hypothetical protein; Provisional |
150-187 |
1.98e-07 |
|
hypothetical protein; Provisional
Pssm-ID: 235967 [Multi-domain] Cd Length: 479 Bit Score: 53.35 E-value: 1.98e-07
10 20 30
....*....|....*....|....*....|....*...
gi 523535166 150 KKVAIIGAGPAGLGCADILARGGVKPVVFDKRPEIGGL 187
Cdd:PRK07208 5 KSVVIIGAGPAGLTAAYELLKRGYPVTVLEADPVVGGI 42
|
|
| HdrA |
COG1148 |
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion]; |
150-464 |
2.18e-07 |
|
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
Pssm-ID: 440762 [Multi-domain] Cd Length: 563 Bit Score: 53.33 E-value: 2.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 150 KKVAIIGAGPAGLGCADILARGGVKPVVFDKRPEIGGL---LTFGIPEFK--------MEKDVMKRRReiftgmgIEFRL 218
Cdd:COG1148 141 KRALVIGGGIAGMTAALELAEQGYEVYLVEKEPELGGRaaqLHKTFPGLDcpqcilepLIAEVEANPN-------ITVYT 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 219 NTEIGK--------DVTI-----DELLAEYDAVFMGMGTYTYMKGGFP----GEDlDGVYDALDF--LISNvnrcqGWEK 279
Cdd:COG1148 214 GAEVEEvsgyvgnfTVTIkkgprEEIEIEVGAIVLATGFKPYDPTKLGeygyGKY-PNVITNLELerLLAA-----GKIL 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 280 DPSeyismDGKK----VIVL--GGGDTAMD---CNR----TSLRQgAH---------DVTCAYR--RdesnMPGSARE-V 334
Cdd:COG1148 288 RPS-----DGKEpksvAFIQcvGSRDEENGlpyCSRvccmYALKQ-ALylkeknpdaDVYIFYRdiR----TYGKYEEfY 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 335 KNAYEEGIKFLfnR-QPIEIV-GENGKVTgVKVVTTQMGEPdsrgrrspepipgseEVLPADAVLLAFGFRPSP-ADWFG 411
Cdd:COG1148 358 RRAREDGVRFI--RgRVAEIEeDEGGKLV-VTVEDTLLGEP---------------VEIEADLVVLATGMVPSEdNEELA 419
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 523535166 412 SV-NINLDGSGRVVAPEQQEFKFQTSNPKIFAGGdMVRGSDLVVTAIWEGRQAA 464
Cdd:COG1148 420 KLlKLPLDQDGFFLEAHPKLRPVETATDGIFLAG-AAHGPKDIPESIAQATAAA 472
|
|
| PTZ00188 |
PTZ00188 |
adrenodoxin reductase; Provisional |
151-243 |
3.26e-07 |
|
adrenodoxin reductase; Provisional
Pssm-ID: 240308 Cd Length: 506 Bit Score: 52.58 E-value: 3.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 151 KVAIIGAGPAGLGCAD-ILARGGVKPVVFDKRPEIGGLLTFGI-PEFKMEKDVMKRRREIFTGMGIEFRLNTEIGKDVTI 228
Cdd:PTZ00188 41 KVGIIGAGPSALYCCKhLLKHERVKVDIFEKLPNPYGLIRYGVaPDHIHVKNTYKTFDPVFLSPNYRFFGNVHVGVDLKM 120
|
90
....*....|....*
gi 523535166 229 DELLAEYDAVFMGMG 243
Cdd:PTZ00188 121 EELRNHYNCVIFCCG 135
|
|
| COG1233 |
COG1233 |
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ... |
150-196 |
6.34e-07 |
|
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440846 [Multi-domain] Cd Length: 491 Bit Score: 51.77 E-value: 6.34e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 523535166 150 KKVAIIGAGPAGLGCADILARGGVKPVVFDKRPEIGGLL-TFGIPEFK 196
Cdd:COG1233 4 YDVVVIGAGIGGLAAAALLARAGYRVTVLEKNDTPGGRArTFERPGFR 51
|
|
| NAD_binding_8 |
pfam13450 |
NAD(P)-binding Rossmann-like domain; |
154-186 |
6.43e-07 |
|
NAD(P)-binding Rossmann-like domain;
Pssm-ID: 433218 [Multi-domain] Cd Length: 67 Bit Score: 46.37 E-value: 6.43e-07
10 20 30
....*....|....*....|....*....|...
gi 523535166 154 IIGAGPAGLGCADILARGGVKPVVFDKRPEIGG 186
Cdd:pfam13450 1 IVGAGLAGLVAAALLAKRGFRVLVLEKRDRLGG 33
|
|
| YobN |
COG1231 |
Monoamine oxidase [Amino acid transport and metabolism]; |
142-186 |
6.65e-07 |
|
Monoamine oxidase [Amino acid transport and metabolism];
Pssm-ID: 440844 [Multi-domain] Cd Length: 440 Bit Score: 51.46 E-value: 6.65e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 523535166 142 MSHVKwTGKKVAIIGAGPAGLGCADILARGGVKPVVFDKRPEIGG 186
Cdd:COG1231 1 MSRRA-RGKDVVIVGAGLAGLAAARELRKAGLDVTVLEARDRVGG 44
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
151-222 |
7.32e-07 |
|
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.
Pssm-ID: 425450 [Multi-domain] Cd Length: 80 Bit Score: 46.81 E-value: 7.32e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 523535166 151 KVAIIGAGPAGLGCADILARGGVKPVVFDKRPEIGGlltfgipefKMEKDVMKRRREIFTGMGIEFRLNTEI 222
Cdd:pfam00070 1 RVVVVGGGYIGLELAGALARLGSKVTVVERRDRLLP---------GFDPEIAKILQEKLEKNGIEFLLNTTV 63
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
122-243 |
1.62e-06 |
|
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: 50.47 E-value: 1.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 122 IGNAEKYI--NDTAFALGWRPdmshvkwtgKKVAIIGAGPAGLGCADILARGGVKPVVFDKRPEIGGlltfgipefKMEK 199
Cdd:COG1249 148 PGLDEVRVltSDEALELEELP---------KSLVVIGGGYIGLEFAQIFARLGSEVTLVERGDRLLP---------GEDP 209
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 523535166 200 DVMKRRREIFTGMGIEFRLNTEI--------GKDVTID----ELLAEYDAVFMGMG 243
Cdd:COG1249 210 EISEALEKALEKEGIDILTGAKVtsvektgdGVTVTLEdgggEEAVEADKVLVATG 265
|
|
| MurD |
COG0771 |
UDP-N-acetylmuramoylalanine-D-glutamate ligase [Cell wall/membrane/envelope biogenesis]; ... |
147-183 |
1.97e-06 |
|
UDP-N-acetylmuramoylalanine-D-glutamate ligase [Cell wall/membrane/envelope biogenesis]; UDP-N-acetylmuramoylalanine-D-glutamate ligase is part of the Pathway/BioSystem: Mureine biosynthesis
Pssm-ID: 440534 [Multi-domain] Cd Length: 445 Bit Score: 50.08 E-value: 1.97e-06
10 20 30
....*....|....*....|....*....|....*..
gi 523535166 147 WTGKKVAIIGAGPAGLGCADILARGGVKPVVFDKRPE 183
Cdd:COG0771 2 LKGKKVLVLGLGKSGLAAARLLAKLGAEVTVSDDRPA 38
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
144-243 |
2.22e-06 |
|
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: 49.24 E-value: 2.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 144 HVKWTGKKVAIIGAGPAGLGCADILARGGVKPVVFDKRPEIGglltfgipeFKMEKDVMKRRREIFTGMGIEFRLNTEI- 222
Cdd:pfam07992 147 RLKLLPKRVVVVGGGYIGVELAAALAKLGKEVTLIEALDRLL---------RAFDEEISAALEKALEKNGVEVRLGTSVk 217
|
90 100
....*....|....*....|....*....
gi 523535166 223 -----GKDVTI---DELLAEYDAVFMGMG 243
Cdd:pfam07992 218 eiigdGDGVEVilkDGTEIDADLVVVAIG 246
|
|
| COG3349 |
COG3349 |
Uncharacterized protein, contains NAD-binding domain and a Fe-S cluster [General function ... |
148-186 |
2.59e-06 |
|
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: 49.47 E-value: 2.59e-06
10 20 30
....*....|....*....|....*....|....*....
gi 523535166 148 TGKKVAIIGAGPAGLGCADILARGGVKPVVFDKRPEIGG 186
Cdd:COG3349 2 MPPRVVVVGGGLAGLAAAVELAEAGFRVTLLEARPRLGG 40
|
|
| DAO |
pfam01266 |
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ... |
151-216 |
1.03e-05 |
|
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: 47.39 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 151 KVAIIGAGPAGLGCADILARGGVKPVVFDKRPEIG--------GLLTFGIPE------FKMEKDVMKRRREIFTGMGIEF 216
Cdd:pfam01266 1 DVVVIGGGIVGLSTAYELARRGLSVTLLERGDDPGsgasgrnaGLIHPGLRYlepselARLALEALDLWEELEEELGIDC 80
|
|
| HI0933_like |
pfam03486 |
HI0933-like protein; |
150-185 |
1.34e-05 |
|
HI0933-like protein;
Pssm-ID: 427330 [Multi-domain] Cd Length: 406 Bit Score: 47.19 E-value: 1.34e-05
10 20 30
....*....|....*....|....*....|....*.
gi 523535166 150 KKVAIIGAGPAGLGCADILARGGVKPVVFDKRPEIG 185
Cdd:pfam03486 1 FDVIVIGGGAAGLMAAISAAKRGRRVLLIEKGKKLG 36
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
291-363 |
1.60e-05 |
|
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.
Pssm-ID: 425450 [Multi-domain] Cd Length: 80 Bit Score: 42.96 E-value: 1.60e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 523535166 291 KVIVLGGGDTAMDCNrTSLRQGAHDVTCAYRRDE--SNMPGSAREV--KNAYEEGIKFLFNRQPIEIVGENGKVTGV 363
Cdd:pfam00070 1 RVVVVGGGYIGLELA-GALARLGSKVTVVERRDRllPGFDPEIAKIlqEKLEKNGIEFLLNTTVEAIEGNGDGVVVV 76
|
|
| YhiN |
COG2081 |
Predicted flavoprotein YhiN [General function prediction only]; |
153-185 |
1.86e-05 |
|
Predicted flavoprotein YhiN [General function prediction only];
Pssm-ID: 441684 [Multi-domain] Cd Length: 402 Bit Score: 46.97 E-value: 1.86e-05
10 20 30
....*....|....*....|....*....|...
gi 523535166 153 AIIGAGPAGLGCADILARGGVKPVVFDKRPEIG 185
Cdd:COG2081 1 IVIGAGAAGLMAAITAAERGARVLLLEKNPKVG 33
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
128-243 |
2.44e-05 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 46.71 E-value: 2.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 128 YINDTAFALGWRPdmshvkwtgKKVAIIGAGPAGLGCADILARGGVKPVVFDKRPEIGGLltfgipefkMEKDVMKRRRE 207
Cdd:PRK06292 157 LTSDDAFELDKLP---------KSLAVIGGGVIGLELGQALSRLGVKVTVFERGDRILPL---------EDPEVSKQAQK 218
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 523535166 208 IFTGMgIEFRLNTEI-----------------GKDVTIdellaEYDAVFMGMG 243
Cdd:PRK06292 219 ILSKE-FKIKLGAKVtsveksgdekveelekgGKTETI-----EADYVLVATG 265
|
|
| UbiH |
COG0654 |
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ... |
151-185 |
3.48e-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: 3.48e-05
10 20 30
....*....|....*....|....*....|....*
gi 523535166 151 KVAIIGAGPAGLGCADILARGGVKPVVFDKRPEIG 185
Cdd:COG0654 5 DVLIVGGGPAGLALALALARAGIRVTVVERAPPPR 39
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
146-243 |
8.80e-05 |
|
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: 44.42 E-value: 8.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 146 KWTGKKVAIIGAGPAGLGCADILARGGVKPVVFDKRPeigGLLTFGIPEF-KMEKDVMKRRreiftgmGIEFRLNTEI-- 222
Cdd:COG0446 121 EFKGKRAVVIGGGPIGLELAEALRKRGLKVTLVERAP---RLLGVLDPEMaALLEEELREH-------GVELRLGETVva 190
|
90 100
....*....|....*....|....*....
gi 523535166 223 ---GKDVTI-----DELlaEYDAVFMGMG 243
Cdd:COG0446 191 idgDDKVAVtltdgEEI--PADLVVVAPG 217
|
|
| PRK08243 |
PRK08243 |
4-hydroxybenzoate 3-monooxygenase; Validated |
151-181 |
1.27e-04 |
|
4-hydroxybenzoate 3-monooxygenase; Validated
Pssm-ID: 236198 [Multi-domain] Cd Length: 392 Bit Score: 44.02 E-value: 1.27e-04
10 20 30
....*....|....*....|....*....|.
gi 523535166 151 KVAIIGAGPAGLGCADILARGGVKPVVFDKR 181
Cdd:PRK08243 4 QVAIIGAGPAGLLLGQLLHLAGIDSVVLERR 34
|
|
| PLN00093 |
PLN00093 |
geranylgeranyl diphosphate reductase; Provisional |
151-205 |
1.79e-04 |
|
geranylgeranyl diphosphate reductase; Provisional
Pssm-ID: 177713 [Multi-domain] Cd Length: 450 Bit Score: 43.97 E-value: 1.79e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 523535166 151 KVAIIGAGPAGLGCADILARGGVKPVVFDKRPE----IGGlltfGIP-----EFKMEKDVMKRR 205
Cdd:PLN00093 41 RVAVIGGGPAGACAAETLAKGGIETFLIERKLDnakpCGG----AIPlcmvgEFDLPLDIIDRK 100
|
|
| PLN02976 |
PLN02976 |
amine oxidase |
149-186 |
2.37e-04 |
|
amine oxidase
Pssm-ID: 215527 [Multi-domain] Cd Length: 1713 Bit Score: 44.09 E-value: 2.37e-04
10 20 30
....*....|....*....|....*....|....*...
gi 523535166 149 GKKVAIIGAGPAGLGCADILARGGVKPVVFDKRPEIGG 186
Cdd:PLN02976 693 RKKIIVVGAGPAGLTAARHLQRQGFSVTVLEARSRIGG 730
|
|
| PRK06116 |
PRK06116 |
glutathione reductase; Validated |
290-465 |
2.38e-04 |
|
glutathione reductase; Validated
Pssm-ID: 235701 [Multi-domain] Cd Length: 450 Bit Score: 43.22 E-value: 2.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 290 KKVIVLGGGDTAMD--CNRTSLrqGAhDVTCAYRRDE--SNMPGSARE--VKNAYEEGIKFLFNRQPIEIV-GENGKVTg 362
Cdd:PRK06116 168 KRVAVVGAGYIAVEfaGVLNGL--GS-ETHLFVRGDAplRGFDPDIREtlVEEMEKKGIRLHTNAVPKAVEkNADGSLT- 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 363 vkvVTTQMGEpdsrgrrspepipgseeVLPADAVLLAFGFRPSpADWFG--SVNINLDGSGRVVAPEQQefkfQTSNPKI 440
Cdd:PRK06116 244 ---LTLEDGE-----------------TLTVDCLIWAIGREPN-TDGLGleNAGVKLNEKGYIIVDEYQ----NTNVPGI 298
|
170 180
....*....|....*....|....*
gi 523535166 441 FAGGDMVRGSDLVVTAIWEGRQAAE 465
Cdd:PRK06116 299 YAVGDVTGRVELTPVAIAAGRRLSE 323
|
|
| Malic_M |
smart00919 |
Malic enzyme, NAD binding domain; Malic enzymes (malate oxidoreductases) catalyse the ... |
148-198 |
2.76e-04 |
|
Malic enzyme, NAD binding domain; Malic enzymes (malate oxidoreductases) catalyse the oxidative decarboxylation of malate to form pyruvate.
Pssm-ID: 214912 Cd Length: 231 Bit Score: 42.40 E-value: 2.76e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 523535166 148 TGK-----KVAIIGAGPAGLGCADILARGGVKP---VVFDKRpeigGLLTFG----IPEFKME 198
Cdd:smart00919 19 TGKkledqRIVVNGAGAAGIGIAKLLVAAGVKRkniWLVDSK----GLLTKGrednLNPYKKP 77
|
|
| AlaDh_PNT_C |
smart01002 |
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the ... |
151-238 |
3.01e-04 |
|
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the NAD-dependent reversible reductive amination of pyruvate into alanine.
Pssm-ID: 214966 [Multi-domain] Cd Length: 149 Bit Score: 40.95 E-value: 3.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 151 KVAIIGAGPAGLGCADILARGGVKPVVFDKRPEigglltfgipefkmekdvmkRRREIFTGMGIEFrlNTEIGKDVTIDE 230
Cdd:smart01002 22 KVVVIGAGVVGLGAAATAKGLGAEVTVLDVRPA--------------------RLRQLESLLGARF--TTLYSQAELLEE 79
|
....*...
gi 523535166 231 LLAEYDAV 238
Cdd:smart01002 80 AVKEADLV 87
|
|
| PLN02172 |
PLN02172 |
flavin-containing monooxygenase FMO GS-OX |
148-187 |
3.14e-04 |
|
flavin-containing monooxygenase FMO GS-OX
Pssm-ID: 215116 [Multi-domain] Cd Length: 461 Bit Score: 42.93 E-value: 3.14e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 523535166 148 TGKKVAIIGAGPAGLGCADILARGGVKPVVFDKRPEIGGL 187
Cdd:PLN02172 9 NSQHVAVIGAGAAGLVAARELRREGHTVVVFEREKQVGGL 48
|
|
| TIGR00275 |
TIGR00275 |
flavoprotein, HI0933 family; The model when searched with a partial length search brings in ... |
153-185 |
3.71e-04 |
|
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: 42.58 E-value: 3.71e-04
10 20 30
....*....|....*....|....*....|...
gi 523535166 153 AIIGAGPAGLGCADILARGGVKPVVFDKRPEIG 185
Cdd:TIGR00275 1 IIIGGGAAGLMAAITAARAGLSVLLLEKNKKIG 33
|
|
| mhpA |
PRK06183 |
bifunctional 3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic acid hydroxylase; |
152-184 |
3.82e-04 |
|
bifunctional 3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic acid hydroxylase;
Pssm-ID: 235727 [Multi-domain] Cd Length: 500 Bit Score: 42.97 E-value: 3.82e-04
10 20 30
....*....|....*....|....*....|...
gi 523535166 152 VAIIGAGPAGLGCADILARGGVKPVVFDKRPEI 184
Cdd:PRK06183 13 VVIVGAGPVGLTLANLLGQYGVRVLVLERWPTL 45
|
|
| YdhS |
COG4529 |
Uncharacterized NAD(P)/FAD-binding protein YdhS [General function prediction only]; |
150-185 |
4.04e-04 |
|
Uncharacterized NAD(P)/FAD-binding protein YdhS [General function prediction only];
Pssm-ID: 443597 [Multi-domain] Cd Length: 466 Bit Score: 42.63 E-value: 4.04e-04
10 20 30
....*....|....*....|....*....|....*....
gi 523535166 150 KKVAIIGAGPAGLGCADILARGGVKP---VVFDKRPEIG 185
Cdd:COG4529 6 KRIAIIGGGASGTALAIHLLRRAPEPlriTLFEPRPELG 44
|
|
| Pyr_redox_3 |
pfam13738 |
Pyridine nucleotide-disulphide oxidoreductase; |
279-444 |
6.44e-04 |
|
Pyridine nucleotide-disulphide oxidoreductase;
Pssm-ID: 404603 [Multi-domain] Cd Length: 296 Bit Score: 41.44 E-value: 6.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 279 KDPSEYismDGKKVIVLGGGDTAMDcnrTSL---RQGAhDVTCAYRRDESNMPGSA----------REVKNAYEEG-IKF 344
Cdd:pfam13738 148 KDFHPY---AGQKVVVIGGYNSAVD---AALelvRKGA-RVTVLYRGSEWEDRDSDpsyslspdtlNRLEELVKNGkIKA 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 345 LFNRQPIEIVGENGKVtgvkVVTTQMGepdsrgrrspepipgsEEVLPADAVLLAFGFRPSpADWFGSVNINLDGSGRvv 424
Cdd:pfam13738 221 HFNAEVKEITEVDVSY----KVHTEDG----------------RKVTSNDDPILATGYHPD-LSFLKKGLFELDEDGR-- 277
|
170 180
....*....|....*....|
gi 523535166 425 aPEQQEFKFQTSNPKIFAGG 444
Cdd:pfam13738 278 -PVLTEETESTNVPGLFLAG 296
|
|
| FAD_oxidored |
pfam12831 |
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases ... |
152-191 |
8.17e-04 |
|
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases and related proteins.
Pssm-ID: 432816 [Multi-domain] Cd Length: 420 Bit Score: 41.83 E-value: 8.17e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 523535166 152 VAIIGAGPAGLGCADILARGGVKPVVFDKRPEIGGLLTFG 191
Cdd:pfam12831 2 VVVVGGGPAGVAAAIAAARAGAKVLLVERRGFLGGMLTSG 41
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
130-222 |
9.78e-04 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 41.34 E-value: 9.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 130 NDTAFALGWRPdmshvkwtgKKVAIIGAGPAGLGCADILARGGVKPVVFDKRPEIgglltfgIPefKMEKDVMKRRREIF 209
Cdd:PRK06370 161 NETIFSLDELP---------EHLVIIGGGYIGLEFAQMFRRFGSEVTVIERGPRL-------LP--REDEDVAAAVREIL 222
|
90
....*....|...
gi 523535166 210 TGMGIEFRLNTEI 222
Cdd:PRK06370 223 EREGIDVRLNAEC 235
|
|
| PRK07588 |
PRK07588 |
FAD-binding domain; |
150-218 |
1.15e-03 |
|
FAD-binding domain;
Pssm-ID: 169028 [Multi-domain] Cd Length: 391 Bit Score: 41.26 E-value: 1.15e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 523535166 150 KKVAIIGAGPAGLGCADILARGGVKPVVFDKRPEI--GG-LLTFGIPEFkmekDVMKRrreiftgMGIEFRL 218
Cdd:PRK07588 1 MKVAISGAGIAGPTLAYWLRRYGHEPTLIERAPELrtGGyMVDFWGVGY----EVAKR-------MGITDQL 61
|
|
| FMO-like |
pfam00743 |
Flavin-binding monooxygenase-like; This family includes FMO proteins, cyclohexanone ... |
149-190 |
1.39e-03 |
|
Flavin-binding monooxygenase-like; This family includes FMO proteins, cyclohexanone mono-oxygenase and a number of different mono-oxygenases.
Pssm-ID: 395602 [Multi-domain] Cd Length: 531 Bit Score: 40.92 E-value: 1.39e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 523535166 149 GKKVAIIGAGPAGLGCADILARGGVKPVVFDKRPEIGGLLTF 190
Cdd:pfam00743 1 AKKVAVIGAGVSGLASIKCCLEEGLEPTCFERSDDIGGLWRF 42
|
|
| FAD_binding_3 |
pfam01494 |
FAD binding domain; This domain is involved in FAD binding in a number of enzymes. |
151-183 |
1.55e-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: 40.77 E-value: 1.55e-03
10 20 30
....*....|....*....|....*....|...
gi 523535166 151 KVAIIGAGPAGLGCADILARGGVKPVVFDKRPE 183
Cdd:pfam01494 3 DVLIVGGGPAGLMLALLLARAGVRVVLVERHAT 35
|
|
| PRK07251 |
PRK07251 |
FAD-containing oxidoreductase; |
150-243 |
1.63e-03 |
|
FAD-containing oxidoreductase;
Pssm-ID: 180907 [Multi-domain] Cd Length: 438 Bit Score: 40.89 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 150 KKVAIIGAGPAGLGCADILARGGVKPVVFDKRPEIGGlltfgipefKMEKDVMKRRREIFTGMGIEFRLN---TEIGKD- 225
Cdd:PRK07251 158 ERLGIIGGGNIGLEFAGLYNKLGSKVTVLDAASTILP---------REEPSVAALAKQYMEEDGITFLLNahtTEVKNDg 228
|
90 100
....*....|....*....|..
gi 523535166 226 ----VTIDELLAEYDAVFMGMG 243
Cdd:PRK07251 229 dqvlVVTEDETYRFDALLYATG 250
|
|
| PRK09126 |
PRK09126 |
FAD-dependent hydroxylase; |
152-183 |
1.95e-03 |
|
FAD-dependent hydroxylase;
Pssm-ID: 236385 [Multi-domain] Cd Length: 392 Bit Score: 40.31 E-value: 1.95e-03
10 20 30
....*....|....*....|....*....|..
gi 523535166 152 VAIIGAGPAGLGCADILARGGVKPVVFDKRPE 183
Cdd:PRK09126 6 IVVVGAGPAGLSFARSLAGSGLKVTLIERQPL 37
|
|
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
386-473 |
2.45e-03 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 40.13 E-value: 2.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 386 GSEEVLPADAVLLAFGFRPSPADwFG--SVNINLDGsGRVVAPEQQefkfQTSNPKIFAGGDMVRGSDLVVTAIWEGRQA 463
Cdd:PRK06416 254 GKEETLEADYVLVAVGRRPNTEN-LGleELGVKTDR-GFIEVDEQL----RTNVPNIYAIGDIVGGPMLAHKASAEGIIA 327
|
90
....*....|....*.
gi 523535166 464 AEGI------LDYLGV 473
Cdd:PRK06416 328 AEAIagnphpIDYRGI 343
|
|
| Thi4 |
pfam01946 |
Thi4 family; This family includes Swiss:P32318 a putative thiamine biosynthetic enzyme. |
152-186 |
4.61e-03 |
|
Thi4 family; This family includes Swiss:P32318 a putative thiamine biosynthetic enzyme.
Pssm-ID: 460393 Cd Length: 232 Bit Score: 38.61 E-value: 4.61e-03
10 20 30
....*....|....*....|....*....|....*.
gi 523535166 152 VAIIGAGPAGLGCADILAR-GGVKPVVFDKRPEIGG 186
Cdd:pfam01946 20 VVIVGAGSSGLTAAYYLAKnRGLKVAIIERSVSPGG 55
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
150-445 |
5.33e-03 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 39.25 E-value: 5.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 150 KKVAIIGAGPAGLGCADILARggVKP----VVFDKRPEIG----GLLTFGIPEFKMEKDVMKRRREIFTGMGIEFRLNTE 221
Cdd:PRK09564 1 MKIIIIGGTAAGMSAAAKAKR--LNKeleiTVYEKTDIVSfgacGLPYFVGGFFDDPNTMIARTPEEFIKSGIDVKTEHE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 222 I------GKDVTIDELLAE------YDAVFMGMGTYTYMKGgFPGEDLDGVYDALDFLISNVNRCQGWEKDpseyismdG 289
Cdd:PRK09564 79 VvkvdakNKTITVKNLKTGsifndtYDKLMIATGARPIIPP-IKNINLENVYTLKSMEDGLALKELLKDEE--------I 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 290 KKVIVLGGGDTAMDCNRTSLRQGAHdVTcAYRRDESNMPGS-AREVKNAYEE-----GIKFLFNRQPIEIVGENgKVTGV 363
Cdd:PRK09564 150 KNIVIIGAGFIGLEAVEAAKHLGKN-VR-IIQLEDRILPDSfDKEITDVMEEelrenGVELHLNEFVKSLIGED-KVEGV 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523535166 364 KvvtTQMGEPDsrgrrspepipgseevlpADAVLLAFGFRPSpADWFGSVNINLDGSGRVVAPEQQEfkfqTSNPKIFAG 443
Cdd:PRK09564 227 V---TDKGEYE------------------ADVVIVATGVKPN-TEFLEDTGLKTLKNGAIIVDEYGE----TSIENIYAA 280
|
..
gi 523535166 444 GD 445
Cdd:PRK09564 281 GD 282
|
|
| PLN02487 |
PLN02487 |
zeta-carotene desaturase |
139-186 |
6.58e-03 |
|
zeta-carotene desaturase
Pssm-ID: 215268 [Multi-domain] Cd Length: 569 Bit Score: 39.01 E-value: 6.58e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 523535166 139 RPDMSHVKWTGKKVAIIGAGPAGLGCADILARGGVKPVVFDKRPEIGG 186
Cdd:PLN02487 65 PPEPEAYKGPKLKVAIIGAGLAGMSTAVELLDQGHEVDIYESRPFIGG 112
|
|
| Glf |
COG0562 |
UDP-galactopyranose mutase [Cell wall/membrane/envelope biogenesis]; |
154-186 |
7.24e-03 |
|
UDP-galactopyranose mutase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440328 [Multi-domain] Cd Length: 365 Bit Score: 38.54 E-value: 7.24e-03
10 20 30
....*....|....*....|....*....|....
gi 523535166 154 IIGAGPAGLGCADILARG-GVKPVVFDKRPEIGG 186
Cdd:COG0562 7 IVGAGFFGAVFAERLAEElGKKVLVIDKRDHIGG 40
|
|
| PRK08132 |
PRK08132 |
FAD-dependent oxidoreductase; Provisional |
151-180 |
8.99e-03 |
|
FAD-dependent oxidoreductase; Provisional
Pssm-ID: 236158 [Multi-domain] Cd Length: 547 Bit Score: 38.31 E-value: 8.99e-03
10 20 30
....*....|....*....|....*....|
gi 523535166 151 KVAIIGAGPAGLGCADILARGGVKPVVFDK 180
Cdd:PRK08132 25 PVVVVGAGPVGLALAIDLAQQGVPVVLLDD 54
|
|
| NAD_bind_2_malic_enz |
cd05311 |
NAD(P) binding domain of malic enzyme (ME), subgroup 2; Malic enzyme (ME), a member of the ... |
146-181 |
9.08e-03 |
|
NAD(P) binding domain of malic enzyme (ME), subgroup 2; Malic enzyme (ME), a member of the amino acid dehydrogenase (DH)-like domain family, catalyzes the oxidative decarboxylation of L-malate to pyruvate in the presence of cations (typically Mg++ or Mn++) with the concomitant reduction of cofactor NAD+ or NADP+. ME has been found in all organisms, and plays important roles in diverse metabolic pathways such as photosynthesis and lipogenesis. This enzyme generally forms homotetramers. The conversion of malate to pyruvate by ME typically involves oxidation of malate to produce oxaloacetate, followed by decarboxylation of oxaloacetate to produce pyruvate and CO2. This subfamily consists primarily of archaeal and bacterial ME. Amino acid DH-like NAD(P)-binding domains are members of the Rossmann fold superfamily and include glutamate, leucine, and phenylalanine DHs, methylene tetrahydrofolate DH, methylene-tetrahydromethanopterin DH, methylene-tetrahydropholate DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DH, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts.
Pssm-ID: 133453 [Multi-domain] Cd Length: 226 Bit Score: 37.63 E-value: 9.08e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 523535166 146 KWTGK-----KVAIIGAGPAGLGCADILARGGVKP---VVFDKR 181
Cdd:cd05311 17 KLVGKkieevKIVINGAGAAGIAIARLLLAAGAKPeniVVVDSK 60
|
|
| PRK06703 |
PRK06703 |
flavodoxin; Provisional |
225-301 |
9.16e-03 |
|
flavodoxin; Provisional
Pssm-ID: 235854 [Multi-domain] Cd Length: 151 Bit Score: 36.66 E-value: 9.16e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 523535166 225 DVTIDELLAeYDAVFMGmgTYTYMKGGFPgedldgvYDALDFLisnvnrcqgwekDPSEYISMDGKKVIVLGGGDTA 301
Cdd:PRK06703 40 GMDAEELLA-YDGIILG--SYTWGDGDLP-------YEAEDFH------------EDLENIDLSGKKVAVFGSGDTA 94
|
|
| |
