|
Name |
Accession |
Description |
Interval |
E-value |
| GlcD |
COG0277 |
FAD/FMN-containing lactate dehydrogenase/glycolate oxidase [Energy production and conversion]; |
14-537 |
1.10e-137 |
|
FAD/FMN-containing lactate dehydrogenase/glycolate oxidase [Energy production and conversion];
Pssm-ID: 440046 [Multi-domain] Cd Length: 462 Bit Score: 421.22 E-value: 1.10e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497367283 14 YPEFLEALRnSGFRGQISADYATRTVLATD-NSIYQRLPQAAVFPLDADDVARVATLMAEARfrhVKLTPRGGGTGTNGQ 92
Cdd:COG0277 3 TAALLAALR-AILAGRVLTDPADRAAYARDgNSLYRGRPDAVVRPRSTEDVAAVVRLAAEHG---VPVVPRGGGTGLAGG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497367283 93 SL--TDGIVVDLSRhMNNILEINVEERWVRVQAGTVKDQLNAALKPYGLFFAPELSTSNRATVGGMINTDASGQGSCTYG 170
Cdd:COG0277 79 AVplDGGVVLDLSR-MNRILEVDPEDRTATVEAGVTLADLNAALAPHGLFFPPDPSSQGTATIGGNIATNAGGPRSLKYG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497367283 171 KTRDHVLELHSVLLGGERLHSLPideaaleqacaapgrvgevyrmardiqqtqgdliertfpKLNRCLTGYDLAHLrdeq 250
Cdd:COG0277 158 LTRDNVLGLEVVLADGEVVRTGG---------------------------------------RVPKNVTGYDLFWL---- 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497367283 251 grfnlnsvLCGAEGSLGYVVEAKLNVLPIPKYAVLVNVRYTSFMDALRDANALMAH--KPLSIETVDSKVLMLamkdivw 328
Cdd:COG0277 195 --------LVGSEGTLGVITEATLRLHPLPEAVATALVAFPDLEAAAAAVRALLAAgiAPAALELMDRAALAL------- 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497367283 329 hsVAEYFPADPERPTLGINLVEFCGDEPAQVNAKVQAFLQHLQSDTSVErlgHTLAEGSEAVTRVYTMRKRSVGLLGNVE 408
Cdd:COG0277 260 --VEAAPPLGLPEDGGALLLVEFDGDDAEEVEAQLARLRAILEAGGATD---VRVAADGAERERLWKARKAALPALGRLD 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497367283 409 GEVRpqpFVEDTAVPPEQLADYIADFRALLDGYGLAYGMFGHVDAGVLHVRPALDMKDPAQAALVKPISDAVAALTKRYG 488
Cdd:COG0277 335 GGAK---LLEDVAVPPSRLPELLRELGALAAKYGLRATAFGHAGDGNLHVRILFDPADPEEVERARAAAEEIFDLVAELG 411
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 497367283 489 GLLWGEHGKGL-RSEYVPEYFGE-LYPALQRLKGAFDPHNQLNPGKICTPP 537
Cdd:COG0277 412 GSISGEHGIGRlKAEFLPAEYGPaALALLRRIKAAFDPDGILNPGKILPPP 462
|
|
| GlpC |
COG0247 |
Fe-S cluster-containing oxidoreductase, includes glycolate oxidase subunit GlcF [Energy ... |
490-1002 |
1.56e-79 |
|
Fe-S cluster-containing oxidoreductase, includes glycolate oxidase subunit GlcF [Energy production and conversion];
Pssm-ID: 440017 [Multi-domain] Cd Length: 420 Bit Score: 265.79 E-value: 1.56e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497367283 490 LLWGEHGKGLRSEYVPEYFGE-LYPALQRLKGAFDPHNQLNPGKICTPPDSAEGLTKVDgvtlrgDLDRSIDERVWQDFG 568
Cdd:COG0247 1 LSGGHGGGLKAEHGTGRFMAPfLELELGKIKYAFDPDNKLNPGKIGLLNPGVELLGDGD------LHDKNLKTLPWKELL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497367283 569 SAVH-CNGNGACYnydpndAMCPSWKATRERQHSPKGRASLMREWLRlqgeanidvlaaarnkvswlkglparlrnnrar 647
Cdd:COG0247 75 DALDaCVGCGFCR------AMCPSYKATGDEKDSPRGRINLLREVLE--------------------------------- 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497367283 648 NQGQADFSHEVYDAMAGCLACKSCAGQCPIKVNVPDFRSRFLELYHGRYQRPLRDYLIGSLEFTIPylahapglynavmg 727
Cdd:COG0247 116 GELPLDLSEEVYEVLDLCLTCKACETACPSGVDIADLIAEARAQLVERGGRPLRDRLLRTFPDRVP-------------- 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497367283 728 skwvsrllaekvgmvdsplisrfnfqatltrcrvgvatvpalrelTPAQRERSIVLVQDAFTRYFETPLLSAFIDLANRL 807
Cdd:COG0247 182 ---------------------------------------------AADKEGAEVLLFPGCFTNYFDPEIGKAAVRLLEAA 216
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497367283 808 GHRVFLAP-YSANGKPLHVQGFLGAFAKAAIRNasqLKALADCGVP-LVGLDPAMTLVYRQEYQKVPGMDGCPQVLLPQE 885
Cdd:COG0247 217 GVEVVLPPeELCCGAPALSKGDLDLARKLARRN---IEALERLGVKaIVTTCPSCGLTLKDEYPELLGDRVAFEVLDISE 293
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497367283 886 WLMNVLPE---QAPTAPGNFRLMAHCTEKtNVPASTRQWEQVFARL-GLKLV--TEATGCCGMSGTYGHEARnqETSRTI 959
Cdd:COG0247 294 FLAELILEgklKLKPLGEKVTYHDPCHLG-RGGGVYDAPRELLKAIpGVEVVemPEDSGCCGGAGGYGFEEP--ELSMRI 370
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 497367283 960 FEQsWATKLDKEGEP--LATGYSCRSQVKRMTE---RQMRHPLEVVLQ 1002
Cdd:COG0247 371 GER-KLEQIRATGADvvVTACPSCRTQLEDGTKeygIEVKHPVELLAE 417
|
|
| FAD-oxidase_C |
pfam02913 |
FAD linked oxidases, C-terminal domain; This domain has a ferredoxin-like fold. |
279-533 |
1.75e-66 |
|
FAD linked oxidases, C-terminal domain; This domain has a ferredoxin-like fold.
Pssm-ID: 397178 Cd Length: 248 Bit Score: 223.73 E-value: 1.75e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497367283 279 IPKYAVLVNVRYTSFMDALRDANALMAHK--PLSIETVDSKVLMLAMKDIVWHSvaeyfpaDPERPTLGINLVEFCGDEP 356
Cdd:pfam02913 1 LPEVRAVALVGFPSFEAAVKAVREIARAGiiPAALELMDNDALDLVEATLGFPK-------GLPRDAAALLLVEFEGDDE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497367283 357 AQVNAKVQAFLQHLQSDTSVERLGhtlAEGSEAVTRVYTMRKRSVGLlGNVEGEVRPQPFVEDTAVPPEQLADYIADFRA 436
Cdd:pfam02913 74 ETAEEELEAVEAILEAGGAGDVVV---ATDEAEAERLWAARKYALPL-RDALGGAGPAVFSEDVSVPRSRLADLVRDIKE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497367283 437 LLDGYGLAYGMFGHVDAGVLHVRPALDMKDPAQAALVKPISDAVAALTKRYGGLLWGEHGKGL-RSEYVPEYFGE-LYPA 514
Cdd:pfam02913 150 LLDKYGLVVCLFGHAGDGNLHLYILFDFRDPEQEERAEKLFDEIMDLALELGGSISGEHGVGRdKKPYLEREFGEeGLAL 229
|
250
....*....|....*....
gi 497367283 515 LQRLKGAFDPHNQLNPGKI 533
Cdd:pfam02913 230 MRRIKAAFDPKGILNPGKV 248
|
|
| glcD |
TIGR00387 |
glycolate oxidase, subunit GlcD; This protein, the glycolate oxidase GlcD subunit, is similar ... |
55-532 |
1.03e-48 |
|
glycolate oxidase, subunit GlcD; This protein, the glycolate oxidase GlcD subunit, is similar in sequence to that of several D-lactate dehydrogenases, including that of E. coli. The glycolate oxidase has been found to have some D-lactate dehydrogenase activity. [Energy metabolism, Other]
Pssm-ID: 273050 [Multi-domain] Cd Length: 413 Bit Score: 178.81 E-value: 1.03e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497367283 55 VFPLDADDVARVATLMAEARfrhVKLTPRGGGTGTNGQSL-TDGIVVDLSRHMNNILEINVEERWVRVQAGTVKDQLNAA 133
Cdd:TIGR00387 2 VFPKNTEQVARILKLCHEHR---IPIVPRGAGTGLSGGALpEEGGLVLVFKHMNKILEIDVVNLTAVVQPGVRNLELEQA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497367283 134 LKPYGLFFAPELSTSNRATVGGMINTDASGQGSCTYGKTRDHVLELHSVLLGGErlhslpideaaleqacaapgrvgevy 213
Cdd:TIGR00387 79 VEEHNLFYPPDPSSQISSTIGGNIAENAGGMRGLKYGTTVDYVLGLEVVTADGE-------------------------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497367283 214 rmardiqqtqgdlIERTFPKLNRCLTGYDLAHLrdeqgrfnlnsvLCGAEGSLGYVVEAKLNVLPIPKYAVLVNVRYTSF 293
Cdd:TIGR00387 133 -------------ILRIGGKTAKDVAGYDLTGL------------FVGSEGTLGIVTEATLKLLPKPENIVVALAFFDSI 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497367283 294 MDALRDANALMAHK--PLSIETVDSKVLMlamkdivwhSVAEYFPADPERPTLGINLVEF-CGDEPAQVN-AKVQaflQH 369
Cdd:TIGR00387 188 EKAMQAVYDIIAAGiiPAGMEFLDNLSIK---------AVEDISGIGLPKDAGAILLVEIdGVHEAVERDeEKIE---QI 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497367283 370 LQSDTSVErlgHTLAEGSEAVTRVYTMRKRSVGLLGnvegEVRPQPFVEDTAVPPEQLADYIADFRALLDGYGLAYGMFG 449
Cdd:TIGR00387 256 CRKNGAVD---VQIAQDEEERALLWAGRRNAFKAAS----KLSPLYLIEDGTVPRSKLPEALRGIADIASKYDFTIANFG 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497367283 450 HVDAGVLHVRPALDMKDPAQAALVKPISDAVAALTKRYGGLLWGEHGKGL-RSEYVPEYFGEL-YPALQRLKGAFDPHNQ 527
Cdd:TIGR00387 329 HAGDGNLHPTILTDPEDKGEMERVEEAGGEIFELAIELGGTISGEHGIGVvKAEFMPYKFNEKeLETMRAIKKAFDPDNI 408
|
....*
gi 497367283 528 LNPGK 532
Cdd:TIGR00387 409 LNPGK 413
|
|
| PLN02805 |
PLN02805 |
D-lactate dehydrogenase [cytochrome] |
16-536 |
6.61e-36 |
|
D-lactate dehydrogenase [cytochrome]
Pssm-ID: 178402 [Multi-domain] Cd Length: 555 Bit Score: 144.38 E-value: 6.61e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497367283 16 EFLEALRnSGFRGQISADYATRTVLAT-DNSIYQ--RLPQAAVFPLDADDVARVatLMAEARFRhVKLTPRGGGTGTNGQ 92
Cdd:PLN02805 97 ELIDELK-AILQDNMTLDYDERYFHGKpQNSFHKavNIPDVVVFPRSEEEVSKI--VKSCNKYK-VPIVPYGGATSIEGH 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497367283 93 SLT--DGIVVDLSRhMNNILEINVEERWVRVQAGTVKDQLNAALKPYGLFFApeLSTSNRATVGGMINTDASGQGSCTYG 170
Cdd:PLN02805 173 TLAphGGVCIDMSL-MKSVKALHVEDMDVVVEPGIGWLELNEYLEPYGLFFP--LDPGPGATIGGMCATRCSGSLAVRYG 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497367283 171 KTRDHVLELHSVLlggerlhslpideaaleqacaapgrvgevyrmardiqqTQGDLIeRTFPKLNRCLTGYDLAHLrdeq 250
Cdd:PLN02805 250 TMRDNVISLKVVL--------------------------------------PNGDVV-KTASRARKSAAGYDLTRL---- 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497367283 251 grfnlnsvLCGAEGSLGYVVEAKLNVLPIPKYAVLVNVRYTSFMDALRDANALMahkpLSIETVdSKVLMLAMKDIVWHS 330
Cdd:PLN02805 287 --------VIGSEGTLGVITEVTLRLQKIPQHSVVAMCNFPTIKDAADVAIATM----LSGIQV-SRVELLDEVQIRAIN 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497367283 331 VAEYfPADPERPTLginLVEFCGDEpaqVNAKVQAFL------QHLQSDtsverlgHTLAEGSEAVTRVYTMRKRSvgLL 404
Cdd:PLN02805 354 MANG-KNLPEAPTL---MFEFIGTE---AYAREQTLIvqkiasKHNGSD-------FVFAEEPEAKKELWKIRKEA--LW 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497367283 405 GNVEGEVRPQPFVEDTAVPPEQLADYIADFRALLDGYGLAYGMFGHVDAGVLHVRPALDMKDPAQAALVKPISDAVAALT 484
Cdd:PLN02805 418 ACFAMEPKYEAMITDVCVPLSHLAELISRSKKELDASPLVCTVIAHAGDGNFHTIILFDPSQEDQRREAERLNHFMVHTA 497
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 497367283 485 KRYGGLLWGEHGKGL-RSEYVPEYFG-ELYPALQRLKGAFDPHNQLNPGKICTP 536
Cdd:PLN02805 498 LSMEGTCTGEHGVGTgKMKYLEKELGiEALQTMKRIKKALDPNNIMNPGKLIPP 551
|
|
| glpC |
PRK11168 |
anaerobic glycerol-3-phosphate dehydrogenase subunit C; |
656-999 |
7.67e-21 |
|
anaerobic glycerol-3-phosphate dehydrogenase subunit C;
Pssm-ID: 236869 [Multi-domain] Cd Length: 396 Bit Score: 96.09 E-value: 7.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497367283 656 HEVYDAMAGCLACKSCAGQCPIKVNVPDFRSRFLELYHGRYQRPLRDYLIGSLEFTIPYLAHAPGLYNAVMGSKWVsRLL 735
Cdd:PRK11168 47 ALYDESLKYCSNCKRCEVACPSGVKIGDIIQRARAKYVTERGPPLRDRILSHTDLMGSLATPFAPLVNAATGLKPV-RWL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497367283 736 AEKVGMVDS--PLiSRFNFQATLTRCRVGVATVPalreltpaQRERSIVLVQDAFTRYFETPLLSAFIDLANRLGHRVFL 813
Cdd:PRK11168 126 LEKTLGIDHrrPL-PKYAFGTFRRWYRKQAAQQA--------QYKKQVAYFHGCYVNYNHPQLGKDLVKVLNAMGYEVLL 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497367283 814 APYSANGKPLHVQGFLGAFAKAAIRNASQLKALADCGVPLVGLDPAMTLVYRQEYQKVPGMDG---CPQVLLPQEWLMNV 890
Cdd:PRK11168 197 PKEKCCGLPLIANGFLDKARKQAEFNVESLREAIEKGIPVIATSSSCTLTLRDEYPELLGVDNagvRDHIEDATEFLRRL 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497367283 891 L--PEQAPTAPGNFRLMAH--C-TEKTnvpASTRQWEQVFARL-GLKLVTEATGCCGMSGTYGHEARNQETSRTI----F 960
Cdd:PRK11168 277 LdqGKLLPLKPLPLKVAYHtpChLEKQ---GWGLYTLELLRLIpGLEVVVLDSQCCGIAGTYGFKKEKYETSQAIgaplF 353
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 497367283 961 EQSWATKLD---KEGEplatgySCRSQVKRMTERQMRHPLEV 999
Cdd:PRK11168 354 RQIEESGADlvvTDCE------TCKWQIEMSTGLECEHPITL 389
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| GlcD |
COG0277 |
FAD/FMN-containing lactate dehydrogenase/glycolate oxidase [Energy production and conversion]; |
14-537 |
1.10e-137 |
|
FAD/FMN-containing lactate dehydrogenase/glycolate oxidase [Energy production and conversion];
Pssm-ID: 440046 [Multi-domain] Cd Length: 462 Bit Score: 421.22 E-value: 1.10e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497367283 14 YPEFLEALRnSGFRGQISADYATRTVLATD-NSIYQRLPQAAVFPLDADDVARVATLMAEARfrhVKLTPRGGGTGTNGQ 92
Cdd:COG0277 3 TAALLAALR-AILAGRVLTDPADRAAYARDgNSLYRGRPDAVVRPRSTEDVAAVVRLAAEHG---VPVVPRGGGTGLAGG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497367283 93 SL--TDGIVVDLSRhMNNILEINVEERWVRVQAGTVKDQLNAALKPYGLFFAPELSTSNRATVGGMINTDASGQGSCTYG 170
Cdd:COG0277 79 AVplDGGVVLDLSR-MNRILEVDPEDRTATVEAGVTLADLNAALAPHGLFFPPDPSSQGTATIGGNIATNAGGPRSLKYG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497367283 171 KTRDHVLELHSVLLGGERLHSLPideaaleqacaapgrvgevyrmardiqqtqgdliertfpKLNRCLTGYDLAHLrdeq 250
Cdd:COG0277 158 LTRDNVLGLEVVLADGEVVRTGG---------------------------------------RVPKNVTGYDLFWL---- 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497367283 251 grfnlnsvLCGAEGSLGYVVEAKLNVLPIPKYAVLVNVRYTSFMDALRDANALMAH--KPLSIETVDSKVLMLamkdivw 328
Cdd:COG0277 195 --------LVGSEGTLGVITEATLRLHPLPEAVATALVAFPDLEAAAAAVRALLAAgiAPAALELMDRAALAL------- 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497367283 329 hsVAEYFPADPERPTLGINLVEFCGDEPAQVNAKVQAFLQHLQSDTSVErlgHTLAEGSEAVTRVYTMRKRSVGLLGNVE 408
Cdd:COG0277 260 --VEAAPPLGLPEDGGALLLVEFDGDDAEEVEAQLARLRAILEAGGATD---VRVAADGAERERLWKARKAALPALGRLD 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497367283 409 GEVRpqpFVEDTAVPPEQLADYIADFRALLDGYGLAYGMFGHVDAGVLHVRPALDMKDPAQAALVKPISDAVAALTKRYG 488
Cdd:COG0277 335 GGAK---LLEDVAVPPSRLPELLRELGALAAKYGLRATAFGHAGDGNLHVRILFDPADPEEVERARAAAEEIFDLVAELG 411
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 497367283 489 GLLWGEHGKGL-RSEYVPEYFGE-LYPALQRLKGAFDPHNQLNPGKICTPP 537
Cdd:COG0277 412 GSISGEHGIGRlKAEFLPAEYGPaALALLRRIKAAFDPDGILNPGKILPPP 462
|
|
| GlpC |
COG0247 |
Fe-S cluster-containing oxidoreductase, includes glycolate oxidase subunit GlcF [Energy ... |
490-1002 |
1.56e-79 |
|
Fe-S cluster-containing oxidoreductase, includes glycolate oxidase subunit GlcF [Energy production and conversion];
Pssm-ID: 440017 [Multi-domain] Cd Length: 420 Bit Score: 265.79 E-value: 1.56e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497367283 490 LLWGEHGKGLRSEYVPEYFGE-LYPALQRLKGAFDPHNQLNPGKICTPPDSAEGLTKVDgvtlrgDLDRSIDERVWQDFG 568
Cdd:COG0247 1 LSGGHGGGLKAEHGTGRFMAPfLELELGKIKYAFDPDNKLNPGKIGLLNPGVELLGDGD------LHDKNLKTLPWKELL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497367283 569 SAVH-CNGNGACYnydpndAMCPSWKATRERQHSPKGRASLMREWLRlqgeanidvlaaarnkvswlkglparlrnnrar 647
Cdd:COG0247 75 DALDaCVGCGFCR------AMCPSYKATGDEKDSPRGRINLLREVLE--------------------------------- 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497367283 648 NQGQADFSHEVYDAMAGCLACKSCAGQCPIKVNVPDFRSRFLELYHGRYQRPLRDYLIGSLEFTIPylahapglynavmg 727
Cdd:COG0247 116 GELPLDLSEEVYEVLDLCLTCKACETACPSGVDIADLIAEARAQLVERGGRPLRDRLLRTFPDRVP-------------- 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497367283 728 skwvsrllaekvgmvdsplisrfnfqatltrcrvgvatvpalrelTPAQRERSIVLVQDAFTRYFETPLLSAFIDLANRL 807
Cdd:COG0247 182 ---------------------------------------------AADKEGAEVLLFPGCFTNYFDPEIGKAAVRLLEAA 216
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497367283 808 GHRVFLAP-YSANGKPLHVQGFLGAFAKAAIRNasqLKALADCGVP-LVGLDPAMTLVYRQEYQKVPGMDGCPQVLLPQE 885
Cdd:COG0247 217 GVEVVLPPeELCCGAPALSKGDLDLARKLARRN---IEALERLGVKaIVTTCPSCGLTLKDEYPELLGDRVAFEVLDISE 293
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497367283 886 WLMNVLPE---QAPTAPGNFRLMAHCTEKtNVPASTRQWEQVFARL-GLKLV--TEATGCCGMSGTYGHEARnqETSRTI 959
Cdd:COG0247 294 FLAELILEgklKLKPLGEKVTYHDPCHLG-RGGGVYDAPRELLKAIpGVEVVemPEDSGCCGGAGGYGFEEP--ELSMRI 370
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 497367283 960 FEQsWATKLDKEGEP--LATGYSCRSQVKRMTE---RQMRHPLEVVLQ 1002
Cdd:COG0247 371 GER-KLEQIRATGADvvVTACPSCRTQLEDGTKeygIEVKHPVELLAE 417
|
|
| FAD-oxidase_C |
pfam02913 |
FAD linked oxidases, C-terminal domain; This domain has a ferredoxin-like fold. |
279-533 |
1.75e-66 |
|
FAD linked oxidases, C-terminal domain; This domain has a ferredoxin-like fold.
Pssm-ID: 397178 Cd Length: 248 Bit Score: 223.73 E-value: 1.75e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497367283 279 IPKYAVLVNVRYTSFMDALRDANALMAHK--PLSIETVDSKVLMLAMKDIVWHSvaeyfpaDPERPTLGINLVEFCGDEP 356
Cdd:pfam02913 1 LPEVRAVALVGFPSFEAAVKAVREIARAGiiPAALELMDNDALDLVEATLGFPK-------GLPRDAAALLLVEFEGDDE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497367283 357 AQVNAKVQAFLQHLQSDTSVERLGhtlAEGSEAVTRVYTMRKRSVGLlGNVEGEVRPQPFVEDTAVPPEQLADYIADFRA 436
Cdd:pfam02913 74 ETAEEELEAVEAILEAGGAGDVVV---ATDEAEAERLWAARKYALPL-RDALGGAGPAVFSEDVSVPRSRLADLVRDIKE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497367283 437 LLDGYGLAYGMFGHVDAGVLHVRPALDMKDPAQAALVKPISDAVAALTKRYGGLLWGEHGKGL-RSEYVPEYFGE-LYPA 514
Cdd:pfam02913 150 LLDKYGLVVCLFGHAGDGNLHLYILFDFRDPEQEERAEKLFDEIMDLALELGGSISGEHGVGRdKKPYLEREFGEeGLAL 229
|
250
....*....|....*....
gi 497367283 515 LQRLKGAFDPHNQLNPGKI 533
Cdd:pfam02913 230 MRRIKAAFDPKGILNPGKV 248
|
|
| glcD |
TIGR00387 |
glycolate oxidase, subunit GlcD; This protein, the glycolate oxidase GlcD subunit, is similar ... |
55-532 |
1.03e-48 |
|
glycolate oxidase, subunit GlcD; This protein, the glycolate oxidase GlcD subunit, is similar in sequence to that of several D-lactate dehydrogenases, including that of E. coli. The glycolate oxidase has been found to have some D-lactate dehydrogenase activity. [Energy metabolism, Other]
Pssm-ID: 273050 [Multi-domain] Cd Length: 413 Bit Score: 178.81 E-value: 1.03e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497367283 55 VFPLDADDVARVATLMAEARfrhVKLTPRGGGTGTNGQSL-TDGIVVDLSRHMNNILEINVEERWVRVQAGTVKDQLNAA 133
Cdd:TIGR00387 2 VFPKNTEQVARILKLCHEHR---IPIVPRGAGTGLSGGALpEEGGLVLVFKHMNKILEIDVVNLTAVVQPGVRNLELEQA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497367283 134 LKPYGLFFAPELSTSNRATVGGMINTDASGQGSCTYGKTRDHVLELHSVLLGGErlhslpideaaleqacaapgrvgevy 213
Cdd:TIGR00387 79 VEEHNLFYPPDPSSQISSTIGGNIAENAGGMRGLKYGTTVDYVLGLEVVTADGE-------------------------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497367283 214 rmardiqqtqgdlIERTFPKLNRCLTGYDLAHLrdeqgrfnlnsvLCGAEGSLGYVVEAKLNVLPIPKYAVLVNVRYTSF 293
Cdd:TIGR00387 133 -------------ILRIGGKTAKDVAGYDLTGL------------FVGSEGTLGIVTEATLKLLPKPENIVVALAFFDSI 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497367283 294 MDALRDANALMAHK--PLSIETVDSKVLMlamkdivwhSVAEYFPADPERPTLGINLVEF-CGDEPAQVN-AKVQaflQH 369
Cdd:TIGR00387 188 EKAMQAVYDIIAAGiiPAGMEFLDNLSIK---------AVEDISGIGLPKDAGAILLVEIdGVHEAVERDeEKIE---QI 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497367283 370 LQSDTSVErlgHTLAEGSEAVTRVYTMRKRSVGLLGnvegEVRPQPFVEDTAVPPEQLADYIADFRALLDGYGLAYGMFG 449
Cdd:TIGR00387 256 CRKNGAVD---VQIAQDEEERALLWAGRRNAFKAAS----KLSPLYLIEDGTVPRSKLPEALRGIADIASKYDFTIANFG 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497367283 450 HVDAGVLHVRPALDMKDPAQAALVKPISDAVAALTKRYGGLLWGEHGKGL-RSEYVPEYFGEL-YPALQRLKGAFDPHNQ 527
Cdd:TIGR00387 329 HAGDGNLHPTILTDPEDKGEMERVEEAGGEIFELAIELGGTISGEHGIGVvKAEFMPYKFNEKeLETMRAIKKAFDPDNI 408
|
....*
gi 497367283 528 LNPGK 532
Cdd:TIGR00387 409 LNPGK 413
|
|
| FAD_binding_4 |
pfam01565 |
FAD binding domain; This family consists of various enzymes that use FAD as a co-factor, most ... |
51-190 |
9.61e-40 |
|
FAD binding domain; This family consists of various enzymes that use FAD as a co-factor, most of the enzymes are similar to oxygen oxidoreductase. One of the enzymes Vanillyl-alcohol oxidase (VAO) has a solved structure, the alignment includes the FAD binding site, called the PP-loop, between residues 99-110. The FAD molecule is covalently bound in the known structure, however the residue that links to the FAD is not in the alignment. VAO catalyzes the oxidation of a wide variety of substrates, ranging form aromatic amines to 4-alkylphenols. Other members of this family include D-lactate dehydrogenase, this enzyme catalyzes the conversion of D-lactate to pyruvate using FAD as a co-factor; mitomycin radical oxidase, this enzyme oxidizes the reduced form of mitomycins and is involved in mitomycin resistance. This family includes MurB an UDP-N-acetylenolpyruvoylglucosamine reductase enzyme EC:1.1.1.158. This enzyme is involved in the biosynthesis of peptidoglycan.
Pssm-ID: 426326 [Multi-domain] Cd Length: 139 Bit Score: 143.50 E-value: 9.61e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497367283 51 PQAAVFPLDADDVARVatlMAEARFRHVKLTPRGGGTGTNGQS-LTDGIVVDLSRhMNNILEINVEERWVRVQAGTVKDQ 129
Cdd:pfam01565 1 PAAVVLPESEEEVAAI---VRLANENGLPVLPRGGGSSLLGGAvQTGGIVLDLSR-LNGILEIDPEDGTATVEAGVTLGD 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 497367283 130 LNAALKPYGLFFAPELSTSNRATVGGMINTDASGQGSCTYGKTRDHVLELHSVLLGGERLH 190
Cdd:pfam01565 77 LVRALAAKGLLLGLDPGSGIPGTVGGAIATNAGGYGSEKYGLTRDNVLGLEVVLADGEVVR 137
|
|
| PLN02805 |
PLN02805 |
D-lactate dehydrogenase [cytochrome] |
16-536 |
6.61e-36 |
|
D-lactate dehydrogenase [cytochrome]
Pssm-ID: 178402 [Multi-domain] Cd Length: 555 Bit Score: 144.38 E-value: 6.61e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497367283 16 EFLEALRnSGFRGQISADYATRTVLAT-DNSIYQ--RLPQAAVFPLDADDVARVatLMAEARFRhVKLTPRGGGTGTNGQ 92
Cdd:PLN02805 97 ELIDELK-AILQDNMTLDYDERYFHGKpQNSFHKavNIPDVVVFPRSEEEVSKI--VKSCNKYK-VPIVPYGGATSIEGH 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497367283 93 SLT--DGIVVDLSRhMNNILEINVEERWVRVQAGTVKDQLNAALKPYGLFFApeLSTSNRATVGGMINTDASGQGSCTYG 170
Cdd:PLN02805 173 TLAphGGVCIDMSL-MKSVKALHVEDMDVVVEPGIGWLELNEYLEPYGLFFP--LDPGPGATIGGMCATRCSGSLAVRYG 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497367283 171 KTRDHVLELHSVLlggerlhslpideaaleqacaapgrvgevyrmardiqqTQGDLIeRTFPKLNRCLTGYDLAHLrdeq 250
Cdd:PLN02805 250 TMRDNVISLKVVL--------------------------------------PNGDVV-KTASRARKSAAGYDLTRL---- 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497367283 251 grfnlnsvLCGAEGSLGYVVEAKLNVLPIPKYAVLVNVRYTSFMDALRDANALMahkpLSIETVdSKVLMLAMKDIVWHS 330
Cdd:PLN02805 287 --------VIGSEGTLGVITEVTLRLQKIPQHSVVAMCNFPTIKDAADVAIATM----LSGIQV-SRVELLDEVQIRAIN 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497367283 331 VAEYfPADPERPTLginLVEFCGDEpaqVNAKVQAFL------QHLQSDtsverlgHTLAEGSEAVTRVYTMRKRSvgLL 404
Cdd:PLN02805 354 MANG-KNLPEAPTL---MFEFIGTE---AYAREQTLIvqkiasKHNGSD-------FVFAEEPEAKKELWKIRKEA--LW 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497367283 405 GNVEGEVRPQPFVEDTAVPPEQLADYIADFRALLDGYGLAYGMFGHVDAGVLHVRPALDMKDPAQAALVKPISDAVAALT 484
Cdd:PLN02805 418 ACFAMEPKYEAMITDVCVPLSHLAELISRSKKELDASPLVCTVIAHAGDGNFHTIILFDPSQEDQRREAERLNHFMVHTA 497
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 497367283 485 KRYGGLLWGEHGKGL-RSEYVPEYFG-ELYPALQRLKGAFDPHNQLNPGKICTP 536
Cdd:PLN02805 498 LSMEGTCTGEHGVGTgKMKYLEKELGiEALQTMKRIKKALDPNNIMNPGKLIPP 551
|
|
| PRK11230 |
PRK11230 |
glycolate oxidase subunit GlcD; Provisional |
45-532 |
2.20e-23 |
|
glycolate oxidase subunit GlcD; Provisional
Pssm-ID: 183043 [Multi-domain] Cd Length: 499 Bit Score: 105.24 E-value: 2.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497367283 45 SIYQRLPQAAVFPldaDDVARVATLMAEARFRHVKLTPRGGGTGTNGQS--LTDGIVVDLSRhMNNILEINVEERWVRVQ 122
Cdd:PRK11230 50 SAYRTRPLLVVLP---KQMEQVQALLAVCHRLRVPVVARGAGTGLSGGAlpLEKGVLLVMAR-FNRILDINPVGRRARVQ 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497367283 123 AGTVKDQLNAALKPYGLFFAPELSTSNRATVGGMINTDASGQGSCTYGKTRDHVLELHSVLLGGERLhSLPIDeaaleqA 202
Cdd:PRK11230 126 PGVRNLAISQAAAPHGLYYAPDPSSQIACSIGGNVAENAGGVHCLKYGLTVHNLLKVEILTLDGEAL-TLGSD------A 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497367283 203 CAAPGrvgevyrmardiqqtqgdliertfpklnrcltgydlahlrdeqgrFNLNSVLCGAEGSLGYVVEAKLNVLPIPKY 282
Cdd:PRK11230 199 LDSPG---------------------------------------------FDLLALFTGSEGMLGVVTEVTVKLLPKPPV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497367283 283 AVLVNVRYTSFMDALRDANALMAHK--PLSIETVDSkVLMLAMKDIVwHsvAEYfPADPErptlGINLVEFCGDEpAQVN 360
Cdd:PRK11230 234 ARVLLASFDSVEKAGLAVGDIIAAGiiPGGLEMMDN-LSIRAAEDFI-H--AGY-PVDAE----AILLCELDGVE-SDVQ 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497367283 361 ---AKVQAFLQHLQSdTSVeRLGHTLAEGseavTRVYTMRKRSVGLLGNVEgevrPQPFVEDTAVPPEQLADYIADFRAL 437
Cdd:PRK11230 304 edcERVNDILLKAGA-TDV-RLAQDEAER----VRFWAGRKNAFPAVGRIS----PDYYCMDGTIPRRELPGVLEGIARL 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497367283 438 LDGYGLAYGMFGHVDAGVLHVRPALDMKDPAQAALVKPISDAVAALTKRYGGLLWGEHGKGLR--SEYVPEYFGELYPAL 515
Cdd:PRK11230 374 SQQYGLRVANVFHAGDGNMHPLILFDANEPGELERAEALGGKILELCVEVGGSITGEHGVGREkiNQMCAQFNSDEITLF 453
|
490
....*....|....*..
gi 497367283 516 QRLKGAFDPHNQLNPGK 532
Cdd:PRK11230 454 HAVKAAFDPDGLLNPGK 470
|
|
| glpC |
PRK11168 |
anaerobic glycerol-3-phosphate dehydrogenase subunit C; |
656-999 |
7.67e-21 |
|
anaerobic glycerol-3-phosphate dehydrogenase subunit C;
Pssm-ID: 236869 [Multi-domain] Cd Length: 396 Bit Score: 96.09 E-value: 7.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497367283 656 HEVYDAMAGCLACKSCAGQCPIKVNVPDFRSRFLELYHGRYQRPLRDYLIGSLEFTIPYLAHAPGLYNAVMGSKWVsRLL 735
Cdd:PRK11168 47 ALYDESLKYCSNCKRCEVACPSGVKIGDIIQRARAKYVTERGPPLRDRILSHTDLMGSLATPFAPLVNAATGLKPV-RWL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497367283 736 AEKVGMVDS--PLiSRFNFQATLTRCRVGVATVPalreltpaQRERSIVLVQDAFTRYFETPLLSAFIDLANRLGHRVFL 813
Cdd:PRK11168 126 LEKTLGIDHrrPL-PKYAFGTFRRWYRKQAAQQA--------QYKKQVAYFHGCYVNYNHPQLGKDLVKVLNAMGYEVLL 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497367283 814 APYSANGKPLHVQGFLGAFAKAAIRNASQLKALADCGVPLVGLDPAMTLVYRQEYQKVPGMDG---CPQVLLPQEWLMNV 890
Cdd:PRK11168 197 PKEKCCGLPLIANGFLDKARKQAEFNVESLREAIEKGIPVIATSSSCTLTLRDEYPELLGVDNagvRDHIEDATEFLRRL 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497367283 891 L--PEQAPTAPGNFRLMAH--C-TEKTnvpASTRQWEQVFARL-GLKLVTEATGCCGMSGTYGHEARNQETSRTI----F 960
Cdd:PRK11168 277 LdqGKLLPLKPLPLKVAYHtpChLEKQ---GWGLYTLELLRLIpGLEVVVLDSQCCGIAGTYGFKKEKYETSQAIgaplF 353
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 497367283 961 EQSWATKLD---KEGEplatgySCRSQVKRMTERQMRHPLEV 999
Cdd:PRK11168 354 RQIEESGADlvvTDCE------TCKWQIEMSTGLECEHPITL 389
|
|
| PLN02465 |
PLN02465 |
L-galactono-1,4-lactone dehydrogenase |
61-217 |
9.69e-09 |
|
L-galactono-1,4-lactone dehydrogenase
Pssm-ID: 215258 [Multi-domain] Cd Length: 573 Bit Score: 59.09 E-value: 9.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497367283 61 DDVARVATLMAEARFRHVKLTPRGGGTGTNGQSLTDGIVVDLSrHMNNILEINVEERWVRVQAGTVKDQLNAALKPYGLF 140
Cdd:PLN02465 104 ESLEELEDIVKEAHEKGRRIRPVGSGLSPNGLAFSREGMVNLA-LMDKVLEVDKEKKRVTVQAGARVQQVVEALRPHGLT 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497367283 141 FaPELSTSNRATVGGMINTDASGQGSctygktrdhvlelhsvllggeRLHslPIDEAALEQACAAPGR---------VGE 211
Cdd:PLN02465 183 L-QNYASIREQQIGGFIQVGAHGTGA---------------------RIP--PIDEQVVSMKLVTPAKgtielskedDPE 238
|
....*.
gi 497367283 212 VYRMAR 217
Cdd:PLN02465 239 LFRLAR 244
|
|
| GLDHase |
TIGR01676 |
galactonolactone dehydrogenase; This model represents L-Galactono-gamma-lactone dehydrogenase ... |
52-166 |
2.77e-07 |
|
galactonolactone dehydrogenase; This model represents L-Galactono-gamma-lactone dehydrogenase (EC 1.3.2.3). This enzyme catalyzes the final step in ascorbic acid biosynthesis in higher plants. This protein is homologous to ascorbic acid biosynthesis enzymes of other species: L-gulono-gamma-lactone oxidase in rat and L-galactono-gamma-lactone oxidase in yeast. All three covalently bind the cofactor FAD.
Pssm-ID: 130737 [Multi-domain] Cd Length: 541 Bit Score: 54.30 E-value: 2.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497367283 52 QAAVFpLDADDVARVATLMAEARFRHVKLTPRGGGTGTNGQSLTDGIVVDLSRhMNNILEINVEERWVRVQAGTVKDQLN 131
Cdd:TIGR01676 61 LTRTF-HQPEAIEELEGIVKQANEKKARIRPVGSGLSPNGIGLSRAGMVNLAL-MDKVLEVDEEKKRVRVQAGIRVQQLV 138
|
90 100 110
....*....|....*....|....*....|....*
gi 497367283 132 AALKPYGLFFApELSTSNRATVGGMINTDASGQGS 166
Cdd:TIGR01676 139 DAIKEYGITLQ-NFASIREQQIGGIIQVGAHGTGA 172
|
|
| PLN02441 |
PLN02441 |
cytokinin dehydrogenase |
28-164 |
7.96e-07 |
|
cytokinin dehydrogenase
Pssm-ID: 215242 [Multi-domain] Cd Length: 525 Bit Score: 52.99 E-value: 7.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497367283 28 GQISADYATRTVLATD-NSIYQRLPQAAVFPLDADDVARvatLMAEARFRHVKLT--PRGGGTGTNGQSLT-DGIVVD-- 101
Cdd:PLN02441 41 GHLSFDPVSTASASKDfGNLVHSLPAAVLYPSSVEDIAS---LVRAAYGSSSPLTvaARGHGHSLNGQAQApGGVVVDmr 117
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 497367283 102 -LSRHMNNILEINV--EERWVRVQAGTV-KDQLNAALKpYGLffAPELSTSN-RATVGGMI-NTDASGQ 164
Cdd:PLN02441 118 sLRGGVRGPPVIVVsgDGPYVDVSGGELwIDVLKATLK-HGL--APRSWTDYlYLTVGGTLsNAGISGQ 183
|
|
| FAD_lactone_ox |
TIGR01678 |
sugar 1,4-lactone oxidases; This model represents a family of at least two different sugar 1,4 ... |
63-182 |
8.30e-04 |
|
sugar 1,4-lactone oxidases; This model represents a family of at least two different sugar 1,4 lactone oxidases, both involved in synthesizing ascorbic acid or a derivative. These include L-gulonolactone oxidase (EC 1.1.3.8) from rat and D-arabinono-1,4-lactone oxidase (EC 1.1.3.37) from Saccharomyces cerevisiae. Members are proposed to have the cofactor FAD covalently bound at a site specified by Prosite motif PS00862; OX2_COVAL_FAD; 1.
Pssm-ID: 273751 [Multi-domain] Cd Length: 438 Bit Score: 42.96 E-value: 8.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497367283 63 VARVATLMAEARFRHVKLTPRGGGTGTNGQSLTDGIVVDLSRhMNNILEINVEERWVRVQAGTVKDQLNAALKPYGLFFa 142
Cdd:TIGR01678 24 VEEVREVLALAREQKKKVKVVGGGHSPSDIACTDGFLIHLDK-MNKVLQFDKEKKQITVEAGIRLYQLHEQLDEHGYSM- 101
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 497367283 143 PELSTSNRATVGGMIntdasgqGSCTYGKTRDHVLELHSV 182
Cdd:TIGR01678 102 SNLGSISEVSVAGII-------STGTHGSSIKHGILATQV 134
|
|
| glcE |
PRK11282 |
glycolate oxidase FAD binding subunit; Provisional |
61-280 |
6.30e-03 |
|
glycolate oxidase FAD binding subunit; Provisional
Pssm-ID: 236893 [Multi-domain] Cd Length: 352 Bit Score: 39.82 E-value: 6.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497367283 61 DDVARVATLMAEARFRHVKLTPRGGGTGT-NGQSLtDGIVVDLSRHmNNILEINVEERWVRVQAGTVKDQLNAALKPYGL 139
Cdd:PRK11282 2 DISAALLERVRQAAADGTPLRIRGGGSKDfYGRAL-AGEVLDTRAH-RGIVSYDPTELVITARAGTPLAELEAALAEAGQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497367283 140 FFA---PELSTsnRATVGGMINTDASGQGSCTYGKTRDHVLelhsvllgGERLhslpIDeaaleqacaapGRvGEVYRMA 216
Cdd:PRK11282 80 MLPfepPHFGG--GATLGGMVAAGLSGPRRPWAGAVRDFVL--------GTRL----IN-----------GR-GEHLRFG 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 497367283 217 rdiqqtqGDLIERtfpklnrcLTGYDLAHLrdeqgrfnlnsvLCGAEGSLGYVVEAKLNVLPIP 280
Cdd:PRK11282 134 -------GQVMKN--------VAGYDVSRL------------MAGSLGTLGVLLEVSLKVLPRP 170
|
|
|