|
Name |
Accession |
Description |
Interval |
E-value |
| GlcD |
COG0277 |
FAD/FMN-containing lactate dehydrogenase/glycolate oxidase [Energy production and conversion]; |
18-543 |
6.84e-150 |
|
FAD/FMN-containing lactate dehydrogenase/glycolate oxidase [Energy production and conversion];
Pssm-ID: 440046 [Multi-domain] Cd Length: 462 Bit Score: 453.58 E-value: 6.84e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446535614 18 FLQELeQQGFTGDTATSYADRLTMSTD-NSIYQLLPDAVVFPRSTADVALIARLAAQERyssLIFTPRGGGTGTNGQALN 96
Cdd:COG0277 6 LLAAL-RAILAGRVLTDPADRAAYARDgNSLYRGRPDAVVRPRSTEDVAAVVRLAAEHG---VPVVPRGGGTGLAGGAVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446535614 97 Q--GIIVDMSRhMNRIIEINPEEGWVRVEAGVIKDQLNQYLKPFGYFFAPELSTSNRATLGGMINTDASGQGSLVYGKTS 174
Cdd:COG0277 82 LdgGVVLDLSR-MNRILEVDPEDRTATVEAGVTLADLNAALAPHGLFFPPDPSSQGTATIGGNIATNAGGPRSLKYGLTR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446535614 175 DHVLGVRAVLLGGDILDTQPlpvelaetlgksnttigriyntvyqrcrqqrqliidnfpKLNRFLTGYDLRHVFndemte 254
Cdd:COG0277 161 DNVLGLEVVLADGEVVRTGG---------------------------------------RVPKNVTGYDLFWLL------ 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446535614 255 fdltrilTGSEGTLAFITEARLDITPLPKVRRLVNVKYDSFDSALRNAPFMVEARAL--SVETVDSKVLNLAREDIvwhs 332
Cdd:COG0277 196 -------VGSEGTLGVITEATLRLHPLPEAVATALVAFPDLEAAAAAVRALLAAGIApaALELMDRAALALVEAAP---- 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446535614 333 vselITDVPDkEMLGLNIVEFAGDDEALIDERVNALCVRLdeliasQQAGVIGWQVCRELAGVERIYAMRKKAVGLLGNA 412
Cdd:COG0277 265 ----PLGLPE-DGGALLLVEFDGDDAEEVEAQLARLRAIL------EAGGATDVRVAADGAERERLWKARKAALPALGRL 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446535614 413 KGAAKpipFAEDTCVPPEHLADYIAEFRALLDSHGLSYGMFGHVDAGVLHVRPALDMCDPQQEILMKQISDDVVALTAKY 492
Cdd:COG0277 334 DGGAK---LLEDVAVPPSRLPELLRELGALAAKYGLRATAFGHAGDGNLHVRILFDPADPEEVERARAAAEEIFDLVAEL 410
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 446535614 493 GGLLWGEHGKG-FRAEYSPAFFGEELFAELRKVKAAFDPHNRLNPGKICPPE 543
Cdd:COG0277 411 GGSISGEHGIGrLKAEFLPAEYGPAALALLRRIKAAFDPDGILNPGKILPPP 462
|
|
| GlpC |
COG0247 |
Fe-S cluster-containing oxidoreductase, includes glycolate oxidase subunit GlcF [Energy ... |
495-1018 |
1.68e-87 |
|
Fe-S cluster-containing oxidoreductase, includes glycolate oxidase subunit GlcF [Energy production and conversion];
Pssm-ID: 440017 [Multi-domain] Cd Length: 420 Bit Score: 287.36 E-value: 1.68e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446535614 495 LLWGEHGKGFRAEYSPAFFGEELFAELRKVKAAFDPHNRLNPGKICPPEGLDAPMMKVDAVkrgtfDRQIPIAVRQQWRG 574
Cdd:COG0247 1 LSGGHGGGLKAEHGTGRFMAPFLELELGKIKYAFDPDNKLNPGKIGLLNPGVELLGDGDLH-----DKNLKTLPWKELLD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446535614 575 AME-CNGNGLCFnfdarsPMCPSMKITQNRIHSPKGRATLVREWLRlladrgvdplkleqelpesgvslrtliartrnsw 653
Cdd:COG0247 76 ALDaCVGCGFCR------AMCPSYKATGDEKDSPRGRINLLREVLE---------------------------------- 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446535614 654 haNKGEYDFSHEVKEAMSGCLACKACSTQCPIKIDVPEFRSRFLQLYHTRYLRPLRDHLVATVESYAPLmarapktfnff 733
Cdd:COG0247 116 --GELPLDLSEEVYEVLDLCLTCKACETACPSGVDIADLIAEARAQLVERGGRPLRDRLLRTFPDRVPA----------- 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446535614 734 inqplvrklsekhigmvdlpllsvpslqqqmvghrsanmtleqlealnAEQKARTVLVVQDPFTSYYDAQVVADFVRLVE 813
Cdd:COG0247 183 ------------------------------------------------ADKEGAEVLLFPGCFTNYFDPEIGKAAVRLLE 214
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446535614 814 KLGFQPVLLP-FSPNGKAQHIKGFLNRFAKTAKKTADFLNRmakLGMP-MVGVDPALVLCYRDEYKLALGEeRGEFNVLL 891
Cdd:COG0247 215 AAGVEVVLPPeELCCGAPALSKGDLDLARKLARRNIEALER---LGVKaIVTTCPSCGLTLKDEYPELLGD-RVAFEVLD 290
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446535614 892 ANEWLASALESQPVA-TVSGESWYFFGHCTEVTALpGAPAQWAAIFARF-GAKLENV--SVGCCGMAGTYGHEAKNhkNS 967
Cdd:COG0247 291 ISEFLAELILEGKLKlKPLGEKVTYHDPCHLGRGG-GVYDAPRELLKAIpGVEVVEMpeDSGCCGGAGGYGFEEPE--LS 367
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 446535614 968 LGIYELsWHQAMQRLPRNRCLATGYSCRSQVKRV---EGTGVRHPVQALLEIIK 1018
Cdd:COG0247 368 MRIGER-KLEQIRATGADVVVTACPSCRTQLEDGtkeYGIEVKHPVELLAEALG 420
|
|
| FAD-oxidase_C |
pfam02913 |
FAD linked oxidases, C-terminal domain; This domain has a ferredoxin-like fold. |
281-539 |
1.21e-76 |
|
FAD linked oxidases, C-terminal domain; This domain has a ferredoxin-like fold.
Pssm-ID: 397178 Cd Length: 248 Bit Score: 251.47 E-value: 1.21e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446535614 281 LPKVRRLVNVKYDSFDSALRNAPFMVEAR--ALSVETVDSKVLNLAREDIVWHsvselitDVPDKEMLGLNIVEFAGDDE 358
Cdd:pfam02913 1 LPEVRAVALVGFPSFEAAVKAVREIARAGiiPAALELMDNDALDLVEATLGFP-------KGLPRDAAALLLVEFEGDDE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446535614 359 ALIDERVNALCVRLDELIASQQAGVIgwqvcrELAGVERIYAMRKKAVGLlGNAKGAAKPIPFAEDTCVPPEHLADYIAE 438
Cdd:pfam02913 74 ETAEEELEAVEAILEAGGAGDVVVAT------DEAEAERLWAARKYALPL-RDALGGAGPAVFSEDVSVPRSRLADLVRD 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446535614 439 FRALLDSHGLSYGMFGHVDAGVLHVRPALDMCDPQQEILMKQISDDVVALTAKYGGLLWGEHGKGF-RAEYSPAFFGEEL 517
Cdd:pfam02913 147 IKELLDKYGLVVCLFGHAGDGNLHLYILFDFRDPEQEERAEKLFDEIMDLALELGGSISGEHGVGRdKKPYLEREFGEEG 226
|
250 260
....*....|....*....|..
gi 446535614 518 FAELRKVKAAFDPHNRLNPGKI 539
Cdd:pfam02913 227 LALMRRIKAAFDPKGILNPGKV 248
|
|
| glcD |
TIGR00387 |
glycolate oxidase, subunit GlcD; This protein, the glycolate oxidase GlcD subunit, is similar ... |
55-538 |
1.28e-55 |
|
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: 198.84 E-value: 1.28e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446535614 55 VVFPRSTADVALIARLAAQERyssLIFTPRGGGTGTNGQAL-NQGIIVDMSRHMNRIIEINPEEGWVRVEAGVIKDQLNQ 133
Cdd:TIGR00387 1 VVFPKNTEQVARILKLCHEHR---IPIVPRGAGTGLSGGALpEEGGLVLVFKHMNKILEIDVVNLTAVVQPGVRNLELEQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446535614 134 YLKPFGYFFAPELSTSNRATLGGMINTDASGQGSLVYGKTSDHVLGVRAVLLGGDILdtqplpvelaETLGKSnttigri 213
Cdd:TIGR00387 78 AVEEHNLFYPPDPSSQISSTIGGNIAENAGGMRGLKYGTTVDYVLGLEVVTADGEIL----------RIGGKT------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446535614 214 yntvyQRCRQqrqliidnfpklnrfltGYDLrhvfndemtefdlTRILTGSEGTLAFITEARLDITPLPKVRRLVNVKYD 293
Cdd:TIGR00387 141 -----AKDVA-----------------GYDL-------------TGLFVGSEGTLGIVTEATLKLLPKPENIVVALAFFD 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446535614 294 SFDSALrNAPFMVEARAL---SVETVDSKVLNlAREDIVwhsvselITDVPdKEMLGLNIVEFAGDDEA--LIDERVNAL 368
Cdd:TIGR00387 186 SIEKAM-QAVYDIIAAGIipaGMEFLDNLSIK-AVEDIS-------GIGLP-KDAGAILLVEIDGVHEAveRDEEKIEQI 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446535614 369 CVRldeliasqqAGVIGWQVCRELAGVERIYAMRKKAVGLLGNAKgaakPIPFAEDTCVPPEHLADYIAEFRALLDSHGL 448
Cdd:TIGR00387 256 CRK---------NGAVDVQIAQDEEERALLWAGRRNAFKAASKLS----PLYLIEDGTVPRSKLPEALRGIADIASKYDF 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446535614 449 SYGMFGHVDAGVLHVRPALDMCDPQQEILMKQISDDVVALTAKYGGLLWGEHGKGF-RAEYSPAFFGEELFAELRKVKAA 527
Cdd:TIGR00387 323 TIANFGHAGDGNLHPTILTDPEDKGEMERVEEAGGEIFELAIELGGTISGEHGIGVvKAEFMPYKFNEKELETMRAIKKA 402
|
490
....*....|.
gi 446535614 528 FDPHNRLNPGK 538
Cdd:TIGR00387 403 FDPDNILNPGK 413
|
|
| PLN02805 |
PLN02805 |
D-lactate dehydrogenase [cytochrome] |
10-542 |
5.68e-39 |
|
D-lactate dehydrogenase [cytochrome]
Pssm-ID: 178402 [Multi-domain] Cd Length: 555 Bit Score: 153.63 E-value: 5.68e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446535614 10 GVVQLVLNFLQELEQQGFTGDTATSYADRLTMSTD---------NSIYQL--LPDAVVFPRSTADVALIARlaAQERYSS 78
Cdd:PLN02805 81 GSTEFVVKGEHKLVPQELIDELKAILQDNMTLDYDeryfhgkpqNSFHKAvnIPDVVVFPRSEEEVSKIVK--SCNKYKV 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446535614 79 LIfTPRGGGTGTNGQAL--NQGIIVDMSRhMNRIIEINPEEGWVRVEAGVIKDQLNQYLKPFGYFFApeLSTSNRATLGG 156
Cdd:PLN02805 159 PI-VPYGGATSIEGHTLapHGGVCIDMSL-MKSVKALHVEDMDVVVEPGIGWLELNEYLEPYGLFFP--LDPGPGATIGG 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446535614 157 MINTDASGQGSLVYGKTSDHVLGVRAVLLGGDILDTQplpvelaetlgksnttigriyntvyQRCRQQRqliidnfpkln 236
Cdd:PLN02805 235 MCATRCSGSLAVRYGTMRDNVISLKVVLPNGDVVKTA-------------------------SRARKSA----------- 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446535614 237 rflTGYdlrhvfndemtefDLTRILTGSEGTLAFITEARLDITPLPK--VRRLVNVKY--DSFDSALrnAPFMVEARALS 312
Cdd:PLN02805 279 ---AGY-------------DLTRLVIGSEGTLGVITEVTLRLQKIPQhsVVAMCNFPTikDAADVAI--ATMLSGIQVSR 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446535614 313 VETVDS---KVLNLAREdivwhsvseliTDVPDKEMLglnIVEFAGdDEALIDERvnALCVrldELIASQQAGViGWQVC 389
Cdd:PLN02805 341 VELLDEvqiRAINMANG-----------KNLPEAPTL---MFEFIG-TEAYAREQ--TLIV---QKIASKHNGS-DFVFA 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446535614 390 RELAGVERIYAMRKKAVGllgnAKGAAKPIPFA--EDTCVPPEHLADYIAEFRALLDSHGLSYGMFGHVDAGVLHvrpAL 467
Cdd:PLN02805 400 EEPEAKKELWKIRKEALW----ACFAMEPKYEAmiTDVCVPLSHLAELISRSKKELDASPLVCTVIAHAGDGNFH---TI 472
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446535614 468 DMCDPQQEILMKQ---ISDDVVALTAKYGGLLWGEHGKGF-RAEYSPAFFGEELFAELRKVKAAFDPHNRLNPGKICPP 542
Cdd:PLN02805 473 ILFDPSQEDQRREaerLNHFMVHTALSMEGTCTGEHGVGTgKMKYLEKELGIEALQTMKRIKKALDPNNIMNPGKLIPP 551
|
|
| glpC |
PRK11168 |
anaerobic glycerol-3-phosphate dehydrogenase subunit C; |
664-1013 |
4.89e-15 |
|
anaerobic glycerol-3-phosphate dehydrogenase subunit C;
Pssm-ID: 236869 [Multi-domain] Cd Length: 396 Bit Score: 78.37 E-value: 4.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446535614 664 HEVKEAMSGCLACKACSTQCPIKIDVPEFRSRFLQLYHTRYLRPLRDHLVATVESYAPLMARAPKTFNFFINQPLVRKLS 743
Cdd:PRK11168 47 ALYDESLKYCSNCKRCEVACPSGVKIGDIIQRARAKYVTERGPPLRDRILSHTDLMGSLATPFAPLVNAATGLKPVRWLL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446535614 744 EKHIGmVDlpllsvpslqqqmvGHRS----ANMTLEQLEALNAEQKART---VLVVQDPFTSYYDAQVVADFVRLVEKLG 816
Cdd:PRK11168 127 EKTLG-ID--------------HRRPlpkyAFGTFRRWYRKQAAQQAQYkkqVAYFHGCYVNYNHPQLGKDLVKVLNAMG 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446535614 817 FQPVLLPFSPNGKAQHIKGFLNRFAKTAKKTADFLNRMAKLGMPMVGVDPALVLCYRDEYKLALGEERGEF--NVLLANE 894
Cdd:PRK11168 192 YEVLLPKEKCCGLPLIANGFLDKARKQAEFNVESLREAIEKGIPVIATSSSCTLTLRDEYPELLGVDNAGVrdHIEDATE 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446535614 895 WLASALESQPVATVSGESWYFFGHctevtalpgAPAQ-----WA----AIFARF-GAKLENVSVGCCGMAGTYGHEAKNH 964
Cdd:PRK11168 272 FLRRLLDQGKLLPLKPLPLKVAYH---------TPCHlekqgWGlytlELLRLIpGLEVVVLDSQCCGIAGTYGFKKEKY 342
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 446535614 965 KNSLGIYElSWHQAMQRLPRNRCLATGYSCRSQVKRVEGTGVRHPVQAL 1013
Cdd:PRK11168 343 ETSQAIGA-PLFRQIEESGADLVVTDCETCKWQIEMSTGLECEHPITLL 390
|
|
| Fer4_8 |
pfam13183 |
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ... |
578-687 |
4.15e-05 |
|
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich. Domain contains two 4Fe4S clusters.
Pssm-ID: 433017 [Multi-domain] Cd Length: 64 Bit Score: 42.30 E-value: 4.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446535614 578 CNGNGLCfnfdarSPMCPSMKITQNRIHSPKGRATLvrewlrlladrgvdplkleqelpesgvslrtliartrnswhANK 657
Cdd:pfam13183 2 CIRCGAC------LAACPVYLVTGGRFPGDPRGGAA-----------------------------------------ALL 34
|
90 100 110
....*....|....*....|....*....|
gi 446535614 658 GEYDFSHEVKEAMSGCLACKACSTQCPIKI 687
Cdd:pfam13183 35 GRLEALEGLAEGLWLCTLCGACTEVCPVGI 64
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| GlcD |
COG0277 |
FAD/FMN-containing lactate dehydrogenase/glycolate oxidase [Energy production and conversion]; |
18-543 |
6.84e-150 |
|
FAD/FMN-containing lactate dehydrogenase/glycolate oxidase [Energy production and conversion];
Pssm-ID: 440046 [Multi-domain] Cd Length: 462 Bit Score: 453.58 E-value: 6.84e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446535614 18 FLQELeQQGFTGDTATSYADRLTMSTD-NSIYQLLPDAVVFPRSTADVALIARLAAQERyssLIFTPRGGGTGTNGQALN 96
Cdd:COG0277 6 LLAAL-RAILAGRVLTDPADRAAYARDgNSLYRGRPDAVVRPRSTEDVAAVVRLAAEHG---VPVVPRGGGTGLAGGAVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446535614 97 Q--GIIVDMSRhMNRIIEINPEEGWVRVEAGVIKDQLNQYLKPFGYFFAPELSTSNRATLGGMINTDASGQGSLVYGKTS 174
Cdd:COG0277 82 LdgGVVLDLSR-MNRILEVDPEDRTATVEAGVTLADLNAALAPHGLFFPPDPSSQGTATIGGNIATNAGGPRSLKYGLTR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446535614 175 DHVLGVRAVLLGGDILDTQPlpvelaetlgksnttigriyntvyqrcrqqrqliidnfpKLNRFLTGYDLRHVFndemte 254
Cdd:COG0277 161 DNVLGLEVVLADGEVVRTGG---------------------------------------RVPKNVTGYDLFWLL------ 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446535614 255 fdltrilTGSEGTLAFITEARLDITPLPKVRRLVNVKYDSFDSALRNAPFMVEARAL--SVETVDSKVLNLAREDIvwhs 332
Cdd:COG0277 196 -------VGSEGTLGVITEATLRLHPLPEAVATALVAFPDLEAAAAAVRALLAAGIApaALELMDRAALALVEAAP---- 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446535614 333 vselITDVPDkEMLGLNIVEFAGDDEALIDERVNALCVRLdeliasQQAGVIGWQVCRELAGVERIYAMRKKAVGLLGNA 412
Cdd:COG0277 265 ----PLGLPE-DGGALLLVEFDGDDAEEVEAQLARLRAIL------EAGGATDVRVAADGAERERLWKARKAALPALGRL 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446535614 413 KGAAKpipFAEDTCVPPEHLADYIAEFRALLDSHGLSYGMFGHVDAGVLHVRPALDMCDPQQEILMKQISDDVVALTAKY 492
Cdd:COG0277 334 DGGAK---LLEDVAVPPSRLPELLRELGALAAKYGLRATAFGHAGDGNLHVRILFDPADPEEVERARAAAEEIFDLVAEL 410
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 446535614 493 GGLLWGEHGKG-FRAEYSPAFFGEELFAELRKVKAAFDPHNRLNPGKICPPE 543
Cdd:COG0277 411 GGSISGEHGIGrLKAEFLPAEYGPAALALLRRIKAAFDPDGILNPGKILPPP 462
|
|
| GlpC |
COG0247 |
Fe-S cluster-containing oxidoreductase, includes glycolate oxidase subunit GlcF [Energy ... |
495-1018 |
1.68e-87 |
|
Fe-S cluster-containing oxidoreductase, includes glycolate oxidase subunit GlcF [Energy production and conversion];
Pssm-ID: 440017 [Multi-domain] Cd Length: 420 Bit Score: 287.36 E-value: 1.68e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446535614 495 LLWGEHGKGFRAEYSPAFFGEELFAELRKVKAAFDPHNRLNPGKICPPEGLDAPMMKVDAVkrgtfDRQIPIAVRQQWRG 574
Cdd:COG0247 1 LSGGHGGGLKAEHGTGRFMAPFLELELGKIKYAFDPDNKLNPGKIGLLNPGVELLGDGDLH-----DKNLKTLPWKELLD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446535614 575 AME-CNGNGLCFnfdarsPMCPSMKITQNRIHSPKGRATLVREWLRlladrgvdplkleqelpesgvslrtliartrnsw 653
Cdd:COG0247 76 ALDaCVGCGFCR------AMCPSYKATGDEKDSPRGRINLLREVLE---------------------------------- 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446535614 654 haNKGEYDFSHEVKEAMSGCLACKACSTQCPIKIDVPEFRSRFLQLYHTRYLRPLRDHLVATVESYAPLmarapktfnff 733
Cdd:COG0247 116 --GELPLDLSEEVYEVLDLCLTCKACETACPSGVDIADLIAEARAQLVERGGRPLRDRLLRTFPDRVPA----------- 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446535614 734 inqplvrklsekhigmvdlpllsvpslqqqmvghrsanmtleqlealnAEQKARTVLVVQDPFTSYYDAQVVADFVRLVE 813
Cdd:COG0247 183 ------------------------------------------------ADKEGAEVLLFPGCFTNYFDPEIGKAAVRLLE 214
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446535614 814 KLGFQPVLLP-FSPNGKAQHIKGFLNRFAKTAKKTADFLNRmakLGMP-MVGVDPALVLCYRDEYKLALGEeRGEFNVLL 891
Cdd:COG0247 215 AAGVEVVLPPeELCCGAPALSKGDLDLARKLARRNIEALER---LGVKaIVTTCPSCGLTLKDEYPELLGD-RVAFEVLD 290
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446535614 892 ANEWLASALESQPVA-TVSGESWYFFGHCTEVTALpGAPAQWAAIFARF-GAKLENV--SVGCCGMAGTYGHEAKNhkNS 967
Cdd:COG0247 291 ISEFLAELILEGKLKlKPLGEKVTYHDPCHLGRGG-GVYDAPRELLKAIpGVEVVEMpeDSGCCGGAGGYGFEEPE--LS 367
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 446535614 968 LGIYELsWHQAMQRLPRNRCLATGYSCRSQVKRV---EGTGVRHPVQALLEIIK 1018
Cdd:COG0247 368 MRIGER-KLEQIRATGADVVVTACPSCRTQLEDGtkeYGIEVKHPVELLAEALG 420
|
|
| FAD-oxidase_C |
pfam02913 |
FAD linked oxidases, C-terminal domain; This domain has a ferredoxin-like fold. |
281-539 |
1.21e-76 |
|
FAD linked oxidases, C-terminal domain; This domain has a ferredoxin-like fold.
Pssm-ID: 397178 Cd Length: 248 Bit Score: 251.47 E-value: 1.21e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446535614 281 LPKVRRLVNVKYDSFDSALRNAPFMVEAR--ALSVETVDSKVLNLAREDIVWHsvselitDVPDKEMLGLNIVEFAGDDE 358
Cdd:pfam02913 1 LPEVRAVALVGFPSFEAAVKAVREIARAGiiPAALELMDNDALDLVEATLGFP-------KGLPRDAAALLLVEFEGDDE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446535614 359 ALIDERVNALCVRLDELIASQQAGVIgwqvcrELAGVERIYAMRKKAVGLlGNAKGAAKPIPFAEDTCVPPEHLADYIAE 438
Cdd:pfam02913 74 ETAEEELEAVEAILEAGGAGDVVVAT------DEAEAERLWAARKYALPL-RDALGGAGPAVFSEDVSVPRSRLADLVRD 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446535614 439 FRALLDSHGLSYGMFGHVDAGVLHVRPALDMCDPQQEILMKQISDDVVALTAKYGGLLWGEHGKGF-RAEYSPAFFGEEL 517
Cdd:pfam02913 147 IKELLDKYGLVVCLFGHAGDGNLHLYILFDFRDPEQEERAEKLFDEIMDLALELGGSISGEHGVGRdKKPYLEREFGEEG 226
|
250 260
....*....|....*....|..
gi 446535614 518 FAELRKVKAAFDPHNRLNPGKI 539
Cdd:pfam02913 227 LALMRRIKAAFDPKGILNPGKV 248
|
|
| glcD |
TIGR00387 |
glycolate oxidase, subunit GlcD; This protein, the glycolate oxidase GlcD subunit, is similar ... |
55-538 |
1.28e-55 |
|
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: 198.84 E-value: 1.28e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446535614 55 VVFPRSTADVALIARLAAQERyssLIFTPRGGGTGTNGQAL-NQGIIVDMSRHMNRIIEINPEEGWVRVEAGVIKDQLNQ 133
Cdd:TIGR00387 1 VVFPKNTEQVARILKLCHEHR---IPIVPRGAGTGLSGGALpEEGGLVLVFKHMNKILEIDVVNLTAVVQPGVRNLELEQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446535614 134 YLKPFGYFFAPELSTSNRATLGGMINTDASGQGSLVYGKTSDHVLGVRAVLLGGDILdtqplpvelaETLGKSnttigri 213
Cdd:TIGR00387 78 AVEEHNLFYPPDPSSQISSTIGGNIAENAGGMRGLKYGTTVDYVLGLEVVTADGEIL----------RIGGKT------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446535614 214 yntvyQRCRQqrqliidnfpklnrfltGYDLrhvfndemtefdlTRILTGSEGTLAFITEARLDITPLPKVRRLVNVKYD 293
Cdd:TIGR00387 141 -----AKDVA-----------------GYDL-------------TGLFVGSEGTLGIVTEATLKLLPKPENIVVALAFFD 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446535614 294 SFDSALrNAPFMVEARAL---SVETVDSKVLNlAREDIVwhsvselITDVPdKEMLGLNIVEFAGDDEA--LIDERVNAL 368
Cdd:TIGR00387 186 SIEKAM-QAVYDIIAAGIipaGMEFLDNLSIK-AVEDIS-------GIGLP-KDAGAILLVEIDGVHEAveRDEEKIEQI 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446535614 369 CVRldeliasqqAGVIGWQVCRELAGVERIYAMRKKAVGLLGNAKgaakPIPFAEDTCVPPEHLADYIAEFRALLDSHGL 448
Cdd:TIGR00387 256 CRK---------NGAVDVQIAQDEEERALLWAGRRNAFKAASKLS----PLYLIEDGTVPRSKLPEALRGIADIASKYDF 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446535614 449 SYGMFGHVDAGVLHVRPALDMCDPQQEILMKQISDDVVALTAKYGGLLWGEHGKGF-RAEYSPAFFGEELFAELRKVKAA 527
Cdd:TIGR00387 323 TIANFGHAGDGNLHPTILTDPEDKGEMERVEEAGGEIFELAIELGGTISGEHGIGVvKAEFMPYKFNEKELETMRAIKKA 402
|
490
....*....|.
gi 446535614 528 FDPHNRLNPGK 538
Cdd:TIGR00387 403 FDPDNILNPGK 413
|
|
| FAD_binding_4 |
pfam01565 |
FAD binding domain; This family consists of various enzymes that use FAD as a co-factor, most ... |
52-192 |
9.88e-43 |
|
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: 152.36 E-value: 9.88e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446535614 52 PDAVVFPRSTADVALIARLAAQERYSsliFTPRGGGTGTNGQA-LNQGIIVDMSRhMNRIIEINPEEGWVRVEAGVIKDQ 130
Cdd:pfam01565 1 PAAVVLPESEEEVAAIVRLANENGLP---VLPRGGGSSLLGGAvQTGGIVLDLSR-LNGILEIDPEDGTATVEAGVTLGD 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446535614 131 LNQYLKPFGYFFAPELSTSNRATLGGMINTDASGQGSLVYGKTSDHVLGVRAVLLGGDILDT 192
Cdd:pfam01565 77 LVRALAAKGLLLGLDPGSGIPGTVGGAIATNAGGYGSEKYGLTRDNVLGLEVVLADGEVVRL 138
|
|
| PLN02805 |
PLN02805 |
D-lactate dehydrogenase [cytochrome] |
10-542 |
5.68e-39 |
|
D-lactate dehydrogenase [cytochrome]
Pssm-ID: 178402 [Multi-domain] Cd Length: 555 Bit Score: 153.63 E-value: 5.68e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446535614 10 GVVQLVLNFLQELEQQGFTGDTATSYADRLTMSTD---------NSIYQL--LPDAVVFPRSTADVALIARlaAQERYSS 78
Cdd:PLN02805 81 GSTEFVVKGEHKLVPQELIDELKAILQDNMTLDYDeryfhgkpqNSFHKAvnIPDVVVFPRSEEEVSKIVK--SCNKYKV 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446535614 79 LIfTPRGGGTGTNGQAL--NQGIIVDMSRhMNRIIEINPEEGWVRVEAGVIKDQLNQYLKPFGYFFApeLSTSNRATLGG 156
Cdd:PLN02805 159 PI-VPYGGATSIEGHTLapHGGVCIDMSL-MKSVKALHVEDMDVVVEPGIGWLELNEYLEPYGLFFP--LDPGPGATIGG 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446535614 157 MINTDASGQGSLVYGKTSDHVLGVRAVLLGGDILDTQplpvelaetlgksnttigriyntvyQRCRQQRqliidnfpkln 236
Cdd:PLN02805 235 MCATRCSGSLAVRYGTMRDNVISLKVVLPNGDVVKTA-------------------------SRARKSA----------- 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446535614 237 rflTGYdlrhvfndemtefDLTRILTGSEGTLAFITEARLDITPLPK--VRRLVNVKY--DSFDSALrnAPFMVEARALS 312
Cdd:PLN02805 279 ---AGY-------------DLTRLVIGSEGTLGVITEVTLRLQKIPQhsVVAMCNFPTikDAADVAI--ATMLSGIQVSR 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446535614 313 VETVDS---KVLNLAREdivwhsvseliTDVPDKEMLglnIVEFAGdDEALIDERvnALCVrldELIASQQAGViGWQVC 389
Cdd:PLN02805 341 VELLDEvqiRAINMANG-----------KNLPEAPTL---MFEFIG-TEAYAREQ--TLIV---QKIASKHNGS-DFVFA 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446535614 390 RELAGVERIYAMRKKAVGllgnAKGAAKPIPFA--EDTCVPPEHLADYIAEFRALLDSHGLSYGMFGHVDAGVLHvrpAL 467
Cdd:PLN02805 400 EEPEAKKELWKIRKEALW----ACFAMEPKYEAmiTDVCVPLSHLAELISRSKKELDASPLVCTVIAHAGDGNFH---TI 472
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446535614 468 DMCDPQQEILMKQ---ISDDVVALTAKYGGLLWGEHGKGF-RAEYSPAFFGEELFAELRKVKAAFDPHNRLNPGKICPP 542
Cdd:PLN02805 473 ILFDPSQEDQRREaerLNHFMVHTALSMEGTCTGEHGVGTgKMKYLEKELGIEALQTMKRIKKALDPNNIMNPGKLIPP 551
|
|
| PRK11230 |
PRK11230 |
glycolate oxidase subunit GlcD; Provisional |
46-541 |
4.74e-30 |
|
glycolate oxidase subunit GlcD; Provisional
Pssm-ID: 183043 [Multi-domain] Cd Length: 499 Bit Score: 125.66 E-value: 4.74e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446535614 46 SIYQLLPDAVVFPRSTADVALIARLAAQERyssLIFTPRGGGTGTNGQA--LNQGIIVDMSRhMNRIIEINPEEGWVRVE 123
Cdd:PRK11230 50 SAYRTRPLLVVLPKQMEQVQALLAVCHRLR---VPVVARGAGTGLSGGAlpLEKGVLLVMAR-FNRILDINPVGRRARVQ 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446535614 124 AGVIKDQLNQYLKPFGYFFAPELSTSNRATLGGMINTDASGQGSLVYGKTSDHVLGVRAVLLGGDILdtqplpvelaeTL 203
Cdd:PRK11230 126 PGVRNLAISQAAAPHGLYYAPDPSSQIACSIGGNVAENAGGVHCLKYGLTVHNLLKVEILTLDGEAL-----------TL 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446535614 204 GKSNTtigriyntvyqrcrqqrqliidnfpklnrfltgydlrhvfndEMTEFDLTRILTGSEGTLAFITEARLDITPLPK 283
Cdd:PRK11230 195 GSDAL------------------------------------------DSPGFDLLALFTGSEGMLGVVTEVTVKLLPKPP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446535614 284 VRRLVNVKYDSFDSALRNAPFMVEARAL--SVETVDSKVLNlAREDIVwHSVSELitdvpDKEMLGLniVEFAGddealI 361
Cdd:PRK11230 233 VARVLLASFDSVEKAGLAVGDIIAAGIIpgGLEMMDNLSIR-AAEDFI-HAGYPV-----DAEAILL--CELDG-----V 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446535614 362 DERVNALCVRLDELIasQQAGVIGWQVCRELAGVERIYAMRKKAVgllgNAKGAAKPIPFAEDTCVPPEHLADYIAEFRA 441
Cdd:PRK11230 299 ESDVQEDCERVNDIL--LKAGATDVRLAQDEAERVRFWAGRKNAF----PAVGRISPDYYCMDGTIPRRELPGVLEGIAR 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446535614 442 LLDSHGLSYGMFGHVDAGVLHVRPALDMCDPQQEILMKQISDDVVALTAKYGGLLWGEHGKGfRAEYSP--AFFGEELFA 519
Cdd:PRK11230 373 LSQQYGLRVANVFHAGDGNMHPLILFDANEPGELERAEALGGKILELCVEVGGSITGEHGVG-REKINQmcAQFNSDEIT 451
|
490 500
....*....|....*....|..
gi 446535614 520 ELRKVKAAFDPHNRLNPGKICP 541
Cdd:PRK11230 452 LFHAVKAAFDPDGLLNPGKNIP 473
|
|
| glpC |
PRK11168 |
anaerobic glycerol-3-phosphate dehydrogenase subunit C; |
664-1013 |
4.89e-15 |
|
anaerobic glycerol-3-phosphate dehydrogenase subunit C;
Pssm-ID: 236869 [Multi-domain] Cd Length: 396 Bit Score: 78.37 E-value: 4.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446535614 664 HEVKEAMSGCLACKACSTQCPIKIDVPEFRSRFLQLYHTRYLRPLRDHLVATVESYAPLMARAPKTFNFFINQPLVRKLS 743
Cdd:PRK11168 47 ALYDESLKYCSNCKRCEVACPSGVKIGDIIQRARAKYVTERGPPLRDRILSHTDLMGSLATPFAPLVNAATGLKPVRWLL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446535614 744 EKHIGmVDlpllsvpslqqqmvGHRS----ANMTLEQLEALNAEQKART---VLVVQDPFTSYYDAQVVADFVRLVEKLG 816
Cdd:PRK11168 127 EKTLG-ID--------------HRRPlpkyAFGTFRRWYRKQAAQQAQYkkqVAYFHGCYVNYNHPQLGKDLVKVLNAMG 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446535614 817 FQPVLLPFSPNGKAQHIKGFLNRFAKTAKKTADFLNRMAKLGMPMVGVDPALVLCYRDEYKLALGEERGEF--NVLLANE 894
Cdd:PRK11168 192 YEVLLPKEKCCGLPLIANGFLDKARKQAEFNVESLREAIEKGIPVIATSSSCTLTLRDEYPELLGVDNAGVrdHIEDATE 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446535614 895 WLASALESQPVATVSGESWYFFGHctevtalpgAPAQ-----WA----AIFARF-GAKLENVSVGCCGMAGTYGHEAKNH 964
Cdd:PRK11168 272 FLRRLLDQGKLLPLKPLPLKVAYH---------TPCHlekqgWGlytlELLRLIpGLEVVVLDSQCCGIAGTYGFKKEKY 342
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 446535614 965 KNSLGIYElSWHQAMQRLPRNRCLATGYSCRSQVKRVEGTGVRHPVQAL 1013
Cdd:PRK11168 343 ETSQAIGA-PLFRQIEESGADLVVTDCETCKWQIEMSTGLECEHPITLL 390
|
|
| PLN02441 |
PLN02441 |
cytokinin dehydrogenase |
28-125 |
2.71e-07 |
|
cytokinin dehydrogenase
Pssm-ID: 215242 [Multi-domain] Cd Length: 525 Bit Score: 54.54 E-value: 2.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446535614 28 TGDTATSYAdrltmSTD-NSIYQLLPDAVVFPRSTADVALIARlAAQERYSSLIFTPRGGGTGTNGQAL-NQGIIVDMS- 104
Cdd:PLN02441 45 FDPVSTASA-----SKDfGNLVHSLPAAVLYPSSVEDIASLVR-AAYGSSSPLTVAARGHGHSLNGQAQaPGGVVVDMRs 118
|
90 100
....*....|....*....|...
gi 446535614 105 --RHMNRIIEINPEEGWVRVEAG 125
Cdd:PLN02441 119 lrGGVRGPPVIVVSGDGPYVDVS 141
|
|
| Fer4_8 |
pfam13183 |
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ... |
578-687 |
4.15e-05 |
|
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich. Domain contains two 4Fe4S clusters.
Pssm-ID: 433017 [Multi-domain] Cd Length: 64 Bit Score: 42.30 E-value: 4.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446535614 578 CNGNGLCfnfdarSPMCPSMKITQNRIHSPKGRATLvrewlrlladrgvdplkleqelpesgvslrtliartrnswhANK 657
Cdd:pfam13183 2 CIRCGAC------LAACPVYLVTGGRFPGDPRGGAA-----------------------------------------ALL 34
|
90 100 110
....*....|....*....|....*....|
gi 446535614 658 GEYDFSHEVKEAMSGCLACKACSTQCPIKI 687
Cdd:pfam13183 35 GRLEALEGLAEGLWLCTLCGACTEVCPVGI 64
|
|
| PLN02465 |
PLN02465 |
L-galactono-1,4-lactone dehydrogenase |
58-166 |
2.07e-04 |
|
L-galactono-1,4-lactone dehydrogenase
Pssm-ID: 215258 [Multi-domain] Cd Length: 573 Bit Score: 45.23 E-value: 2.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446535614 58 PRSTADVALIARLAAQERYSsliFTPRGGGTGTNGQALNQGIIVDMSrHMNRIIEINPEEGWVRVEAGVIKDQLNQYLKP 137
Cdd:PLN02465 103 PESLEELEDIVKEAHEKGRR---IRPVGSGLSPNGLAFSREGMVNLA-LMDKVLEVDKEKKRVTVQAGARVQQVVEALRP 178
|
90 100 110
....*....|....*....|....*....|....
gi 446535614 138 FGyffapeLSTSNRAT-----LGGMINTDASGQG 166
Cdd:PLN02465 179 HG------LTLQNYASireqqIGGFIQVGAHGTG 206
|
|
| FAD_lactone_ox |
TIGR01678 |
sugar 1,4-lactone oxidases; This model represents a family of at least two different sugar 1,4 ... |
47-190 |
2.25e-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: 44.89 E-value: 2.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446535614 47 IYQLLPDAVVFPRSTADVALIARLAAQERYSSLIFtprGGGTGTNGQALNQGIIVDMSRhMNRIIEINPEEGWVRVEAGV 126
Cdd:TIGR01678 10 TYSASPEVYYQPTSVEEVREVLALAREQKKKVKVV---GGGHSPSDIACTDGFLIHLDK-MNKVLQFDKEKKQITVEAGI 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446535614 127 IKDQLNQYLKPFGYFFaPELSTSNRATLGGMINTDASGQgSLVYGKTSDHVLGVRAVLLGGDIL 190
Cdd:TIGR01678 86 RLYQLHEQLDEHGYSM-SNLGSISEVSVAGIISTGTHGS-SIKHGILATQVVALTIMTADGEVL 147
|
|
| GLDHase |
TIGR01676 |
galactonolactone dehydrogenase; This model represents L-Galactono-gamma-lactone dehydrogenase ... |
37-167 |
7.93e-04 |
|
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: 43.13 E-value: 7.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446535614 37 DRLTMSTDNSIYQLLPDAVVFPRSTADVALIARLAAQERYSsliFTPRGGGTGTNGQALNQGIIVDMSRhMNRIIEINPE 116
Cdd:TIGR01676 47 DLHTVSNWSGTHEVLTRTFHQPEAIEELEGIVKQANEKKAR---IRPVGSGLSPNGIGLSRAGMVNLAL-MDKVLEVDEE 122
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 446535614 117 EGWVRVEAGVIKDQLNQYLKPFGYFFApELSTSNRATLGGMINTDASGQGS 167
Cdd:TIGR01676 123 KKRVRVQAGIRVQQLVDAIKEYGITLQ-NFASIREQQIGGIIQVGAHGTGA 172
|
|
| |
