|
Name |
Accession |
Description |
Interval |
E-value |
| GlcD |
COG0277 |
FAD/FMN-containing lactate dehydrogenase/glycolate oxidase [Energy production and conversion]; |
18-543 |
3.03e-148 |
|
FAD/FMN-containing lactate dehydrogenase/glycolate oxidase [Energy production and conversion];
Pssm-ID: 440046 [Multi-domain] Cd Length: 462 Bit Score: 448.96 E-value: 3.03e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522179794 18 FLQALeQQGFTGDTATNYADRLTMATD-NSIYQLLPDAVVFPRSTADVALIARLATQERfsaLVFTPRGGGTGTNGQALN 96
Cdd:COG0277 6 LLAAL-RAILAGRVLTDPADRAAYARDgNSLYRGRPDAVVRPRSTEDVAAVVRLAAEHG---VPVVPRGGGTGLAGGAVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522179794 97 Q--GIIIDMSRyMNRIIEINPEEGWVRVEAGVIKDQLNQYLKPYGYFFAPELSTSNRATIGGMINTDASGQGSLVYGKTS 174
Cdd:COG0277 82 LdgGVVLDLSR-MNRILEVDPEDRTATVEAGVTLADLNAALAPHGLFFPPDPSSQGTATIGGNIATNAGGPRSLKYGLTR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522179794 175 DHVLGVRAVllggdildtqpvpvelaetlgkenTASGRIYRTVlercrdnrqlildkfPKLNRFLTGYDLRHVFndeltq 254
Cdd:COG0277 161 DNVLGLEVV------------------------LADGEVVRTG---------------GRVPKNVTGYDLFWLL------ 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522179794 255 fdltrvlTGSEGTLAFITEARLDITRLPKVRRLVNVKYDSFDSALRNAPFMVEAQAL--SVETVDSKVLNLAREdivwHS 332
Cdd:COG0277 196 -------VGSEGTLGVITEATLRLHPLPEAVATALVAFPDLEAAAAAVRALLAAGIApaALELMDRAALALVEA----AP 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522179794 333 VRELITDVPdkemlGLNIVEFAGDDAELIDSQVTTLCQRLDEliahgeGGVIGWQLCNDLAGIERIYAMRKKAVGLLGNA 412
Cdd:COG0277 265 PLGLPEDGG-----ALLLVEFDGDDAEEVEAQLARLRAILEA------GGATDVRVAADGAERERLWKARKAALPALGRL 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522179794 413 KGAAKpipFAEDTCVPPEHLADYIVEFRALLDSHGLSYGMFGHVDAGVLHVRPALDMCDPQQEILMKQISDEVVALTAKY 492
Cdd:COG0277 334 DGGAK---LLEDVAVPPSRLPELLRELGALAAKYGLRATAFGHAGDGNLHVRILFDPADPEEVERARAAAEEIFDLVAEL 410
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 522179794 493 GGLLWGEHGKG-FRAEYSPAFFGEQLFGELRKVKAAFDPNNRLNPGKICPPE 543
Cdd:COG0277 411 GGSISGEHGIGrLKAEFLPAEYGPAALALLRRIKAAFDPDGILNPGKILPPP 462
|
|
| GlpC |
COG0247 |
Fe-S cluster-containing oxidoreductase, includes glycolate oxidase subunit GlcF [Energy ... |
495-1018 |
1.11e-82 |
|
Fe-S cluster-containing oxidoreductase, includes glycolate oxidase subunit GlcF [Energy production and conversion];
Pssm-ID: 440017 [Multi-domain] Cd Length: 420 Bit Score: 274.26 E-value: 1.11e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522179794 495 LLWGEHGKGFRAEYSPAFFGEQLFGELRKVKAAFDPNNRLNPGKICPPEGVDAPMLQVDAvkrgtYDRQIPIAVRASWRG 574
Cdd:COG0247 1 LSGGHGGGLKAEHGTGRFMAPFLELELGKIKYAFDPDNKLNPGKIGLLNPGVELLGDGDL-----HDKNLKTLPWKELLD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522179794 575 ALE-CNGNGLCFnfdvksPMCPSMKITSNRIHSPKGRATLVREWLRlladrgidplkleqelpekraslrsliertrnsw 653
Cdd:COG0247 76 ALDaCVGCGFCR------AMCPSYKATGDEKDSPRGRINLLREVLE---------------------------------- 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522179794 654 haNKGEYDFSHEVKEAMSGCLACKACSTQCPIKIDVPEFRSRFLQLYHTRYLRPMRDHLVATVESYAPlmarapktfnff 733
Cdd:COG0247 116 --GELPLDLSEEVYEVLDLCLTCKACETACPSGVDIADLIAEARAQLVERGGRPLRDRLLRTFPDRVP------------ 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522179794 734 inqplvrklsekhigmvdlpllsvpslqrqlvghrsanmtleqlealSPEQKAKVVLVVQDPFTSYYDAQVVADFVRLAE 813
Cdd:COG0247 182 -----------------------------------------------AADKEGAEVLLFPGCFTNYFDPEIGKAAVRLLE 214
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522179794 814 KLGYQPVVLP-FSPNGKAQHIKGFLNRFAKTAQKTSDFLNRvagLGMP-MVGVDPALVLCYRDEYKQTLGDkRGAFHVML 891
Cdd:COG0247 215 AAGVEVVLPPeELCCGAPALSKGDLDLARKLARRNIEALER---LGVKaIVTTCPSCGLTLKDEYPELLGD-RVAFEVLD 290
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522179794 892 VHEWLPAALEQTS-AMEVSGEPWYLFGHCTEVTALpGAPAQWASIFARF-GAKLESV--SVGCCGMAGTYGHEVKNHANS 967
Cdd:COG0247 291 ISEFLAELILEGKlKLKPLGEKVTYHDPCHLGRGG-GVYDAPRELLKAIpGVEVVEMpeDSGCCGGAGGYGFEEPELSMR 369
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 522179794 968 LGiyeLSWHQAMQRLPRNRCLATGYSCRSQVKR-VEGNG--VRHPLQALLEIIG 1018
Cdd:COG0247 370 IG---ERKLEQIRATGADVVVTACPSCRTQLEDgTKEYGieVKHPVELLAEALG 420
|
|
| FAD-oxidase_C |
pfam02913 |
FAD linked oxidases, C-terminal domain; This domain has a ferredoxin-like fold. |
281-539 |
1.72e-73 |
|
FAD linked oxidases, C-terminal domain; This domain has a ferredoxin-like fold.
Pssm-ID: 397178 Cd Length: 248 Bit Score: 242.99 E-value: 1.72e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522179794 281 LPKVRRLVNVKYDSFDSALRNAPFMVEA--QALSVETVDSKVLNLAREDIVWHsvrelitDVPDKEMLGLNIVEFAGDDA 358
Cdd:pfam02913 1 LPEVRAVALVGFPSFEAAVKAVREIARAgiIPAALELMDNDALDLVEATLGFP-------KGLPRDAAALLLVEFEGDDE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522179794 359 ELIDSQVTTLCQRLdeliahGEGGVIGWQLCNDLAGIERIYAMRKKAVGLlGNAKGAAKPIPFAEDTCVPPEHLADYIVE 438
Cdd:pfam02913 74 ETAEEELEAVEAIL------EAGGAGDVVVATDEAEAERLWAARKYALPL-RDALGGAGPAVFSEDVSVPRSRLADLVRD 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522179794 439 FRALLDSHGLSYGMFGHVDAGVLHVRPALDMCDPQQEILMKQISDEVVALTAKYGGLLWGEHGKGF-RAEYSPAFFGEQL 517
Cdd:pfam02913 147 IKELLDKYGLVVCLFGHAGDGNLHLYILFDFRDPEQEERAEKLFDEIMDLALELGGSISGEHGVGRdKKPYLEREFGEEG 226
|
250 260
....*....|....*....|..
gi 522179794 518 FGELRKVKAAFDPNNRLNPGKI 539
Cdd:pfam02913 227 LALMRRIKAAFDPKGILNPGKV 248
|
|
| glcD |
TIGR00387 |
glycolate oxidase, subunit GlcD; This protein, the glycolate oxidase GlcD subunit, is similar ... |
55-538 |
1.38e-53 |
|
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: 193.07 E-value: 1.38e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522179794 55 VVFPRSTADVALIARLATQERfsaLVFTPRGGGTGTNGQAL--NQGIIIDMSRyMNRIIEINPEEGWVRVEAGVIKDQLN 132
Cdd:TIGR00387 1 VVFPKNTEQVARILKLCHEHR---IPIVPRGAGTGLSGGALpeEGGLVLVFKH-MNKILEIDVVNLTAVVQPGVRNLELE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522179794 133 QYLKPYGYFFAPELSTSNRATIGGMINTDASGQGSLVYGKTSDHVLGVRAVLLGGDILdtqpvpvelaETLGKentasgr 212
Cdd:TIGR00387 77 QAVEEHNLFYPPDPSSQISSTIGGNIAENAGGMRGLKYGTTVDYVLGLEVVTADGEIL----------RIGGK------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522179794 213 iyrTVLERcrdnrqlildkfpklnrflTGYDLrhvfndeltqfdlTRVLTGSEGTLAFITEARLDITRLPKVRRLVNVKY 292
Cdd:TIGR00387 140 ---TAKDV-------------------AGYDL-------------TGLFVGSEGTLGIVTEATLKLLPKPENIVVALAFF 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522179794 293 DSFDSALrNAPFMVEAQAL---SVETVDSKVLNlAREDIVwhsvrelITDVPdKEMLGLNIVEFAG--DDAELIDSQVTT 367
Cdd:TIGR00387 185 DSIEKAM-QAVYDIIAAGIipaGMEFLDNLSIK-AVEDIS-------GIGLP-KDAGAILLVEIDGvhEAVERDEEKIEQ 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522179794 368 LCQRldeliahgeGGVIGWQLCNDLAGIERIYAMRKKAVGLLGNAKgaakPIPFAEDTCVPPEHLADYIVEFRALLDSHG 447
Cdd:TIGR00387 255 ICRK---------NGAVDVQIAQDEEERALLWAGRRNAFKAASKLS----PLYLIEDGTVPRSKLPEALRGIADIASKYD 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522179794 448 LSYGMFGHVDAGVLHVRPALDMCDPQQEILMKQISDEVVALTAKYGGLLWGEHGKGF-RAEYSPAFFGEQLFGELRKVKA 526
Cdd:TIGR00387 322 FTIANFGHAGDGNLHPTILTDPEDKGEMERVEEAGGEIFELAIELGGTISGEHGIGVvKAEFMPYKFNEKELETMRAIKK 401
|
490
....*....|..
gi 522179794 527 AFDPNNRLNPGK 538
Cdd:TIGR00387 402 AFDPDNILNPGK 413
|
|
| PLN02805 |
PLN02805 |
D-lactate dehydrogenase [cytochrome] |
30-542 |
3.64e-41 |
|
D-lactate dehydrogenase [cytochrome]
Pssm-ID: 178402 [Multi-domain] Cd Length: 555 Bit Score: 160.17 E-value: 3.64e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522179794 30 DTATNYADRLTMAT-DNSIYQL--LPDAVVFPRSTADVALIARLATQERfsaLVFTPRGGGTGTNGQAL--NQGIIIDMS 104
Cdd:PLN02805 109 NMTLDYDERYFHGKpQNSFHKAvnIPDVVVFPRSEEEVSKIVKSCNKYK---VPIVPYGGATSIEGHTLapHGGVCIDMS 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522179794 105 rYMNRIIEINPEEGWVRVEAGVIKDQLNQYLKPYGYFFApeLSTSNRATIGGMINTDASGQGSLVYGKTSDHVLGVRAVL 184
Cdd:PLN02805 186 -LMKSVKALHVEDMDVVVEPGIGWLELNEYLEPYGLFFP--LDPGPGATIGGMCATRCSGSLAVRYGTMRDNVISLKVVL 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522179794 185 LGGDILdtqpvpvelaetlgkeNTASgriyrtvleRCRDNRqlildkfpklnrflTGYdlrhvfndeltqfDLTRVLTGS 264
Cdd:PLN02805 263 PNGDVV----------------KTAS---------RARKSA--------------AGY-------------DLTRLVIGS 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522179794 265 EGTLAFITEARLDITRLPK--VRRLVNVKY--DSFDSALrnAPFMVEAQALSVETVDS---KVLNLAREdivwhsvreli 337
Cdd:PLN02805 291 EGTLGVITEVTLRLQKIPQhsVVAMCNFPTikDAADVAI--ATMLSGIQVSRVELLDEvqiRAINMANG----------- 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522179794 338 TDVPDKEMLglnIVEFAGDDAELIDSqvTTLCQRldelIAHGEGGViGWQLCNDLAGIERIYAMRKKAVGllgnAKGAAK 417
Cdd:PLN02805 358 KNLPEAPTL---MFEFIGTEAYAREQ--TLIVQK----IASKHNGS-DFVFAEEPEAKKELWKIRKEALW----ACFAME 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522179794 418 PIPFA--EDTCVPPEHLADYIVEFRALLDSHGLSYGMFGHVDAGVLHvrpALDMCDPQQEILMKQ---ISDEVVALTAKY 492
Cdd:PLN02805 424 PKYEAmiTDVCVPLSHLAELISRSKKELDASPLVCTVIAHAGDGNFH---TIILFDPSQEDQRREaerLNHFMVHTALSM 500
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 522179794 493 GGLLWGEHGKGF-RAEYSPAFFGEQLFGELRKVKAAFDPNNRLNPGKICPP 542
Cdd:PLN02805 501 EGTCTGEHGVGTgKMKYLEKELGIEALQTMKRIKKALDPNNIMNPGKLIPP 551
|
|
| glpC |
PRK11168 |
anaerobic glycerol-3-phosphate dehydrogenase subunit C; |
664-1018 |
6.52e-15 |
|
anaerobic glycerol-3-phosphate dehydrogenase subunit C;
Pssm-ID: 236869 [Multi-domain] Cd Length: 396 Bit Score: 77.99 E-value: 6.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522179794 664 HEVKEAMSGCLACKACSTQCPIKIDVPEFRSRFLQLYHTRYLRPMRDHLVATVESYAPLMARAPKTFNFFINQPLVRKLS 743
Cdd:PRK11168 47 ALYDESLKYCSNCKRCEVACPSGVKIGDIIQRARAKYVTERGPPLRDRILSHTDLMGSLATPFAPLVNAATGLKPVRWLL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522179794 744 EKHIGM---VDLPLLSVPSLQRQLVGHrsanmtleqleALSPEQKAKVVLVVQDPFTSYYDAQVVADFVRLAEKLGYQPV 820
Cdd:PRK11168 127 EKTLGIdhrRPLPKYAFGTFRRWYRKQ-----------AAQQAQYKKQVAYFHGCYVNYNHPQLGKDLVKVLNAMGYEVL 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522179794 821 VLPFSPNGKAQHIKGFLNRFAKTAQKTSDFLNRVAGLGMPMVGVDPALVLCYRDEYKQTLG--DKRGAFHVMLVHEWLPA 898
Cdd:PRK11168 196 LPKEKCCGLPLIANGFLDKARKQAEFNVESLREAIEKGIPVIATSSSCTLTLRDEYPELLGvdNAGVRDHIEDATEFLRR 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522179794 899 ALEQTSAMEVSGEPWYLFGHctevtalpgAPAQ-----WA----SIFARF-GAKLESVSVGCCGMAGTYGHEVKNHANSL 968
Cdd:PRK11168 276 LLDQGKLLPLKPLPLKVAYH---------TPCHlekqgWGlytlELLRLIpGLEVVVLDSQCCGIAGTYGFKKEKYETSQ 346
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 522179794 969 GIYElSWHQAMQRLPRNRCLATGYSCRSQVKRVEGNGVRHPLQALLEIIG 1018
Cdd:PRK11168 347 AIGA-PLFRQIEESGADLVVTDCETCKWQIEMSTGLECEHPITLLAEALG 395
|
|
| Fer4_8 |
pfam13183 |
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ... |
578-687 |
4.36e-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: 4.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522179794 578 CNGNGLCfnfdvkSPMCPSMKITSNRIHSPKGRATLvrewlrlladrgidplkleqelpekraslrsliertrnswhANK 657
Cdd:pfam13183 2 CIRCGAC------LAACPVYLVTGGRFPGDPRGGAA-----------------------------------------ALL 34
|
90 100 110
....*....|....*....|....*....|
gi 522179794 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 |
3.03e-148 |
|
FAD/FMN-containing lactate dehydrogenase/glycolate oxidase [Energy production and conversion];
Pssm-ID: 440046 [Multi-domain] Cd Length: 462 Bit Score: 448.96 E-value: 3.03e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522179794 18 FLQALeQQGFTGDTATNYADRLTMATD-NSIYQLLPDAVVFPRSTADVALIARLATQERfsaLVFTPRGGGTGTNGQALN 96
Cdd:COG0277 6 LLAAL-RAILAGRVLTDPADRAAYARDgNSLYRGRPDAVVRPRSTEDVAAVVRLAAEHG---VPVVPRGGGTGLAGGAVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522179794 97 Q--GIIIDMSRyMNRIIEINPEEGWVRVEAGVIKDQLNQYLKPYGYFFAPELSTSNRATIGGMINTDASGQGSLVYGKTS 174
Cdd:COG0277 82 LdgGVVLDLSR-MNRILEVDPEDRTATVEAGVTLADLNAALAPHGLFFPPDPSSQGTATIGGNIATNAGGPRSLKYGLTR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522179794 175 DHVLGVRAVllggdildtqpvpvelaetlgkenTASGRIYRTVlercrdnrqlildkfPKLNRFLTGYDLRHVFndeltq 254
Cdd:COG0277 161 DNVLGLEVV------------------------LADGEVVRTG---------------GRVPKNVTGYDLFWLL------ 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522179794 255 fdltrvlTGSEGTLAFITEARLDITRLPKVRRLVNVKYDSFDSALRNAPFMVEAQAL--SVETVDSKVLNLAREdivwHS 332
Cdd:COG0277 196 -------VGSEGTLGVITEATLRLHPLPEAVATALVAFPDLEAAAAAVRALLAAGIApaALELMDRAALALVEA----AP 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522179794 333 VRELITDVPdkemlGLNIVEFAGDDAELIDSQVTTLCQRLDEliahgeGGVIGWQLCNDLAGIERIYAMRKKAVGLLGNA 412
Cdd:COG0277 265 PLGLPEDGG-----ALLLVEFDGDDAEEVEAQLARLRAILEA------GGATDVRVAADGAERERLWKARKAALPALGRL 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522179794 413 KGAAKpipFAEDTCVPPEHLADYIVEFRALLDSHGLSYGMFGHVDAGVLHVRPALDMCDPQQEILMKQISDEVVALTAKY 492
Cdd:COG0277 334 DGGAK---LLEDVAVPPSRLPELLRELGALAAKYGLRATAFGHAGDGNLHVRILFDPADPEEVERARAAAEEIFDLVAEL 410
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 522179794 493 GGLLWGEHGKG-FRAEYSPAFFGEQLFGELRKVKAAFDPNNRLNPGKICPPE 543
Cdd:COG0277 411 GGSISGEHGIGrLKAEFLPAEYGPAALALLRRIKAAFDPDGILNPGKILPPP 462
|
|
| GlpC |
COG0247 |
Fe-S cluster-containing oxidoreductase, includes glycolate oxidase subunit GlcF [Energy ... |
495-1018 |
1.11e-82 |
|
Fe-S cluster-containing oxidoreductase, includes glycolate oxidase subunit GlcF [Energy production and conversion];
Pssm-ID: 440017 [Multi-domain] Cd Length: 420 Bit Score: 274.26 E-value: 1.11e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522179794 495 LLWGEHGKGFRAEYSPAFFGEQLFGELRKVKAAFDPNNRLNPGKICPPEGVDAPMLQVDAvkrgtYDRQIPIAVRASWRG 574
Cdd:COG0247 1 LSGGHGGGLKAEHGTGRFMAPFLELELGKIKYAFDPDNKLNPGKIGLLNPGVELLGDGDL-----HDKNLKTLPWKELLD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522179794 575 ALE-CNGNGLCFnfdvksPMCPSMKITSNRIHSPKGRATLVREWLRlladrgidplkleqelpekraslrsliertrnsw 653
Cdd:COG0247 76 ALDaCVGCGFCR------AMCPSYKATGDEKDSPRGRINLLREVLE---------------------------------- 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522179794 654 haNKGEYDFSHEVKEAMSGCLACKACSTQCPIKIDVPEFRSRFLQLYHTRYLRPMRDHLVATVESYAPlmarapktfnff 733
Cdd:COG0247 116 --GELPLDLSEEVYEVLDLCLTCKACETACPSGVDIADLIAEARAQLVERGGRPLRDRLLRTFPDRVP------------ 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522179794 734 inqplvrklsekhigmvdlpllsvpslqrqlvghrsanmtleqlealSPEQKAKVVLVVQDPFTSYYDAQVVADFVRLAE 813
Cdd:COG0247 182 -----------------------------------------------AADKEGAEVLLFPGCFTNYFDPEIGKAAVRLLE 214
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522179794 814 KLGYQPVVLP-FSPNGKAQHIKGFLNRFAKTAQKTSDFLNRvagLGMP-MVGVDPALVLCYRDEYKQTLGDkRGAFHVML 891
Cdd:COG0247 215 AAGVEVVLPPeELCCGAPALSKGDLDLARKLARRNIEALER---LGVKaIVTTCPSCGLTLKDEYPELLGD-RVAFEVLD 290
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522179794 892 VHEWLPAALEQTS-AMEVSGEPWYLFGHCTEVTALpGAPAQWASIFARF-GAKLESV--SVGCCGMAGTYGHEVKNHANS 967
Cdd:COG0247 291 ISEFLAELILEGKlKLKPLGEKVTYHDPCHLGRGG-GVYDAPRELLKAIpGVEVVEMpeDSGCCGGAGGYGFEEPELSMR 369
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 522179794 968 LGiyeLSWHQAMQRLPRNRCLATGYSCRSQVKR-VEGNG--VRHPLQALLEIIG 1018
Cdd:COG0247 370 IG---ERKLEQIRATGADVVVTACPSCRTQLEDgTKEYGieVKHPVELLAEALG 420
|
|
| FAD-oxidase_C |
pfam02913 |
FAD linked oxidases, C-terminal domain; This domain has a ferredoxin-like fold. |
281-539 |
1.72e-73 |
|
FAD linked oxidases, C-terminal domain; This domain has a ferredoxin-like fold.
Pssm-ID: 397178 Cd Length: 248 Bit Score: 242.99 E-value: 1.72e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522179794 281 LPKVRRLVNVKYDSFDSALRNAPFMVEA--QALSVETVDSKVLNLAREDIVWHsvrelitDVPDKEMLGLNIVEFAGDDA 358
Cdd:pfam02913 1 LPEVRAVALVGFPSFEAAVKAVREIARAgiIPAALELMDNDALDLVEATLGFP-------KGLPRDAAALLLVEFEGDDE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522179794 359 ELIDSQVTTLCQRLdeliahGEGGVIGWQLCNDLAGIERIYAMRKKAVGLlGNAKGAAKPIPFAEDTCVPPEHLADYIVE 438
Cdd:pfam02913 74 ETAEEELEAVEAIL------EAGGAGDVVVATDEAEAERLWAARKYALPL-RDALGGAGPAVFSEDVSVPRSRLADLVRD 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522179794 439 FRALLDSHGLSYGMFGHVDAGVLHVRPALDMCDPQQEILMKQISDEVVALTAKYGGLLWGEHGKGF-RAEYSPAFFGEQL 517
Cdd:pfam02913 147 IKELLDKYGLVVCLFGHAGDGNLHLYILFDFRDPEQEERAEKLFDEIMDLALELGGSISGEHGVGRdKKPYLEREFGEEG 226
|
250 260
....*....|....*....|..
gi 522179794 518 FGELRKVKAAFDPNNRLNPGKI 539
Cdd:pfam02913 227 LALMRRIKAAFDPKGILNPGKV 248
|
|
| glcD |
TIGR00387 |
glycolate oxidase, subunit GlcD; This protein, the glycolate oxidase GlcD subunit, is similar ... |
55-538 |
1.38e-53 |
|
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: 193.07 E-value: 1.38e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522179794 55 VVFPRSTADVALIARLATQERfsaLVFTPRGGGTGTNGQAL--NQGIIIDMSRyMNRIIEINPEEGWVRVEAGVIKDQLN 132
Cdd:TIGR00387 1 VVFPKNTEQVARILKLCHEHR---IPIVPRGAGTGLSGGALpeEGGLVLVFKH-MNKILEIDVVNLTAVVQPGVRNLELE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522179794 133 QYLKPYGYFFAPELSTSNRATIGGMINTDASGQGSLVYGKTSDHVLGVRAVLLGGDILdtqpvpvelaETLGKentasgr 212
Cdd:TIGR00387 77 QAVEEHNLFYPPDPSSQISSTIGGNIAENAGGMRGLKYGTTVDYVLGLEVVTADGEIL----------RIGGK------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522179794 213 iyrTVLERcrdnrqlildkfpklnrflTGYDLrhvfndeltqfdlTRVLTGSEGTLAFITEARLDITRLPKVRRLVNVKY 292
Cdd:TIGR00387 140 ---TAKDV-------------------AGYDL-------------TGLFVGSEGTLGIVTEATLKLLPKPENIVVALAFF 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522179794 293 DSFDSALrNAPFMVEAQAL---SVETVDSKVLNlAREDIVwhsvrelITDVPdKEMLGLNIVEFAG--DDAELIDSQVTT 367
Cdd:TIGR00387 185 DSIEKAM-QAVYDIIAAGIipaGMEFLDNLSIK-AVEDIS-------GIGLP-KDAGAILLVEIDGvhEAVERDEEKIEQ 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522179794 368 LCQRldeliahgeGGVIGWQLCNDLAGIERIYAMRKKAVGLLGNAKgaakPIPFAEDTCVPPEHLADYIVEFRALLDSHG 447
Cdd:TIGR00387 255 ICRK---------NGAVDVQIAQDEEERALLWAGRRNAFKAASKLS----PLYLIEDGTVPRSKLPEALRGIADIASKYD 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522179794 448 LSYGMFGHVDAGVLHVRPALDMCDPQQEILMKQISDEVVALTAKYGGLLWGEHGKGF-RAEYSPAFFGEQLFGELRKVKA 526
Cdd:TIGR00387 322 FTIANFGHAGDGNLHPTILTDPEDKGEMERVEEAGGEIFELAIELGGTISGEHGIGVvKAEFMPYKFNEKELETMRAIKK 401
|
490
....*....|..
gi 522179794 527 AFDPNNRLNPGK 538
Cdd:TIGR00387 402 AFDPDNILNPGK 413
|
|
| FAD_binding_4 |
pfam01565 |
FAD binding domain; This family consists of various enzymes that use FAD as a co-factor, most ... |
52-192 |
1.15e-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: 155.05 E-value: 1.15e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522179794 52 PDAVVFPRSTADVALIARLATQERfsaLVFTPRGGGTGTNGQA-LNQGIIIDMSRyMNRIIEINPEEGWVRVEAGVIKDQ 130
Cdd:pfam01565 1 PAAVVLPESEEEVAAIVRLANENG---LPVLPRGGGSSLLGGAvQTGGIVLDLSR-LNGILEIDPEDGTATVEAGVTLGD 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 522179794 131 LNQYLKPYGYFFAPELSTSNRATIGGMINTDASGQGSLVYGKTSDHVLGVRAVLLGGDILDT 192
Cdd:pfam01565 77 LVRALAAKGLLLGLDPGSGIPGTVGGAIATNAGGYGSEKYGLTRDNVLGLEVVLADGEVVRL 138
|
|
| PLN02805 |
PLN02805 |
D-lactate dehydrogenase [cytochrome] |
30-542 |
3.64e-41 |
|
D-lactate dehydrogenase [cytochrome]
Pssm-ID: 178402 [Multi-domain] Cd Length: 555 Bit Score: 160.17 E-value: 3.64e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522179794 30 DTATNYADRLTMAT-DNSIYQL--LPDAVVFPRSTADVALIARLATQERfsaLVFTPRGGGTGTNGQAL--NQGIIIDMS 104
Cdd:PLN02805 109 NMTLDYDERYFHGKpQNSFHKAvnIPDVVVFPRSEEEVSKIVKSCNKYK---VPIVPYGGATSIEGHTLapHGGVCIDMS 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522179794 105 rYMNRIIEINPEEGWVRVEAGVIKDQLNQYLKPYGYFFApeLSTSNRATIGGMINTDASGQGSLVYGKTSDHVLGVRAVL 184
Cdd:PLN02805 186 -LMKSVKALHVEDMDVVVEPGIGWLELNEYLEPYGLFFP--LDPGPGATIGGMCATRCSGSLAVRYGTMRDNVISLKVVL 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522179794 185 LGGDILdtqpvpvelaetlgkeNTASgriyrtvleRCRDNRqlildkfpklnrflTGYdlrhvfndeltqfDLTRVLTGS 264
Cdd:PLN02805 263 PNGDVV----------------KTAS---------RARKSA--------------AGY-------------DLTRLVIGS 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522179794 265 EGTLAFITEARLDITRLPK--VRRLVNVKY--DSFDSALrnAPFMVEAQALSVETVDS---KVLNLAREdivwhsvreli 337
Cdd:PLN02805 291 EGTLGVITEVTLRLQKIPQhsVVAMCNFPTikDAADVAI--ATMLSGIQVSRVELLDEvqiRAINMANG----------- 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522179794 338 TDVPDKEMLglnIVEFAGDDAELIDSqvTTLCQRldelIAHGEGGViGWQLCNDLAGIERIYAMRKKAVGllgnAKGAAK 417
Cdd:PLN02805 358 KNLPEAPTL---MFEFIGTEAYAREQ--TLIVQK----IASKHNGS-DFVFAEEPEAKKELWKIRKEALW----ACFAME 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522179794 418 PIPFA--EDTCVPPEHLADYIVEFRALLDSHGLSYGMFGHVDAGVLHvrpALDMCDPQQEILMKQ---ISDEVVALTAKY 492
Cdd:PLN02805 424 PKYEAmiTDVCVPLSHLAELISRSKKELDASPLVCTVIAHAGDGNFH---TIILFDPSQEDQRREaerLNHFMVHTALSM 500
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 522179794 493 GGLLWGEHGKGF-RAEYSPAFFGEQLFGELRKVKAAFDPNNRLNPGKICPP 542
Cdd:PLN02805 501 EGTCTGEHGVGTgKMKYLEKELGIEALQTMKRIKKALDPNNIMNPGKLIPP 551
|
|
| PRK11230 |
PRK11230 |
glycolate oxidase subunit GlcD; Provisional |
46-541 |
1.93e-30 |
|
glycolate oxidase subunit GlcD; Provisional
Pssm-ID: 183043 [Multi-domain] Cd Length: 499 Bit Score: 126.82 E-value: 1.93e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522179794 46 SIYQLLPDAVVFPRSTADVALIARLATQERFSALVftpRGGGTGTNGQA--LNQGIIIDMSRYmNRIIEINPEEGWVRVE 123
Cdd:PRK11230 50 SAYRTRPLLVVLPKQMEQVQALLAVCHRLRVPVVA---RGAGTGLSGGAlpLEKGVLLVMARF-NRILDINPVGRRARVQ 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522179794 124 AGVIKDQLNQYLKPYGYFFAPELSTSNRATIGGMINTDASGQGSLVYGKTSDHVLGVRAVLLGGDILdtqpvpvelaeTL 203
Cdd:PRK11230 126 PGVRNLAISQAAAPHGLYYAPDPSSQIACSIGGNVAENAGGVHCLKYGLTVHNLLKVEILTLDGEAL-----------TL 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522179794 204 GKEntasgriyrtvlercrdnrqlILDKfpklnrfltgydlrhvfndelTQFDLTRVLTGSEGTLAFITEARLDITRLPK 283
Cdd:PRK11230 195 GSD---------------------ALDS---------------------PGFDLLALFTGSEGMLGVVTEVTVKLLPKPP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522179794 284 VRRLVNVKYDSFDSALRNAPFMVEAQAL--SVETVDSKVLNlAREDIVwHSVRELitdvpDKEMLGLniVEFAGDDAELI 361
Cdd:PRK11230 233 VARVLLASFDSVEKAGLAVGDIIAAGIIpgGLEMMDNLSIR-AAEDFI-HAGYPV-----DAEAILL--CELDGVESDVQ 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522179794 362 DSqvttlCQRLDELIAHgeGGVIGWQLCNDLAGIERIYAMRKKAVgllgNAKGAAKPIPFAEDTCVPPEHLADYIVEFRA 441
Cdd:PRK11230 304 ED-----CERVNDILLK--AGATDVRLAQDEAERVRFWAGRKNAF----PAVGRISPDYYCMDGTIPRRELPGVLEGIAR 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522179794 442 LLDSHGLSYGMFGHVDAGVLHVRPALDMCDPQQEILMKQISDEVVALTAKYGGLLWGEHGKGfRAEYSP--AFFGEQLFG 519
Cdd:PRK11230 373 LSQQYGLRVANVFHAGDGNMHPLILFDANEPGELERAEALGGKILELCVEVGGSITGEHGVG-REKINQmcAQFNSDEIT 451
|
490 500
....*....|....*....|..
gi 522179794 520 ELRKVKAAFDPNNRLNPGKICP 541
Cdd:PRK11230 452 LFHAVKAAFDPDGLLNPGKNIP 473
|
|
| glpC |
PRK11168 |
anaerobic glycerol-3-phosphate dehydrogenase subunit C; |
664-1018 |
6.52e-15 |
|
anaerobic glycerol-3-phosphate dehydrogenase subunit C;
Pssm-ID: 236869 [Multi-domain] Cd Length: 396 Bit Score: 77.99 E-value: 6.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522179794 664 HEVKEAMSGCLACKACSTQCPIKIDVPEFRSRFLQLYHTRYLRPMRDHLVATVESYAPLMARAPKTFNFFINQPLVRKLS 743
Cdd:PRK11168 47 ALYDESLKYCSNCKRCEVACPSGVKIGDIIQRARAKYVTERGPPLRDRILSHTDLMGSLATPFAPLVNAATGLKPVRWLL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522179794 744 EKHIGM---VDLPLLSVPSLQRQLVGHrsanmtleqleALSPEQKAKVVLVVQDPFTSYYDAQVVADFVRLAEKLGYQPV 820
Cdd:PRK11168 127 EKTLGIdhrRPLPKYAFGTFRRWYRKQ-----------AAQQAQYKKQVAYFHGCYVNYNHPQLGKDLVKVLNAMGYEVL 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522179794 821 VLPFSPNGKAQHIKGFLNRFAKTAQKTSDFLNRVAGLGMPMVGVDPALVLCYRDEYKQTLG--DKRGAFHVMLVHEWLPA 898
Cdd:PRK11168 196 LPKEKCCGLPLIANGFLDKARKQAEFNVESLREAIEKGIPVIATSSSCTLTLRDEYPELLGvdNAGVRDHIEDATEFLRR 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522179794 899 ALEQTSAMEVSGEPWYLFGHctevtalpgAPAQ-----WA----SIFARF-GAKLESVSVGCCGMAGTYGHEVKNHANSL 968
Cdd:PRK11168 276 LLDQGKLLPLKPLPLKVAYH---------TPCHlekqgWGlytlELLRLIpGLEVVVLDSQCCGIAGTYGFKKEKYETSQ 346
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 522179794 969 GIYElSWHQAMQRLPRNRCLATGYSCRSQVKRVEGNGVRHPLQALLEIIG 1018
Cdd:PRK11168 347 AIGA-PLFRQIEESGADLVVTDCETCKWQIEMSTGLECEHPITLLAEALG 395
|
|
| PLN02441 |
PLN02441 |
cytokinin dehydrogenase |
47-165 |
6.81e-06 |
|
cytokinin dehydrogenase
Pssm-ID: 215242 [Multi-domain] Cd Length: 525 Bit Score: 49.91 E-value: 6.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522179794 47 IYQLLPDAVVFPRSTADVALIARLAtQERFSALVFTPRGGGTGTNGQAL-NQGIIIDMS---RYMNRIIEINP--EEGWV 120
Cdd:PLN02441 60 LVHSLPAAVLYPSSVEDIASLVRAA-YGSSSPLTVAARGHGHSLNGQAQaPGGVVVDMRslrGGVRGPPVIVVsgDGPYV 138
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 522179794 121 RVEAGVI-KDQLNQYLKpYGyfFAPELSTSN-RATIGGMI-NTDASGQ 165
Cdd:PLN02441 139 DVSGGELwIDVLKATLK-HG--LAPRSWTDYlYLTVGGTLsNAGISGQ 183
|
|
| PLN02465 |
PLN02465 |
L-galactono-1,4-lactone dehydrogenase |
58-166 |
1.74e-05 |
|
L-galactono-1,4-lactone dehydrogenase
Pssm-ID: 215258 [Multi-domain] Cd Length: 573 Bit Score: 48.69 E-value: 1.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522179794 58 PRSTADVALIARLATQERfsaLVFTPRGGGTGTNGQALNQGIIIDMSrYMNRIIEINPEEGWVRVEAGVIKDQLNQYLKP 137
Cdd:PLN02465 103 PESLEELEDIVKEAHEKG---RRIRPVGSGLSPNGLAFSREGMVNLA-LMDKVLEVDKEKKRVTVQAGARVQQVVEALRP 178
|
90 100 110
....*....|....*....|....*....|....
gi 522179794 138 YGyffapeLSTSNRATI-----GGMINTDASGQG 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 |
3.06e-05 |
|
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: 47.59 E-value: 3.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522179794 47 IYQLLPDAVVFPRSTADVALIARLATQERFSALVFtprGGGTGTNGQALNQGIIIDMSRyMNRIIEINPEEGWVRVEAGV 126
Cdd:TIGR01678 10 TYSASPEVYYQPTSVEEVREVLALAREQKKKVKVV---GGGHSPSDIACTDGFLIHLDK-MNKVLQFDKEKKQITVEAGI 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 522179794 127 IKDQLNQYLKPYGYFFaPELSTSNRATIGGMINTDASGQgSLVYGKTSDHVLGVRAVLLGGDIL 190
Cdd:TIGR01678 86 RLYQLHEQLDEHGYSM-SNLGSISEVSVAGIISTGTHGS-SIKHGILATQVVALTIMTADGEVL 147
|
|
| Fer4_8 |
pfam13183 |
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ... |
578-687 |
4.36e-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: 4.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522179794 578 CNGNGLCfnfdvkSPMCPSMKITSNRIHSPKGRATLvrewlrlladrgidplkleqelpekraslrsliertrnswhANK 657
Cdd:pfam13183 2 CIRCGAC------LAACPVYLVTGGRFPGDPRGGAA-----------------------------------------ALL 34
|
90 100 110
....*....|....*....|....*....|
gi 522179794 658 GEYDFSHEVKEAMSGCLACKACSTQCPIKI 687
Cdd:pfam13183 35 GRLEALEGLAEGLWLCTLCGACTEVCPVGI 64
|
|
| GLDHase |
TIGR01676 |
galactonolactone dehydrogenase; This model represents L-Galactono-gamma-lactone dehydrogenase ... |
83-167 |
1.17e-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: 45.82 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522179794 83 PRGGGTGTNGQALNQGIIIDMSrYMNRIIEINPEEGWVRVEAGVIKDQLNQYLKPYGYFFApELSTSNRATIGGMINTDA 162
Cdd:TIGR01676 90 PVGSGLSPNGIGLSRAGMVNLA-LMDKVLEVDEEKKRVRVQAGIRVQQLVDAIKEYGITLQ-NFASIREQQIGGIIQVGA 167
|
....*
gi 522179794 163 SGQGS 167
Cdd:TIGR01676 168 HGTGA 172
|
|
| pln_FAD_oxido |
TIGR01677 |
plant-specific FAD-dependent oxidoreductase; This model represents an uncharacterized ... |
43-187 |
6.12e-04 |
|
plant-specific FAD-dependent oxidoreductase; This model represents an uncharacterized plant-specific family of FAD-dependent oxidoreductases. At least seven distinct members are found in Arabidopsis thaliana. The family shows considerable sequence similarity to three different enzymes of ascorbic acid biosynthesis: L-galactono-1,4-lactone dehydrogenase (EC 1.3.2.3) from higher plants, D-arabinono-1,4-lactone oxidase (EC 1.1.3.37 from Saccharomyces cerevisiae, and L-gulonolactone oxidase (EC 1.1.3.8) from mouse, as well as to a bacterial sorbitol oxidase. The class of compound acted on by members of this family is unknown.
Pssm-ID: 273750 [Multi-domain] Cd Length: 557 Bit Score: 43.70 E-value: 6.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522179794 43 TDNSIYQLLPD-------AVVFPRSTADVALIARLATQERFSALVFT------PR----GGGTGtngqalnqGIIIDMSR 105
Cdd:TIGR01677 16 TVSNAYGAFPDrstcraaNVAYPKTEAELVSVVAAATAAGRKMKVVTryshsiPKlacpDGSDG--------ALLISTKR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522179794 106 YmNRIIEINPEEGWVRVEAGVIKDQLNQYLKPYGyFFAPELSTSNRATIGGMINTDAsgQGSLVYGKTS---DHVLGVRA 182
Cdd:TIGR01677 88 L-NHVVAVDATAMTVTVESGMSLRELIVEAEKAG-LALPYAPYWWGLTVGGMMGTGA--HGSSLWGKGSavhDYVVGIRL 163
|
....*
gi 522179794 183 VLLGG 187
Cdd:TIGR01677 164 VVPAS 168
|
|
| PRK12831 |
PRK12831 |
putative oxidoreductase; Provisional |
643-692 |
6.20e-03 |
|
putative oxidoreductase; Provisional
Pssm-ID: 183780 [Multi-domain] Cd Length: 464 Bit Score: 40.39 E-value: 6.20e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 522179794 643 RSLIERTRNSWHANKGeYDFSHEVKEAmSGCLACK--ACSTQCPIKIDVPEF 692
Cdd:PRK12831 14 QDPEVRATNFEEVCLG-YNEEEAVKEA-SRCLQCKkpKCVKGCPVSINIPGF 63
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
629-692 |
9.38e-03 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 39.78 E-value: 9.38e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 522179794 629 LKLEQELPEKRaslrSLIERTRNsWHANKGEYDFSHEVKEAmSGCLACK--ACSTQCPIKIDVPEF 692
Cdd:PRK11749 4 LTTPRIPMPRQ----DAEERAQN-FDEVAPGYTPEEAIEEA-SRCLQCKdaPCVKACPVSIDIPEF 63
|
|
| |
