|
Name |
Accession |
Description |
Interval |
E-value |
| GlpC |
COG0247 |
Fe-S cluster-containing oxidoreductase, includes glycolate oxidase subunit GlcF [Energy ... |
420-865 |
9.93e-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: 283.12 E-value: 9.93e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502884468 420 LGENLVNEIWAYKQKIDPQGILNPGKIIPSSLDknspaktlskamsLANAGKGliglagkfmnKVQGDDFASPLSPQITN 499
Cdd:COG0247 19 MAPFLELELGKIKYAFDPDNKLNPGKIGLLNPG-------------VELLGDG----------DLHDKNLKTLPWKELLD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502884468 500 DTFACALCGYCRNTCTVFDAVPWESNSPRGKYYLLTQYIKGNIQ--LDEEVSKALFSCTTCAKCDKVCQIQAHNAHNWMS 577
Cdd:COG0247 76 ALDACVGCGFCRAMCPSYKATGDEKDSPRGRINLLREVLEGELPldLSEEVYEVLDLCLTCKACETACPSGVDIADLIAE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502884468 578 LRpcfhaNGLENTGLAGVRENVLKTGNFWgVPADQKfkwldvptlKKGKIAYWAGCWANIVMPNMPRNITRIFNKIGVEF 657
Cdd:COG0247 156 AR-----AQLVERGGRPLRDRLLRTFPDR-VPAADK---------EGAEVLLFPGCFTNYFDPEIGKAAVRLLEAAGVEV 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502884468 658 VhFGEGETCCGLYLALGGYMDDFTGLVKKNLEMFKEAGIETMVFSCPGCFATFSENYPAIaqqLGTECNIKFRHVTVFLS 737
Cdd:COG0247 221 V-LPPEELCCGAPALSKGDLDLARKLARRNIEALERLGVKAIVTTCPSCGLTLKDEYPEL---LGDRVAFEVLDISEFLA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502884468 738 ELINQGKLKFdRPVNCKVTYHDSCHVGRWFGHYEEPRSVIKAIPGVELVEMPhnrENALCCGLVSAFDSL-PTV-QHAGI 815
Cdd:COG0247 297 ELILEGKLKL-KPLGEKVTYHDPCHLGRGGGVYDAPRELLKAIPGVEVVEMP---EDSGCCGGAGGYGFEePELsMRIGE 372
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 502884468 816 KRVSEAEGTGADFLITNCAGCGSQFNATSCAMQTRVrqKDFTDLVAEALG 865
Cdd:COG0247 373 RKLEQIRATGADVVVTACPSCRTQLEDGTKEYGIEV--KHPVELLAEALG 420
|
|
| GlcD |
COG0277 |
FAD/FMN-containing lactate dehydrogenase/glycolate oxidase [Energy production and conversion]; |
6-448 |
7.07e-83 |
|
FAD/FMN-containing lactate dehydrogenase/glycolate oxidase [Energy production and conversion];
Pssm-ID: 440046 [Multi-domain] Cd Length: 462 Bit Score: 274.08 E-value: 7.07e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502884468 6 LPVALKKKLEELFGDRVRFNKVERLVYSHDMGvlpsqvmKLIDTMPDAVAQPVSEEEVIAATNLAREFSWPLIPRGSGTS 85
Cdd:COG0277 2 LTAALLAALRAILAGRVLTDPADRAAYARDGN-------SLYRGRPDAVVRPRSTEDVAAVVRLAAEHGVPVVPRGGGTG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502884468 86 GFGGALPTRGGIVLDFVRMNRIIAVDEHNLTVTVEPGVVWGDLQEYLQAKGFDLRLYPSSTPSATVAGWVAQGGSGYGSF 165
Cdd:COG0277 75 LAGGAVPLDGGVVLDLSRMNRILEVDPEDRTATVEAGVTLADLNAALAPHGLFFPPDPSSQGTATIGGNIATNAGGPRSL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502884468 166 EYGFCGENIVSVDVVTTEG--------ITRSYAGEELK--FVNGLcGITGIITKVTVKIKEKDEDV-VVLAAFDKLNDAA 234
Cdd:COG0277 155 KYGLTRDNVLGLEVVLADGevvrtggrVPKNVTGYDLFwlLVGSE-GTLGVITEATLRLHPLPEAVaTALVAFPDLEAAA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502884468 235 EALRMIRQQAVPLWSATMSTPAYIRLkQKASQHIVLPED-RYFLLFVYPKTRRTAVEMALKGIIASCHGELMREAL---- 309
Cdd:COG0277 234 AAVRALLAAGIAPAALELMDRAALAL-VEAAPPLGLPEDgGALLLVEFDGDDAEEVEAQLARLRAILEAGGATDVRvaad 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502884468 310 ---AREEWNERFY-PMRFKKLGPTL-IATEVIVPIDRLSEFVSEVERKYKgEFALEGTM--------IHndkisiLGFML 376
Cdd:COG0277 313 gaeRERLWKARKAaLPALGRLDGGAkLLEDVAVPPSRLPELLRELGALAA-KYGLRATAfghagdgnLH------VRILF 385
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502884468 377 SDERKAGFPLAYTNSLTVIEIGEKLGGRV---FTLGLYFADKAKDVLGENLVNEIWAYKQKIDPQGILNPGKIIP 448
Cdd:COG0277 386 DPADPEEVERARAAAEEIFDLVAELGGSIsgeHGIGRLKAEFLPAEYGPAALALLRRIKAAFDPDGILNPGKILP 460
|
|
| FAD_binding_4 |
pfam01565 |
FAD binding domain; This family consists of various enzymes that use FAD as a co-factor, most ... |
51-184 |
8.04e-46 |
|
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: 160.83 E-value: 8.04e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502884468 51 PDAVAQPVSEEEVIAATNLAREFSWPLIPRGSGTSGFGGALPTrGGIVLDFVRMNRIIAVDEHNLTVTVEPGVVWGDLQE 130
Cdd:pfam01565 1 PAAVVLPESEEEVAAIVRLANENGLPVLPRGGGSSLLGGAVQT-GGIVLDLSRLNGILEIDPEDGTATVEAGVTLGDLVR 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 502884468 131 YLQAKGFDLRLYPSSTPSATVAGWVAQGGSGYGSFEYGFCGENIVSVDVVTTEG 184
Cdd:pfam01565 80 ALAAKGLLLGLDPGSGIPGTVGGAIATNAGGYGSEKYGLTRDNVLGLEVVLADG 133
|
|
| PRK06259 |
PRK06259 |
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Provisional |
544-841 |
3.69e-38 |
|
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Provisional
Pssm-ID: 235756 [Multi-domain] Cd Length: 486 Bit Score: 149.39 E-value: 3.69e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502884468 544 LDEEVSKALFSCTTCAKCDKVCQIQAHNAHNWM-SLRPCFHANGLentGLAG---VRENVLKTGNfwGVPADQKfkwldv 619
Cdd:PRK06259 176 EKEAFDEGLYNCTTCGKCVEVCPKEIDIPGKAIeKLRALAFKKGL---GLPAhleVRENVLKTGR--SVPKEKP------ 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502884468 620 PTLK-----------KGKIAYWAGCWANIVMPNMPRNITRIFNKIGVEfVHFGEGETCCGLYLALGGYMDDFTGLVKKNL 688
Cdd:PRK06259 245 SFLEevsdiypygneKLRVAFFTGCLVDYRLQEVGKDAIRVLNAHGIS-VIIPKNQVCCGSPLIRTGQTDVAEELKKKNL 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502884468 689 EMFKEAGIETMVFSCPGCFATFSENYPaiaqqlgtECNIKFRHVTVFLSELinqGKLKFdRPVNCKVTYHDSCHVGRWFG 768
Cdd:PRK06259 324 EIFNKLDVDTVVTICAGCGSTLKNDYK--------EKEFNVMDITEVLVEV---GLEKY-KPLDITVTYHDPCHLRRGQG 391
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502884468 769 HYEEPRSVIKAIPGVELVEMphnRENALCCGLVSAFDS-LPTVQHA-GIKRVSEAEGTGADFLITNCAGCgsQFN 841
Cdd:PRK06259 392 IYEEPRKILRSIPGLEFVEM---EIPDQCCGAGGGVRSgKPEIAEAlGKRKAEMIRETGADYVITVCPFC--EYH 461
|
|
| PLN02805 |
PLN02805 |
D-lactate dehydrogenase [cytochrome] |
3-448 |
6.52e-29 |
|
D-lactate dehydrogenase [cytochrome]
Pssm-ID: 178402 [Multi-domain] Cd Length: 555 Bit Score: 122.42 E-value: 6.52e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502884468 3 QKELPVALKKKLEELFGDRVRFNKVERlvYSHdmGVLPSQVMKLIDtMPDAVAQPVSEEEVIAATNLAREFSWPLIPRGS 82
Cdd:PLN02805 91 HKLVPQELIDELKAILQDNMTLDYDER--YFH--GKPQNSFHKAVN-IPDVVVFPRSEEEVSKIVKSCNKYKVPIVPYGG 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502884468 83 GTSGFGGALPTRGGIVLDFVRMNRIIAVDEHNLTVTVEPGVVWGDLQEYLQAKGFDLRLYPSstPSATVAGWVAQGGSGY 162
Cdd:PLN02805 166 ATSIEGHTLAPHGGVCIDMSLMKSVKALHVEDMDVVVEPGIGWLELNEYLEPYGLFFPLDPG--PGATIGGMCATRCSGS 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502884468 163 GSFEYGFCGENIVSV-------DVVTTEGITR-SYAGEEL-KFVNGLCGITGIITKVTVKI-KEKDEDVVVLAAFDKLND 232
Cdd:PLN02805 244 LAVRYGTMRDNVISLkvvlpngDVVKTASRARkSAAGYDLtRLVIGSEGTLGVITEVTLRLqKIPQHSVVAMCNFPTIKD 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502884468 233 AAEALRMIRQQAVPLWSATMSTPAYIRLKQKASQHiVLPEDRYfLLFVYPKTRRTAVEMAL--KGIIASCHGE---LMRE 307
Cdd:PLN02805 324 AADVAIATMLSGIQVSRVELLDEVQIRAINMANGK-NLPEAPT-LMFEFIGTEAYAREQTLivQKIASKHNGSdfvFAEE 401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502884468 308 ALAREE-W---NERFYPMRFKKLGPTLIATEVIVPIDRLSEFVSEVERKYKGEFALEGTMIHNDKISILGFMLSD----- 378
Cdd:PLN02805 402 PEAKKElWkirKEALWACFAMEPKYEAMITDVCVPLSHLAELISRSKKELDASPLVCTVIAHAGDGNFHTIILFDpsqed 481
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502884468 379 -----ERKAGFPLAYTNSLTVIEIGEKLGGrvfTLGLYFADKAkdvLGENLVNEIWAYKQKIDPQGILNPGKIIP 448
Cdd:PLN02805 482 qrreaERLNHFMVHTALSMEGTCTGEHGVG---TGKMKYLEKE---LGIEALQTMKRIKKALDPNNIMNPGKLIP 550
|
|
| CCG |
pfam02754 |
Cysteine-rich domain; The key element of this family is the CX31-38CCX33-34CXXC sequence motif ... |
755-840 |
8.21e-18 |
|
Cysteine-rich domain; The key element of this family is the CX31-38CCX33-34CXXC sequence motif normally found at the C-terminus in archaeal and bacterial Hdr-like proteins. There may be one or two copies, and the motif is probably an iron-sulfur binding cluster. In some instances one of the cysteines is replaced by an aspartate, and aspartate can in principle also function as a ligand of an iron-sulfur cluster. The family includes a subunit from heterodisulphide reductase and a subunit from glycolate oxidase and glycerol-3-phosphate dehydrogenase.
Pssm-ID: 397052 [Multi-domain] Cd Length: 84 Bit Score: 78.89 E-value: 8.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502884468 755 VTYHDSCHVGRwfGHYEEPRSVIKAIPGVELVEMPHNrENALCCG---LVSAFDslPTVQHAGIKRVSEAEGTGADFLIT 831
Cdd:pfam02754 1 VAYFDGCHLGR--ALYPEPRKALKKVLGALGVEVVIL-EKQSCCGaggGFSGKE--DVAEALAKRNIDTAEETGADAIVT 75
|
....*....
gi 502884468 832 NCAGCGSQF 840
Cdd:pfam02754 76 ACPGCLLQL 84
|
|
| FAD_lactone_ox |
TIGR01678 |
sugar 1,4-lactone oxidases; This model represents a family of at least two different sugar 1,4 ... |
51-241 |
7.75e-11 |
|
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: 65.30 E-value: 7.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502884468 51 PDAVAQPVSEEEVIAATNLAREFSWPLIPRGSGTSGfgGALPTRGGIVLDFVRMNRIIAVDEHNLTVTVEPGVVWGDLQE 130
Cdd:TIGR01678 15 PEVYYQPTSVEEVREVLALAREQKKKVKVVGGGHSP--SDIACTDGFLIHLDKMNKVLQFDKEKKQITVEAGIRLYQLHE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502884468 131 YLQAKGFDLRLYpSSTPSATVAGWVAQGGSGyGSFEYGFCGENIVSVDVVTTEG----ITRSYAGEELKFVNGLCGITGI 206
Cdd:TIGR01678 93 QLDEHGYSMSNL-GSISEVSVAGIISTGTHG-SSIKHGILATQVVALTIMTADGevleCSEERNADVFQAARVSLGCLGI 170
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 502884468 207 ITKVTVK------IKEKDEDVVVLAAFDKLNDAAEALRMIR 241
Cdd:TIGR01678 171 IVTVTIQvvpqfhLQETSFVSTLKELLDNWDSHWKSSEFFR 211
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| GlpC |
COG0247 |
Fe-S cluster-containing oxidoreductase, includes glycolate oxidase subunit GlcF [Energy ... |
420-865 |
9.93e-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: 283.12 E-value: 9.93e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502884468 420 LGENLVNEIWAYKQKIDPQGILNPGKIIPSSLDknspaktlskamsLANAGKGliglagkfmnKVQGDDFASPLSPQITN 499
Cdd:COG0247 19 MAPFLELELGKIKYAFDPDNKLNPGKIGLLNPG-------------VELLGDG----------DLHDKNLKTLPWKELLD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502884468 500 DTFACALCGYCRNTCTVFDAVPWESNSPRGKYYLLTQYIKGNIQ--LDEEVSKALFSCTTCAKCDKVCQIQAHNAHNWMS 577
Cdd:COG0247 76 ALDACVGCGFCRAMCPSYKATGDEKDSPRGRINLLREVLEGELPldLSEEVYEVLDLCLTCKACETACPSGVDIADLIAE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502884468 578 LRpcfhaNGLENTGLAGVRENVLKTGNFWgVPADQKfkwldvptlKKGKIAYWAGCWANIVMPNMPRNITRIFNKIGVEF 657
Cdd:COG0247 156 AR-----AQLVERGGRPLRDRLLRTFPDR-VPAADK---------EGAEVLLFPGCFTNYFDPEIGKAAVRLLEAAGVEV 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502884468 658 VhFGEGETCCGLYLALGGYMDDFTGLVKKNLEMFKEAGIETMVFSCPGCFATFSENYPAIaqqLGTECNIKFRHVTVFLS 737
Cdd:COG0247 221 V-LPPEELCCGAPALSKGDLDLARKLARRNIEALERLGVKAIVTTCPSCGLTLKDEYPEL---LGDRVAFEVLDISEFLA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502884468 738 ELINQGKLKFdRPVNCKVTYHDSCHVGRWFGHYEEPRSVIKAIPGVELVEMPhnrENALCCGLVSAFDSL-PTV-QHAGI 815
Cdd:COG0247 297 ELILEGKLKL-KPLGEKVTYHDPCHLGRGGGVYDAPRELLKAIPGVEVVEMP---EDSGCCGGAGGYGFEePELsMRIGE 372
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 502884468 816 KRVSEAEGTGADFLITNCAGCGSQFNATSCAMQTRVrqKDFTDLVAEALG 865
Cdd:COG0247 373 RKLEQIRATGADVVVTACPSCRTQLEDGTKEYGIEV--KHPVELLAEALG 420
|
|
| GlcD |
COG0277 |
FAD/FMN-containing lactate dehydrogenase/glycolate oxidase [Energy production and conversion]; |
6-448 |
7.07e-83 |
|
FAD/FMN-containing lactate dehydrogenase/glycolate oxidase [Energy production and conversion];
Pssm-ID: 440046 [Multi-domain] Cd Length: 462 Bit Score: 274.08 E-value: 7.07e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502884468 6 LPVALKKKLEELFGDRVRFNKVERLVYSHDMGvlpsqvmKLIDTMPDAVAQPVSEEEVIAATNLAREFSWPLIPRGSGTS 85
Cdd:COG0277 2 LTAALLAALRAILAGRVLTDPADRAAYARDGN-------SLYRGRPDAVVRPRSTEDVAAVVRLAAEHGVPVVPRGGGTG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502884468 86 GFGGALPTRGGIVLDFVRMNRIIAVDEHNLTVTVEPGVVWGDLQEYLQAKGFDLRLYPSSTPSATVAGWVAQGGSGYGSF 165
Cdd:COG0277 75 LAGGAVPLDGGVVLDLSRMNRILEVDPEDRTATVEAGVTLADLNAALAPHGLFFPPDPSSQGTATIGGNIATNAGGPRSL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502884468 166 EYGFCGENIVSVDVVTTEG--------ITRSYAGEELK--FVNGLcGITGIITKVTVKIKEKDEDV-VVLAAFDKLNDAA 234
Cdd:COG0277 155 KYGLTRDNVLGLEVVLADGevvrtggrVPKNVTGYDLFwlLVGSE-GTLGVITEATLRLHPLPEAVaTALVAFPDLEAAA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502884468 235 EALRMIRQQAVPLWSATMSTPAYIRLkQKASQHIVLPED-RYFLLFVYPKTRRTAVEMALKGIIASCHGELMREAL---- 309
Cdd:COG0277 234 AAVRALLAAGIAPAALELMDRAALAL-VEAAPPLGLPEDgGALLLVEFDGDDAEEVEAQLARLRAILEAGGATDVRvaad 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502884468 310 ---AREEWNERFY-PMRFKKLGPTL-IATEVIVPIDRLSEFVSEVERKYKgEFALEGTM--------IHndkisiLGFML 376
Cdd:COG0277 313 gaeRERLWKARKAaLPALGRLDGGAkLLEDVAVPPSRLPELLRELGALAA-KYGLRATAfghagdgnLH------VRILF 385
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502884468 377 SDERKAGFPLAYTNSLTVIEIGEKLGGRV---FTLGLYFADKAKDVLGENLVNEIWAYKQKIDPQGILNPGKIIP 448
Cdd:COG0277 386 DPADPEEVERARAAAEEIFDLVAELGGSIsgeHGIGRLKAEFLPAEYGPAALALLRRIKAAFDPDGILNPGKILP 460
|
|
| FAD_binding_4 |
pfam01565 |
FAD binding domain; This family consists of various enzymes that use FAD as a co-factor, most ... |
51-184 |
8.04e-46 |
|
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: 160.83 E-value: 8.04e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502884468 51 PDAVAQPVSEEEVIAATNLAREFSWPLIPRGSGTSGFGGALPTrGGIVLDFVRMNRIIAVDEHNLTVTVEPGVVWGDLQE 130
Cdd:pfam01565 1 PAAVVLPESEEEVAAIVRLANENGLPVLPRGGGSSLLGGAVQT-GGIVLDLSRLNGILEIDPEDGTATVEAGVTLGDLVR 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 502884468 131 YLQAKGFDLRLYPSSTPSATVAGWVAQGGSGYGSFEYGFCGENIVSVDVVTTEG 184
Cdd:pfam01565 80 ALAAKGLLLGLDPGSGIPGTVGGAIATNAGGYGSEKYGLTRDNVLGLEVVLADG 133
|
|
| PRK06259 |
PRK06259 |
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Provisional |
544-841 |
3.69e-38 |
|
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Provisional
Pssm-ID: 235756 [Multi-domain] Cd Length: 486 Bit Score: 149.39 E-value: 3.69e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502884468 544 LDEEVSKALFSCTTCAKCDKVCQIQAHNAHNWM-SLRPCFHANGLentGLAG---VRENVLKTGNfwGVPADQKfkwldv 619
Cdd:PRK06259 176 EKEAFDEGLYNCTTCGKCVEVCPKEIDIPGKAIeKLRALAFKKGL---GLPAhleVRENVLKTGR--SVPKEKP------ 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502884468 620 PTLK-----------KGKIAYWAGCWANIVMPNMPRNITRIFNKIGVEfVHFGEGETCCGLYLALGGYMDDFTGLVKKNL 688
Cdd:PRK06259 245 SFLEevsdiypygneKLRVAFFTGCLVDYRLQEVGKDAIRVLNAHGIS-VIIPKNQVCCGSPLIRTGQTDVAEELKKKNL 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502884468 689 EMFKEAGIETMVFSCPGCFATFSENYPaiaqqlgtECNIKFRHVTVFLSELinqGKLKFdRPVNCKVTYHDSCHVGRWFG 768
Cdd:PRK06259 324 EIFNKLDVDTVVTICAGCGSTLKNDYK--------EKEFNVMDITEVLVEV---GLEKY-KPLDITVTYHDPCHLRRGQG 391
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502884468 769 HYEEPRSVIKAIPGVELVEMphnRENALCCGLVSAFDS-LPTVQHA-GIKRVSEAEGTGADFLITNCAGCgsQFN 841
Cdd:PRK06259 392 IYEEPRKILRSIPGLEFVEM---EIPDQCCGAGGGVRSgKPEIAEAlGKRKAEMIRETGADYVITVCPFC--EYH 461
|
|
| PLN02805 |
PLN02805 |
D-lactate dehydrogenase [cytochrome] |
3-448 |
6.52e-29 |
|
D-lactate dehydrogenase [cytochrome]
Pssm-ID: 178402 [Multi-domain] Cd Length: 555 Bit Score: 122.42 E-value: 6.52e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502884468 3 QKELPVALKKKLEELFGDRVRFNKVERlvYSHdmGVLPSQVMKLIDtMPDAVAQPVSEEEVIAATNLAREFSWPLIPRGS 82
Cdd:PLN02805 91 HKLVPQELIDELKAILQDNMTLDYDER--YFH--GKPQNSFHKAVN-IPDVVVFPRSEEEVSKIVKSCNKYKVPIVPYGG 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502884468 83 GTSGFGGALPTRGGIVLDFVRMNRIIAVDEHNLTVTVEPGVVWGDLQEYLQAKGFDLRLYPSstPSATVAGWVAQGGSGY 162
Cdd:PLN02805 166 ATSIEGHTLAPHGGVCIDMSLMKSVKALHVEDMDVVVEPGIGWLELNEYLEPYGLFFPLDPG--PGATIGGMCATRCSGS 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502884468 163 GSFEYGFCGENIVSV-------DVVTTEGITR-SYAGEEL-KFVNGLCGITGIITKVTVKI-KEKDEDVVVLAAFDKLND 232
Cdd:PLN02805 244 LAVRYGTMRDNVISLkvvlpngDVVKTASRARkSAAGYDLtRLVIGSEGTLGVITEVTLRLqKIPQHSVVAMCNFPTIKD 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502884468 233 AAEALRMIRQQAVPLWSATMSTPAYIRLKQKASQHiVLPEDRYfLLFVYPKTRRTAVEMAL--KGIIASCHGE---LMRE 307
Cdd:PLN02805 324 AADVAIATMLSGIQVSRVELLDEVQIRAINMANGK-NLPEAPT-LMFEFIGTEAYAREQTLivQKIASKHNGSdfvFAEE 401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502884468 308 ALAREE-W---NERFYPMRFKKLGPTLIATEVIVPIDRLSEFVSEVERKYKGEFALEGTMIHNDKISILGFMLSD----- 378
Cdd:PLN02805 402 PEAKKElWkirKEALWACFAMEPKYEAMITDVCVPLSHLAELISRSKKELDASPLVCTVIAHAGDGNFHTIILFDpsqed 481
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502884468 379 -----ERKAGFPLAYTNSLTVIEIGEKLGGrvfTLGLYFADKAkdvLGENLVNEIWAYKQKIDPQGILNPGKIIP 448
Cdd:PLN02805 482 qrreaERLNHFMVHTALSMEGTCTGEHGVG---TGKMKYLEKE---LGIEALQTMKRIKKALDPNNIMNPGKLIP 550
|
|
| PRK11230 |
PRK11230 |
glycolate oxidase subunit GlcD; Provisional |
49-449 |
1.04e-21 |
|
glycolate oxidase subunit GlcD; Provisional
Pssm-ID: 183043 [Multi-domain] Cd Length: 499 Bit Score: 99.85 E-value: 1.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502884468 49 TMPDAVAQPVSEEEVIAATNLAREFSWPLIPRGSGTSGFGGALPTRGGIVLDFVRMNRIIAVDEHNLTVTVEPGVvwGDL 128
Cdd:PRK11230 54 TRPLLVVLPKQMEQVQALLAVCHRLRVPVVARGAGTGLSGGALPLEKGVLLVMARFNRILDINPVGRRARVQPGV--RNL 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502884468 129 QEYLQAKGFDLrLY---PSSTPSATVAGWVAQGGSGYGSFEYGFCGENIVSVDVVTTEGITRSYAGEELK--------FV 197
Cdd:PRK11230 132 AISQAAAPHGL-YYapdPSSQIACSIGGNVAENAGGVHCLKYGLTVHNLLKVEILTLDGEALTLGSDALDspgfdllaLF 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502884468 198 NGLCGITGIITKVTVKIKEKDEDV-VVLAAFDKLNDAAEAL-RMIRQQAVPLWSATMSTPAyirlkqkasqhIVLPEDry 275
Cdd:PRK11230 211 TGSEGMLGVVTEVTVKLLPKPPVArVLLASFDSVEKAGLAVgDIIAAGIIPGGLEMMDNLS-----------IRAAED-- 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502884468 276 FLLFVYPKTRRTAVEMALKGIIASCH------GELMREA------LAREEWNE-RFYPMR---FKKLG---PTLIATEVI 336
Cdd:PRK11230 278 FIHAGYPVDAEAILLCELDGVESDVQedcervNDILLKAgatdvrLAQDEAERvRFWAGRknaFPAVGrisPDYYCMDGT 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502884468 337 VP---IDRLSEFVSEVERKYKGEFAlegTMIHNDKISILGFMLSDERKAGfplaytnsltVIEIGEKLGGRVFTLGLyfa 413
Cdd:PRK11230 358 IPrreLPGVLEGIARLSQQYGLRVA---NVFHAGDGNMHPLILFDANEPG----------ELERAEALGGKILELCV--- 421
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 502884468 414 DKAKDVLGENLV--------------NEI---WAYKQKIDPQGILNPGKIIPS 449
Cdd:PRK11230 422 EVGGSITGEHGVgrekinqmcaqfnsDEItlfHAVKAAFDPDGLLNPGKNIPT 474
|
|
| glpC |
PRK11168 |
anaerobic glycerol-3-phosphate dehydrogenase subunit C; |
545-865 |
5.22e-20 |
|
anaerobic glycerol-3-phosphate dehydrogenase subunit C;
Pssm-ID: 236869 [Multi-domain] Cd Length: 396 Bit Score: 93.40 E-value: 5.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502884468 545 DEEVSKALFSCTTCAKCDKVC-------QIQA-----HNAHNWMSLRPCFHAN------------GLEN--TGLAGVR-- 596
Cdd:PRK11168 46 GALYDESLKYCSNCKRCEVACpsgvkigDIIQrarakYVTERGPPLRDRILSHtdlmgslatpfaPLVNaaTGLKPVRwl 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502884468 597 -ENVLK-----------TGNF--W--GVPADQKfkwldvptLKKGKIAYWAGCWANIVMPNMPRNITRIFNKIGVEFVHf 660
Cdd:PRK11168 126 lEKTLGidhrrplpkyaFGTFrrWyrKQAAQQA--------QYKKQVAYFHGCYVNYNHPQLGKDLVKVLNAMGYEVLL- 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502884468 661 gEGETCCGLYLALGGYMDDFTGLVKKNLEMFKEA---GIeTMVFSCPGCFATFSENYPAIaqqLGTEcNIKFRH----VT 733
Cdd:PRK11168 197 -PKEKCCGLPLIANGFLDKARKQAEFNVESLREAiekGI-PVIATSSSCTLTLRDEYPEL---LGVD-NAGVRDhiedAT 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502884468 734 VFLSELINQGKLKFDRPVNCKVTYHDSCHVGR--WfGHYEepRSVIKAIPGVELVEMPhnrenALCCGLVSAFdslptvq 811
Cdd:PRK11168 271 EFLRRLLDQGKLLPLKPLPLKVAYHTPCHLEKqgW-GLYT--LELLRLIPGLEVVVLD-----SQCCGIAGTY------- 335
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502884468 812 haGIKR----VSEAEG---------TGADFLITNCAGCGSQFNatscaMQTRVRQKDFTDLVAEALG 865
Cdd:PRK11168 336 --GFKKekyeTSQAIGaplfrqieeSGADLVVTDCETCKWQIE-----MSTGLECEHPITLLAEALG 395
|
|
| CCG |
pfam02754 |
Cysteine-rich domain; The key element of this family is the CX31-38CCX33-34CXXC sequence motif ... |
755-840 |
8.21e-18 |
|
Cysteine-rich domain; The key element of this family is the CX31-38CCX33-34CXXC sequence motif normally found at the C-terminus in archaeal and bacterial Hdr-like proteins. There may be one or two copies, and the motif is probably an iron-sulfur binding cluster. In some instances one of the cysteines is replaced by an aspartate, and aspartate can in principle also function as a ligand of an iron-sulfur cluster. The family includes a subunit from heterodisulphide reductase and a subunit from glycolate oxidase and glycerol-3-phosphate dehydrogenase.
Pssm-ID: 397052 [Multi-domain] Cd Length: 84 Bit Score: 78.89 E-value: 8.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502884468 755 VTYHDSCHVGRwfGHYEEPRSVIKAIPGVELVEMPHNrENALCCG---LVSAFDslPTVQHAGIKRVSEAEGTGADFLIT 831
Cdd:pfam02754 1 VAYFDGCHLGR--ALYPEPRKALKKVLGALGVEVVIL-EKQSCCGaggGFSGKE--DVAEALAKRNIDTAEETGADAIVT 75
|
....*....
gi 502884468 832 NCAGCGSQF 840
Cdd:pfam02754 76 ACPGCLLQL 84
|
|
| HdrB |
COG2048 |
Heterodisulfide reductase, subunit B [Energy production and conversion]; |
626-870 |
2.04e-14 |
|
Heterodisulfide reductase, subunit B [Energy production and conversion];
Pssm-ID: 441651 [Multi-domain] Cd Length: 285 Bit Score: 74.47 E-value: 2.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502884468 626 KIAYWAGCwaniVMPNMPRNI---TR-IFNKIGVEFVHFgEGETCCGlylalGGYMDDF-----TGLVKKNLEMFKEAGI 696
Cdd:COG2048 2 KYAYYPGC----SLPGTAPEYeksTRaVAKALGIELVEL-PDWNCCG-----ASSAHSVdellwLALAARNLALAEKMGL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502884468 697 ETMVfSCPGCFATFSE------NYPAIAQQ----LGTE-----CNIKFRHVTVFLSELINQGKLK--FDRPVNC-KV-TY 757
Cdd:COG2048 72 DIVT-PCNACYGSLKEanhelkEDPELREKvneiLAEAgleykGTVKVRHLLEVLYEDVGLEKIKekVKKPLKGlKVaPY 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502884468 758 HdSCHVGR-----WFGHYEEPRS---VIKAIpGVELVEMPHNREnalCCGLVSAFDSLPTVQHAGIKRVSEAEGTGADFL 829
Cdd:COG2048 151 Y-GCHLLRpseiaGFDDPENPTSldeLVEAL-GAEPVDYPYKTE---CCGASLRLSNPEVSLKLTGKILESAKEAGADAI 225
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 502884468 830 ITNCAGCGSQFNatscAMQTRVRQKD----------FTDLVAEALGIETED 870
Cdd:COG2048 226 VTACPLCHLNLD----MYQPEINKKFgtefnipvlyFTQLLGLALGLSPKE 272
|
|
| CCG |
pfam02754 |
Cysteine-rich domain; The key element of this family is the CX31-38CCX33-34CXXC sequence motif ... |
627-710 |
1.22e-13 |
|
Cysteine-rich domain; The key element of this family is the CX31-38CCX33-34CXXC sequence motif normally found at the C-terminus in archaeal and bacterial Hdr-like proteins. There may be one or two copies, and the motif is probably an iron-sulfur binding cluster. In some instances one of the cysteines is replaced by an aspartate, and aspartate can in principle also function as a ligand of an iron-sulfur cluster. The family includes a subunit from heterodisulphide reductase and a subunit from glycolate oxidase and glycerol-3-phosphate dehydrogenase.
Pssm-ID: 397052 [Multi-domain] Cd Length: 84 Bit Score: 66.95 E-value: 1.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502884468 627 IAYWAGC-WANIVMPNMPRNITRIFNKIGVEFVHFgEGETCCGLYLALGGYMDDFTGLVKKNLEMFKEAGIETMVFSCPG 705
Cdd:pfam02754 1 VAYFDGChLGRALYPEPRKALKKVLGALGVEVVIL-EKQSCCGAGGGFSGKEDVAEALAKRNIDTAEETGADAIVTACPG 79
|
....*
gi 502884468 706 CFATF 710
Cdd:pfam02754 80 CLLQL 84
|
|
| FAD_lactone_ox |
TIGR01678 |
sugar 1,4-lactone oxidases; This model represents a family of at least two different sugar 1,4 ... |
51-241 |
7.75e-11 |
|
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: 65.30 E-value: 7.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502884468 51 PDAVAQPVSEEEVIAATNLAREFSWPLIPRGSGTSGfgGALPTRGGIVLDFVRMNRIIAVDEHNLTVTVEPGVVWGDLQE 130
Cdd:TIGR01678 15 PEVYYQPTSVEEVREVLALAREQKKKVKVVGGGHSP--SDIACTDGFLIHLDKMNKVLQFDKEKKQITVEAGIRLYQLHE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502884468 131 YLQAKGFDLRLYpSSTPSATVAGWVAQGGSGyGSFEYGFCGENIVSVDVVTTEG----ITRSYAGEELKFVNGLCGITGI 206
Cdd:TIGR01678 93 QLDEHGYSMSNL-GSISEVSVAGIISTGTHG-SSIKHGILATQVVALTIMTADGevleCSEERNADVFQAARVSLGCLGI 170
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 502884468 207 ITKVTVK------IKEKDEDVVVLAAFDKLNDAAEALRMIR 241
Cdd:TIGR01678 171 IVTVTIQvvpqfhLQETSFVSTLKELLDNWDSHWKSSEFFR 211
|
|
| FAD-oxidase_C |
pfam02913 |
FAD linked oxidases, C-terminal domain; This domain has a ferredoxin-like fold. |
221-446 |
2.62e-10 |
|
FAD linked oxidases, C-terminal domain; This domain has a ferredoxin-like fold.
Pssm-ID: 397178 Cd Length: 248 Bit Score: 61.95 E-value: 2.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502884468 221 VVVLAAFDKLNDAAEALRMIRQQAVPLWSATMSTPAYIRLKQKASQHIVLPEDR--YFLLFVYPKTRRTAVEMALKGIIA 298
Cdd:pfam02913 6 AVALVGFPSFEAAVKAVREIARAGIIPAALELMDNDALDLVEATLGFPKGLPRDaaALLLVEFEGDDEETAEEELEAVEA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502884468 299 SCHGEL---------MREALAREEWNERFYPMR--FKKLGPTLIATEVIVPIDRLSEFVSEVERKYKgEFALEGTMI-H- 365
Cdd:pfam02913 86 ILEAGGagdvvvatdEAEAERLWAARKYALPLRdaLGGAGPAVFSEDVSVPRSRLADLVRDIKELLD-KYGLVVCLFgHa 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502884468 366 ---NDKISILGFMLSDERKAGFPLAYTNsltVIEIGEKLGGrvfTL------GLYFADKAKDVLGENLVNEIWAYKQKID 436
Cdd:pfam02913 165 gdgNLHLYILFDFRDPEQEERAEKLFDE---IMDLALELGG---SIsgehgvGRDKKPYLEREFGEEGLALMRRIKAAFD 238
|
250
....*....|
gi 502884468 437 PQGILNPGKI 446
Cdd:pfam02913 239 PKGILNPGKV 248
|
|
| Fer4_17 |
pfam13534 |
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ... |
503-565 |
2.58e-07 |
|
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. The structure of the domain is an alpha-antiparallel beta sandwich.
Pssm-ID: 433287 [Multi-domain] Cd Length: 61 Bit Score: 48.23 E-value: 2.58e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502884468 503 ACALCGYCRNTCTVFDAVPWESNSPRGKYYLltqyikgNIQLDEEVSKALFSCTTCAKCDKVC 565
Cdd:pfam13534 1 RCIQCGCCVDECPRYLLNGDEPKKLMRAAYL-------GDLEELQANKVANLCSECGLCEYAC 56
|
|
| PLN02465 |
PLN02465 |
L-galactono-1,4-lactone dehydrogenase |
56-213 |
3.94e-07 |
|
L-galactono-1,4-lactone dehydrogenase
Pssm-ID: 215258 [Multi-domain] Cd Length: 573 Bit Score: 53.70 E-value: 3.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502884468 56 QPVSEEEVIAATNLAREFSWPLIPRGSGTSGFGGALPTRGgiVLDFVRMNRIIAVDEHNLTVTVEPGVVWGDLQEYLQAK 135
Cdd:PLN02465 102 QPESLEELEDIVKEAHEKGRRIRPVGSGLSPNGLAFSREG--MVNLALMDKVLEVDKEKKRVTVQAGARVQQVVEALRPH 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502884468 136 GFDLRLYpSSTPSATVAGWVAQGGSGYGSfEYGFCGENIVSVDVVT-TEG-ITRSYAGEELKFVNGLCGI--TGIITKVT 211
Cdd:PLN02465 180 GLTLQNY-ASIREQQIGGFIQVGAHGTGA-RIPPIDEQVVSMKLVTpAKGtIELSKEDDPELFRLARCGLggLGVVAEVT 257
|
..
gi 502884468 212 VK 213
Cdd:PLN02465 258 LQ 259
|
|
| pln_FAD_oxido |
TIGR01677 |
plant-specific FAD-dependent oxidoreductase; This model represents an uncharacterized ... |
53-215 |
7.26e-07 |
|
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: 52.94 E-value: 7.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502884468 53 AVAQPVSEEEVIAATNLAREFSWPLiprgSGTSGFGGALP-------TRGGIVLDFVRMNRIIAVDEHNLTVTVEPGVVW 125
Cdd:TIGR01677 34 NVAYPKTEAELVSVVAAATAAGRKM----KVVTRYSHSIPklacpdgSDGALLISTKRLNHVVAVDATAMTVTVESGMSL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502884468 126 GDLQEYLQAKGFDLRLYPSSTpSATVAGWVAQGgsGYGSFEYGFCG---ENIVSVDVVTTEGITRSYA----------GE 192
Cdd:TIGR01677 110 RELIVEAEKAGLALPYAPYWW-GLTVGGMMGTG--AHGSSLWGKGSavhDYVVGIRLVVPASAAEGFAkvrilsegdtPN 186
|
170 180
....*....|....*....|...
gi 502884468 193 ELKFVNGLCGITGIITKVTVKIK 215
Cdd:TIGR01677 187 EFNAAKVSLGVLGVISQVTLALQ 209
|
|
| GLDHase |
TIGR01676 |
galactonolactone dehydrogenase; This model represents L-Galactono-gamma-lactone dehydrogenase ... |
56-221 |
9.71e-06 |
|
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: 49.29 E-value: 9.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502884468 56 QPVSEEEVIAATNLAREFSWPLIPRGSGTSGFGGALpTRGGIVlDFVRMNRIIAVDEHNLTVTVEPGVVWGDLQEYLQAK 135
Cdd:TIGR01676 67 QPEAIEELEGIVKQANEKKARIRPVGSGLSPNGIGL-SRAGMV-NLALMDKVLEVDEEKKRVRVQAGIRVQQLVDAIKEY 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502884468 136 GFDLRLYpSSTPSATVAGWVAQGGSGYGSfEYGFCGENIVSVDVVTTEGITRSYAGE---ELKFVN--GLCGItGIITKV 210
Cdd:TIGR01676 145 GITLQNF-ASIREQQIGGIIQVGAHGTGA-KLPPIDEQVIAMKLVTPAKGTIEISKDkdpELFFLArcGLGGL-GVVAEV 221
|
170
....*....|.
gi 502884468 211 TVKIKEKDEDV 221
Cdd:TIGR01676 222 TLQCVERQELV 232
|
|
| Fer4_8 |
pfam13183 |
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ... |
503-565 |
1.59e-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: 43.45 E-value: 1.59e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502884468 503 ACALCGYCRNTCTVFDAVPWESNSPRGKYYLLtqyIKGNIQLDEEVSKALFSCTTCAKCDKVC 565
Cdd:pfam13183 1 RCIRCGACLAACPVYLVTGGRFPGDPRGGAAA---LLGRLEALEGLAEGLWLCTLCGACTEVC 60
|
|
| Fer4_10 |
pfam13237 |
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ... |
500-565 |
4.41e-03 |
|
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. The structure of the domain is an alpha-antiparallel beta sandwich.
Pssm-ID: 404174 [Multi-domain] Cd Length: 56 Bit Score: 36.07 E-value: 4.41e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502884468 500 DTFACALCGYCRNTCtvfdavPWESNSPRGKYYLLtqyikgniqLDEEVSKALFSCTTCAKCDKVC 565
Cdd:pfam13237 5 DPDKCIGCGRCTAAC------PAGLTRVGAIVERL---------EGEAVRIGVWKCIGCGACVEAC 55
|
|
| |
