|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
1-538 |
0e+00 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 716.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966470505 1 MAEEnkIKVPDIGGATNVDVIEILVNEGDEIDTDTPLITLESEKASMDIPSPKAGKVKEIQVKAGDKVSEGDLILTLEGQ 80
Cdd:PRK11855 1 MAIE--FKVPDIGEVVEVEVIEWLVKEGDTVEEDQPLVTVETDKATMEIPSPAAGVVKEIKVKVGDTVSVGGLLAVIEAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966470505 81 EAKSSKEDKSTEKKTEKDIESGKKSTPSEQQEETHEKT-EIKEVRIPDIGGATDVDVIEIMVQSGDKISKDQALITLEGD 159
Cdd:PRK11855 79 GAAAAAAAPAAAAAPAAAAAAAPAPAAAAPAAAAAAAGgGVVEVKVPDIGEITEVEVIEWLVKVGDTVEEDQSLITVETD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966470505 160 KATMDIPAPCAGVVDKISMNVGDKVSQGDLILTLQVKTDKKVEIEASEETENKKKEKEEKLPTTETKSE-AVKAPVQEKE 238
Cdd:PRK11855 159 KATMEIPSPVAGVVKEIKVKVGDKVSVGSLLVVIEVAAAAPAAAAAPAAAAPAAAAAAAPAPAPAAAAApAAAAPAAAAA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966470505 239 EAVMLPAGPAVRKIAREFGVDLGKVKGTGRKSRITKEDIQNYVKQKLSEK---------TTATGVSLPPAPQIDFSKYGE 309
Cdd:PRK11855 239 PGKAPHASPAVRRLARELGVDLSQVKGTGKKGRITKEDVQAFVKGAMSAAaaaaaaaaaAGGGGLGLLPWPKVDFSKFGE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966470505 310 IDIKPLNKIKRLTGINVHRSWINIPHVTQFDEADITELESFRKTEQEKAKKAGYKLTVLAFVCKVVSKALKEFPQFNTSL 389
Cdd:PRK11855 319 IETKPLSRIKKISAANLHRSWVTIPHVTQFDEADITDLEALRKQLKKEAEKAGVKLTMLPFFIKAVVAALKEFPVFNASL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966470505 390 DESGENLIYKKYFNIGIAVETENGLVVPVIRDVGQLSVADIAKEMARLSSKARDKGLMPVEMSGGCFTISSLGGIGGTAF 469
Cdd:PRK11855 399 DEDGDELTYKKYFNIGFAVDTPNGLVVPVIKDVDKKSLLEIAREIAELAKKARDGKLKPDDMQGGCFTISSLGGIGGTAF 478
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 966470505 470 TPIVNGPEVAILGLSRSSVKPVYDGDKFAPRLMLPLSLSYDHRVIDGAEAARFTRYIAETLGDIRRVLL 538
Cdd:PRK11855 479 TPIINAPEVAILGVGKSQMKPVWDGKEFVPRLMLPLSLSYDHRVIDGATAARFTNYLKQLLADPRRMLL 547
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
7-538 |
0e+00 |
|
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model describes a subset of pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase specifically close by both phylogenetic and per cent identity (UPGMA) trees. Members of this set include two or three copies of the lipoyl-binding domain. E. coli AceF is a member of this model, while mitochondrial and some other bacterial forms belong to a separate model. [Energy metabolism, Pyruvate dehydrogenase]
Pssm-ID: 273566 [Multi-domain] Cd Length: 546 Bit Score: 616.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966470505 7 IKVPDIGGATNVDVIEILVNEGDEIDTDTPLITLESEKASMDIPSPKAGKVKEIQVKAGDKVSEGDLILTLEGQEAKSSK 86
Cdd:TIGR01348 3 IKVPDIGDNEEGEVIEVLVKPGDKVEAGQSLITLESDKASMEVPSSAAGIIKEIKVKVGDTLPVGGVIATLEVGAGAQAQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966470505 87 EDkstEKKTEKDIESGKKSTPSEQQEETHE---KTEIKEVRIPDIGGATDVDVIEIMVQSGDKISKDQALITLEGDKATM 163
Cdd:TIGR01348 83 AE---AKKEAAPAPTAGAPAPAAQAQAAPAagqSSGVQEVTVPDIGDIEKVTVIEVLVKVGDTVSADQSLITLESDKASM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966470505 164 DIPAPCAGVVDKISMNVGDKVSQGDLILTLQVK--------TDKKVEIEASEETENKKKEKEeklPTTETKSEAvKAPVQ 235
Cdd:TIGR01348 160 EVPAPASGVVKSVKVKVGDSVPTGDLILTLSVAgstpatapAPASAQPAAQSPAATQPEPAA---APAAAKAQA-PAPQQ 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966470505 236 EKEE--AVMLPAGPAVRKIAREFGVDLGKVKGTGRKSRITKEDIQNYVKQKL------SEKTTATGVSLPPAPQIDFSKY 307
Cdd:TIGR01348 236 AGTQnpAKVDHAAPAVRRLAREFGVDLSAVKGTGIKGRILREDVQRFVKEPSvraqaaAASAAGGAPGALPWPNVDFSKF 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966470505 308 GEIDIKPLNKIKRLTGINVHRSWINIPHVTQFDEADITELESFRKTEQEKAKKAGYKLTVLAFVCKVVSKALKEFPQFNT 387
Cdd:TIGR01348 316 GEVEEVDMSRIRKISGANLTRNWTMIPHVTHFDKADITEMEAFRKQQNAAVEKEGVKLTVLHILMKAVAAALKKFPKFNA 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966470505 388 SLDESGENLIYKKYFNIGIAVETENGLVVPVIRDVGQLSVADIAKEMARLSSKARDKGLMPVEMSGGCFTISSLGGIGGT 467
Cdd:TIGR01348 396 SLDLGGEQLILKKYVNIGVAVDTPNGLLVPVIKDVDRKGITELALELSDLAKKARDGKLTPDEMQGACFTISSLGGIGGT 475
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 966470505 468 AFTPIVNGPEVAILGLSRSSVKPVYDGDKFAPRLMLPLSLSYDHRVIDGAEAARFTRYIAETLGDIRRVLL 538
Cdd:TIGR01348 476 AFTPIVNAPEVAILGVSKSGMEPVWNGKEFEPRLMLPLSLSYDHRVIDGADAARFTTYICESLADIRRLLL 546
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
2-538 |
0e+00 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 612.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966470505 2 AEENKIKVPDIGGaTNVDVIEILVNEGDEIDTDTPLITLESEKASMDIPSPKAGKVKEIQVKAGDKVSEGDLILTLEGQE 81
Cdd:PRK11854 103 AAAKDVHVPDIGS-DEVEVTEILVKVGDTVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVSTGSLIMVFEVAG 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966470505 82 AKSSkedkstekktekdiESGKKSTPSEQQEETHEKTEIKEVRIPDIGGaTDVDVIEIMVQSGDKISKDQALITLEGDKA 161
Cdd:PRK11854 182 EAPA--------------AAPAAAEAAAPAAAPAAAAGVKDVNVPDIGG-DEVEVTEVMVKVGDKVEAEQSLITVEGDKA 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966470505 162 TMDIPAPCAGVVDKISMNVGDKVSQGDLILTLQVKTDKKVEIEASEETENKKKEKEEKLPTTETKSEAVKAPVQEKEEAV 241
Cdd:PRK11854 247 SMEVPAPFAGTVKEIKVNVGDKVKTGSLIMRFEVEGAAPAAAPAKQEAAAPAPAAAKAEAPAAAPAAKAEGKSEFAENDA 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966470505 242 MLPAGPAVRKIAREFGVDLGKVKGTGRKSRITKEDIQNYVKQKLSEKTTAT--------GVSLPPAPQIDFSKYGEIDIK 313
Cdd:PRK11854 327 YVHATPLVRRLAREFGVNLAKVKGTGRKGRILKEDVQAYVKDAVKRAEAAPaaaaagggGPGLLPWPKVDFSKFGEIEEV 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966470505 314 PLNKIKRLTGINVHRSWINIPHVTQFDEADITELESFRKTEQEKA--KKAGYKLTVLAFVCKVVSKALKEFPQFNTSLDE 391
Cdd:PRK11854 407 ELGRIQKISGANLHRNWVMIPHVTQFDKADITELEAFRKQQNAEAekRKLGVKITPLVFIMKAVAAALEQMPRFNSSLSE 486
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966470505 392 SGENLIYKKYFNIGIAVETENGLVVPVIRDVGQLSVADIAKEMARLSSKARDKGLMPVEMSGGCFTISSLGGIGGTAFTP 471
Cdd:PRK11854 487 DGQRLTLKKYVNIGIAVDTPNGLVVPVFKDVNKKGIIELSRELMDISKKARDGKLTAGDMQGGCFTISSIGGLGTTHFTP 566
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 966470505 472 IVNGPEVAILGLSRSSVKPVYDGDKFAPRLMLPLSLSYDHRVIDGAEAARFTRYIAETLGDIRRVLL 538
Cdd:PRK11854 567 IVNAPEVAILGVSKSAMEPVWNGKEFAPRLMLPLSLSYDHRVIDGADGARFITIINDRLSDIRRLVL 633
|
|
| PRK11856 |
PRK11856 |
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed |
120-530 |
1.86e-141 |
|
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
Pssm-ID: 237001 [Multi-domain] Cd Length: 411 Bit Score: 414.19 E-value: 1.86e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966470505 120 IKEVRIPDIG-GATDVDVIEIMVQSGDKISKDQALITLEGDKATMDIPAPCAGVVDKISMNVGDKVSQGDLILTLQVKTD 198
Cdd:PRK11856 2 MFEFKMPDLGeGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDVVPVGSVIAVIEEEGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966470505 199 KKVEiEASEETENKKKEKEEKLPTTETKSEAVKAPVQEKEEAVMLPAGPAVRKIAREFGVDLGKVKGTGRKSRITKEDIQ 278
Cdd:PRK11856 82 AEAA-AAAEAAPEAPAPEPAPAAAAAAAAAPAAAAAPAAPAAAAAKASPAVRKLARELGVDLSTVKGSGPGGRITKEDVE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966470505 279 NYVKQKLSEKTTATGVSLPPAPqidfSKYGEIDIKPLNKIKRLTGINVHRSWINIPHVTQFDEADITELESFRKteqeKA 358
Cdd:PRK11856 161 AAAAAAAPAAAAAAAAAAAPPA----AAAEGEERVPLSGMRKAIAKRMVESKREIPHFTLTDEVDVTALLALRK----QL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966470505 359 KKAGYKLTVLAFVCKVVSKALKEFPQFNTSLDEsgENLIYKKYFNIGIAVETENGLVVPVIRDVGQLSVADIAKEMARLS 438
Cdd:PRK11856 233 KAIGVKLTVTDFLIKAVALALKKFPELNASWDD--DAIVLKKYVNIGIAVATDGGLIVPVIRDADKKSLFELAREIKDLA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966470505 439 SKARDKGLMPVEMSGGCFTISSLGGIGGTAFTPIVNGPEVAILGLSRSSVKPVYDGDKFAPRLMLPLSLSYDHRVIDGAE 518
Cdd:PRK11856 311 EKAREGKLKPEELQGGTFTISNLGMFGGDYFTPIINPPEVAILGVGAIVERPVVVDGEIVVRKVMPLSLSFDHRVIDGAD 390
|
410
....*....|..
gi 966470505 519 AARFTRYIAETL 530
Cdd:PRK11856 391 AARFLKALKELL 402
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
327-537 |
7.13e-95 |
|
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to three copies of a lipoyl binding domain followed by the catalytic domain.
Pssm-ID: 425518 [Multi-domain] Cd Length: 212 Bit Score: 287.52 E-value: 7.13e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966470505 327 HRSWINIPHVTQFDEADITELESFRKTEQEKAKKAGYKLTVLAFVCKVVSKALKEFPQFNTSLDESGENLIYKKYFNIGI 406
Cdd:pfam00198 2 TESKQTIPHFTLTDEVDVTELLALREELKEDAADEETKLTFLPFLVKAVALALKKFPELNASWDGEEGEIVYKKYVNIGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966470505 407 AVETENGLVVPVIRDVGQLSVADIAKEMARLSSKARDKGLMPVEMSGGCFTISSLGGIGGTAFTPIVNGPEVAILGLSRS 486
Cdd:pfam00198 82 AVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVGRI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 966470505 487 SVKPVYDGDKFAPRLMLPLSLSYDHRVIDGAEAARFTRYIAETLGDIRRVL 537
Cdd:pfam00198 162 RKRPVVVDGEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELLL 212
|
|
| PRK05704 |
PRK05704 |
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase; |
122-538 |
2.71e-86 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
Pssm-ID: 235571 [Multi-domain] Cd Length: 407 Bit Score: 272.48 E-value: 2.71e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966470505 122 EVRIPDIG-GATDVDVIEIMVQSGDKISKDQALITLEGDKATMDIPAPCAGVVDKISMNVGDKVSQGDLIltlqvktdKK 200
Cdd:PRK05704 4 EIKVPTLPeSVTEATIATWHKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGDTVTVGQVL--------GR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966470505 201 VEIEASEETENKKKEkeeklPTTETKSEAVKAPVQEKEEAVMLPAGPAVRKIAREFGVDLGKVKGTGRKSRITKEDIQNY 280
Cdd:PRK05704 76 IDEGAAAGAAAAAAA-----AAAAAAAAPAQAQAAAAAEQSNDALSPAARKLAAENGLDASAVKGTGKGGRVTKEDVLAA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966470505 281 VKQKLSEKTTATGVSLPPAPQIDFSKyGEIDIkPLNKI-----KRL------TGInvhrswiniphVTQFDEADITELES 349
Cdd:PRK05704 151 LAAAAAAPAAPAAAAPAAAPAPLGAR-PEERV-PMTRLrktiaERLleaqntTAM-----------LTTFNEVDMTPVMD 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966470505 350 FRKTEQEK-AKKAGYKLTVLAFVCKVVSKALKEFPQFNTSLDesGENLIYKKYFNIGIAVETENGLVVPVIRDVGQLSVA 428
Cdd:PRK05704 218 LRKQYKDAfEKKHGVKLGFMSFFVKAVVEALKRYPEVNASID--GDDIVYHNYYDIGIAVGTPRGLVVPVLRDADQLSFA 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966470505 429 DIAKEMARLSSKARDKGLMPVEMSGGCFTISSlGGIGGTAF-TPIVNGPEVAILGLSRSSVKPVYDGDKFAPRLMLPLSL 507
Cdd:PRK05704 296 EIEKKIAELAKKARDGKLSIEELTGGTFTITN-GGVFGSLMsTPIINPPQSAILGMHKIKERPVAVNGQIVIRPMMYLAL 374
|
410 420 430
....*....|....*....|....*....|.
gi 966470505 508 SYDHRVIDGAEAARFTRYIAETLGDIRRVLL 538
Cdd:PRK05704 375 SYDHRIIDGKEAVGFLVTIKELLEDPERLLL 405
|
|
| sucB |
TIGR01347 |
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ... |
122-538 |
2.38e-79 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This model describes the TCA cycle 2-oxoglutarate system E2 component, dihydrolipoamide succinyltransferase. It is closely related to the pyruvate dehydrogenase E2 component, dihydrolipoamide acetyltransferase. The seed for this model includes mitochondrial and Gram-negative bacterial forms. Mycobacterial candidates are highly derived, differ in having and extra copy of the lipoyl-binding domain at the N-terminus. They score below the trusted cutoff, but above the noise cutoff and above all examples of dihydrolipoamide acetyltransferase. [Energy metabolism, TCA cycle]
Pssm-ID: 273565 [Multi-domain] Cd Length: 403 Bit Score: 254.27 E-value: 2.38e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966470505 122 EVRIPDIGGA-TDVDVIEIMVQSGDKISKDQALITLEGDKATMDIPAPCAGVVDKISMNVGDKVSQGDLILTLQVKTDKK 200
Cdd:TIGR01347 2 EIKVPELAESiTEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAILEEGNDAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966470505 201 VEIEAseetenkkkekeeklPTTETKSEAVKAPVQEK--EEAVMLPAGPAVRKIAREFGVDLGKVKGTGRKSRITKEDIQ 278
Cdd:TIGR01347 82 AAPPA---------------KSGEEKEETPAASAAAAptAAANRPSLSPAARRLAKEHGIDLSAVPGTGVTGRVTKEDII 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966470505 279 NYVKQKLSekttatgvSLPPAPQIDFSKYGEIDiKPLNKIK--RLTGINVHR---SWINIPHVTQFDEADITELESFRKT 353
Cdd:TIGR01347 147 KKTEAPAS--------AQPPAAAAAAAAPAAAT-RPEERVKmtRLRQRIAERlkeAQNSTAMLTTFNEVDMSAVMELRKR 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966470505 354 EQEK-AKKAGYKLTVLAFVCKVVSKALKEFPQFNTSLDesGENLIYKKYFNIGIAVETENGLVVPVIRDVGQLSVADIAK 432
Cdd:TIGR01347 218 YKEEfEKKHGVKLGFMSFFVKAVVAALKRFPEVNAEID--GDDIVYKDYYDISVAVSTDRGLVVPVVRNADRMSFADIEK 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966470505 433 EMARLSSKARDKGLMPVEMSGGCFTISSlGGIGGTAF-TPIVNGPEVAILGLSRSSVKPVYDGDKFAPRLMLPLSLSYDH 511
Cdd:TIGR01347 296 EIADLGKKARDGKLTLEDMTGGTFTITN-GGVFGSLMsTPIINPPQSAILGMHGIKERPVAVNGQIEIRPMMYLALSYDH 374
|
410 420
....*....|....*....|....*..
gi 966470505 512 RVIDGAEAARFTRYIAETLGDIRRVLL 538
Cdd:TIGR01347 375 RLIDGKEAVTFLVTIKELLEDPRRLLL 401
|
|
| SucB_Actino |
TIGR02927 |
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model ... |
1-530 |
1.87e-74 |
|
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model represents an Actinobacterial clade of E2 enzyme, a component of the 2-oxoglutarate dehydrogenase complex involved in the TCA cycle. These proteins have multiple domains including the catalytic domain (pfam00198), one or two biotin domains (pfam00364) and an E3-component binding domain (pfam02817).
Pssm-ID: 200219 [Multi-domain] Cd Length: 579 Bit Score: 246.85 E-value: 1.87e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966470505 1 MAEEnkIKVPDIG-GATNVDVIEILVNEGDEIDTDTPLITLESEKASMDIPSPKAGKVKEIQVKAGDKVSEGDLILTL-E 78
Cdd:TIGR02927 1 MAES--VKMPALGeSVTEGTVTSWLKAVGDTVEADEPLLEVSTDKVDTEIPSPAAGVLLEIRAPEDDTVEVGGVLAIIgE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966470505 79 GQEAKSSKEDKSTEKKTEKDIESGK------KSTPSEQQEETHEKTEIKEVRIPDIG-GATDVDVIEIMVQSGDKISKDQ 151
Cdd:TIGR02927 79 PGEAGSEPAPAAPEPEAAPEPEAPApaptpaAEAPAPAAPQAGGSGEATEVKMPELGeSVTEGTVTSWLKAVGDTVEVDE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966470505 152 ALITLEGDKATMDIPAPCAGVVDKISMNVGDKVSQGDLILTLqvkTDKKVEIEASEETENKKKEKEEKLPTTETKSEAVK 231
Cdd:TIGR02927 159 PLLEVSTDKVDTEIPSPVAGTLLEIRAPEDDTVEVGTVLAII---GDANAAPAEPAEEEAPAPSEAGSEPAPDPAARAPH 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966470505 232 APVQ-----EKEEAVMLPAGPA--------------VRKIAREFGVDLGKVKGTGRKSRITKEDIQNYVK--QKLSEKTT 290
Cdd:TIGR02927 236 AAPDppapaPAPAKTAAPAAAApvssgdsgpyvtplVRKLAKDKGVDLSTVKGTGVGGRIRKQDVLAAAKaaEEARAAAA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966470505 291 ATGVSLPPAPQIDFSKYGEIDIKPL-------NKIKRLTGINVHRSWINIPHVTQFDEADITELESFRKTEQ-EKAKKAG 362
Cdd:TIGR02927 316 APAAAAAPAAPAAAAKPAEPDTAKLrgttqkmNRIRQITADKTIESLQTSAQLTQVHEVDMTRVAALRARAKnDFLEKNG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966470505 363 YKLTVLAFVCKVVSKALKEFPQFNTSLDESGENLIYKKYFNIGIAVETENGLVVPVIRDVGQLSVADIAKEMARLSSKAR 442
Cdd:TIGR02927 396 VNLTFLPFFVQAVTEALKAHPNVNASYNAETKEVTYHDVEHVGIAVDTPRGLLVPVIHNAGDLSLPGLAKAINDLAARAR 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966470505 443 DKGLMPVEMSGGCFTISSLGGIGGTAFTPIVNGPEVAILGLSRSSVKPV-----YDGDKFAPRLMLPLSLSYDHRVIDGA 517
Cdd:TIGR02927 476 DNKLKPDELSGGTFTITNIGSGGALFDTPILNPPQAAILGTGAIVKRPRvikdeDGGESIAIRSVCYLPLTYDHRLVDGA 555
|
570
....*....|...
gi 966470505 518 EAARFTRYIAETL 530
Cdd:TIGR02927 556 DAGRFLTTIKKRL 568
|
|
| PLN02528 |
PLN02528 |
2-oxoisovalerate dehydrogenase E2 component |
127-522 |
3.29e-68 |
|
2-oxoisovalerate dehydrogenase E2 component
Pssm-ID: 215289 [Multi-domain] Cd Length: 416 Bit Score: 225.75 E-value: 3.29e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966470505 127 DIG-GATDVDVIEIMVQSGDKISKDQALITLEGDKATMDIPAPCAGVVDKISMNVGDKVSQGDLILtlqvktdkKVEIEA 205
Cdd:PLN02528 5 QTGeGIAECELLRWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGKVAQINFSPGDIVKVGETLL--------KIMVED 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966470505 206 SEETENKKKEkeekLPTTETKSEAVKAPVQEKEEAVMLPAGPAVRKIAREFGVDLGKVKGTGRKSRITKEDIQNYVKQKL 285
Cdd:PLN02528 77 SQHLRSDSLL----LPTDSSNIVSLAESDERGSNLSGVLSTPAVRHLAKQYGIDLNDILGTGKDGRVLKEDVLKYAAQKG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966470505 286 SEKTTATGVSLPPAPQIDFSKYGEIDIKPLNKIKRLTGINVHRSWI-------NIPHVTQFDEADITELESFRKTEQEKA 358
Cdd:PLN02528 153 VVKDSSSAEEATIAEQEEFSTSVSTPTEQSYEDKTIPLRGFQRAMVktmtaaaKVPHFHYVEEINVDALVELKASFQENN 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966470505 359 KKAGYKLTVLAFVCKVVSKALKEFPQFNTSLDESGENLIYKKYFNIGIAVETENGLVVPVIRDVGQLSVADIAKEMARLS 438
Cdd:PLN02528 233 TDPTVKHTFLPFLIKSLSMALSKYPLLNSCFNEETSEIRLKGSHNIGVAMATEHGLVVPNIKNVQSLSLLEITKELSRLQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966470505 439 SKARDKGLMPVEMSGGCFTISSLGGIGGTAFTPIVNGPEVAILGLSR--SSVKPVYDGDKFAPRLMlPLSLSYDHRVIDG 516
Cdd:PLN02528 313 HLAAENKLNPEDITGGTITLSNIGAIGGKFGSPVLNLPEVAIIALGRiqKVPRFVDDGNVYPASIM-TVTIGADHRVLDG 391
|
....*.
gi 966470505 517 AEAARF 522
Cdd:PLN02528 392 ATVARF 397
|
|
| PRK11857 |
PRK11857 |
dihydrolipoamide acetyltransferase; Reviewed |
245-530 |
8.99e-57 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237002 [Multi-domain] Cd Length: 306 Bit Score: 191.93 E-value: 8.99e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966470505 245 AGPAVRKIAREFGVDLGKVKGTGRKSRITKEDIQNYVKQKLSEKTTATGVSLPPAPQ-------IDFSKYGEIDIKPLNK 317
Cdd:PRK11857 4 ATPIARALAKKLGIDISLLKGSGRDGKILAEDVENFIKSLKSAPTPAEAASVSSAQQaaktaapAAAPPKLEGKREKVAP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966470505 318 IKRLTGINVHRSWINIPHVTQFDEADITELESFRKTEQEKAKK-AGYKLTVLAFVCKVVSKALKEFPQFNTSLDESGENL 396
Cdd:PRK11857 84 IRKAIARAMTNSWSNVAYVNLVNEIDMTKLWDLRKSVKDPVLKtEGVKLTFLPFIAKAILIALKEFPIFAAKYDEATSEL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966470505 397 IYKKYFNIGIAVETENGLVVPVIRDVGQLSVADIAKEMARLSSKARDKGLMPVEMSGGCFTISSLGGIGGTAFTPIVNGP 476
Cdd:PRK11857 164 VYPDTLNLGIAVDTEAGLMVPVIKNAQKLSIVEIAKEISRLAKAARERKIKPDEMKGGSFTITNYGSVGSLYGVPVINYP 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 966470505 477 EVAILGLSRSSVKPVYDGDKFAPRLMLPLSLSYDHRVIDGAEAARFTRYIAETL 530
Cdd:PRK11857 244 ELAIAGVGAIIDKAIVKNGQIVAGKVMHLTVAADHRWIDGATIGRFASRVKELL 297
|
|
| PTZ00144 |
PTZ00144 |
dihydrolipoamide succinyltransferase; Provisional |
119-538 |
6.26e-55 |
|
dihydrolipoamide succinyltransferase; Provisional
Pssm-ID: 240289 [Multi-domain] Cd Length: 418 Bit Score: 190.66 E-value: 6.26e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966470505 119 EIKEVRIPDIGGA-TDVDVIEIMVQSGDKISKDQALITLEGDKATMDIPAPCAGVVDKISMNVGDKVSQGDLILTlqVKT 197
Cdd:PTZ00144 43 SIKVIKVPTMGDSiSEGTVVEWKKKVGDYVKEDEVICIIETDKVSVDIRAPASGVITKIFAEEGDTVEVGAPLSE--IDT 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966470505 198 DKKVEIEASEETENKKKekeeklPTTETKSEAVKAPVQEKEEAVMLPAGPAVRKiarefgvdlgkvkgtgrksritkedi 277
Cdd:PTZ00144 121 GGAPPAAAPAAAAAAKA------EKTTPEKPKAAAPTPEPPAASKPTPPAAAKP-------------------------- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966470505 278 qnyVKQKLSEKTTATGVS--LPPAPQIdfskygeidikPLNKIKRLTGINVHRSWINIPHVTQFDEADITELESFRKTEQ 355
Cdd:PTZ00144 169 ---PEPAPAAKPPPTPVAraDPRETRV-----------PMSRMRQRIAERLKASQNTCAMLTTFNECDMSALMELRKEYK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966470505 356 EK-AKKAGYKLTVLAFVCKVVSKALKEFPQFNTSLDesGENLIYKKYFNIGIAVETENGLVVPVIRDVGQLSVADIAKEM 434
Cdd:PTZ00144 235 DDfQKKHGVKLGFMSAFVKASTIALKKMPIVNAYID--GDEIVYRNYVDISVAVATPTGLVVPVIRNCENKSFAEIEKEL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966470505 435 ARLSSKARDKGLMPVEMSGGCFTISSlGGIGGTAF-TPIVNGPEVAILGLSRSSVKPVYDGDKFAPRLMLPLSLSYDHRV 513
Cdd:PTZ00144 313 ADLAEKARNNKLTLEDMTGGTFTISN-GGVFGSLMgTPIINPPQSAILGMHAIKKRPVVVGNEIVIRPIMYLALTYDHRL 391
|
410 420
....*....|....*....|....*
gi 966470505 514 IDGAEAARFTRYIAETLGDIRRVLL 538
Cdd:PTZ00144 392 IDGRDAVTFLKKIKDLIEDPARMLL 416
|
|
| PDHac_trf_mito |
TIGR01349 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
141-523 |
2.73e-54 |
|
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model represents one of several closely related clades of the dihydrolipoamide acetyltransferase subunit of the pyruvate dehydrogenase complex. It includes sequences from mitochondria and from alpha and beta branches of the proteobacteria, as well as from some other bacteria. Sequences from Gram-positive bacteria are not included. The non-enzymatic homolog protein X, which serves as an E3 component binding protein, falls within the clade phylogenetically but is rejected by its low score. [Energy metabolism, Pyruvate dehydrogenase]
Pssm-ID: 273567 [Multi-domain] Cd Length: 436 Bit Score: 189.23 E-value: 2.73e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966470505 141 VQSGDKISKDQALITLEGDKATMDIPAPCAGVVDKISMNVGDK-VSQGDLILTLQVK------TDKKVEIEASEETENKK 213
Cdd:TIGR01349 21 KKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEGTKdVPVNKPIAVLVEEkedvadAFKNYKLESSASPAPKP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966470505 214 KEKEEKLPTT----------ETKSEAVKAPVQEKEEAVMLPAGPAVRKIAREFGVDLGKVKGTGRKSRITKEDIQNYVKQ 283
Cdd:TIGR01349 101 SEIAPTAPPSapkpspapqkQSPEPSSPAPLSDKESGDRIFASPLAKKLAKEKGIDLSAVAGSGPNGRIVKKDIESFVPQ 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966470505 284 KL-SEKTTATGVSLPPAPQIDFSKYGEIDIKPLNKIKRLTGINVHRSWINIPHVTQFDEADITELESFRKtEQEKAKKAG 362
Cdd:TIGR01349 181 SPaSANQQAAATTPATYPAAAPVSTGSYEDVPLSNIRKIIAKRLLESKQTIPHYYVSIECNVDKLLALRK-ELNAMASEV 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966470505 363 YKLTVLAFVCKVVSKALKEFPQFNTSLdeSGENLIYKKYFNIGIAVETENGLVVPVIRDVGQLSVADIAKEMARLSSKAR 442
Cdd:TIGR01349 260 YKLSVNDFIIKASALALREVPEANSSW--TDNFIRRYKNVDISVAVATPDGLITPIVRNADAKGLSTISNEIKDLAKRAR 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966470505 443 DKGLMPVEMSGGCFTISSLGGIGGTAFTPIVNGPEVAILGLSRSSVKPVYDGDK---FAPRLMLPLSLSYDHRVIDGAEA 519
Cdd:TIGR01349 338 NNKLKPEEFQGGTFTISNLGMFGIKDFTAIINPPQACILAVGAVEDVAVVDNDEekgFAVASIMSVTLSCDHRVIDGAVG 417
|
....
gi 966470505 520 ARFT 523
Cdd:TIGR01349 418 AEFL 421
|
|
| PLN02226 |
PLN02226 |
2-oxoglutarate dehydrogenase E2 component |
116-538 |
1.18e-49 |
|
2-oxoglutarate dehydrogenase E2 component
Pssm-ID: 177871 [Multi-domain] Cd Length: 463 Bit Score: 177.64 E-value: 1.18e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966470505 116 EKTEIKEVRIPDIGGA-TDVDVIEIMVQSGDKISKDQALITLEGDKATMDIPAPCAGVVDKISMNVGDKVSQGDLILTLQ 194
Cdd:PLN02226 87 ESGDTVEAVVPHMGESiTDGTLATFLKKPGERVQADEAIAQIETDKVTIDIASPASGVIQEFLVKEGDTVEPGTKVAIIS 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966470505 195 VKTDKKVEIEASEETENKKKEKEEKLPTTETKSEAVKAPVQEKEEAVMLPAGPavrkiarefgvdlgkvkgtgrksritk 274
Cdd:PLN02226 167 KSEDAASQVTPSQKIPETTDPKPSPPAEDKQKPKVESAPVAEKPKAPSSPPPP--------------------------- 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966470505 275 ediqnyvkqklseKTTATGVSLPPapqidfsKYGEIDIkPLNKIKRLTGINVHRSWINIPHVTQFDEADITELESFRKTE 354
Cdd:PLN02226 220 -------------KQSAKEPQLPP-------KERERRV-PMTRLRKRVATRLKDSQNTFALLTTFNEVDMTNLMKLRSQY 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966470505 355 QEK-AKKAGYKLTVLAFVCKVVSKALKEFPQFNTSLDesGENLIYKKYFNIGIAVETENGLVVPVIRDVGQLSVADIAKE 433
Cdd:PLN02226 279 KDAfYEKHGVKLGLMSGFIKAAVSALQHQPVVNAVID--GDDIIYRDYVDISIAVGTSKGLVVPVIRGADKMNFAEIEKT 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966470505 434 MARLSSKARDKGLMPVEMSGGCFTISSLGGIGGTAFTPIVNGPEVAILGLSRSSVKPVYDGDKFAPRLMLPLSLSYDHRV 513
Cdd:PLN02226 357 INGLAKKANEGTISIDEMAGGSFTVSNGGVYGSLISTPIINPPQSAILGMHSIVSRPMVVGGSVVPRPMMYVALTYDHRL 436
|
410 420
....*....|....*....|....*
gi 966470505 514 IDGAEAARFTRYIAETLGDIRRVLL 538
Cdd:PLN02226 437 IDGREAVYFLRRVKDVVEDPQRLLL 461
|
|
| PLN02744 |
PLN02744 |
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex |
144-522 |
1.90e-45 |
|
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
Pssm-ID: 215397 [Multi-domain] Cd Length: 539 Bit Score: 167.72 E-value: 1.90e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966470505 144 GDKISKDQALITLEGDKATMDIPAPCAGVVDKISMNVGDK-VSQGDLI-LTLQVKTD----KKVEIEASEETENKKKEKE 217
Cdd:PLN02744 137 GDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVKGDGAKeIKVGEVIaITVEEEEDigkfKDYKPSSSAAPAAPKAKPS 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966470505 218 EKLPTTETKSEAVKAPVQEKEEAVMLP-------AGPAVRKIAREFGVDLGKVKGTGRKSRITKEDIQNYVKQKLSEKTT 290
Cdd:PLN02744 217 PPPPKEEEVEKPASSPEPKASKPSAPPssgdrifASPLARKLAEDNNVPLSSIKGTGPDGRIVKADIEDYLASGGKGATA 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966470505 291 ATGVSlPPAPQIDFskygeIDIkPLNKIKRLTGINVHRSWINIPHV-----TQFDEadITELESFRKTEQEKAKkaGYKL 365
Cdd:PLN02744 297 PPSTD-SKAPALDY-----TDI-PNTQIRKVTASRLLQSKQTIPHYyltvdTRVDK--LMALRSQLNSLQEASG--GKKI 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966470505 366 TVLAFVCKVVSKALKEFPQFNTSLDESgenliYKKYF---NIGIAVETENGLVVPVIRDVGQLSVADIAKEMARLSSKAR 442
Cdd:PLN02744 366 SVNDLVIKAAALALRKVPQCNSSWTDD-----YIRQYhnvNINVAVQTENGLYVPVVKDADKKGLSTIAEEVKQLAQKAR 440
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966470505 443 DKGLMPVEMSGGCFTISSLGG-IGGTAFTPIVNGPEVAIL--GLSRSSVKPVYDGDKFAPRLMLPLSLSYDHRVIDGAEA 519
Cdd:PLN02744 441 ENSLKPEDYEGGTFTVSNLGGpFGIKQFCAIINPPQSAILavGSAEKRVIPGSGPDQYNFASFMSVTLSCDHRVIDGAIG 520
|
...
gi 966470505 520 ARF 522
Cdd:PLN02744 521 AEW 523
|
|
| PRK14843 |
PRK14843 |
dihydrolipoamide acetyltransferase; Provisional |
247-532 |
1.53e-43 |
|
dihydrolipoamide acetyltransferase; Provisional
Pssm-ID: 184847 [Multi-domain] Cd Length: 347 Bit Score: 158.14 E-value: 1.53e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966470505 247 PAVRKIAREFGVDLGKVKGTGRKSRITKEDIQNYVKQKLSEKTTATGVSLPPAPQID--FSKYGEIDIKPLNKIKRLTGI 324
Cdd:PRK14843 53 PLAKRIALEHNIAWQEIQGTGHRGKIMKKDVLALLPENIENDSIKSPAQIEKVEEVPdnVTPYGEIERIPMTPMRKVIAQ 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966470505 325 NVHRSWINIPHVTQFDEADITELESFRKTEQEKAKKA-GYKLTVLAFVCKVVSKALKEFPQFNTSLDESGENLIYKKYFN 403
Cdd:PRK14843 133 RMVESYLTAPTFTLNYEVDMTEMLALRKKVLEPIMEAtGKKTTVTDLLSLAVVKTLMKHPYINASLTEDGKTIITHNYVN 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966470505 404 IGIAVETENGLVVPVIRDVGQLSVADIAKEMARLSSKARDKGLMPVEMSGGCFTISSLGGIGGTAFTPIVNGPEVAILGL 483
Cdd:PRK14843 213 LAMAVGMDNGLMTPVVYNAEKMSLSELVVAFKDVIGRTLDGKLAPSELQNSTFTISNLGMFGVQSFGPIINQPNSAILGV 292
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 966470505 484 SRSSVKPVYDGDKFAPRLMLPLSLSYDHRVIDGAEAARFTRYIAETLGD 532
Cdd:PRK14843 293 SSTIEKPVVVNGEIVIRPIMSLGLTIDHRVVDGMAGAKFMKDLKELIET 341
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
1-77 |
7.03e-21 |
|
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component [Energy production and conversion]; Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component is part of the Pathway/BioSystem: Pyruvate oxidation
Pssm-ID: 440274 [Multi-domain] Cd Length: 77 Bit Score: 86.66 E-value: 7.03e-21
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 966470505 1 MAEEnkIKVPDIG-GATNVDVIEILVNEGDEIDTDTPLITLESEKASMDIPSPKAGKVKEIQVKAGDKVSEGDLILTL 77
Cdd:COG0508 1 MAIE--IKMPDLGeSMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
120-193 |
4.30e-20 |
|
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component [Energy production and conversion]; Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component is part of the Pathway/BioSystem: Pyruvate oxidation
Pssm-ID: 440274 [Multi-domain] Cd Length: 77 Bit Score: 84.35 E-value: 4.30e-20
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 966470505 120 IKEVRIPDIG-GATDVDVIEIMVQSGDKISKDQALITLEGDKATMDIPAPCAGVVDKISMNVGDKVSQGDLILTL 193
Cdd:COG0508 2 AIEIKMPDLGeSMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
121-193 |
2.82e-18 |
|
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. 2-oxo acid dehydrogenase multienzyme complexes, like pyruvate dehydrogenase (PDH), 2-oxoglutarate dehydrogenase (OGDH) and branched-chain 2-oxo acid dehydrogenase (BCDH), contain at least three different enzymes, 2-oxo acid dehydrogenase (E1), dihydrolipoyl acyltransferase (E2) and dihydrolipoamide dehydrogenase (E3) and play a key role in redox regulation. E2, the central component of the complex, catalyzes the transfer of the acyl group of CoA from E1 to E3 via reductive acetylation of a lipoyl group covalently attached to a lysine residue.
Pssm-ID: 133458 [Multi-domain] Cd Length: 74 Bit Score: 78.99 E-value: 2.82e-18
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 966470505 121 KEVRIPDIG-GATDVDVIEIMVQSGDKISKDQALITLEGDKATMDIPAPCAGVVDKISMNVGDKVSQGDLILTL 193
Cdd:cd06849 1 TEIKMPDLGeSMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
6-77 |
1.21e-17 |
|
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. 2-oxo acid dehydrogenase multienzyme complexes, like pyruvate dehydrogenase (PDH), 2-oxoglutarate dehydrogenase (OGDH) and branched-chain 2-oxo acid dehydrogenase (BCDH), contain at least three different enzymes, 2-oxo acid dehydrogenase (E1), dihydrolipoyl acyltransferase (E2) and dihydrolipoamide dehydrogenase (E3) and play a key role in redox regulation. E2, the central component of the complex, catalyzes the transfer of the acyl group of CoA from E1 to E3 via reductive acetylation of a lipoyl group covalently attached to a lysine residue.
Pssm-ID: 133458 [Multi-domain] Cd Length: 74 Bit Score: 77.44 E-value: 1.21e-17
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 966470505 6 KIKVPDIG-GATNVDVIEILVNEGDEIDTDTPLITLESEKASMDIPSPKAGKVKEIQVKAGDKVSEGDLILTL 77
Cdd:cd06849 2 EIKMPDLGeSMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
121-193 |
5.55e-17 |
|
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue binds biotin in one group and lipoic acid in the other. Note that the HMM does not currently recognize the Glycine cleavage system H proteins.
Pssm-ID: 395290 [Multi-domain] Cd Length: 73 Bit Score: 75.33 E-value: 5.55e-17
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 966470505 121 KEVRIPDIGGATDVDVIEIMVQSGDKISKDQALITLEGDKATMDIPAPCAGVVDKISMNVGDKVSQGDLILTL 193
Cdd:pfam00364 1 TEIKSPMIGESVREGVVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
5-77 |
1.75e-16 |
|
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue binds biotin in one group and lipoic acid in the other. Note that the HMM does not currently recognize the Glycine cleavage system H proteins.
Pssm-ID: 395290 [Multi-domain] Cd Length: 73 Bit Score: 74.17 E-value: 1.75e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 966470505 5 NKIKVPDIGGATNVDVIEILVNEGDEIDTDTPLITLESEKASMDIPSPKAGKVKEIQVKAGDKVSEGDLILTL 77
Cdd:pfam00364 1 TEIKSPMIGESVREGVVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
|
|
| E3_binding |
pfam02817 |
e3 binding domain; This family represents a small domain of the E2 subunit of 2-oxo-acid ... |
244-278 |
1.52e-12 |
|
e3 binding domain; This family represents a small domain of the E2 subunit of 2-oxo-acid dehydrogenases responsible for the binding of the E3 subunit.
Pssm-ID: 460710 [Multi-domain] Cd Length: 36 Bit Score: 61.55 E-value: 1.52e-12
10 20 30
....*....|....*....|....*....|....*
gi 966470505 244 PAGPAVRKIAREFGVDLGKVKGTGRKSRITKEDIQ 278
Cdd:pfam02817 2 LASPAARKLARELGIDLSDVKGTGPGGRITKEDVE 36
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
20-77 |
1.95e-12 |
|
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all biotin-dependent enzymes, such as acetyl-CoA carboxylase, pyruvate carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA carboxylase, geranyl-CoA carboxylase, oxaloacetate decarboxylase, methylmalonyl-CoA decarboxylase, transcarboxylase and urea amidolyase. This domain functions in transferring CO2 from one subsite to another, allowing carboxylation, decarboxylation, or transcarboxylation. During this process, biotin is covalently attached to a specific lysine.
Pssm-ID: 133459 [Multi-domain] Cd Length: 67 Bit Score: 62.43 E-value: 1.95e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 966470505 20 VIEILVNEGDEIDTDTPLITLESEKASMDIPSPKAGKVKEIQVKAGDKVSEGDLILTL 77
Cdd:cd06850 10 VVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
20-77 |
7.16e-10 |
|
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the Pathway/BioSystem: Urea cycle
Pssm-ID: 440660 [Multi-domain] Cd Length: 1144 Bit Score: 62.02 E-value: 7.16e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 966470505 20 VIEILVNEGDEIDTDTPLITLESEKASMDIPSPKAGKVKEIQVKAGDKVSEGDLILTL 77
Cdd:COG1038 1087 VVKVLVKEGDEVKKGDPLLTIEAMKMETTITAPRDGTVKEVLVKEGDQVEAGDLLIEL 1144
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
136-193 |
7.27e-10 |
|
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all biotin-dependent enzymes, such as acetyl-CoA carboxylase, pyruvate carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA carboxylase, geranyl-CoA carboxylase, oxaloacetate decarboxylase, methylmalonyl-CoA decarboxylase, transcarboxylase and urea amidolyase. This domain functions in transferring CO2 from one subsite to another, allowing carboxylation, decarboxylation, or transcarboxylation. During this process, biotin is covalently attached to a specific lysine.
Pssm-ID: 133459 [Multi-domain] Cd Length: 67 Bit Score: 55.11 E-value: 7.27e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 966470505 136 VIEIMVQSGDKISKDQALITLEGDKATMDIPAPCAGVVDKISMNVGDKVSQGDLILTL 193
Cdd:cd06850 10 VVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
19-79 |
7.49e-10 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 61.69 E-value: 7.49e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 966470505 19 DVIEILVNEGDEIDTDTPLITLESEKASMDIPSPKAGKVKEIQVKAGDKVSEGDLILTLEG 79
Cdd:PRK12999 1086 SVVTVLVKEGDEVKAGDPLAVIEAMKMETTITAPVDGTVKRVLVKAGDQVEAGDLLVELEP 1146
|
|
| kgd |
PRK12270 |
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ... |
377-530 |
7.98e-09 |
|
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;
Pssm-ID: 237030 [Multi-domain] Cd Length: 1228 Bit Score: 58.75 E-value: 7.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966470505 377 KALKEFPQFNTSLDESG--ENLIYKKYFNIGIA--VETENG---LVVPVIRDVGQLSVADIAKEMARLSSKARDKGLMPV 449
Cdd:PRK12270 182 QALKAFPNMNRHYAEVDgkPTLVTPAHVNLGLAidLPKKDGsrqLVVPAIKGAETMDFAQFWAAYEDIVRRARDGKLTAD 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966470505 450 EMSGGCFTISSLGGIGGTAFTP-IVNGpEVAILG-----------------LSRSSVKPVydgdkfaprlmLPLSLSYDH 511
Cdd:PRK12270 262 DFQGTTISLTNPGGIGTVHSVPrLMKG-QGAIIGvgameypaefqgaseerLAELGISKV-----------MTLTSTYDH 329
|
170
....*....|....*....
gi 966470505 512 RVIDGAEAARFTRYIAETL 530
Cdd:PRK12270 330 RIIQGAESGEFLRTIHQLL 348
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
136-193 |
1.74e-08 |
|
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the Pathway/BioSystem: Urea cycle
Pssm-ID: 440660 [Multi-domain] Cd Length: 1144 Bit Score: 57.40 E-value: 1.74e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 966470505 136 VIEIMVQSGDKISKDQALITLEGDKATMDIPAPCAGVVDKISMNVGDKVSQGDLILTL 193
Cdd:COG1038 1087 VVKVLVKEGDEVKKGDPLLTIEAMKMETTITAPRDGTVKEVLVKEGDQVEAGDLLIEL 1144
|
|
| PRK05641 |
PRK05641 |
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
20-77 |
3.27e-08 |
|
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235540 [Multi-domain] Cd Length: 153 Bit Score: 52.94 E-value: 3.27e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 966470505 20 VIEILVNEGDEIDTDTPLITLESEKASMDIPSPKAGKVKEIQVKAGDKVSEGDLILTL 77
Cdd:PRK05641 95 ILRILVREGQQVKVGQGLLILEAMKMENEIPAPKDGVVKKILVKEGDTVDTGQPLIEL 152
|
|
| PRK09282 |
PRK09282 |
pyruvate carboxylase subunit B; Validated |
20-79 |
4.68e-08 |
|
pyruvate carboxylase subunit B; Validated
Pssm-ID: 236449 [Multi-domain] Cd Length: 592 Bit Score: 55.62 E-value: 4.68e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 966470505 20 VIEILVNEGDEIDTDTPLITLESEKASMDIPSPKAGKVKEIQVKAGDKVSEGDLILTLEG 79
Cdd:PRK09282 533 VVKVKVKEGDKVKAGDTVLVLEAMKMENEIQAPVDGTVKEILVKEGDRVNPGDVLMEIEP 592
|
|
| PRK08225 |
PRK08225 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
19-78 |
1.91e-07 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 181304 [Multi-domain] Cd Length: 70 Bit Score: 48.24 E-value: 1.91e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 966470505 19 DVIEILVNEGDEIDTDTPLITLESEKASMDIPSPKAGKVKEIQVKAGDKVSEGDLILTLE 78
Cdd:PRK08225 11 NVWKIVVKVGDTVEEGQDVVILESMKMEIPIVAEEAGTVKKINVQEGDFVNEGDVLLEIE 70
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
135-194 |
1.94e-07 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 53.99 E-value: 1.94e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 966470505 135 DVIEIMVQSGDKISKDQALITLEGDKATMDIPAPCAGVVDKISMNVGDKVSQGDLILTLQ 194
Cdd:PRK12999 1086 SVVTVLVKEGDEVKAGDPLAVIEAMKMETTITAPVDGTVKRVLVKAGDQVEAGDLLVELE 1145
|
|
| AccB |
COG0511 |
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ... |
22-78 |
7.33e-07 |
|
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440277 [Multi-domain] Cd Length: 136 Bit Score: 48.35 E-value: 7.33e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 966470505 22 EILVNEGDEIDTDTPLITLESEKASMDIPSPKAGKVKEIQVKAGDKVSEGDLILTLE 78
Cdd:COG0511 80 KPFVKVGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVVEILVENGQPVEYGQPLFVIE 136
|
|
| PRK14042 |
PRK14042 |
pyruvate carboxylase subunit B; Provisional |
40-195 |
1.06e-06 |
|
pyruvate carboxylase subunit B; Provisional
Pssm-ID: 172536 [Multi-domain] Cd Length: 596 Bit Score: 51.26 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966470505 40 LESEKASMDIPSPKAgkvkeIQVKAGDK--VSEGDLILTLEGQEAKSSKEDKstekktekdIESGKKS-------TPSE- 109
Cdd:PRK14042 438 LEQRKNNQLIPEPLL-----TQSSAPDNsvMSEFDIILHGESYHVKVAGYGM---------IEHGQQScflwvdgVPEEv 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966470505 110 --QQEETHEKTEIKEVRIP----DIGGATDVDVIEIMVQSGDKISKDQALITLEGDKATMDIPAPCAGVVDKISMNVGDK 183
Cdd:PRK14042 504 vvQHSELHDKIERSSVNNKigpgDITVAIPGSIIAIHVSAGDEVKAGQAVLVIEAMKMETEIKAPANGVVAEILCQKGDK 583
|
170
....*....|..
gi 966470505 184 VSQGDLILTLQV 195
Cdd:PRK14042 584 VTPGQVLIRVEV 595
|
|
| PRK06549 |
PRK06549 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
20-77 |
1.32e-06 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235826 [Multi-domain] Cd Length: 130 Bit Score: 47.50 E-value: 1.32e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 966470505 20 VIEILVNEGDEIDTDTPLITLESEKASMDIPSPKAGKVKEIQVKAGDKVSEGDLILTL 77
Cdd:PRK06549 72 ILKVLVAVGDQVTENQPLLILEAMKMENEIVASSAGTVTAIHVTPGQVVNPGDGLITI 129
|
|
| PRK14040 |
PRK14040 |
oxaloacetate decarboxylase subunit alpha; |
23-77 |
2.14e-06 |
|
oxaloacetate decarboxylase subunit alpha;
Pssm-ID: 237592 [Multi-domain] Cd Length: 593 Bit Score: 50.31 E-value: 2.14e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 966470505 23 ILVNEGDEIDTDTPLITLESEKASMDIPSPKAGKVKEIQVKAGDKVSEGDLILTL 77
Cdd:PRK14040 538 VIVTEGQTVAEGDVLLILEAMKMETEIRAAQAGTVRGIAVKEGDAVAVGDTLLTL 592
|
|
| RND_mfp |
TIGR01730 |
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ... |
54-194 |
2.51e-06 |
|
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion protein) component of the RND family of transporters. RND refers to Resistance, Nodulation, and cell Division. It is, in part, a subfamily of pfam00529 (Pfam release 7.5) but hits substantial numbers of proteins missed by that model. The related HlyD secretion protein, for which pfam00529 is named, is outside the scope of this model. Attributed functions imply outward transport. These functions include nodulation, acriflavin resistance, heavy metal efflux, and multidrug resistance proteins. Most members of this family are found in Gram-negative bacteria. The proposed function of MFP proteins is to bring the inner and outer membranes together and enable transport to the outside of the outer membrane. Note, however, that a few members of this family are found in Gram-positive bacteria, where there is no outer membrane. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 273776 [Multi-domain] Cd Length: 322 Bit Score: 49.62 E-value: 2.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966470505 54 AGKVKEIQVKAGDKVSEGDLILTLEGQEAKSS-KEDKSTEKKTEKDIESGKKStpSEQQEETHEKTEIKEVripDIGGA- 131
Cdd:TIGR01730 34 AGKITKISVREGQKVKKGQVLARLDDDDYQLAlQAALAQLAAAEAQLELAQRS--FERAERLVKRNAVSQA---DLDDAk 108
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 966470505 132 TDVDVIEIMVQsGDKISKDQALITLegdkATMDIPAPCAGVVDKISMNVGDKVSQGDLILTLQ 194
Cdd:TIGR01730 109 AAVEAAQADLE-AAKASLASAQLNL----RYTEIRAPFDGTIGRRLVEVGAYVTAGQTLATIV 166
|
|
| PRK09282 |
PRK09282 |
pyruvate carboxylase subunit B; Validated |
53-194 |
3.10e-06 |
|
pyruvate carboxylase subunit B; Validated
Pssm-ID: 236449 [Multi-domain] Cd Length: 592 Bit Score: 49.84 E-value: 3.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966470505 53 KAGKVKE--IQVKAGDKVSEG---DLILTLEGQEAKSSKEdkSTEKKTEKDIESGKKSTPSEQQEEthEKTEIKEVRIPD 127
Cdd:PRK09282 443 EAGELKPepEPKEAAAAGAEGiptEFKVEVDGEKYEVKIE--GVKAEGKRPFYLRVDGMPEEVVVE--PLKEIVVGGRPR 518
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 966470505 128 IGGATDV------DVIEIMVQSGDKISKDQALITLEGDKATMDIPAPCAGVVDKISMNVGDKVSQGDLILTLQ 194
Cdd:PRK09282 519 ASAPGAVtspmpgTVVKVKVKEGDKVKAGDTVLVLEAMKMENEIQAPVDGTVKEILVKEGDRVNPGDVLMEIE 591
|
|
| PRK14040 |
PRK14040 |
oxaloacetate decarboxylase subunit alpha; |
139-193 |
1.55e-05 |
|
oxaloacetate decarboxylase subunit alpha;
Pssm-ID: 237592 [Multi-domain] Cd Length: 593 Bit Score: 47.62 E-value: 1.55e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 966470505 139 IMVQSGDKISKDQALITLEGDKATMDIPAPCAGVVDKISMNVGDKVSQGDLILTL 193
Cdd:PRK14040 538 VIVTEGQTVAEGDVLLILEAMKMETEIRAAQAGTVRGIAVKEGDAVAVGDTLLTL 592
|
|
| PRK05641 |
PRK05641 |
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
136-193 |
1.67e-05 |
|
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235540 [Multi-domain] Cd Length: 153 Bit Score: 44.85 E-value: 1.67e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 966470505 136 VIEIMVQSGDKISKDQALITLEGDKATMDIPAPCAGVVDKISMNVGDKVSQGDLILTL 193
Cdd:PRK05641 95 ILRILVREGQQVKVGQGLLILEAMKMENEIPAPKDGVVKKILVKEGDTVDTGQPLIEL 152
|
|
| PRK05889 |
PRK05889 |
biotin/lipoyl-binding carrier protein; |
136-190 |
1.91e-05 |
|
biotin/lipoyl-binding carrier protein;
Pssm-ID: 180306 [Multi-domain] Cd Length: 71 Bit Score: 42.87 E-value: 1.91e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 966470505 136 VIEIMVQSGDKISKDQALITLEGDKATMDIPAPCAGVVDKISMNVGDKVSQGDLI 190
Cdd:PRK05889 13 VLEVVVNEGDQIGKGDTLVLLESMKMEIPVLAEVAGTVSKVSVSVGDVIQAGDLI 67
|
|
| PRK08225 |
PRK08225 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
135-194 |
3.34e-05 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 181304 [Multi-domain] Cd Length: 70 Bit Score: 42.08 E-value: 3.34e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 966470505 135 DVIEIMVQSGDKISKDQALITLEGDKATMDIPAPCAGVVDKISMNVGDKVSQGDLILTLQ 194
Cdd:PRK08225 11 NVWKIVVKVGDTVEEGQDVVILESMKMEIPIVAEEAGTVKKINVQEGDFVNEGDVLLEIE 70
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
122-187 |
4.12e-05 |
|
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases, and the H-protein of the glycine cleavage system (GCS). These domains transport CO2, acyl, or methylamine, respectively, between components of the complex/protein via a biotinyl or lipoyl group, which is covalently attached to a highly conserved lysine residue.
Pssm-ID: 133456 [Multi-domain] Cd Length: 73 Bit Score: 41.66 E-value: 4.12e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 966470505 122 EVRIPDIGGA-TDVDVIEIMVQSGDKISKDQALITLEGDKATMDIPAPCAGVVDKISMNVGDKVSQG 187
Cdd:cd06663 1 TILIPDLAQHlGDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKVEGD 67
|
|
| PRK14042 |
PRK14042 |
pyruvate carboxylase subunit B; Provisional |
5-78 |
4.23e-05 |
|
pyruvate carboxylase subunit B; Provisional
Pssm-ID: 172536 [Multi-domain] Cd Length: 596 Bit Score: 46.25 E-value: 4.23e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 966470505 5 NKIKVPDIGGATNVDVIEILVNEGDEIDTDTPLITLESEKASMDIPSPKAGKVKEIQVKAGDKVSEGDLILTLE 78
Cdd:PRK14042 521 NKIGPGDITVAIPGSIIAIHVSAGDEVKAGQAVLVIEAMKMETEIKAPANGVVAEILCQKGDKVTPGQVLIRVE 594
|
|
| PRK05889 |
PRK05889 |
biotin/lipoyl-binding carrier protein; |
20-74 |
6.77e-05 |
|
biotin/lipoyl-binding carrier protein;
Pssm-ID: 180306 [Multi-domain] Cd Length: 71 Bit Score: 41.33 E-value: 6.77e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 966470505 20 VIEILVNEGDEIDTDTPLITLESEKASMDIPSPKAGKVKEIQVKAGDKVSEGDLI 74
Cdd:PRK05889 13 VLEVVVNEGDQIGKGDTLVLLESMKMEIPVLAEVAGTVSKVSVSVGDVIQAGDLI 67
|
|
| PRK09282 |
PRK09282 |
pyruvate carboxylase subunit B; Validated |
48-158 |
2.05e-04 |
|
pyruvate carboxylase subunit B; Validated
Pssm-ID: 236449 [Multi-domain] Cd Length: 592 Bit Score: 44.06 E-value: 2.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966470505 48 DIPSPKAGKVKEIQVKAGDKVSEGDLILTLEGQeaksskedkstekKTEKDIESGKKSTpseqqeethekteikevripd 127
Cdd:PRK09282 524 AVTSPMPGTVVKVKVKEGDKVKAGDTVLVLEAM-------------KMENEIQAPVDGT--------------------- 569
|
90 100 110
....*....|....*....|....*....|.
gi 966470505 128 iggatdvdVIEIMVQSGDKISKDQALITLEG 158
Cdd:PRK09282 570 --------VKEILVKEGDRVNPGDVLMEIEP 592
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
16-71 |
2.08e-04 |
|
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases, and the H-protein of the glycine cleavage system (GCS). These domains transport CO2, acyl, or methylamine, respectively, between components of the complex/protein via a biotinyl or lipoyl group, which is covalently attached to a highly conserved lysine residue.
Pssm-ID: 133456 [Multi-domain] Cd Length: 73 Bit Score: 39.73 E-value: 2.08e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 966470505 16 TNVDVIEILVNEGDEIDTDTPLITLESEKASMDIPSPKAGKVKEIQVKAGDKVSEG 71
Cdd:cd06663 12 GDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKVEGD 67
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
140-277 |
2.78e-04 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 43.39 E-value: 2.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966470505 140 MVQSGDKISKDQALITLEGDKATMDIPAPCAGVVDKISMNVGDKVSQGDLIltlqvktdkkveieaseetenkkkekeek 219
Cdd:PRK14875 23 LVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGETLPVGALL----------------------------- 73
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 966470505 220 lpttetkseAVKAPVQEKEEAVMLPAGPAVRKIAREfGVDLGKVKGTGRKSRITKEDI 277
Cdd:PRK14875 74 ---------AVVADAEVSDAEIDAFIAPFARRFAPE-GIDEEDAGPAPRKARIGGRTV 121
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
49-78 |
4.05e-04 |
|
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all biotin-dependent enzymes, such as acetyl-CoA carboxylase, pyruvate carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA carboxylase, geranyl-CoA carboxylase, oxaloacetate decarboxylase, methylmalonyl-CoA decarboxylase, transcarboxylase and urea amidolyase. This domain functions in transferring CO2 from one subsite to another, allowing carboxylation, decarboxylation, or transcarboxylation. During this process, biotin is covalently attached to a specific lysine.
Pssm-ID: 133459 [Multi-domain] Cd Length: 67 Bit Score: 38.94 E-value: 4.05e-04
10 20 30
....*....|....*....|....*....|
gi 966470505 49 IPSPKAGKVKEIQVKAGDKVSEGDLILTLE 78
Cdd:cd06850 2 VTAPMPGTVVKVLVKEGDKVEAGQPLAVLE 31
|
|
| Biotin_lipoyl_2 |
pfam13533 |
Biotin-lipoyl like; |
49-81 |
6.79e-04 |
|
Biotin-lipoyl like;
Pssm-ID: 433286 Cd Length: 50 Bit Score: 37.81 E-value: 6.79e-04
10 20 30
....*....|....*....|....*....|...
gi 966470505 49 IPSPKAGKVKEIQVKAGDKVSEGDLILTLEGQE 81
Cdd:pfam13533 5 IASPVSGKVVAVNVKEGQQVKKGDVLATLDSPE 37
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
43-78 |
7.50e-04 |
|
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the Pathway/BioSystem: Urea cycle
Pssm-ID: 440660 [Multi-domain] Cd Length: 1144 Bit Score: 42.37 E-value: 7.50e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 966470505 43 EKASMD----IPSPKAGKVKEIQVKAGDKVSEGDLILTLE 78
Cdd:COG1038 1069 EKADPGnpghIGAPMPGTVVKVLVKEGDEVKKGDPLLTIE 1108
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
48-205 |
1.06e-03 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 41.19 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966470505 48 DIPSPKAGKVKEIQVKAGDKVSEGDLILTLEGQEAKSSKEDKSTEKKTEKDIESGKKSTPSEQQEETHEKTEIKEVRI-- 125
Cdd:COG1566 47 TVAAKVSGRVTEVLVKEGDRVKKGQVLARLDPTDLQAALAQAEAQLAAAEAQLARLEAELGAEAEIAAAEAQLAAAQAql 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966470505 126 ---------------PDIGGATDVD---------------------VIEIMVQSGDKISKDQA--------LITLEGDKA 161
Cdd:COG1566 127 dlaqreleryqalykKGAVSQQELDearaaldaaqaqleaaqaqlaQAQAGLREEEELAAAQAqvaqaeaaLAQAELNLA 206
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 966470505 162 TMDIPAPCAGVVDKISMNVGDKVSQGDLILTLqVKTDkKVEIEA 205
Cdd:COG1566 207 RTTIRAPVDGVVTNLNVEPGEVVSAGQPLLTI-VPLD-DLWVEA 248
|
|
| GCS_H |
cd06848 |
Glycine cleavage H-protein. Glycine cleavage H-proteins are part of the glycine cleavage ... |
24-60 |
1.63e-03 |
|
Glycine cleavage H-protein. Glycine cleavage H-proteins are part of the glycine cleavage system (GCS) found in bacteria, archea and the mitochondria of eukaryotes. GCS is a multienzyme complex consisting of 4 different components (P-, H-, T- and L-proteins) which catalyzes the oxidative cleavage of glycine. The H-protein shuttles the methylamine group of glycine from the P-protein (glycine dehydrogenase) to the T-protein (aminomethyltransferase) via a lipoyl group, attached to a completely conserved lysine residue.
Pssm-ID: 133457 [Multi-domain] Cd Length: 96 Bit Score: 37.90 E-value: 1.63e-03
10 20 30
....*....|....*....|....*....|....*..
gi 966470505 24 LVNEGDEIDTDTPLITLESEKASMDIPSPKAGKVKEI 60
Cdd:cd06848 36 LPEVGTEVKKGDPFGSVESVKAASDLYSPVSGEVVEV 72
|
|
| CatA |
COG4845 |
Chloramphenicol O-acetyltransferase [Defense mechanisms]; |
334-522 |
1.91e-03 |
|
Chloramphenicol O-acetyltransferase [Defense mechanisms];
Pssm-ID: 443873 Cd Length: 210 Bit Score: 39.83 E-value: 1.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966470505 334 PHVTQFDEADITELEsfrkteqEKAKKAGYKLTvlAFVCKVVSKALKEFPQFNTSLDesGENLIYKKYFNIGIAV----- 408
Cdd:COG4845 26 PTFSITVELDVTALY-------KYAKKNGLSFF--PAYLYAILKAVNEIPEFRYRIE--DGEVVEYDVIHPSFTIfhked 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966470505 409 ETENGLVVPVIRDVGQLSvADIAKEMARLsskARDKGLMPVEMSG-GCFTISSLGGIGGTAFTPIVNGpevailglsrss 487
Cdd:COG4845 95 ETFSFVWIPYDEDFETFY-ANYLEDIERY---KNSTGLFPKEGNPdNLFYISCLPWLSFTSFSHAIPG------------ 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 966470505 488 vkpvyDGDKFAP------------RLMLPLSLSYDHRVIDGAEAARF 522
Cdd:COG4845 159 -----NPDDSIPiitfgkyyeengRLLMPVSIQVHHALVDGYHVGRF 200
|
|
| AccB |
COG0511 |
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ... |
138-194 |
3.38e-03 |
|
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440277 [Multi-domain] Cd Length: 136 Bit Score: 37.95 E-value: 3.38e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 966470505 138 EIMVQSGDKISKDQALITLEGDKATMDIPAPCAGVVDKISMNVGDKVSQGDLILTLQ 194
Cdd:COG0511 80 KPFVKVGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVVEILVENGQPVEYGQPLFVIE 136
|
|
| GcvH |
COG0509 |
Glycine cleavage system protein H (lipoate-binding) [Amino acid transport and metabolism]; ... |
24-60 |
7.39e-03 |
|
Glycine cleavage system protein H (lipoate-binding) [Amino acid transport and metabolism]; Glycine cleavage system protein H (lipoate-binding) is part of the Pathway/BioSystem: Glycine cleavage
Pssm-ID: 440275 Cd Length: 128 Bit Score: 36.64 E-value: 7.39e-03
10 20 30
....*....|....*....|....*....|....*..
gi 966470505 24 LVNEGDEIDTDTPLITLESEKASMDIPSPKAGKVKEI 60
Cdd:COG0509 44 LPEVGTEVEAGEPFGVVESVKAVSDLYAPVSGEVVEV 80
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
43-78 |
9.54e-03 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 38.97 E-value: 9.54e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 966470505 43 EKA----SMDIPSPKAGKVKEIQVKAGDKVSEGDLILTLE 78
Cdd:PRK12999 1069 EKAdpgnPGHVGAPMPGSVVTVLVKEGDEVKAGDPLAVIE 1108
|
|
| |
