|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11856 |
PRK11856 |
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed |
5-454 |
5.00e-131 |
|
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
Pssm-ID: 237001 [Multi-domain] Cd Length: 411 Bit Score: 384.53 E-value: 5.00e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096876122 5 KTFNLPDLGEGLPDATIVEWFVKEGDVIRLDEPLVSMETAKAVVEVPSPVSGKVLKLAGGAGDVVVTGSMLAVFqpdpnl 84
Cdd:PRK11856 3 FEFKMPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDVVPVGSVIAVI------ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096876122 85 pqRAEGQDTGhhhgpakahapepapaaAAPAPAPAAPETERDDAGTVVGAMQTSNAVHTEQAVAVGGVKAMPAVRAMAKK 164
Cdd:PRK11856 77 --EEEGEAEA-----------------AAAAEAAPEAPAPEPAPAAAAAAAAAPAAAAAPAAPAAAAAKASPAVRKLARE 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096876122 165 LGVDLARVRATGADGAVTMADVKQAAADGSaragaapaapvraavaeatpapapavaqrTTLSASGKPMRTQPPGVAVTG 244
Cdd:PRK11856 138 LGVDLSTVKGSGPGGRITKEDVEAAAAAAA-----------------------------PAAAAAAAAAAAPPAAAAEGE 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096876122 245 QPEQLKGVRRNMARVMADAHAKVVPTTLSDDADVHAW----------TPGNDVTVRLIRAIVRACKAVPAMNAWFDGDKL 314
Cdd:PRK11856 189 ERVPLSGMRKAIAKRMVESKREIPHFTLTDEVDVTALlalrkqlkaiGVKLTVTDFLIKAVALALKKFPELNASWDDDAI 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096876122 315 TRtlHPQVDVGIAVDTDDGLFVPALRNADILDARGVREGINRLRAQVEDRSIPASELSGYTISLSNFGMFAGRYATPVVV 394
Cdd:PRK11856 269 VL--KKYVNIGIAVATDGGLIVPVIRDADKKSLFELAREIKDLAEKAREGKLKPEELQGGTFTISNLGMFGGDYFTPIIN 346
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096876122 395 PPCVAIVAAGRARHQVTPVMGGFESHKIIPLSVTFDHRACTGGEAARFLKALIDDLALPA 454
Cdd:PRK11856 347 PPEVAILGVGAIVERPVVVDGEIVVRKVMPLSLSFDHRVIDGADAARFLKALKELLENPA 406
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
7-444 |
2.97e-60 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 205.83 E-value: 2.97e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096876122 7 FNLPDLGEgLPDATIVEWFVKEGDVIRLDEPLVSMETAKAVVEVPSPVSGKVLKLAGGAGDVVVTGSMLAVFQPDPNLPQ 86
Cdd:PRK11855 122 VKVPDIGE-ITEVEVIEWLVKVGDTVEEDQSLITVETDKATMEIPSPVAGVVKEIKVKVGDKVSVGSLLVVIEVAAAAPA 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096876122 87 RAEGQdtghhhgpakahapepapaaaapAPAPAAPETERDDAGTVVGAMQTSNAVHTEQAVAVGGVKAMPAVRAMAKKLG 166
Cdd:PRK11855 201 AAAAP-----------------------AAAAPAAAAAAAPAPAPAAAAAPAAAAPAAAAAPGKAPHASPAVRRLARELG 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096876122 167 VDLARVRATGADGAVTMADVkQAAADGSARAGAAPAAPVraavaeatpapapavaqrttlSASGKPMRTQPPGVAV---- 242
Cdd:PRK11855 258 VDLSQVKGTGKKGRITKEDV-QAFVKGAMSAAAAAAAAA---------------------AAAGGGGLGLLPWPKVdfsk 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096876122 243 --TGQPEQLKGVRRNMARVMadaHAKVVPT---TLSDDADV------------HAWTPGNDVTVR--LIRAIVRACKAVP 303
Cdd:PRK11855 316 fgEIETKPLSRIKKISAANL---HRSWVTIphvTQFDEADItdlealrkqlkkEAEKAGVKLTMLpfFIKAVVAALKEFP 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096876122 304 AMNAWFDGDKLTRTLHPQVDVGIAVDTDDGLFVPALRNADILDARGVREGINRLRAQVEDRSIPASELSGYTISLSNFGM 383
Cdd:PRK11855 393 VFNASLDEDGDELTYKKYFNIGFAVDTPNGLVVPVIKDVDKKSLLEIAREIAELAKKARDGKLKPDDMQGGCFTISSLGG 472
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2096876122 384 FAGRYATPVVVPPCVAIVAAGRArhQVTPVMGG--FESHKIIPLSVTFDHRACTGGEAARFLK 444
Cdd:PRK11855 473 IGGTAFTPIINAPEVAILGVGKS--QMKPVWDGkeFVPRLMLPLSLSYDHRVIDGATAARFTN 533
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
260-448 |
4.67e-54 |
|
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: 179.66 E-value: 4.67e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096876122 260 MADAHAKVVPTTLSDDADV------------HAWTPGNDVTV--RLIRAIVRACKAVPAMNAWFDGDKLTRTLHPQVDVG 325
Cdd:pfam00198 1 MTESKQTIPHFTLTDEVDVtellalreelkeDAADEETKLTFlpFLVKAVALALKKFPELNASWDGEEGEIVYKKYVNIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096876122 326 IAVDTDDGLFVPALRNADILDARGVREGINRLRAQVEDRSIPASELSGYTISLSNFGMFAGRYATPVVVPPCVAIVAAGR 405
Cdd:pfam00198 81 IAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVGR 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2096876122 406 ARHQVTPVMGGFESHKIIPLSVTFDHRACTGGEAARFLKALID 448
Cdd:pfam00198 161 IRKRPVVVDGEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKE 203
|
|
| PLN02528 |
PLN02528 |
2-oxoisovalerate dehydrogenase E2 component |
7-442 |
1.18e-46 |
|
2-oxoisovalerate dehydrogenase E2 component
Pssm-ID: 215289 [Multi-domain] Cd Length: 416 Bit Score: 166.43 E-value: 1.18e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096876122 7 FNLPDLGEGLPDATIVEWFVKEGDVIRLDEPLVSMETAKAVVEVPSPVSGKVLKLAGGAGDVVVTGSMLavfqpdpnLPQ 86
Cdd:PLN02528 1 VPLAQTGEGIAECELLRWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGKVAQINFSPGDIVKVGETL--------LKI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096876122 87 RAEGQDTghhhgpakahapepapaaaapapapaapETERDDAGTVVGAMQTSNAVHTEQAVAVGGVKAMPAVRAMAKKLG 166
Cdd:PLN02528 73 MVEDSQH----------------------------LRSDSLLLPTDSSNIVSLAESDERGSNLSGVLSTPAVRHLAKQYG 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096876122 167 VDLARVRATGADGAVTMADV-KQAAADGsaragaapaapvraavaeatpapAPAVAQRTTLSASGKPMRTQPPGVAVTGQ 245
Cdd:PLN02528 125 IDLNDILGTGKDGRVLKEDVlKYAAQKG-----------------------VVKDSSSAEEATIAEQEEFSTSVSTPTEQ 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096876122 246 PEQ-----LKGVRRNMARVMADAhAKVVPTTLSDDADVHAWT-------PGN-DVTVR------LIRAIVRACKAVPAMN 306
Cdd:PLN02528 182 SYEdktipLRGFQRAMVKTMTAA-AKVPHFHYVEEINVDALVelkasfqENNtDPTVKhtflpfLIKSLSMALSKYPLLN 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096876122 307 AWFDGDKLTRTLHPQVDVGIAVDTDDGLFVPALRNADILDARGVREGINRLRAQVEDRSIPASELSGYTISLSNFGMFAG 386
Cdd:PLN02528 261 SCFNEETSEIRLKGSHNIGVAMATEHGLVVPNIKNVQSLSLLEITKELSRLQHLAAENKLNPEDITGGTITLSNIGAIGG 340
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 2096876122 387 RYATPVVVPPCVAIVAAGRARHQVTPVMGGF-ESHKIIPLSVTFDHRACTGGEAARF 442
Cdd:PLN02528 341 KFGSPVLNLPEVAIIALGRIQKVPRFVDDGNvYPASIMTVTIGADHRVLDGATVARF 397
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
2-451 |
7.94e-40 |
|
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: 150.41 E-value: 7.94e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096876122 2 SDSKTFNLPDLGeGLPDATIVEWFVKEGDVIRLDEPLVSMETAKAVVEVPSPVSGKVLKLAGGAGDVVVTGSMLAVFQPD 81
Cdd:TIGR01348 114 SGVQEVTVPDIG-DIEKVTVIEVLVKVGDTVSADQSLITLESDKASMEVPAPASGVVKSVKVKVGDSVPTGDLILTLSVA 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096876122 82 PNLPQRAEgqdtghhhgpakahapepapAAAAPAPAPAAPETERDDAGTVVGAMQTSNAVhTEQAVAVGGVK---AMPAV 158
Cdd:TIGR01348 193 GSTPATAP--------------------APASAQPAAQSPAATQPEPAAAPAAAKAQAPA-PQQAGTQNPAKvdhAAPAV 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096876122 159 RAMAKKLGVDLARVRATGADGAVTMADVKQAAADGSARAGAAPAApvraavaeatpapapavaqrttlSASGKPMRTQPP 238
Cdd:TIGR01348 252 RRLAREFGVDLSAVKGTGIKGRILREDVQRFVKEPSVRAQAAAAS-----------------------AAGGAPGALPWP 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096876122 239 GVAV----TGQPEQLKGVRRNMARVMADAHAKVVPTTLSDDADVHAWTPGN--------------DVTVRLIRAIVRACK 300
Cdd:TIGR01348 309 NVDFskfgEVEEVDMSRIRKISGANLTRNWTMIPHVTHFDKADITEMEAFRkqqnaavekegvklTVLHILMKAVAAALK 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096876122 301 AVPAMNAWFDGDKLTRTLHPQVDVGIAVDTDDGLFVPALRNADildargvREGINRLRAQV-------EDRSIPASELSG 373
Cdd:TIGR01348 389 KFPKFNASLDLGGEQLILKKYVNIGVAVDTPNGLLVPVIKDVD-------RKGITELALELsdlakkaRDGKLTPDEMQG 461
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096876122 374 YTISLSNFGMFAGRYATPVVVPPCVAIVAAGRARHQvtPVMGG--FESHKIIPLSVTFDHRACTGGEAARFLKALIDDLA 451
Cdd:TIGR01348 462 ACFTISSLGGIGGTAFTPIVNAPEVAILGVSKSGME--PVWNGkeFEPRLMLPLSLSYDHRVIDGADAARFTTYICESLA 539
|
|
| SucB_Actino |
TIGR02927 |
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model ... |
9-450 |
3.84e-38 |
|
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: 145.93 E-value: 3.84e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096876122 9 LPDLGEGLPDATIVEWFVKEGDVIRLDEPLVSMETAKAVVEVPSPVSGKVLKLAGGAGDVVVTGSMLAVF-----QPDPN 83
Cdd:TIGR02927 131 MPELGESVTEGTVTSWLKAVGDTVEVDEPLLEVSTDKVDTEIPSPVAGTLLEIRAPEDDTVEVGTVLAIIgdanaAPAEP 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096876122 84 LPQRAEGQDtghhhgpakahapEPAPAAAAPAPAPAAPETERDDAGTVVGAMQTSNAVHTEQAVAVGGVKAMPAVRAMAK 163
Cdd:TIGR02927 211 AEEEAPAPS-------------EAGSEPAPDPAARAPHAAPDPPAPAPAPAKTAAPAAAAPVSSGDSGPYVTPLVRKLAK 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096876122 164 KLGVDLARVRATGADGAVTMADVKQAAADGSARAGAAPAAPVRAAVAEATPAPAPAVAQRTTLSASGKPM--------RT 235
Cdd:TIGR02927 278 DKGVDLSTVKGTGVGGRIRKQDVLAAAKAAEEARAAAAAPAAAAAPAAPAAAAKPAEPDTAKLRGTTQKMnrirqitaDK 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096876122 236 QPPGVAVTGQPEQLKGVrrNMARVmADAHAKVVPTTLSDDADVHAWTPgndvtvRLIRAIVRACKAVPAMNAWFDGDKLT 315
Cdd:TIGR02927 358 TIESLQTSAQLTQVHEV--DMTRV-AALRARAKNDFLEKNGVNLTFLP------FFVQAVTEALKAHPNVNASYNAETKE 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096876122 316 RTLHPQVDVGIAVDTDDGLFVPALRNADILDARGVREGINRLRAQVEDRSIPASELSGYTISLSNFGMFAGRYATPVVVP 395
Cdd:TIGR02927 429 VTYHDVEHVGIAVDTPRGLLVPVIHNAGDLSLPGLAKAINDLAARARDNKLKPDELSGGTFTITNIGSGGALFDTPILNP 508
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096876122 396 PCVAIVAAG--RARHQVTPVMGGFES---HKIIPLSVTFDHRACTGGEAARFLKALIDDL 450
Cdd:TIGR02927 509 PQAAILGTGaiVKRPRVIKDEDGGESiaiRSVCYLPLTYDHRLVDGADAGRFLTTIKKRL 568
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
2-451 |
1.20e-37 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 145.15 E-value: 1.20e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096876122 2 SDSKTFNLPDLGEGlpDATIVEWFVKEGDVIRLDEPLVSMETAKAVVEVPSPVSGKVLKLAGGAGDVVVTGSMLAVFQPD 81
Cdd:PRK11854 204 AGVKDVNVPDIGGD--EVEVTEVMVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVKTGSLIMRFEVE 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096876122 82 PNLPQRAEgqdtghhhgpakahAPEPAPAAAAPAPAPAAPETERDDAGTVVGAMQTSNAVhteqavavggVKAMPAVRAM 161
Cdd:PRK11854 282 GAAPAAAP--------------AKQEAAAPAPAAAKAEAPAAAPAAKAEGKSEFAENDAY----------VHATPLVRRL 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096876122 162 AKKLGVDLARVRATGADGAVTMADVKQAAADGSARAGAAPaapvraavaeatpapapavaqrTTLSASGKPMRTQP-PGV 240
Cdd:PRK11854 338 AREFGVNLAKVKGTGRKGRILKEDVQAYVKDAVKRAEAAP----------------------AAAAAGGGGPGLLPwPKV 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096876122 241 AVTGQPE----QLKGVRRNMARVMADAHAKVVPTTLSDDADV------------HAWTPGNDVT----VRLIRAIVRACK 300
Cdd:PRK11854 396 DFSKFGEieevELGRIQKISGANLHRNWVMIPHVTQFDKADIteleafrkqqnaEAEKRKLGVKitplVFIMKAVAAALE 475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096876122 301 AVPAMNAWFDGDKLTRTLHPQVDVGIAVDTDDGLFVPALRNAdilDARGVREgINRLRAQVEDRS----IPASELSGYTI 376
Cdd:PRK11854 476 QMPRFNSSLSEDGQRLTLKKYVNIGIAVDTPNGLVVPVFKDV---NKKGIIE-LSRELMDISKKArdgkLTAGDMQGGCF 551
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2096876122 377 SLSNFGMFAGRYATPVVVPPCVAIVAAGRArhQVTPVMGG--FESHKIIPLSVTFDHRACTGGEAARFLKALIDDLA 451
Cdd:PRK11854 552 TISSIGGLGTTHFTPIVNAPEVAILGVSKS--AMEPVWNGkeFAPRLMLPLSLSYDHRVIDGADGARFITIINDRLS 626
|
|
| sucB |
TIGR01347 |
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ... |
8-449 |
6.18e-37 |
|
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: 139.87 E-value: 6.18e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096876122 8 NLPDLGEGLPDATIVEWFVKEGDVIRLDEPLVSMETAKAVVEVPSPVSGKVLKLAGGAGDVVVTGSMLAVFqpdpnlpqr 87
Cdd:TIGR01347 4 KVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAIL--------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096876122 88 AEGQDTGHHhgpakahapepapaaaapapapAAPETERDDAGTVVgamqtsNAVHTEQAVAVGGVKAMPAVRAMAKKLGV 167
Cdd:TIGR01347 75 EEGNDATAA----------------------PPAKSGEEKEETPA------ASAAAAPTAAANRPSLSPAARRLAKEHGI 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096876122 168 DLARVRATGADGAVTMADV-KQAAADGSARAGAAPAAPVRAAVAEATPAPAPAVAQRTTLSasgkpmrtqppgvavtgqp 246
Cdd:TIGR01347 127 DLSAVPGTGVTGRVTKEDIiKKTEAPASAQPPAAAAAAAAPAAATRPEERVKMTRLRQRIA------------------- 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096876122 247 EQLKGVRRNMArvMADAHAKVVPTTLSDDADVHAWTPGNDVTVRL------IRAIVRACKAVPAMNAWFDGDKLtrTLHP 320
Cdd:TIGR01347 188 ERLKEAQNSTA--MLTTFNEVDMSAVMELRKRYKEEFEKKHGVKLgfmsffVKAVVAALKRFPEVNAEIDGDDI--VYKD 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096876122 321 QVDVGIAVDTDDGLFVPALRNADILDARGVREGINRLRAQVEDRSIPASELSGYTISLSNFGMFAGRYATPVVVPPCVAI 400
Cdd:TIGR01347 264 YYDISVAVSTDRGLVVPVVRNADRMSFADIEKEIADLGKKARDGKLTLEDMTGGTFTITNGGVFGSLMSTPIINPPQSAI 343
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 2096876122 401 VAAGRARHQVTPVMGGFESHKIIPLSVTFDHRACTGGEAARFL---KALIDD 449
Cdd:TIGR01347 344 LGMHGIKERPVAVNGQIEIRPMMYLALSYDHRLIDGKEAVTFLvtiKELLED 395
|
|
| PRK05704 |
PRK05704 |
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase; |
10-454 |
1.97e-34 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
Pssm-ID: 235571 [Multi-domain] Cd Length: 407 Bit Score: 133.04 E-value: 1.97e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096876122 10 PDLGEGLPDATIVEWFVKEGDVIRLDEPLVSMETAKAVVEVPSPVSGKVLKLAGGAGDVVVTGSMLAVFqpdpnlpqrAE 89
Cdd:PRK05704 8 PTLPESVTEATIATWHKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGDTVTVGQVLGRI---------DE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096876122 90 GQDTGhhhgpakahapepapaaaapapaPAAPETERDDAGTVVGAMQTSNAVHTEQAVAvggvkAMPAVRAMAKKLGVDL 169
Cdd:PRK05704 79 GAAAG-----------------------AAAAAAAAAAAAAAAPAQAQAAAAAEQSNDA-----LSPAARKLAAENGLDA 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096876122 170 ARVRATGADGAVTMADVKQAAAdgsaRAGAAPAAPVRAAVAEATPAPAPAVAQRTtlsasgkPMRTQPPGVAvtgqpEQL 249
Cdd:PRK05704 131 SAVKGTGKGGRVTKEDVLAALA----AAAAAPAAPAAAAPAAAPAPLGARPEERV-------PMTRLRKTIA-----ERL 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096876122 250 KGVRR-----------NMARVMA------DAHAKvvpttlsddadVHAwtpgndvtVRL------IRAIVRACKAVPAMN 306
Cdd:PRK05704 195 LEAQNttamlttfnevDMTPVMDlrkqykDAFEK-----------KHG--------VKLgfmsffVKAVVEALKRYPEVN 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096876122 307 AWFDGDKLtrTLHPQVDVGIAVDTDDGLFVPALRNADILDARGVREGINRLRAQVEDRSIPASELSGYTISLSNFGMFAG 386
Cdd:PRK05704 256 ASIDGDDI--VYHNYYDIGIAVGTPRGLVVPVLRDADQLSFAEIEKKIAELAKKARDGKLSIEELTGGTFTITNGGVFGS 333
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096876122 387 RYATPVVVPPCVAIVaaGRARHQVTPVM--GGFESHKIIPLSVTFDHRACTGGEAARFLKALIDDLALPA 454
Cdd:PRK05704 334 LMSTPIINPPQSAIL--GMHKIKERPVAvnGQIVIRPMMYLALSYDHRIIDGKEAVGFLVTIKELLEDPE 401
|
|
| PRK11857 |
PRK11857 |
dihydrolipoamide acetyltransferase; Reviewed |
152-442 |
1.87e-26 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237002 [Multi-domain] Cd Length: 306 Bit Score: 108.73 E-value: 1.87e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096876122 152 VKAMPAVRAMAKKLGVDLARVRATGADGAVTMADVKQAAADgsaragaapaapvraavaeatPAPAPAVAQRTTLSASGK 231
Cdd:PRK11857 2 ILATPIARALAKKLGIDISLLKGSGRDGKILAEDVENFIKS---------------------LKSAPTPAEAASVSSAQQ 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096876122 232 PMRTQPPGVA---VTGQPEQLKGVRRNMARVMADAHAKVVPTTLSDDADVHA-W------------TPGNDVTVR--LIR 293
Cdd:PRK11857 61 AAKTAAPAAAppkLEGKREKVAPIRKAIARAMTNSWSNVAYVNLVNEIDMTKlWdlrksvkdpvlkTEGVKLTFLpfIAK 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096876122 294 AIVRACKAVPAMNAWFDGDKLTRTLHPQVDVGIAVDTDDGLFVPALRNADILDARGVREGINRLRAQVEDRSIPASELSG 373
Cdd:PRK11857 141 AILIALKEFPIFAAKYDEATSELVYPDTLNLGIAVDTEAGLMVPVIKNAQKLSIVEIAKEISRLAKAARERKIKPDEMKG 220
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2096876122 374 YTISLSNFGMFAGRYATPVVVPPCVAIVAAGRARHQVTPVMGGFESHKIIPLSVTFDHRACTGGEAARF 442
Cdd:PRK11857 221 GSFTITNYGSVGSLYGVPVINYPELAIAGVGAIIDKAIVKNGQIVAGKVMHLTVAADHRWIDGATIGRF 289
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
4-78 |
1.28e-24 |
|
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: 96.67 E-value: 1.28e-24
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2096876122 4 SKTFNLPDLGEGLPDATIVEWFVKEGDVIRLDEPLVSMETAKAVVEVPSPVSGKVLKLAGGAGDVVVTGSMLAVF 78
Cdd:COG0508 2 AIEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
5-78 |
1.40e-23 |
|
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: 93.62 E-value: 1.40e-23
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2096876122 5 KTFNLPDLGEGLPDATIVEWFVKEGDVIRLDEPLVSMETAKAVVEVPSPVSGKVLKLAGGAGDVVVTGSMLAVF 78
Cdd:cd06849 1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
|
|
| PTZ00144 |
PTZ00144 |
dihydrolipoamide succinyltransferase; Provisional |
3-452 |
6.35e-21 |
|
dihydrolipoamide succinyltransferase; Provisional
Pssm-ID: 240289 [Multi-domain] Cd Length: 418 Bit Score: 94.36 E-value: 6.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096876122 3 DSKTFNLPDLGEGLPDATIVEWFVKEGDVIRLDEPLVSMETAKAVVEVPSPVSGKVLKLAGGAGDVVVTGSMLAVFQPDP 82
Cdd:PTZ00144 43 SIKVIKVPTMGDSISEGTVVEWKKKVGDYVKEDEVICIIETDKVSVDIRAPASGVITKIFAEEGDTVEVGAPLSEIDTGG 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096876122 83 NLPQRAegqdtghhhgpakahapepaPAAAAPAPAPAAPETERDDAGTVVGAMQTSNAVHTEQAVAVggvKAMPAVRAMA 162
Cdd:PTZ00144 123 APPAAA--------------------PAAAAAAKAEKTTPEKPKAAAPTPEPPAASKPTPPAAAKPP---EPAPAAKPPP 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096876122 163 KKLGVDLARVRAtgadgaVTMADVKQAAADgsaragaapaapvraavaeatpapapavaqrtTLSASgkpmrtQPPGVAV 242
Cdd:PTZ00144 180 TPVARADPRETR------VPMSRMRQRIAE--------------------------------RLKAS------QNTCAML 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096876122 243 TGQPEQlkgvrrNMARVMAdahakvVPTTLSDDadvhaWTPGNDVTVRLIRAIVRAC----KAVPAMNAWFDGDKLTrtL 318
Cdd:PTZ00144 216 TTFNEC------DMSALME------LRKEYKDD-----FQKKHGVKLGFMSAFVKAStialKKMPIVNAYIDGDEIV--Y 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096876122 319 HPQVDVGIAVDTDDGLFVPALRNADILDARGVREGINRLRAQVEDRSIPASELSGYTISLSNFGMFAGRYATPVVVPPCV 398
Cdd:PTZ00144 277 RNYVDISVAVATPTGLVVPVIRNCENKSFAEIEKELADLAEKARNNKLTLEDMTGGTFTISNGGVFGSLMGTPIINPPQS 356
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2096876122 399 AIVAAgrarHQVT--PVMGGFE--SHKIIPLSVTFDHRACTGGEAARFLKA---LIDDLAL 452
Cdd:PTZ00144 357 AILGM----HAIKkrPVVVGNEivIRPIMYLALTYDHRLIDGRDAVTFLKKikdLIEDPAR 413
|
|
| PLN02226 |
PLN02226 |
2-oxoglutarate dehydrogenase E2 component |
291-453 |
2.23e-17 |
|
2-oxoglutarate dehydrogenase E2 component
Pssm-ID: 177871 [Multi-domain] Cd Length: 463 Bit Score: 84.04 E-value: 2.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096876122 291 LIRAIVRACKAVPAMNAWFDGDKLTrtLHPQVDVGIAVDTDDGLFVPALRNADILDARGVREGINRLRAQVEDRSIPASE 370
Cdd:PLN02226 296 FIKAAVSALQHQPVVNAVIDGDDII--YRDYVDISIAVGTSKGLVVPVIRGADKMNFAEIEKTINGLAKKANEGTISIDE 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096876122 371 LSGYTISLSNFGMFAGRYATPVVVPPCVAIVAAGRARHQVTPVMGGFESHKIIPLSVTFDHRACTGGEAARFLKALIDDL 450
Cdd:PLN02226 374 MAGGSFTVSNGGVYGSLISTPIINPPQSAILGMHSIVSRPMVVGGSVVPRPMMYVALTYDHRLIDGREAVYFLRRVKDVV 453
|
...
gi 2096876122 451 ALP 453
Cdd:PLN02226 454 EDP 456
|
|
| PLN02744 |
PLN02744 |
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex |
9-445 |
1.38e-16 |
|
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
Pssm-ID: 215397 [Multi-domain] Cd Length: 539 Bit Score: 81.82 E-value: 1.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096876122 9 LPDLGEGLPDATIVEWFVKEGDVIRLDEPLVSMETAKAVVEVPSPVSGKVLKL--AGGAGDVVVtGSMLAVfqpdpnlpQ 86
Cdd:PLN02744 117 MPSLSPTMTEGNIARWLKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIvkGDGAKEIKV-GEVIAI--------T 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096876122 87 RAEGQDTGHHHGPAKAHAPEPAPAAAAPAPAPAAPETERDDAGTvvgamQTSNAVHTEQAVAVGG-VKAMPAVRAMAKKL 165
Cdd:PLN02744 188 VEEEEDIGKFKDYKPSSSAAPAAPKAKPSPPPPKEEEVEKPASS-----PEPKASKPSAPPSSGDrIFASPLARKLAEDN 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096876122 166 GVDLARVRATGADGAVTMADVKQAAAdgsaragaapaapvraavaeatpapapavaQRTTLSASGKPMRTQPPGVAVTGQ 245
Cdd:PLN02744 263 NVPLSSIKGTGPDGRIVKADIEDYLA------------------------------SGGKGATAPPSTDSKAPALDYTDI 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096876122 246 PEQlkGVRRNMARVMADAHAKVVPTTLSDDADVHAW-------------TPGNDVTVR--LIRAIVRACKAVPAMNA-WF 309
Cdd:PLN02744 313 PNT--QIRKVTASRLLQSKQTIPHYYLTVDTRVDKLmalrsqlnslqeaSGGKKISVNdlVIKAAALALRKVPQCNSsWT 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096876122 310 DgdKLTRTLHpQVDVGIAVDTDDGLFVPALRNADILDARGVREGINRLRAQVEDRSIPASELSGYTISLSNFG-MFAGRY 388
Cdd:PLN02744 391 D--DYIRQYH-NVNINVAVQTENGLYVPVVKDADKKGLSTIAEEVKQLAQKARENSLKPEDYEGGTFTVSNLGgPFGIKQ 467
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 2096876122 389 ATPVVVPPCVAIVAAGRARHQVTP--VMGGFESHKIIPLSVTFDHRACTGGEAARFLKA 445
Cdd:PLN02744 468 FCAIINPPQSAILAVGSAEKRVIPgsGPDQYNFASFMSVTLSCDHRVIDGAIGAEWLKA 526
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
5-78 |
1.68e-14 |
|
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: 68.01 E-value: 1.68e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2096876122 5 KTFNLPDLGEGLpDATIVEWFVKEGDVIRLDEPLVSMETAKAVVEVPSPVSGKVLKLAGGAGDVVVTGSMLAVF 78
Cdd:pfam00364 1 TEIKSPMIGESV-REGVVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
|
|
| PRK14843 |
PRK14843 |
dihydrolipoamide acetyltransferase; Provisional |
152-449 |
1.03e-13 |
|
dihydrolipoamide acetyltransferase; Provisional
Pssm-ID: 184847 [Multi-domain] Cd Length: 347 Bit Score: 72.25 E-value: 1.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096876122 152 VKAMPAVRAMAKKLGVDLARVRATGADGAVTMADV---------------KQAAADGSARAGAAPAAPVRAAVAEATPAP 216
Cdd:PRK14843 6 LRATPAARKLADDLGINLYDVSGSGANGRVHKEDVetykdtnvvrisplaKRIALEHNIAWQEIQGTGHRGKIMKKDVLA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096876122 217 APAVAQRT-TLSASGKPMRTQ--PPGVAVTGQPEQ--LKGVRRNMARVMADAHAKVVPTTLSDDADVHAW---------- 281
Cdd:PRK14843 86 LLPENIENdSIKSPAQIEKVEevPDNVTPYGEIERipMTPMRKVIAQRMVESYLTAPTFTLNYEVDMTEMlalrkkvlep 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096876122 282 ---TPGNDVTVR--LIRAIVRACKAVPAMNAWFDGDKLTRTLHPQVDVGIAVDTDDGLFVPALRNADILDARGVREGINR 356
Cdd:PRK14843 166 imeATGKKTTVTdlLSLAVVKTLMKHPYINASLTEDGKTIITHNYVNLAMAVGMDNGLMTPVVYNAEKMSLSELVVAFKD 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096876122 357 LRAQVEDRSIPASELSGYTISLSNFGMFAGRYATPVVVPPCVAIVAAGRARHQVTPVMGGFESHKIIPLSVTFDHRACTG 436
Cdd:PRK14843 246 VIGRTLDGKLAPSELQNSTFTISNLGMFGVQSFGPIINQPNSAILGVSSTIEKPVVVNGEIVIRPIMSLGLTIDHRVVDG 325
|
330
....*....|....*.
gi 2096876122 437 GEAARF---LKALIDD 449
Cdd:PRK14843 326 MAGAKFmkdLKELIET 341
|
|
| kgd |
PRK12270 |
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ... |
294-444 |
9.17e-12 |
|
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;
Pssm-ID: 237030 [Multi-domain] Cd Length: 1228 Bit Score: 67.61 E-value: 9.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096876122 294 AIVRACKAVPAMNAWF---DGdKLTRTLHPQVDVGIAVDT--DDG---LFVPALRNADILDARGVREGINRLRAQVEDRS 365
Cdd:PRK12270 179 ALVQALKAFPNMNRHYaevDG-KPTLVTPAHVNLGLAIDLpkKDGsrqLVVPAIKGAETMDFAQFWAAYEDIVRRARDGK 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096876122 366 IPASELSGYTISLSNFGMFAGRYATPVVVPPCVAIVAAG----RARHQVTP--VMGGFESHKIIPLSVTFDHRACTGGEA 439
Cdd:PRK12270 258 LTADDFQGTTISLTNPGGIGTVHSVPRLMKGQGAIIGVGameyPAEFQGASeeRLAELGISKVMTLTSTYDHRIIQGAES 337
|
....*
gi 2096876122 440 ARFLK 444
Cdd:PRK12270 338 GEFLR 342
|
|
| E3_binding |
pfam02817 |
e3 binding domain; This family represents a small domain of the E2 subunit of 2-oxo-acid ... |
152-187 |
2.01e-09 |
|
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: 52.69 E-value: 2.01e-09
10 20 30
....*....|....*....|....*....|....*.
gi 2096876122 152 VKAMPAVRAMAKKLGVDLARVRATGADGAVTMADVK 187
Cdd:pfam02817 1 VLASPAARKLARELGIDLSDVKGTGPGGRITKEDVE 36
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
9-78 |
3.39e-09 |
|
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: 53.21 E-value: 3.39e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096876122 9 LPDLGEGLPDATIVEWFVKEGDVIRLDEPLVSMETAKAVVEVPSPVSGKVLKLAGGAGDVVVTGSMLAVF 78
Cdd:cd06663 4 IPDLAQHLGDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKVEGDTPLVKI 73
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
20-78 |
3.30e-08 |
|
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: 50.11 E-value: 3.30e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 2096876122 20 TIVEWFVKEGDVIRLDEPLVSMETAKAVVEVPSPVSGKVLKLAGGAGDVVVTGSMLAVF 78
Cdd:cd06850 9 TVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
9-77 |
6.54e-07 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 51.10 E-value: 6.54e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2096876122 9 LPDLGEGLPDATIVEWFVKEGDVIRLDEPLVSMETAKAVVEVPSPVSGKVLKLAGGAGDVVVTGSMLAV 77
Cdd:PRK14875 7 MPKWGLSMTEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGETLPVGALLAV 75
|
|
| GCS_H |
cd06848 |
Glycine cleavage H-protein. Glycine cleavage H-proteins are part of the glycine cleavage ... |
16-60 |
6.28e-06 |
|
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: 44.45 E-value: 6.28e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 2096876122 16 LPDATIVEwFVKEGDVIRLDEPLVSMETAKAVVEVPSPVSGKVLK 60
Cdd:cd06848 28 LGDIVFVE-LPEVGTEVKKGDPFGSVESVKAASDLYSPVSGEVVE 71
|
|
| GcvH |
COG0509 |
Glycine cleavage system protein H (lipoate-binding) [Amino acid transport and metabolism]; ... |
16-59 |
1.08e-04 |
|
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: 41.65 E-value: 1.08e-04
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 2096876122 16 LPDATIVEWfVKEGDVIRLDEPLVSMETAKAVVEVPSPVSGKVL 59
Cdd:COG0509 36 LGDIVFVEL-PEVGTEVEAGEPFGVVESVKAVSDLYAPVSGEVV 78
|
|
| PRK09282 |
PRK09282 |
pyruvate carboxylase subunit B; Validated |
20-80 |
7.90e-04 |
|
pyruvate carboxylase subunit B; Validated
Pssm-ID: 236449 [Multi-domain] Cd Length: 592 Bit Score: 41.75 E-value: 7.90e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2096876122 20 TIVEWFVKEGDVIRLDEPLVSMETAKAVVEVPSPVSGKVLKLAGGAGDVVVTGSMLAVFQP 80
Cdd:PRK09282 532 TVVKVKVKEGDKVKAGDTVLVLEAMKMENEIQAPVDGTVKEILVKEGDRVNPGDVLMEIEP 592
|
|
| PRK00624 |
PRK00624 |
glycine cleavage system protein H; Provisional |
8-61 |
4.53e-03 |
|
glycine cleavage system protein H; Provisional
Pssm-ID: 167014 Cd Length: 114 Bit Score: 36.73 E-value: 4.53e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 2096876122 8 NLPDLGEglpdativewFVKEGDVirldepLVSMETAKAVVEVPSPVSGKVLKL 61
Cdd:PRK00624 38 DLPSVGS----------FCKEGEV------LVILESSKSAIEVLSPVSGEVIEV 75
|
|
| PRK06748 |
PRK06748 |
hypothetical protein; Validated |
25-81 |
4.96e-03 |
|
hypothetical protein; Validated
Pssm-ID: 180678 [Multi-domain] Cd Length: 83 Bit Score: 36.00 E-value: 4.96e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 2096876122 25 FVKEGDVIRLDEPLVSMET-AKAVVEVPSPVSGKVLKLAGGAGDVVVTGSMLAVFQPD 81
Cdd:PRK06748 19 FVRESSYVYEWEKLALIETiDKQKVEIKVGISGYIESLEVVEGQAIADQKLLITVRDD 76
|
|
| AccB |
COG0511 |
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ... |
25-77 |
5.90e-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: 37.18 E-value: 5.90e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 2096876122 25 FVKEGDVIRLDEPLVSMETAKAVVEVPSPVSGKVLKLAGGAGDVVVTGSMLAV 77
Cdd:COG0511 82 FVKVGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVVEILVENGQPVEYGQPLFV 134
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
20-80 |
8.68e-03 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 38.58 E-value: 8.68e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2096876122 20 TIVEWFVKEGDVIRLDEPLVS-----METAkavveVPSPVSGKVLKLAGGAGDVVVTGSMLAVFQP 80
Cdd:PRK12999 1086 SVVTVLVKEGDEVKAGDPLAVieamkMETT-----ITAPVDGTVKRVLVKAGDQVEAGDLLVELEP 1146
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
20-78 |
8.81e-03 |
|
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: 38.52 E-value: 8.81e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2096876122 20 TIVEWFVKEGDVIRLDEPLVS-----METAkavveVPSPVSGKVLKLAGGAGDVVVTGSMLAVF 78
Cdd:COG1038 1086 TVVKVLVKEGDEVKKGDPLLTieamkMETT-----ITAPRDGTVKEVLVKEGDQVEAGDLLIEL 1144
|
|
| |
