|
Name |
Accession |
Description |
Interval |
E-value |
| sucB |
TIGR01347 |
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ... |
72-453 |
0e+00 |
|
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: 569.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980730 72 ITVQTPAFAESVTEGDV-RWEKAVGDAVAEDEVVCEIETDKTSVQVPSPANGIIEALLVPDGGKVEGGTPLFTLRKTAAP 150
Cdd:TIGR01347 1 IEIKVPELAESITEGTVaEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAILEEGNDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980730 151 AKAKPAETPAPA--HKAEPAAPAAPPPPAAPVLT------------QMPPVPSPSQPPSSKPVSAIKPTAAPPLAEAGAA 216
Cdd:TIGR01347 81 TAAPPAKSGEEKeeTPAASAAAAPTAAANRPSLSpaarrlakehgiDLSAVPGTGVTGRVTKEDIIKKTEAPASAQPPAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980730 217 --------KGLRSEHREKMNRMRQRIAQRLKEAQNTCAMLTTFNEVDMSNIQEMRARHKDAFLKKHNLKLGFMSAFVKAS 288
Cdd:TIGR01347 161 aaaaaapaAATRPEERVKMTRLRQRIAERLKEAQNSTAMLTTFNEVDMSAVMELRKRYKEEFEKKHGVKLGFMSFFVKAV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980730 289 AFALQEQPVVNAVIDDatKEVVYRDYIDISVAVATPRGLVVPVIRNVETMNYADIERTINELGEKARKNELAIEDMDGGT 368
Cdd:TIGR01347 241 VAALKRFPEVNAEIDG--DDIVYKDYYDISVAVSTDRGLVVPVVRNADRMSFADIEKEIADLGKKARDGKLTLEDMTGGT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980730 369 FTISNGGVFGSLFGTPIINPPQSAILGMHAIFDRPVAVGGKVEVRPMMYVALTYDHRLIDGREAVTFLRKIKAAVEDPRV 448
Cdd:TIGR01347 319 FTITNGGVFGSLMSTPIINPPQSAILGMHGIKERPVAVNGQIEIRPMMYLALSYDHRLIDGKEAVTFLVTIKELLEDPRR 398
|
....*
gi 568980730 449 LLLDL 453
Cdd:TIGR01347 399 LLLDL 403
|
|
| PTZ00144 |
PTZ00144 |
dihydrolipoamide succinyltransferase; Provisional |
51-453 |
0e+00 |
|
dihydrolipoamide succinyltransferase; Provisional
Pssm-ID: 240289 [Multi-domain] Cd Length: 418 Bit Score: 523.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980730 51 NSGSVFRVRFFQTTAVCK-------NDVITVQTPAFAESVTEGDV-RWEKAVGDAVAEDEVVCEIETDKTSVQVPSPANG 122
Cdd:PTZ00144 17 VKGMFRRFSLRKLQPACSahfsksyFSIKVIKVPTMGDSISEGTVvEWKKKVGDYVKEDEVICIIETDKVSVDIRAPASG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980730 123 IIEALLVPDGGKVEGGTPLFTLrKTAAPAKAKPAETPAPAHKAEPAAPAAPPPpaapvlTQMPPVPSPSQPPSSKPVSAI 202
Cdd:PTZ00144 97 VITKIFAEEGDTVEVGAPLSEI-DTGGAPPAAAPAAAAAAKAEKTTPEKPKAA------APTPEPPAASKPTPPAAAKPP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980730 203 KPTAAPPLAEAGAAKGLRSEHREKMNRMRQRIAQRLKEAQNTCAMLTTFNEVDMSNIQEMRARHKDAFLKKHNLKLGFMS 282
Cdd:PTZ00144 170 EPAPAAKPPPTPVARADPRETRVPMSRMRQRIAERLKASQNTCAMLTTFNECDMSALMELRKEYKDDFQKKHGVKLGFMS 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980730 283 AFVKASAFALQEQPVVNAVIDdaTKEVVYRDYIDISVAVATPRGLVVPVIRNVETMNYADIERTINELGEKARKNELAIE 362
Cdd:PTZ00144 250 AFVKASTIALKKMPIVNAYID--GDEIVYRNYVDISVAVATPTGLVVPVIRNCENKSFAEIEKELADLAEKARNNKLTLE 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980730 363 DMDGGTFTISNGGVFGSLFGTPIINPPQSAILGMHAIFDRPVAVGGKVEVRPMMYVALTYDHRLIDGREAVTFLRKIKAA 442
Cdd:PTZ00144 328 DMTGGTFTISNGGVFGSLMGTPIINPPQSAILGMHAIKKRPVVVGNEIVIRPIMYLALTYDHRLIDGRDAVTFLKKIKDL 407
|
410
....*....|.
gi 568980730 443 VEDPRVLLLDL 453
Cdd:PTZ00144 408 IEDPARMLLDL 418
|
|
| PRK05704 |
PRK05704 |
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase; |
72-453 |
1.12e-170 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
Pssm-ID: 235571 [Multi-domain] Cd Length: 407 Bit Score: 485.11 E-value: 1.12e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980730 72 ITVQTPAFAESVTEGDV-RWEKAVGDAVAEDEVVCEIETDKTSVQVPSPANGIIEALLVPDGGKVEGGTPLFTLRKTAAP 150
Cdd:PRK05704 3 VEIKVPTLPESVTEATIaTWHKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGDTVTVGQVLGRIDEGAAA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980730 151 AKAKPAETPAPAHKAEPAAPAAPPPPAAPVLTQMPPVPSPSQ------------------------PPSSKPVSAIKPTA 206
Cdd:PRK05704 83 GAAAAAAAAAAAAAAAPAQAQAAAAAEQSNDALSPAARKLAAengldasavkgtgkggrvtkedvlAALAAAAAAPAAPA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980730 207 APPLAEAGAAKGLRSEHREKMNRMRQRIAQRLKEAQNTCAMLTTFNEVDMSNIQEMRARHKDAFLKKHNLKLGFMSAFVK 286
Cdd:PRK05704 163 AAAPAAAPAPLGARPEERVPMTRLRKTIAERLLEAQNTTAMLTTFNEVDMTPVMDLRKQYKDAFEKKHGVKLGFMSFFVK 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980730 287 ASAFALQEQPVVNAVIDDatKEVVYRDYIDISVAVATPRGLVVPVIRNVETMNYADIERTINELGEKARKNELAIEDMDG 366
Cdd:PRK05704 243 AVVEALKRYPEVNASIDG--DDIVYHNYYDIGIAVGTPRGLVVPVLRDADQLSFAEIEKKIAELAKKARDGKLSIEELTG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980730 367 GTFTISNGGVFGSLFGTPIINPPQSAILGMHAIFDRPVAVGGKVEVRPMMYVALTYDHRLIDGREAVTFLRKIKAAVEDP 446
Cdd:PRK05704 321 GTFTITNGGVFGSLMSTPIINPPQSAILGMHKIKERPVAVNGQIVIRPMMYLALSYDHRIIDGKEAVGFLVTIKELLEDP 400
|
....*..
gi 568980730 447 RVLLLDL 453
Cdd:PRK05704 401 ERLLLDL 407
|
|
| PLN02226 |
PLN02226 |
2-oxoglutarate dehydrogenase E2 component |
40-453 |
5.25e-129 |
|
2-oxoglutarate dehydrogenase E2 component
Pssm-ID: 177871 [Multi-domain] Cd Length: 463 Bit Score: 381.41 E-value: 5.25e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980730 40 PGYPDNRKMVINSGSVFRvRFFQTTAVCKNDVITVQTPAFAESVTEGDV-RWEKAVGDAVAEDEVVCEIETDKTSVQVPS 118
Cdd:PLN02226 61 PGNSGISRSASLVSSTLQ-RWVRPFSSESGDTVEAVVPHMGESITDGTLaTFLKKPGERVQADEAIAQIETDKVTIDIAS 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980730 119 PANGIIEALLVPDGGKVEGGTPLFTLRKTAAPAKAKPAETPAPAHKAEPAAPAAPPPPAAPVltqmppvpspsqPPSSKP 198
Cdd:PLN02226 140 PASGVIQEFLVKEGDTVEPGTKVAIISKSEDAASQVTPSQKIPETTDPKPSPPAEDKQKPKV------------ESAPVA 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980730 199 VSAIKPTAAPPLAEAGAAKGLRSEHREK---MNRMRQRIAQRLKEAQNTCAMLTTFNEVDMSNIQEMRARHKDAFLKKHN 275
Cdd:PLN02226 208 EKPKAPSSPPPPKQSAKEPQLPPKERERrvpMTRLRKRVATRLKDSQNTFALLTTFNEVDMTNLMKLRSQYKDAFYEKHG 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980730 276 LKLGFMSAFVKASAFALQEQPVVNAVIDDatKEVVYRDYIDISVAVATPRGLVVPVIRNVETMNYADIERTINELGEKAR 355
Cdd:PLN02226 288 VKLGLMSGFIKAAVSALQHQPVVNAVIDG--DDIIYRDYVDISIAVGTSKGLVVPVIRGADKMNFAEIEKTINGLAKKAN 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980730 356 KNELAIEDMDGGTFTISNGGVFGSLFGTPIINPPQSAILGMHAIFDRPVAVGGKVEVRPMMYVALTYDHRLIDGREAVTF 435
Cdd:PLN02226 366 EGTISIDEMAGGSFTVSNGGVYGSLISTPIINPPQSAILGMHSIVSRPMVVGGSVVPRPMMYVALTYDHRLIDGREAVYF 445
|
410
....*....|....*...
gi 568980730 436 LRKIKAAVEDPRVLLLDL 453
Cdd:PLN02226 446 LRRVKDVVEDPQRLLLDI 463
|
|
| PRK11856 |
PRK11856 |
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed |
77-452 |
6.51e-106 |
|
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
Pssm-ID: 237001 [Multi-domain] Cd Length: 411 Bit Score: 320.20 E-value: 6.51e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980730 77 PAFAESVTEGD-VRWEKAVGDAVAEDEVVCEIETDKTSVQVPSPANGIIEALLVPDGGKVEGGTPLFTLRKTAAPAKAKP 155
Cdd:PRK11856 8 PDLGEGMTEGEiVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDVVPVGSVIAVIEEEGEAEAAAA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980730 156 AETPAPAHKAEPAAPAAPPPPAAPVLTQMPPVPSPSQPP----------------------------------SSKPVSA 201
Cdd:PRK11856 88 AEAAPEAPAPEPAPAAAAAAAAAPAAAAAPAAPAAAAAKaspavrklarelgvdlstvkgsgpggritkedveAAAAAAA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980730 202 IKPTAAPPLAEAGAAKGLRSEHREKMNRMRQRIAQRLKEAQNTCAMLTTFNEVDMSNIQEMRARhkdafLKKHNLKLGFM 281
Cdd:PRK11856 168 PAAAAAAAAAAAPPAAAAEGEERVPLSGMRKAIAKRMVESKREIPHFTLTDEVDVTALLALRKQ-----LKAIGVKLTVT 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980730 282 SAFVKASAFALQEQPVVNAVIDDATkeVVYRDYIDISVAVATPRGLVVPVIRNVETMNYADIERTINELGEKARKNELAI 361
Cdd:PRK11856 243 DFLIKAVALALKKFPELNASWDDDA--IVLKKYVNIGIAVATDGGLIVPVIRDADKKSLFELAREIKDLAEKAREGKLKP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980730 362 EDMDGGTFTISNGGVFGSLFGTPIINPPQSAILGMHAIFDRPVAVGGKVEVRPMMYVALTYDHRLIDGREAVTFLRKIKA 441
Cdd:PRK11856 321 EELQGGTFTISNLGMFGGDYFTPIINPPEVAILGVGAIVERPVVVDGEIVVRKVMPLSLSFDHRVIDGADAARFLKALKE 400
|
410
....*....|.
gi 568980730 442 AVEDPRVLLLD 452
Cdd:PRK11856 401 LLENPALLLLE 411
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
238-450 |
1.90e-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: 286.36 E-value: 1.90e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980730 238 LKEAQNTCAMLTTFNEVDMSNIQEMRARHKDAFLKKHNlKLGFMSAFVKASAFALQEQPVVNAVIDDATKEVVYRDYIDI 317
Cdd:pfam00198 1 MTESKQTIPHFTLTDEVDVTELLALREELKEDAADEET-KLTFLPFLVKAVALALKKFPELNASWDGEEGEIVYKKYVNI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980730 318 SVAVATPRGLVVPVIRNVETMNYADIERTINELGEKARKNELAIEDMDGGTFTISNGGVFGSLFGTPIINPPQSAILGMH 397
Cdd:pfam00198 80 GIAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVG 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 568980730 398 AIFDRPVAVGGKVEVRPMMYVALTYDHRLIDGREAVTFLRKIKAAVEDPRVLL 450
Cdd:pfam00198 160 RIRKRPVVVDGEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELLL 212
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
82-451 |
3.89e-84 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 268.61 E-value: 3.89e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980730 82 SVTEGDV-RWEKAVGDAVAEDEVVCEIETDKTSVQVPSPANGIIEALLVPDGGKVEGGTPLFTLRKTAAPAKAKPAETPA 160
Cdd:PRK11855 129 EITEVEViEWLVKVGDTVEEDQSLITVETDKATMEIPSPVAGVVKEIKVKVGDKVSVGSLLVVIEVAAAAPAAAAAPAAA 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980730 161 PAHKAEPAAPAAPPPPAAPVLTQMPPVPSPSQPPS--------------------------------------SKPVSAI 202
Cdd:PRK11855 209 APAAAAAAAPAPAPAAAAAPAAAAPAAAAAPGKAPhaspavrrlarelgvdlsqvkgtgkkgritkedvqafvKGAMSAA 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980730 203 KPTAAPPLAEAGAAKGL----------RSEHREK-MNRMRQRIAQRLKEAQNTCAMLTTFNEVDMSNIQEMRARHKDAFl 271
Cdd:PRK11855 289 AAAAAAAAAAGGGGLGLlpwpkvdfskFGEIETKpLSRIKKISAANLHRSWVTIPHVTQFDEADITDLEALRKQLKKEA- 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980730 272 KKHNLKLGFMSAFVKASAFALQEQPVVNAVIDDATKEVVYRDYIDISVAVATPRGLVVPVIRNVETMNYADIERTINELG 351
Cdd:PRK11855 368 EKAGVKLTMLPFFIKAVVAALKEFPVFNASLDEDGDELTYKKYFNIGFAVDTPNGLVVPVIKDVDKKSLLEIAREIAELA 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980730 352 EKARKNELAIEDMDGGTFTISNGGVFGSLFGTPIINPPQSAILGMHAIFDRPVAVGGKVEVRPMMYVALTYDHRLIDGRE 431
Cdd:PRK11855 448 KKARDGKLKPDDMQGGCFTISSLGGIGGTAFTPIINAPEVAILGVGKSQMKPVWDGKEFVPRLMLPLSLSYDHRVIDGAT 527
|
410 420
....*....|....*....|
gi 568980730 432 AVTFLRKIKAAVEDPRVLLL 451
Cdd:PRK11855 528 AARFTNYLKQLLADPRRMLL 547
|
|
| SucB_Actino |
TIGR02927 |
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model ... |
74-445 |
2.85e-77 |
|
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: 251.47 E-value: 2.85e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980730 74 VQTPAFAESVTEGDV-RWEKAVGDAVAEDEVVCEIETDKTSVQVPSPANGIIEALLVPDGGKVEGGTPLFTLRKTAAPAK 152
Cdd:TIGR02927 129 VKMPELGESVTEGTVtSWLKAVGDTVEVDEPLLEVSTDKVDTEIPSPVAGTLLEIRAPEDDTVEVGTVLAIIGDANAAPA 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980730 153 AKPAETPAPAHKAEPAAPAAPPPPAAPVLTQMPPVPSPSQPPSSKPVSAIK----------------------------- 203
Cdd:TIGR02927 209 EPAEEEAPAPSEAGSEPAPDPAARAPHAAPDPPAPAPAPAKTAAPAAAAPVssgdsgpyvtplvrklakdkgvdlstvkg 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980730 204 -----------------------------PTAAPPLAEAGAAKGLRSE------HREKMNRMRQRIAQRLKEAQNTCAML 248
Cdd:TIGR02927 289 tgvggrirkqdvlaaakaaeearaaaaapAAAAAPAAPAAAAKPAEPDtaklrgTTQKMNRIRQITADKTIESLQTSAQL 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980730 249 TTFNEVDMSNIQEMRARHKDAFLKKHNLKLGFMSAFVKASAFALQEQPVVNAVIDDATKEVVYRDYIDISVAVATPRGLV 328
Cdd:TIGR02927 369 TQVHEVDMTRVAALRARAKNDFLEKNGVNLTFLPFFVQAVTEALKAHPNVNASYNAETKEVTYHDVEHVGIAVDTPRGLL 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980730 329 VPVIRNVETMNYADIERTINELGEKARKNELAIEDMDGGTFTISNGGVFGSLFGTPIINPPQSAILGMHAIFDRPVAV-- 406
Cdd:TIGR02927 449 VPVIHNAGDLSLPGLAKAINDLAARARDNKLKPDELSGGTFTITNIGSGGALFDTPILNPPQAAILGTGAIVKRPRVIkd 528
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 568980730 407 ---GGKVEVRPMMYVALTYDHRLIDGREAVTFLRKIKAAVED 445
Cdd:TIGR02927 529 edgGESIAIRSVCYLPLTYDHRLVDGADAGRFLTTIKKRLEE 570
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
83-451 |
5.78e-62 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 212.17 E-value: 5.78e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980730 83 VTEGDV-RWEKAVGDAVAEDEVVCEIETDKTSVQVPSPANGIIEALLVPDGGKVEGGTPLFTLrKTAAPAKAKPAETPAP 161
Cdd:PRK11854 216 GDEVEVtEVMVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVKTGSLIMRF-EVEGAAPAAAPAKQEA 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980730 162 AHKAEPAAPAAPPPPAAPVLTQMPPVPSPSQPPS-----------------------------------SKPVSAIKP-- 204
Cdd:PRK11854 295 AAPAPAAAKAEAPAAAPAAKAEGKSEFAENDAYVhatplvrrlarefgvnlakvkgtgrkgrilkedvqAYVKDAVKRae 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980730 205 TAAPPLAEAGAAKGL---------RSEHRE--KMNRMRQRIAQRLKEAQNTCAMLTTFNEVDMSNIQEMR-ARHKDAFLK 272
Cdd:PRK11854 375 AAPAAAAAGGGGPGLlpwpkvdfsKFGEIEevELGRIQKISGANLHRNWVMIPHVTQFDKADITELEAFRkQQNAEAEKR 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980730 273 KHNLKLGFMSAFVKASAFALQEQPVVNAVIDDATKEVVYRDYIDISVAVATPRGLVVPVIRNVETMNYADIERTINELGE 352
Cdd:PRK11854 455 KLGVKITPLVFIMKAVAAALEQMPRFNSSLSEDGQRLTLKKYVNIGIAVDTPNGLVVPVFKDVNKKGIIELSRELMDISK 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980730 353 KARKNELAIEDMDGGTFTISNGGVFGSLFGTPIINPPQSAILGMHAIFDRPVAVGGKVEVRPMMYVALTYDHRLIDGREA 432
Cdd:PRK11854 535 KARDGKLTAGDMQGGCFTISSIGGLGTTHFTPIVNAPEVAILGVSKSAMEPVWNGKEFAPRLMLPLSLSYDHRVIDGADG 614
|
410
....*....|....*....
gi 568980730 433 VTFLRKIKAAVEDPRVLLL 451
Cdd:PRK11854 615 ARFITIINDRLSDIRRLVL 633
|
|
| PRK11857 |
PRK11857 |
dihydrolipoamide acetyltransferase; Reviewed |
205-449 |
8.27e-57 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237002 [Multi-domain] Cd Length: 306 Bit Score: 190.00 E-value: 8.27e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980730 205 TAAPPLAEAGAAKGLRSEHREKMNRMRQRIAQRLKEAQNTCAMLTTFNEVDMSNIQEMRARHKDAFLKKHNLKLGFMSAF 284
Cdd:PRK11857 59 QQAAKTAAPAAAPPKLEGKREKVAPIRKAIARAMTNSWSNVAYVNLVNEIDMTKLWDLRKSVKDPVLKTEGVKLTFLPFI 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980730 285 VKASAFALQEQPVVNAVIDDATKEVVYRDYIDISVAVATPRGLVVPVIRNVETMNYADIERTINELGEKARKNELAIEDM 364
Cdd:PRK11857 139 AKAILIALKEFPIFAAKYDEATSELVYPDTLNLGIAVDTEAGLMVPVIKNAQKLSIVEIAKEISRLAKAARERKIKPDEM 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980730 365 DGGTFTISNGGVFGSLFGTPIINPPQSAILGMHAIFDRPVAVGGKVEVRPMMYVALTYDHRLIDGREAVTFLRKIKAAVE 444
Cdd:PRK11857 219 KGGSFTITNYGSVGSLYGVPVINYPELAIAGVGAIIDKAIVKNGQIVAGKVMHLTVAADHRWIDGATIGRFASRVKELLE 298
|
....*
gi 568980730 445 DPRVL 449
Cdd:PRK11857 299 KPEIL 303
|
|
| PDHac_trf_mito |
TIGR01349 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
77-451 |
4.71e-52 |
|
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: 181.15 E-value: 4.71e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980730 77 PAFAESVTEGD-VRWEKAVGDAVAEDEVVCEIETDKTSVQVPSPANGIIEALLVPDGGK-VEGGTPL------------- 141
Cdd:TIGR01349 5 PALSPTMTTGNlAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEGTKdVPVNKPIavlveekedvada 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980730 142 ---FTLRKTAAPAKAKPAETPAPAHKAEPAAPAAPPPPAAPVLTQMPPVPSPSQPPSS---------------------- 196
Cdd:TIGR01349 85 fknYKLESSASPAPKPSEIAPTAPPSAPKPSPAPQKQSPEPSSPAPLSDKESGDRIFAsplakklakekgidlsavagsg 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980730 197 ----------KPVSAIKPTAAP-------PLAEAGAAKGLRSEHRE-KMNRMRQRIAQRLKEAQNTCAMLTTFNEVDMSN 258
Cdd:TIGR01349 165 pngrivkkdiESFVPQSPASANqqaaattPATYPAAAPVSTGSYEDvPLSNIRKIIAKRLLESKQTIPHYYVSIECNVDK 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980730 259 IQEMRARHKDAFLKKHnlKLGFMSAFVKASAFALQEQPVVNAVIDDATkeVVYRDYIDISVAVATPRGLVVPVIRNVETM 338
Cdd:TIGR01349 245 LLALRKELNAMASEVY--KLSVNDFIIKASALALREVPEANSSWTDNF--IRRYKNVDISVAVATPDGLITPIVRNADAK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980730 339 NYADIERTINELGEKARKNELAIEDMDGGTFTISNGGVFGSLFGTPIINPPQSAILGMHAIFDRPVAVGGK---VEVRPM 415
Cdd:TIGR01349 321 GLSTISNEIKDLAKRARNNKLKPEEFQGGTFTISNLGMFGIKDFTAIINPPQACILAVGAVEDVAVVDNDEekgFAVASI 400
|
410 420 430
....*....|....*....|....*....|....*.
gi 568980730 416 MYVALTYDHRLIDGREAVTFLRKIKAAVEDPRVLLL 451
Cdd:TIGR01349 401 MSVTLSCDHRVIDGAVGAEFLKSFKKYLENPIEMLL 436
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
94-451 |
4.48e-51 |
|
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: 181.23 E-value: 4.48e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980730 94 VGDAVAEDEVVCEIETDKTSVQVPSPANGIIEALLV------PDGG-----KVEGGTPLFTLRKTAAPAKAKPAETPAPA 162
Cdd:TIGR01348 139 VGDTVSADQSLITLESDKASMEVPAPASGVVKSVKVkvgdsvPTGDliltlSVAGSTPATAPAPASAQPAAQSPAATQPE 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980730 163 HKAEPAAPAAPPPPAAPVLTQMPPVPSPSQPP-----------------------------SSKPVSAIKPTAAPPLAEA 213
Cdd:TIGR01348 219 PAAAPAAAKAQAPAPQQAGTQNPAKVDHAAPAvrrlarefgvdlsavkgtgikgrilredvQRFVKEPSVRAQAAAASAA 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980730 214 GAAKGLR-----------SEHREKMNRMRQRIAQRLKEAQNTCAMLTTFNEVDMSNIQEMRARHKdAFLKKHNLKLGFMS 282
Cdd:TIGR01348 299 GGAPGALpwpnvdfskfgEVEEVDMSRIRKISGANLTRNWTMIPHVTHFDKADITEMEAFRKQQN-AAVEKEGVKLTVLH 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980730 283 AFVKASAFALQEQPVVNAVIDDATKEVVYRDYIDISVAVATPRGLVVPVIRNVETMNYADIERTINELGEKARKNELAIE 362
Cdd:TIGR01348 378 ILMKAVAAALKKFPKFNASLDLGGEQLILKKYVNIGVAVDTPNGLLVPVIKDVDRKGITELALELSDLAKKARDGKLTPD 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980730 363 DMDGGTFTISN-GGVFGSLFgTPIINPPQSAILGMHAIFDRPVAVGGKVEVRPMMYVALTYDHRLIDGREAVTFLRKIKA 441
Cdd:TIGR01348 458 EMQGACFTISSlGGIGGTAF-TPIVNAPEVAILGVSKSGMEPVWNGKEFEPRLMLPLSLSYDHRVIDGADAARFTTYICE 536
|
410
....*....|
gi 568980730 442 AVEDPRVLLL 451
Cdd:TIGR01348 537 SLADIRRLLL 546
|
|
| PRK14843 |
PRK14843 |
dihydrolipoamide acetyltransferase; Provisional |
227-451 |
3.19e-41 |
|
dihydrolipoamide acetyltransferase; Provisional
Pssm-ID: 184847 [Multi-domain] Cd Length: 347 Bit Score: 150.06 E-value: 3.19e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980730 227 MNRMRQRIAQRLKEAQNTCAMLTTFNEVDMSNIQEMRARHKDAFLKKHNLKLGFMSAFVKASAFALQEQPVVNAVIDDAT 306
Cdd:PRK14843 123 MTPMRKVIAQRMVESYLTAPTFTLNYEVDMTEMLALRKKVLEPIMEATGKKTTVTDLLSLAVVKTLMKHPYINASLTEDG 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980730 307 KEVVYRDYIDISVAVATPRGLVVPVIRNVETMNYADIERTINELGEKARKNELAIEDMDGGTFTISNGGVFG-SLFGtPI 385
Cdd:PRK14843 203 KTIITHNYVNLAMAVGMDNGLMTPVVYNAEKMSLSELVVAFKDVIGRTLDGKLAPSELQNSTFTISNLGMFGvQSFG-PI 281
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568980730 386 INPPQSAILGMHAIFDRPVAVGGKVEVRPMMYVALTYDHRLIDGREAVTFLRKIKAAVEDPRVLLL 451
Cdd:PRK14843 282 INQPNSAILGVSSTIEKPVVVNGEIVIRPIMSLGLTIDHRVVDGMAGAKFMKDLKELIETPISMLI 347
|
|
| PLN02528 |
PLN02528 |
2-oxoisovalerate dehydrogenase E2 component |
253-453 |
1.82e-37 |
|
2-oxoisovalerate dehydrogenase E2 component
Pssm-ID: 215289 [Multi-domain] Cd Length: 416 Bit Score: 141.40 E-value: 1.82e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980730 253 EVDMSNIQEMRARHKDAfLKKHNLKLGFMSAFVKASAFALQEQPVVNAVIDDATKEVVYRDYIDISVAVATPRGLVVPVI 332
Cdd:PLN02528 215 EINVDALVELKASFQEN-NTDPTVKHTFLPFLIKSLSMALSKYPLLNSCFNEETSEIRLKGSHNIGVAMATEHGLVVPNI 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980730 333 RNVETMNYADIERTINELGEKARKNELAIEDMDGGTFTISNGGVFGSLFGTPIINPPQSAILGMHAIFDRPVAVG-GKVE 411
Cdd:PLN02528 294 KNVQSLSLLEITKELSRLQHLAAENKLNPEDITGGTITLSNIGAIGGKFGSPVLNLPEVAIIALGRIQKVPRFVDdGNVY 373
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 568980730 412 VRPMMYVALTYDHRLIDGREAVTFLRKIKAAVEDPRVLLLDL 453
Cdd:PLN02528 374 PASIMTVTIGADHRVLDGATVARFCNEWKSYVEKPELLMLHM 415
|
|
| PLN02744 |
PLN02744 |
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex |
77-451 |
1.24e-33 |
|
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
Pssm-ID: 215397 [Multi-domain] Cd Length: 539 Bit Score: 132.67 E-value: 1.24e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980730 77 PAFAESVTEGDV-RWEKAVGDAVAEDEVVCEIETDKTSVQVPSPANGIIEALLVPDGGK--VEGGTPLFTLRKTAAPAKA 153
Cdd:PLN02744 118 PSLSPTMTEGNIaRWLKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVKGDGAKeiKVGEVIAITVEEEEDIGKF 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980730 154 KPAETPAPAHKAEPAAPAAPPPPAAPVLTQMPPVPSPSQPPSSKPVSAIKPTAAPPLA---------------------- 211
Cdd:PLN02744 198 KDYKPSSSAAPAAPKAKPSPPPPKEEEVEKPASSPEPKASKPSAPPSSGDRIFASPLArklaednnvplssikgtgpdgr 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980730 212 ------EAGAAKGLRSEHREKMN---------------RMRQRIAQRLKEAQNTCA--MLTTFNEVDmsNIQEMRAR--- 265
Cdd:PLN02744 278 ivkadiEDYLASGGKGATAPPSTdskapaldytdipntQIRKVTASRLLQSKQTIPhyYLTVDTRVD--KLMALRSQlns 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980730 266 HKDAFLKKhnlKLGFMSAFVKASAFALQEQPVVNAvidDATKEVVyRDY--IDISVAVATPRGLVVPVIRNVETMNYADI 343
Cdd:PLN02744 356 LQEASGGK---KISVNDLVIKAAALALRKVPQCNS---SWTDDYI-RQYhnVNINVAVQTENGLYVPVVKDADKKGLSTI 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980730 344 ERTINELGEKARKNELAIEDMDGGTFTISN-GGVFGSLFGTPIINPPQSAILGMHAIFDR--PVAVGGKVEVRPMMYVAL 420
Cdd:PLN02744 429 AEEVKQLAQKARENSLKPEDYEGGTFTVSNlGGPFGIKQFCAIINPPQSAILAVGSAEKRviPGSGPDQYNFASFMSVTL 508
|
410 420 430
....*....|....*....|....*....|.
gi 568980730 421 TYDHRLIDGREAVTFLRKIKAAVEDPRVLLL 451
Cdd:PLN02744 509 SCDHRVIDGAIGAEWLKAFKGYIENPESMLL 539
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
72-144 |
3.77e-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: 92.47 E-value: 3.77e-23
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568980730 72 ITVQTPAFAESVTEGDV-RWEKAVGDAVAEDEVVCEIETDKTSVQVPSPANGIIEALLVPDGGKVEGGTPLFTL 144
Cdd:cd06849 1 TEIKMPDLGESMTEGTIvEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
72-144 |
1.09e-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: 88.59 E-value: 1.09e-21
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568980730 72 ITVQTPAFAESVTEGDV-RWEKAVGDAVAEDEVVCEIETDKTSVQVPSPANGIIEALLVPDGGKVEGGTPLFTL 144
Cdd:COG0508 3 IEIKMPDLGESMTEGTIvEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
73-144 |
1.96e-21 |
|
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: 87.65 E-value: 1.96e-21
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568980730 73 TVQTPAFAESVTEGDVRWEKAVGDAVAEDEVVCEIETDKTSVQVPSPANGIIEALLVPDGGKVEGGTPLFTL 144
Cdd:pfam00364 2 EIKSPMIGESVREGVVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
|
|
| kgd |
PRK12270 |
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ... |
283-439 |
2.41e-18 |
|
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;
Pssm-ID: 237030 [Multi-domain] Cd Length: 1228 Bit Score: 88.02 E-value: 2.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980730 283 AFVKAsafaLQEQPVVNAVID--DATKEVVYRDYIDISVAVATP-----RGLVVPVIRNVETMNYADIERTINELGEKAR 355
Cdd:PRK12270 179 ALVQA----LKAFPNMNRHYAevDGKPTLVTPAHVNLGLAIDLPkkdgsRQLVVPAIKGAETMDFAQFWAAYEDIVRRAR 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980730 356 KNELAIEDMDGGTFTISNGGVFGSLFGTPIINPPQSAILGMHAIfDRPVAVGGKVE-------VRPMMYVALTYDHRLID 428
Cdd:PRK12270 255 DGKLTADDFQGTTISLTNPGGIGTVHSVPRLMKGQGAIIGVGAM-EYPAEFQGASEerlaelgISKVMTLTSTYDHRIIQ 333
|
170
....*....|.
gi 568980730 429 GREAVTFLRKI 439
Cdd:PRK12270 334 GAESGEFLRTI 344
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
73-142 |
4.88e-16 |
|
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: 72.47 E-value: 4.88e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568980730 73 TVQTPAFAESVTEGDV-RWEKAVGDAVAEDEVVCEIETDKTSVQVPSPANGIIEALLVPDGGKVEGGTPLF 142
Cdd:cd06663 1 TILIPDLAQHLGDGTVvKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKVEGDTPLV 71
|
|
| SucB_Actino |
TIGR02927 |
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model ... |
72-141 |
1.26e-13 |
|
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: 72.74 E-value: 1.26e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568980730 72 ITVQTPAFAESVTEGDV-RWEKAVGDAVAEDEVVCEIETDKTSVQVPSPANGIIEALLVPDGGKVEGGTPL 141
Cdd:TIGR02927 3 ESVKMPALGESVTEGTVtSWLKAVGDTVEADEPLLEVSTDKVDTEIPSPAAGVLLEIRAPEDDTVEVGGVL 73
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
88-144 |
3.95e-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: 55.50 E-value: 3.95e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 568980730 88 VRWEKAVGDAVAEDEVVCEIETDKTSVQVPSPANGIIEALLVPDGGKVEGGTPLFTL 144
Cdd:cd06850 11 VKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
83-144 |
7.26e-10 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 61.17 E-value: 7.26e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568980730 83 VTEGDV-RWEKAVGDAVAEDEVVCEIETDKTSVQVPSPANGIIEALLVPDGGKVEGGTPLFTL 144
Cdd:PRK11854 12 ADEVEVtEILVKVGDKVEAEQSLITVEGDKASMEVPSPQAGVVKEIKVKVGDKVETGALIMIF 74
|
|
| AccB |
COG0511 |
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ... |
94-145 |
2.27e-09 |
|
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: 55.67 E-value: 2.27e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 568980730 94 VGDAVAEDEVVCEIETDKTSVQVPSPANGIIEALLVPDGGKVEGGTPLFTLR 145
Cdd:COG0511 85 VGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVVEILVENGQPVEYGQPLFVIE 136
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
77-141 |
2.01e-08 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 56.11 E-value: 2.01e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568980730 77 PAFAESVTEGDV-RWEKAVGDAVAEDEVVCEIETDKTSVQVPSPANGIIEALLVPDGGKVEGGTPL 141
Cdd:PRK14875 8 PKWGLSMTEGKVaGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGETLPVGALL 73
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
72-144 |
1.69e-06 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 50.30 E-value: 1.69e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568980730 72 ITVQTPAFAESVTEGDV-RWEKAVGDAVAEDEVVCEIETDKTSVQVPSPANGIIEALLVPDGGK-VEGGTPLFTL 144
Cdd:PRK11892 3 IEILMPALSPTMEEGTLaKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKILVPEGTEgVKVNTPIAVL 77
|
|
| PRK07051 |
PRK07051 |
biotin carboxyl carrier domain-containing protein; |
92-144 |
8.80e-06 |
|
biotin carboxyl carrier domain-containing protein;
Pssm-ID: 180811 [Multi-domain] Cd Length: 80 Bit Score: 43.85 E-value: 8.80e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 568980730 92 KAVGDAVAEDEVVCEIETDKTSVQVPSPANGIIEALLVPDGGKVEGGTPLFTL 144
Cdd:PRK07051 26 VEVGDAVAAGDVVGLIEVMKQFTEVEAEAAGRVVEFLVEDGEPVEAGQVLARI 78
|
|
| PRK09282 |
PRK09282 |
pyruvate carboxylase subunit B; Validated |
94-146 |
7.03e-04 |
|
pyruvate carboxylase subunit B; Validated
Pssm-ID: 236449 [Multi-domain] Cd Length: 592 Bit Score: 42.14 E-value: 7.03e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 568980730 94 VGDAVAEDEVVCEIETDKTSVQVPSPANGIIEALLVPDGGKVEGGTPLFTLRK 146
Cdd:PRK09282 540 EGDKVKAGDTVLVLEAMKMENEIQAPVDGTVKEILVKEGDRVNPGDVLMEIEP 592
|
|
| |
