|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05704 |
PRK05704 |
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase; |
1-399 |
0e+00 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
Pssm-ID: 235571 [Multi-domain] Cd Length: 407 Bit Score: 688.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502034004 1 MAIDIKAPTFPESIADGTVATWHKKPGEAVKRDELIVDIETDKVVMEVLAEADGVIAEIVKNEGDTVLSGELLGKLTEGG 80
Cdd:PRK05704 1 MMVEIKVPTLPESVTEATIATWHKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGDTVTVGQVLGRIDEGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502034004 81 AATAAPAAAPAPAAAAPAAAEA----------PILSPAARKIAEENAIAADSITGTGKGGRVTKEDAVAAAEAKKSAPAG 150
Cdd:PRK05704 81 AAGAAAAAAAAAAAAAAAPAQAqaaaaaeqsnDALSPAARKLAAENGLDASAVKGTGKGGRVTKEDVLAALAAAAAAPAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502034004 151 QPAPAATAAPLFAaGDRVEKRVPMTRLRAKVAERLVEAQSSMAMLTTFNEVNMKPVMELRAKYKDLFEKTHnGVRLGFMS 230
Cdd:PRK05704 161 PAAAAPAAAPAPL-GARPEERVPMTRLRKTIAERLLEAQNTTAMLTTFNEVDMTPVMDLRKQYKDAFEKKH-GVKLGFMS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502034004 231 FFVKAAVEALKRQPGVNASIDGNDIVYHGYQDIGVAVSSDRGLVVPVLRNAEFMSLAEIEGGINEFGKKAKAGKLTIEEM 310
Cdd:PRK05704 239 FFVKAVVEALKRYPEVNASIDGDDIVYHNYYDIGIAVGTPRGLVVPVLRDADQLSFAEIEKKIAELAKKARDGKLSIEEL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502034004 311 TGGTFTISNGGVFGSLLSTPIVNPPQTAILGMHKIQERPMAVNGQVVILPMMYLALSYDHRLIDGKEAVTFLVTMKDLLE 390
Cdd:PRK05704 319 TGGTFTITNGGVFGSLMSTPIINPPQSAILGMHKIKERPVAVNGQIVIRPMMYLALSYDHRIIDGKEAVGFLVTIKELLE 398
|
....*....
gi 502034004 391 DPARLLLDV 399
Cdd:PRK05704 399 DPERLLLDL 407
|
|
| sucB |
TIGR01347 |
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ... |
3-399 |
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: 632.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502034004 3 IDIKAPTFPESIADGTVATWHKKPGEAVKRDELIVDIETDKVVMEVLAEADGVIAEIVKNEGDTVLSGELLGKLTEGGAA 82
Cdd:TIGR01347 1 IEIKVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAILEEGNDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502034004 83 TAAP----------AAAPAPAAAAPAAAEAPILSPAARKIAEENAIAADSITGTGKGGRVTKEDAVAAAEAKKSAPAGQP 152
Cdd:TIGR01347 81 TAAPpaksgeekeeTPAASAAAAPTAAANRPSLSPAARRLAKEHGIDLSAVPGTGVTGRVTKEDIIKKTEAPASAQPPAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502034004 153 APAATAAPLFaagDRVEKRVPMTRLRAKVAERLVEAQSSMAMLTTFNEVNMKPVMELRAKYKDLFEKTHnGVRLGFMSFF 232
Cdd:TIGR01347 161 AAAAAAPAAA---TRPEERVKMTRLRQRIAERLKEAQNSTAMLTTFNEVDMSAVMELRKRYKEEFEKKH-GVKLGFMSFF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502034004 233 VKAAVEALKRQPGVNASIDGNDIVYHGYQDIGVAVSSDRGLVVPVLRNAEFMSLAEIEGGINEFGKKAKAGKLTIEEMTG 312
Cdd:TIGR01347 237 VKAVVAALKRFPEVNAEIDGDDIVYKDYYDISVAVSTDRGLVVPVVRNADRMSFADIEKEIADLGKKARDGKLTLEDMTG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502034004 313 GTFTISNGGVFGSLLSTPIVNPPQTAILGMHKIQERPMAVNGQVVILPMMYLALSYDHRLIDGKEAVTFLVTMKDLLEDP 392
Cdd:TIGR01347 317 GTFTITNGGVFGSLMSTPIINPPQSAILGMHGIKERPVAVNGQIEIRPMMYLALSYDHRLIDGKEAVTFLVTIKELLEDP 396
|
....*..
gi 502034004 393 ARLLLDV 399
Cdd:TIGR01347 397 RRLLLDL 403
|
|
| PTZ00144 |
PTZ00144 |
dihydrolipoamide succinyltransferase; Provisional |
5-399 |
5.56e-165 |
|
dihydrolipoamide succinyltransferase; Provisional
Pssm-ID: 240289 [Multi-domain] Cd Length: 418 Bit Score: 468.78 E-value: 5.56e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502034004 5 IKAPTFPESIADGTVATWHKKPGEAVKRDELIVDIETDKVVMEVLAEADGVIAEIVKNEGDTVLSGELLGKLTEGGAATA 84
Cdd:PTZ00144 47 IKVPTMGDSISEGTVVEWKKKVGDYVKEDEVICIIETDKVSVDIRAPASGVITKIFAEEGDTVEVGAPLSEIDTGGAPPA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502034004 85 APAAAPAPAAAAPAAAEapilSPAARKIAEEnAIAADSITGTGKGGRVTkedavAAAEAKKSAPAGQPapaataaplfaa 164
Cdd:PTZ00144 127 AAPAAAAAAKAEKTTPE----KPKAAAPTPE-PPAASKPTPPAAAKPPE-----PAPAAKPPPTPVAR------------ 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502034004 165 GDRVEKRVPMTRLRAKVAERLVEAQSSMAMLTTFNEVNMKPVMELRAKYKDLFEKTHnGVRLGFMSFFVKAAVEALKRQP 244
Cdd:PTZ00144 185 ADPRETRVPMSRMRQRIAERLKASQNTCAMLTTFNECDMSALMELRKEYKDDFQKKH-GVKLGFMSAFVKASTIALKKMP 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502034004 245 GVNASIDGNDIVYHGYQDIGVAVSSDRGLVVPVLRNAEFMSLAEIEGGINEFGKKAKAGKLTIEEMTGGTFTISNGGVFG 324
Cdd:PTZ00144 264 IVNAYIDGDEIVYRNYVDISVAVATPTGLVVPVIRNCENKSFAEIEKELADLAEKARNNKLTLEDMTGGTFTISNGGVFG 343
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502034004 325 SLLSTPIVNPPQTAILGMHKIQERPMAVNGQVVILPMMYLALSYDHRLIDGKEAVTFLVTMKDLLEDPARLLLDV 399
Cdd:PTZ00144 344 SLMGTPIINPPQSAILGMHAIKKRPVVVGNEIVIRPIMYLALTYDHRLIDGRDAVTFLKKIKDLIEDPARMLLDL 418
|
|
| PRK11856 |
PRK11856 |
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed |
1-398 |
2.38e-127 |
|
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
Pssm-ID: 237001 [Multi-domain] Cd Length: 411 Bit Score: 372.97 E-value: 2.38e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502034004 1 MAIDIKAPTFPESIADGTVATWHKKPGEAVKRDELIVDIETDKVVMEVLAEADGVIAEIVKNEGDTVLSGELLGKLTEGG 80
Cdd:PRK11856 1 MMFEFKMPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDVVPVGSVIAVIEEEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502034004 81 ----------------------AATAAPAAAPAPAAAAPAAAEAPILSPAARKIAEENAIAADSITGTGKGGRVTKEDAV 138
Cdd:PRK11856 81 eaeaaaaaeaapeapapepapaAAAAAAAAPAAAAAPAAPAAAAAKASPAVRKLARELGVDLSTVKGSGPGGRITKEDVE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502034004 139 AAAEAKKSAPAGQPAPAATAAPLFAAGdrvEKRVPMTRLRAKVAERLVEAQSSMAMLTTFNEVNMKPVMELRAKYKDlfe 218
Cdd:PRK11856 161 AAAAAAAPAAAAAAAAAAAPPAAAAEG---EERVPLSGMRKAIAKRMVESKREIPHFTLTDEVDVTALLALRKQLKA--- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502034004 219 kthNGVRLGFMSFFVKAAVEALKRQPGVNASIDGNDIVYHGYQDIGVAVSSDRGLVVPVLRNAEFMSLAEIEGGINEFGK 298
Cdd:PRK11856 235 ---IGVKLTVTDFLIKAVALALKKFPELNASWDDDAIVLKKYVNIGIAVATDGGLIVPVIRDADKKSLFELAREIKDLAE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502034004 299 KAKAGKLTIEEMTGGTFTISNGGVFGSLLSTPIVNPPQTAILGMHKIQERPMAVNGQVVILPMMYLALSYDHRLIDGKEA 378
Cdd:PRK11856 312 KAREGKLKPEELQGGTFTISNLGMFGGDYFTPIINPPEVAILGVGAIVERPVVVDGEIVVRKVMPLSLSFDHRVIDGADA 391
|
410 420
....*....|....*....|
gi 502034004 379 VTFLVTMKDLLEDPARLLLD 398
Cdd:PRK11856 392 ARFLKALKELLENPALLLLE 411
|
|
| PLN02226 |
PLN02226 |
2-oxoglutarate dehydrogenase E2 component |
8-399 |
1.78e-124 |
|
2-oxoglutarate dehydrogenase E2 component
Pssm-ID: 177871 [Multi-domain] Cd Length: 463 Bit Score: 367.54 E-value: 1.78e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502034004 8 PTFPESIADGTVATWHKKPGEAVKRDELIVDIETDKVVMEVLAEADGVIAEIVKNEGDTVLSGELLGKLTEGGAATAApa 87
Cdd:PLN02226 97 PHMGESITDGTLATFLKKPGERVQADEAIAQIETDKVTIDIASPASGVIQEFLVKEGDTVEPGTKVAIISKSEDAASQ-- 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502034004 88 aapapaaaapaaaeapiLSPAaRKIAEENAIAADSITGTGKGGRVtkeDAVAAAEAKKSAPAGQPAPAATAAPLFAAGDR 167
Cdd:PLN02226 175 -----------------VTPS-QKIPETTDPKPSPPAEDKQKPKV---ESAPVAEKPKAPSSPPPPKQSAKEPQLPPKER 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502034004 168 vEKRVPMTRLRAKVAERLVEAQSSMAMLTTFNEVNMKPVMELRAKYKDLFEKTHnGVRLGFMSFFVKAAVEALKRQPGVN 247
Cdd:PLN02226 234 -ERRVPMTRLRKRVATRLKDSQNTFALLTTFNEVDMTNLMKLRSQYKDAFYEKH-GVKLGLMSGFIKAAVSALQHQPVVN 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502034004 248 ASIDGNDIVYHGYQDIGVAVSSDRGLVVPVLRNAEFMSLAEIEGGINEFGKKAKAGKLTIEEMTGGTFTISNGGVFGSLL 327
Cdd:PLN02226 312 AVIDGDDIIYRDYVDISIAVGTSKGLVVPVIRGADKMNFAEIEKTINGLAKKANEGTISIDEMAGGSFTVSNGGVYGSLI 391
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502034004 328 STPIVNPPQTAILGMHKIQERPMAVNGQVVILPMMYLALSYDHRLIDGKEAVTFLVTMKDLLEDPARLLLDV 399
Cdd:PLN02226 392 STPIINPPQSAILGMHSIVSRPMVVGGSVVPRPMMYVALTYDHRLIDGREAVYFLRRVKDVVEDPQRLLLDI 463
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
2-397 |
7.44e-99 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 304.44 E-value: 7.44e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502034004 2 AIDIKAPTFPEsIADGTVATWHKKPGEAVKRDELIVDIETDKVVMEVLAEADGVIAEIVKNEGDTVLSGELLGKLTEGGA 81
Cdd:PRK11855 119 VVEVKVPDIGE-ITEVEVIEWLVKVGDTVEEDQSLITVETDKATMEIPSPVAGVVKEIKVKVGDKVSVGSLLVVIEVAAA 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502034004 82 A------------------------TAAPAAAPAPAAAAPAAAEAPILSPAARKIAEENAIAADSITGTGKGGRVTKEDA 137
Cdd:PRK11855 198 ApaaaaapaaaapaaaaaaapapapAAAAAPAAAAPAAAAAPGKAPHASPAVRRLARELGVDLSQVKGTGKKGRITKEDV 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502034004 138 VAAAEAKKSAPAGQPAPAATAAPLFAA-----------GDRVEKrVPMTRLRAKVAERLVEAQSSMAMLTTFNEVNMKPV 206
Cdd:PRK11855 278 QAFVKGAMSAAAAAAAAAAAAGGGGLGllpwpkvdfskFGEIET-KPLSRIKKISAANLHRSWVTIPHVTQFDEADITDL 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502034004 207 MELRAKYKDLFEKthNGVRLGFMSFFVKAAVEALKRQPGVNASID--GNDIVYHGYQDIGVAVSSDRGLVVPVLRNAEFM 284
Cdd:PRK11855 357 EALRKQLKKEAEK--AGVKLTMLPFFIKAVVAALKEFPVFNASLDedGDELTYKKYFNIGFAVDTPNGLVVPVIKDVDKK 434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502034004 285 SLAEIEGGINEFGKKAKAGKLTIEEMTGGTFTISNGGVFGSLLSTPIVNPPQTAILGMHKIQERPMAVNGQVVILPMMYL 364
Cdd:PRK11855 435 SLLEIAREIAELAKKARDGKLKPDDMQGGCFTISSLGGIGGTAFTPIINAPEVAILGVGKSQMKPVWDGKEFVPRLMLPL 514
|
410 420 430
....*....|....*....|....*....|...
gi 502034004 365 ALSYDHRLIDGKEAVTFLVTMKDLLEDPARLLL 397
Cdd:PRK11855 515 SLSYDHRVIDGATAARFTNYLKQLLADPRRMLL 547
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
185-396 |
8.66e-92 |
|
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: 274.81 E-value: 8.66e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502034004 185 LVEAQSSMAMLTTFNEVNMKPVMELRAKYKDLFEKThnGVRLGFMSFFVKAAVEALKRQPGVNASIDGND--IVYHGYQD 262
Cdd:pfam00198 1 MTESKQTIPHFTLTDEVDVTELLALREELKEDAADE--ETKLTFLPFLVKAVALALKKFPELNASWDGEEgeIVYKKYVN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502034004 263 IGVAVSSDRGLVVPVLRNAEFMSLAEIEGGINEFGKKAKAGKLTIEEMTGGTFTISNGGVFGSLLSTPIVNPPQTAILGM 342
Cdd:pfam00198 79 IGIAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGV 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 502034004 343 HKIQERPMAVNGQVVILPMMYLALSYDHRLIDGKEAVTFLVTMKDLLEDPARLL 396
Cdd:pfam00198 159 GRIRKRPVVVDGEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELLL 212
|
|
| SucB_Actino |
TIGR02927 |
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model ... |
2-391 |
1.46e-83 |
|
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: 266.11 E-value: 1.46e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502034004 2 AIDIKAPTFPESIADGTVATWHKKPGEAVKRDELIVDIETDKVVMEVLAEADGVIAEIVKNEGDTVLSGELLGKLTEGGA 81
Cdd:TIGR02927 126 ATEVKMPELGESVTEGTVTSWLKAVGDTVEVDEPLLEVSTDKVDTEIPSPVAGTLLEIRAPEDDTVEVGTVLAIIGDANA 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502034004 82 ATAAPAAAPAPAAA---------------------------------------APAAAEAPILSPAARKIAEENAIAADS 122
Cdd:TIGR02927 206 APAEPAEEEAPAPSeagsepapdpaaraphaapdppapapapaktaapaaaapVSSGDSGPYVTPLVRKLAKDKGVDLST 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502034004 123 ITGTGKGGRVTKEDAVAAAEAKKSAPAGQPAPAATAAPLFAAGD-------------RVEKrvpMTRLRAKVAERLVEAQ 189
Cdd:TIGR02927 286 VKGTGVGGRIRKQDVLAAAKAAEEARAAAAAPAAAAAPAAPAAAakpaepdtaklrgTTQK---MNRIRQITADKTIESL 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502034004 190 SSMAMLTTFNEVNMKPVMELRAKYKDLFEKTHnGVRLGFMSFFVKAAVEALKRQPGVNASI--DGNDIVYHGYQDIGVAV 267
Cdd:TIGR02927 363 QTSAQLTQVHEVDMTRVAALRARAKNDFLEKN-GVNLTFLPFFVQAVTEALKAHPNVNASYnaETKEVTYHDVEHVGIAV 441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502034004 268 SSDRGLVVPVLRNAEFMSLAEIEGGINEFGKKAKAGKLTIEEMTGGTFTISNGGVFGSLLSTPIVNPPQTAILGMHKIQE 347
Cdd:TIGR02927 442 DTPRGLLVPVIHNAGDLSLPGLAKAINDLAARARDNKLKPDELSGGTFTITNIGSGGALFDTPILNPPQAAILGTGAIVK 521
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 502034004 348 RPMAV-----NGQVVILPMMYLALSYDHRLIDGKEAVTFLVTMKDLLED 391
Cdd:TIGR02927 522 RPRVIkdedgGESIAIRSVCYLPLTYDHRLVDGADAGRFLTTIKKRLEE 570
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
17-397 |
3.53e-76 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 247.99 E-value: 3.53e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502034004 17 GTVATWHKKPGEAVKRDELIVDIETDKVVMEVLAEADGVIAEIVKNEGDTVLSGELLGKLTEGG---------------- 80
Cdd:PRK11854 219 VEVTEVMVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVKTGSLIMRFEVEGaapaaapakqeaaapa 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502034004 81 -------AATAAPAAAPAPAAAAPAAAEAPILSPAARKIAEENAIAADSITGTGKGGRVTKED-------AVAAAEAKKS 146
Cdd:PRK11854 299 paaakaeAPAAAPAAKAEGKSEFAENDAYVHATPLVRRLAREFGVNLAKVKGTGRKGRILKEDvqayvkdAVKRAEAAPA 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502034004 147 APAGQPAPAATAAPLFAAGDRVEKR--VPMTRLRAKVAERLVEAQSSMAMLTTFNEVNMKPVMELRAKYKDLFEKTHNGV 224
Cdd:PRK11854 379 AAAAGGGGPGLLPWPKVDFSKFGEIeeVELGRIQKISGANLHRNWVMIPHVTQFDKADITELEAFRKQQNAEAEKRKLGV 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502034004 225 RLGFMSFFVKAAVEALKRQPGVNASI--DGNDIVYHGYQDIGVAVSSDRGLVVPVLRNAEFMSLAEIEGGINEFGKKAKA 302
Cdd:PRK11854 459 KITPLVFIMKAVAAALEQMPRFNSSLseDGQRLTLKKYVNIGIAVDTPNGLVVPVFKDVNKKGIIELSRELMDISKKARD 538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502034004 303 GKLTIEEMTGGTFTISNGGVFGSLLSTPIVNPPQTAILGMHKIQERPMAVNGQVVILPMMYLALSYDHRLIDGKEAVTFL 382
Cdd:PRK11854 539 GKLTAGDMQGGCFTISSIGGLGTTHFTPIVNAPEVAILGVSKSAMEPVWNGKEFAPRLMLPLSLSYDHRVIDGADGARFI 618
|
410
....*....|....*
gi 502034004 383 VTMKDLLEDPARLLL 397
Cdd:PRK11854 619 TIINDRLSDIRRLVL 633
|
|
| PDHac_trf_mito |
TIGR01349 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
5-397 |
5.75e-67 |
|
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: 218.89 E-value: 5.75e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502034004 5 IKAPTFPESIADGTVATWHKKPGEAVKRDELIVDIETDKVVMEVLAEADGVIAEIVKNEGD---------TVLSGE---- 71
Cdd:TIGR01349 2 ITMPALSPTMTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEGTkdvpvnkpiAVLVEEkedv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502034004 72 ----LLGKLTEGGAATAAPAAAPAPAAAAPAAAEAPIL-----------------------SPAARKIAEENAIAADSIT 124
Cdd:TIGR01349 82 adafKNYKLESSASPAPKPSEIAPTAPPSAPKPSPAPQkqspepsspaplsdkesgdrifaSPLAKKLAKEKGIDLSAVA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502034004 125 GTGKGGRVTKEDAVAAAE-AKKSAPAGQPAPAATAAPLFAAGDRVEKR-VPMTRLRAKVAERLVEAQSSMAMLTTFNEVN 202
Cdd:TIGR01349 162 GSGPNGRIVKKDIESFVPqSPASANQQAAATTPATYPAAAPVSTGSYEdVPLSNIRKIIAKRLLESKQTIPHYYVSIECN 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502034004 203 MKPVMELRAKYKDLFEKThngVRLGFMSFFVKAAVEALKRQPGVNASIDGNDIVYHGYQDIGVAVSSDRGLVVPVLRNAE 282
Cdd:TIGR01349 242 VDKLLALRKELNAMASEV---YKLSVNDFIIKASALALREVPEANSSWTDNFIRRYKNVDISVAVATPDGLITPIVRNAD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502034004 283 FMSLAEIEGGINEFGKKAKAGKLTIEEMTGGTFTISNGGVFGSLLSTPIVNPPQTAILGMHKIQERPMAVNGQ---VVIL 359
Cdd:TIGR01349 319 AKGLSTISNEIKDLAKRARNNKLKPEEFQGGTFTISNLGMFGIKDFTAIINPPQACILAVGAVEDVAVVDNDEekgFAVA 398
|
410 420 430
....*....|....*....|....*....|....*...
gi 502034004 360 PMMYLALSYDHRLIDGKEAVTFLVTMKDLLEDPARLLL 397
Cdd:TIGR01349 399 SIMSVTLSCDHRVIDGAVGAEFLKSFKKYLENPIEMLL 436
|
|
| PLN02528 |
PLN02528 |
2-oxoisovalerate dehydrogenase E2 component |
12-397 |
3.33e-57 |
|
2-oxoisovalerate dehydrogenase E2 component
Pssm-ID: 215289 [Multi-domain] Cd Length: 416 Bit Score: 192.63 E-value: 3.33e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502034004 12 ESIADGTVATWHKKPGEAVKRDELIVDIETDKVVMEVLAEADGVIAEIVKNEGDTVLSGELLGKL-TEGGAATAAPAAAP 90
Cdd:PLN02528 8 EGIAECELLRWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGKVAQINFSPGDIVKVGETLLKImVEDSQHLRSDSLLL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502034004 91 APAAAAPAAAEAP----------ILSPAARKIAEENAIAADSITGTGKGGRVTKEDAVAAAEAKK----SAPAGQPAPAA 156
Cdd:PLN02528 88 PTDSSNIVSLAESdergsnlsgvLSTPAVRHLAKQYGIDLNDILGTGKDGRVLKEDVLKYAAQKGvvkdSSSAEEATIAE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502034004 157 TAAPLFAAGDRVE-----KRVPM---TRLRAKvaerlveaqsSMAMLTTF------NEVNMKPVMELRAKYKDlfEKTHN 222
Cdd:PLN02528 168 QEEFSTSVSTPTEqsyedKTIPLrgfQRAMVK----------TMTAAAKVphfhyvEEINVDALVELKASFQE--NNTDP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502034004 223 GVRLGFMSFFVKAAVEALKRQPGVNASIDG--NDIVYHGYQDIGVAVSSDRGLVVPVLRNAEFMSLAEIEGGINEFGKKA 300
Cdd:PLN02528 236 TVKHTFLPFLIKSLSMALSKYPLLNSCFNEetSEIRLKGSHNIGVAMATEHGLVVPNIKNVQSLSLLEITKELSRLQHLA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502034004 301 KAGKLTIEEMTGGTFTISN----GGVFGSllstPIVNPPQTAILGMHKIQERPMAVN-GQVVILPMMYLALSYDHRLIDG 375
Cdd:PLN02528 316 AENKLNPEDITGGTITLSNigaiGGKFGS----PVLNLPEVAIIALGRIQKVPRFVDdGNVYPASIMTVTIGADHRVLDG 391
|
410 420
....*....|....*....|..
gi 502034004 376 KEAVTFLVTMKDLLEDPARLLL 397
Cdd:PLN02528 392 ATVARFCNEWKSYVEKPELLML 413
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
3-397 |
6.27e-56 |
|
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: 192.40 E-value: 6.27e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502034004 3 IDIKAPTFpESIADGTVATWHKKPGEAVKRDELIVDIETDKVVMEVLAEADGVIAEIVKNEGDTVLSGELLGKLTEGGAA 82
Cdd:TIGR01348 117 QEVTVPDI-GDIEKVTVIEVLVKVGDTVSADQSLITLESDKASMEVPAPASGVVKSVKVKVGDSVPTGDLILTLSVAGST 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502034004 83 TAAPAAAPAPAAAAPAAAEAPI-----------------------------LSPAARKIAEENAIAADSITGTGKGGRVT 133
Cdd:TIGR01348 196 PATAPAPASAQPAAQSPAATQPepaaapaaakaqapapqqagtqnpakvdhAAPAVRRLAREFGVDLSAVKGTGIKGRIL 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502034004 134 KED--AVAAAEAKKSAPAGQPAPAATAAPLFAAGDRVEK-----RVPMTRLRAKVAERLVEAQSSMAMLTTFNEVNMKPV 206
Cdd:TIGR01348 276 REDvqRFVKEPSVRAQAAAASAAGGAPGALPWPNVDFSKfgeveEVDMSRIRKISGANLTRNWTMIPHVTHFDKADITEM 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502034004 207 MELRAKYKDLFEKThnGVRLGFMSFFVKAAVEALKRQPGVNASID--GNDIVYHGYQDIGVAVSSDRGLVVPVLRNAEFM 284
Cdd:TIGR01348 356 EAFRKQQNAAVEKE--GVKLTVLHILMKAVAAALKKFPKFNASLDlgGEQLILKKYVNIGVAVDTPNGLLVPVIKDVDRK 433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502034004 285 SLAEIEGGINEFGKKAKAGKLTIEEMTGGTFTISNGGVFGSLLSTPIVNPPQTAILGMHKIQERPMAVNGQVVILPMMYL 364
Cdd:TIGR01348 434 GITELALELSDLAKKARDGKLTPDEMQGACFTISSLGGIGGTAFTPIVNAPEVAILGVSKSGMEPVWNGKEFEPRLMLPL 513
|
410 420 430
....*....|....*....|....*....|...
gi 502034004 365 ALSYDHRLIDGKEAVTFLVTMKDLLEDPARLLL 397
Cdd:TIGR01348 514 SLSYDHRVIDGADAARFTTYICESLADIRRLLL 546
|
|
| PRK14843 |
PRK14843 |
dihydrolipoamide acetyltransferase; Provisional |
105-397 |
8.65e-56 |
|
dihydrolipoamide acetyltransferase; Provisional
Pssm-ID: 184847 [Multi-domain] Cd Length: 347 Bit Score: 187.03 E-value: 8.65e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502034004 105 LSPAARKIAEENAIAADSITGTGKGGRVTKEDAVA-AAEAKKSAPAGQPAPAATAAPLFAAGDRVEK--RVPMTRLRAKV 181
Cdd:PRK14843 51 ISPLAKRIALEHNIAWQEIQGTGHRGKIMKKDVLAlLPENIENDSIKSPAQIEKVEEVPDNVTPYGEieRIPMTPMRKVI 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502034004 182 AERLVEAQSSMAMLTTFNEVNMKPVMELRAKYKD-LFEKThnGVRLGFMSFFVKAAVEALKRQPGVNASI--DGNDIVYH 258
Cdd:PRK14843 131 AQRMVESYLTAPTFTLNYEVDMTEMLALRKKVLEpIMEAT--GKKTTVTDLLSLAVVKTLMKHPYINASLteDGKTIITH 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502034004 259 GYQDIGVAVSSDRGLVVPVLRNAEFMSLAEIEGGINEFGKKAKAGKLTIEEMTGGTFTISNGGVFGSLLSTPIVNPPQTA 338
Cdd:PRK14843 209 NYVNLAMAVGMDNGLMTPVVYNAEKMSLSELVVAFKDVIGRTLDGKLAPSELQNSTFTISNLGMFGVQSFGPIINQPNSA 288
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 502034004 339 ILGMHKIQERPMAVNGQVVILPMMYLALSYDHRLIDGKEAVTFLVTMKDLLEDPARLLL 397
Cdd:PRK14843 289 ILGVSSTIEKPVVVNGEIVIRPIMSLGLTIDHRVVDGMAGAKFMKDLKELIETPISMLI 347
|
|
| PRK11857 |
PRK11857 |
dihydrolipoamide acetyltransferase; Reviewed |
104-392 |
5.04e-50 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237002 [Multi-domain] Cd Length: 306 Bit Score: 170.74 E-value: 5.04e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502034004 104 ILSPAARKIAEENAIAADSITGTGKGGRVTKED-----------AVAAAEAKKSAPAGQPAPAATAAPLFAAGDRVEKRV 172
Cdd:PRK11857 3 LATPIARALAKKLGIDISLLKGSGRDGKILAEDvenfikslksaPTPAEAASVSSAQQAAKTAAPAAAPPKLEGKREKVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502034004 173 PmtrLRAKVAERLVEAQSSMAMLTTFNEVNMKPVMELRAKYKDLFEKThNGVRLGFMSFFVKAAVEALKRQPGVNASID- 251
Cdd:PRK11857 83 P---IRKAIARAMTNSWSNVAYVNLVNEIDMTKLWDLRKSVKDPVLKT-EGVKLTFLPFIAKAILIALKEFPIFAAKYDe 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502034004 252 -GNDIVYHGYQDIGVAVSSDRGLVVPVLRNAEFMSLAEIEGGINEFGKKAKAGKLTIEEMTGGTFTISNGGVFGSLLSTP 330
Cdd:PRK11857 159 aTSELVYPDTLNLGIAVDTEAGLMVPVIKNAQKLSIVEIAKEISRLAKAARERKIKPDEMKGGSFTITNYGSVGSLYGVP 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502034004 331 IVNPPQTAILGMHKIQERPMAVNGQVVILPMMYLALSYDHRLIDGKEAVTFLVTMKDLLEDP 392
Cdd:PRK11857 239 VINYPELAIAGVGAIIDKAIVKNGQIVAGKVMHLTVAADHRWIDGATIGRFASRVKELLEKP 300
|
|
| PLN02744 |
PLN02744 |
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex |
4-397 |
7.50e-48 |
|
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
Pssm-ID: 215397 [Multi-domain] Cd Length: 539 Bit Score: 170.80 E-value: 7.50e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502034004 4 DIKAPTFPESIADGTVATWHKKPGEAVKRDELIVDIETDKVVMEVLAEADGVIAEIVKNEGD-----------TVLSGEL 72
Cdd:PLN02744 114 EIGMPSLSPTMTEGNIARWLKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVKGDGAkeikvgeviaiTVEEEED 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502034004 73 LGKL-------------------------TEGGAATAAPAAAPAPAAAAPAAAEAPILSPAARKIAEENAIAADSITGTG 127
Cdd:PLN02744 194 IGKFkdykpsssaapaapkakpsppppkeEEVEKPASSPEPKASKPSAPPSSGDRIFASPLARKLAEDNNVPLSSIKGTG 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502034004 128 KGGRVTKED--AVAAAEAKKSAPAGQPAPAATAAplfaagDRVEkrVPMTRLRAKVAERLVEAQSSMAMLTTFNEVNMKP 205
Cdd:PLN02744 274 PDGRIVKADieDYLASGGKGATAPPSTDSKAPAL------DYTD--IPNTQIRKVTASRLLQSKQTIPHYYLTVDTRVDK 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502034004 206 VMELRAKYKDLFEKThNGVRLGFMSFFVKAAVEALKRQPGVNASIDGNDIVYHGYQDIGVAVSSDRGLVVPVLRNAEFMS 285
Cdd:PLN02744 346 LMALRSQLNSLQEAS-GGKKISVNDLVIKAAALALRKVPQCNSSWTDDYIRQYHNVNINVAVQTENGLYVPVVKDADKKG 424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502034004 286 LAEIEGGINEFGKKAKAGKLTIEEMTGGTFTISN-GGVFGSLLSTPIVNPPQTAILGMHKIQER--PMAVNGQVVILPMM 362
Cdd:PLN02744 425 LSTIAEEVKQLAQKARENSLKPEDYEGGTFTVSNlGGPFGIKQFCAIINPPQSAILAVGSAEKRviPGSGPDQYNFASFM 504
|
410 420 430
....*....|....*....|....*....|....*
gi 502034004 363 YLALSYDHRLIDGKEAVTFLVTMKDLLEDPARLLL 397
Cdd:PLN02744 505 SVTLSCDHRVIDGAIGAEWLKAFKGYIENPESMLL 539
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
1-76 |
6.32e-27 |
|
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: 102.07 E-value: 6.32e-27
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502034004 1 MAIDIKAPTFPESIADGTVATWHKKPGEAVKRDELIVDIETDKVVMEVLAEADGVIAEIVKNEGDTVLSGELLGKL 76
Cdd:COG0508 1 MAIEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
3-76 |
3.73e-25 |
|
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: 97.48 E-value: 3.73e-25
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502034004 3 IDIKAPTFPESIADGTVATWHKKPGEAVKRDELIVDIETDKVVMEVLAEADGVIAEIVKNEGDTVLSGELLGKL 76
Cdd:cd06849 1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
|
|
| kgd |
PRK12270 |
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ... |
235-389 |
1.05e-16 |
|
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;
Pssm-ID: 237030 [Multi-domain] Cd Length: 1228 Bit Score: 82.25 E-value: 1.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502034004 235 AAVEALKRQPGVNAS---IDGN-DIVYHGYQDIGVAV-----SSDRGLVVPVLRNAEFMSLAEIEGGINEFGKKAKAGKL 305
Cdd:PRK12270 179 ALVQALKAFPNMNRHyaeVDGKpTLVTPAHVNLGLAIdlpkkDGSRQLVVPAIKGAETMDFAQFWAAYEDIVRRARDGKL 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502034004 306 TIEEMTGGTFTISNGGVFGSLLSTPIVNPPQTAILGMHKIqERPMAVNG-------QVVILPMMYLALSYDHRLIDGKEA 378
Cdd:PRK12270 259 TADDFQGTTISLTNPGGIGTVHSVPRLMKGQGAIIGVGAM-EYPAEFQGaseerlaELGISKVMTLTSTYDHRIIQGAES 337
|
170
....*....|.
gi 502034004 379 VTFLVTMKDLL 389
Cdd:PRK12270 338 GEFLRTIHQLL 348
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
4-76 |
1.61e-14 |
|
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: 67.85 E-value: 1.61e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502034004 4 DIKAPTFPESIADGTVATWHKKPGEAVKRDELIVDIETDKVVMEVLAEADGVIAEIVKNEGDTVLSGELLGKL 76
Cdd:cd06663 1 TILIPDLAQHLGDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKVEGDTPLVKI 73
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
1-136 |
2.16e-14 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 73.82 E-value: 2.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502034004 1 MAIDIKAPTFPESIADGTVATWHKKPGEAVKRDELIVDIETDKVVMEVLAEADGVIAEIVKNEGDTVLSGELLGKLTEGG 80
Cdd:PRK14875 1 SITPITMPKWGLSMTEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGETLPVGALLAVVADAE 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 502034004 81 aataapaaapapaaaAPAAAEAPILSPAARKIAEEnAIAADSITGTGKGGRVTKED 136
Cdd:PRK14875 81 ---------------VSDAEIDAFIAPFARRFAPE-GIDEEDAGPAPRKARIGGRT 120
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
4-76 |
6.71e-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: 66.08 E-value: 6.71e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502034004 4 DIKAPTFPESIADGtVATWHKKPGEAVKRDELIVDIETDKVVMEVLAEADGVIAEIVKNEGDTVLSGELLGKL 76
Cdd:pfam00364 2 EIKSPMIGESVREG-VVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
1-64 |
4.15e-11 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 64.17 E-value: 4.15e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502034004 1 MAIDIKAPTFPESIADGTVATWHKKPGEAVKRDELIVDIETDKVVMEVLAEADGVIAEIVKNEG 64
Cdd:PRK11892 1 MAIEILMPALSPTMEEGTLAKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKILVPEG 64
|
|
| E3_binding |
pfam02817 |
e3 binding domain; This family represents a small domain of the E2 subunit of 2-oxo-acid ... |
104-136 |
2.34e-10 |
|
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: 55.00 E-value: 2.34e-10
10 20 30
....*....|....*....|....*....|...
gi 502034004 104 ILSPAARKIAEENAIAADSITGTGKGGRVTKED 136
Cdd:pfam02817 2 LASPAARKLARELGIDLSDVKGTGPGGRITKED 34
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
17-76 |
1.75e-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: 50.88 E-value: 1.75e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 502034004 17 GTVATWHKKPGEAVKRDELIVDIETDKVVMEVLAEADGVIAEIVKNEGDTVLSGELLGKL 76
Cdd:cd06850 8 GTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
1-73 |
1.96e-08 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 56.16 E-value: 1.96e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502034004 1 MAIDIKAPTFpeSIADGTVATWHKKPGEAVKRDELIVDIETDKVVMEVLAEADGVIAEIVKNEGDTVLSGELL 73
Cdd:PRK11854 1 MAIEIKVPDI--GADEVEVTEILVKVGDKVEAEQSLITVEGDKASMEVPSPQAGVVKEIKVKVGDKVETGALI 71
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
17-73 |
4.47e-07 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 52.06 E-value: 4.47e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 502034004 17 GTVATWHKKPGEAVKRDELIVDIETDKvvME--VLAEADGVIAEIVKNEGDTVLSGELL 73
Cdd:PRK12999 1085 GSVVTVLVKEGDEVKAGDPLAVIEAMK--MEttITAPVDGTVKRVLVKAGDQVEAGDLL 1141
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
17-73 |
5.00e-06 |
|
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: 48.92 E-value: 5.00e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 502034004 17 GTVATWHKKPGEAVKRDELIVDIETDKvvME--VLAEADGVIAEIVKNEGDTVLSGELL 73
Cdd:COG1038 1085 GTVVKVLVKEGDEVKKGDPLLTIEAMK--MEttITAPRDGTVKEVLVKEGDQVEAGDLL 1141
|
|
| PRK08225 |
PRK08225 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
17-73 |
5.17e-04 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 181304 [Multi-domain] Cd Length: 70 Bit Score: 38.23 E-value: 5.17e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 502034004 17 GTVATWHKKPGEAVKRDELIVDIETDKVVMEVLAEADGVIAEIVKNEGDTVLSGELL 73
Cdd:PRK08225 10 GNVWKIVVKVGDTVEEGQDVVILESMKMEIPIVAEEAGTVKKINVQEGDFVNEGDVL 66
|
|
| PRK14042 |
PRK14042 |
pyruvate carboxylase subunit B; Provisional |
17-73 |
1.01e-03 |
|
pyruvate carboxylase subunit B; Provisional
Pssm-ID: 172536 [Multi-domain] Cd Length: 596 Bit Score: 41.25 E-value: 1.01e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 502034004 17 GTVATWHKKPGEAVKRDELIVDIETDKVVMEVLAEADGVIAEIVKNEGDTVLSGELL 73
Cdd:PRK14042 534 GSIIAIHVSAGDEVKAGQAVLVIEAMKMETEIKAPANGVVAEILCQKGDKVTPGQVL 590
|
|
| AccB |
COG0511 |
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ... |
25-73 |
2.10e-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: 2.10e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 502034004 25 KPGEAVKRDELIVDIETDKVVMEVLAEADGVIAEIVKNEGDTVLSGELL 73
Cdd:COG0511 84 KVGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVVEILVENGQPVEYGQPL 132
|
|
| PRK09282 |
PRK09282 |
pyruvate carboxylase subunit B; Validated |
17-73 |
4.85e-03 |
|
pyruvate carboxylase subunit B; Validated
Pssm-ID: 236449 [Multi-domain] Cd Length: 592 Bit Score: 39.06 E-value: 4.85e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 502034004 17 GTVATWHKKPGEAVKRDELIVDIETDKVVMEVLAEADGVIAEIVKNEGDTVLSGELL 73
Cdd:PRK09282 531 GTVVKVKVKEGDKVKAGDTVLVLEAMKMENEIQAPVDGTVKEILVKEGDRVNPGDVL 587
|
|
| PRK14040 |
PRK14040 |
oxaloacetate decarboxylase subunit alpha; |
17-73 |
5.68e-03 |
|
oxaloacetate decarboxylase subunit alpha;
Pssm-ID: 237592 [Multi-domain] Cd Length: 593 Bit Score: 38.76 E-value: 5.68e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 502034004 17 GTVATWHKKPGEAVKRDELIVDIETDKVVMEVLAEADGVIAEIVKNEGDTVLSGELL 73
Cdd:PRK14040 533 GNIFKVIVTEGQTVAEGDVLLILEAMKMETEIRAAQAGTVRGIAVKEGDAVAVGDTL 589
|
|
| |
