|
Name |
Accession |
Description |
Interval |
E-value |
| SucB_Actino |
TIGR02927 |
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model ... |
1-586 |
0e+00 |
|
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: 710.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522119224 1 MAYSVTLPELGESVTEGTVTRWLKQEGDTVEVDEPLLEISTDKVDTEVPSPVAGKVVKISAQEDETVEVGGELAVIDDGT 80
Cdd:TIGR02927 1 MAESVKMPALGESVTEGTVTSWLKAVGDTVEADEPLLEVSTDKVDTEIPSPAAGVLLEIRAPEDDTVEVGGVLAIIGEPG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522119224 81 GGVPESSGSAAPAAEEAQPEPEPEPVQEQASAPSQPAAAPASGGEGTEVKLPELGESVTEGTVTRWLKQVGDSVEVDEPL 160
Cdd:TIGR02927 81 EAGSEPAPAAPEPEAAPEPEAPAPAPTPAAEAPAPAAPQAGGSGEATEVKMPELGESVTEGTVTSWLKAVGDTVEVDEPL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522119224 161 LEISTDKVDTEVPSPVAGTVLEIRAGEDETVEVGGVLAVIGAAGSAPAPKAEPKPEPKPEPKPEPKPEPKPEPKVEAAPA 240
Cdd:TIGR02927 161 LEVSTDKVDTEIPSPVAGTLLEIRAPEDDTVEVGTVLAIIGDANAAPAEPAEEEAPAPSEAGSEPAPDPAARAPHAAPDP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522119224 241 PKPVEAPKPVAQPAPKPAAASSDNGsdnaPYVTPLVRKLASEHGIDLSSLTGSGVGGRIRKQDVLAAAEAKQKAAPAPAA 320
Cdd:TIGR02927 241 PAPAPAPAKTAAPAAAAPVSSGDSG----PYVTPLVRKLAKDKGVDLSTVKGTGVGGRIRKQDVLAAAKAAEEARAAAAA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522119224 321 QPAAAAPAAAAPSAPRkaaVSPELAALRGTVQKASRIRQITAVKTRESLQLSAQLTQVHEVDVTKIAKLRQRAKAAFKER 400
Cdd:TIGR02927 317 PAAAAAPAAPAAAAKP---AEPDTAKLRGTTQKMNRIRQITADKTIESLQTSAQLTQVHEVDMTRVAALRARAKNDFLEK 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522119224 401 EGVNLTFLPFFAKATVEALKQHPNVNASYNEDTKEITYHGAVHLGIAVDTEKGLLSVVIHDAGELSLAGLAHRIADLAGR 480
Cdd:TIGR02927 394 NGVNLTFLPFFVQAVTEALKAHPNVNASYNAETKEVTYHDVEHVGIAVDTPRGLLVPVIHNAGDLSLPGLAKAINDLAAR 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522119224 481 ARAGQIKPDELSGGTFTITNIGSNGALFDTPIIVQPQSGMLGTGAVVKRPVVIADADGNDTIAVRSMAFLPLTYDHRLVD 560
Cdd:TIGR02927 474 ARDNKLKPDELSGGTFTITNIGSGGALFDTPILNPPQAAILGTGAIVKRPRVIKDEDGGESIAIRSVCYLPLTYDHRLVD 553
|
570 580
....*....|....*....|....*.
gi 522119224 561 GADAGRFVTTIKQRLEEGNFEDELGL 586
Cdd:TIGR02927 554 GADAGRFLTTIKKRLEEGDFEGDLGL 579
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
1-581 |
0e+00 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 571.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522119224 1 MAYSVTLPELGEsVTEGTVTRWLKQEGDTVEVDEPLLEISTDKVDTEVPSPVAGKVVKISAQEDETVEVGGELAVIDDGT 80
Cdd:PRK11855 1 MAIEFKVPDIGE-VVEVEVIEWLVKEGDTVEEDQPLVTVETDKATMEIPSPAAGVVKEIKVKVGDTVSVGGLLAVIEAAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522119224 81 GGVPESsgsaapAAEEAQPEPEPEPVQEQASAPSQPAAAPASGGEGTEVKLPELGEsVTEGTVTRWLKQVGDSVEVDEPL 160
Cdd:PRK11855 80 AAAAAA------APAAAAAPAAAAAAAPAPAAAAPAAAAAAAGGGVVEVKVPDIGE-ITEVEVIEWLVKVGDTVEEDQSL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522119224 161 LEISTDKVDTEVPSPVAGTVLEIRAGEDETVEVGGVLAVIGAAGSAPAPKAEPKPEPKpepkpepkpepkpepkvEAAPA 240
Cdd:PRK11855 153 ITVETDKATMEIPSPVAGVVKEIKVKVGDKVSVGSLLVVIEVAAAAPAAAAAPAAAAP-----------------AAAAA 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522119224 241 PKPVEAPKPVAQPAPKPAAASSDNGsdNAPYVTPLVRKLASEHGIDLSSLTGSGVGGRIRKQDVLAAAEAKQKAAPAPAA 320
Cdd:PRK11855 216 AAPAPAPAAAAAPAAAAPAAAAAPG--KAPHASPAVRRLARELGVDLSQVKGTGKKGRITKEDVQAFVKGAMSAAAAAAA 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522119224 321 QPAAAAPAAAAPSAPRKAAVSPelaalRGTVQKA--SRIRQITAVKTRESLQLSAQLTQVHEVDVTKIAKLRQRAKAAFk 398
Cdd:PRK11855 294 AAAAAGGGGLGLLPWPKVDFSK-----FGEIETKplSRIKKISAANLHRSWVTIPHVTQFDEADITDLEALRKQLKKEA- 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522119224 399 EREGVNLTFLPFFAKATVEALKQHPNVNASYNEDTKEITYHGAVHLGIAVDTEKGLLSVVIHDAGELSLAGLAHRIADLA 478
Cdd:PRK11855 368 EKAGVKLTMLPFFIKAVVAALKEFPVFNASLDEDGDELTYKKYFNIGFAVDTPNGLVVPVIKDVDKKSLLEIAREIAELA 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522119224 479 GRARAGQIKPDELSGGTFTITNIGSNGALFDTPIIVQPQSGMLGTGAVVKRPVviadaDGNDTIAVRSMAFLPLTYDHRL 558
Cdd:PRK11855 448 KKARDGKLKPDDMQGGCFTISSLGGIGGTAFTPIINAPEVAILGVGKSQMKPV-----WDGKEFVPRLMLPLSLSYDHRV 522
|
570 580
....*....|....*....|...
gi 522119224 559 VDGADAGRFVTTIKQRLEEGNFE 581
Cdd:PRK11855 523 IDGATAARFTNYLKQLLADPRRM 545
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
5-579 |
4.92e-174 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 507.23 E-value: 4.92e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522119224 5 VTLPELGesVTEGTVTRWLKQEGDTVEVDEPLLEISTDKVDTEVPSPVAGKVVKISAQEDETVEVGGELAVIDDGTGGVP 84
Cdd:PRK11854 108 VHVPDIG--SDEVEVTEILVKVGDTVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVSTGSLIMVFEVAGEAPA 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522119224 85 ESSgsaapaaeeaqpepepepvqeQASAPSQPAAAPASGGEGTEVKLPELGesVTEGTVTRWLKQVGDSVEVDEPLLEIS 164
Cdd:PRK11854 186 AAP---------------------AAAEAAAPAAAPAAAAGVKDVNVPDIG--GDEVEVTEVMVKVGDKVEAEQSLITVE 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522119224 165 TDKVDTEVPSPVAGTVLEIRAGEDETVEVGGVLAVIGAAGSAPAPKAEPKPepkpepkpepkpepkpepkvEAAPAPKPV 244
Cdd:PRK11854 243 GDKASMEVPAPFAGTVKEIKVNVGDKVKTGSLIMRFEVEGAAPAAAPAKQE--------------------AAAPAPAAA 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522119224 245 EAPKPVAQPAPKPAAASSDNGSDNAPYVTPLVRKLASEHGIDLSSLTGSGVGGRIRKQDVLAAAEAKQKAAPAPAAQPAA 324
Cdd:PRK11854 303 KAEAPAAAPAAKAEGKSEFAENDAYVHATPLVRRLAREFGVNLAKVKGTGRKGRILKEDVQAYVKDAVKRAEAAPAAAAA 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522119224 325 AAPAAAAPSAPRkaaVSPELAALRGTVQkASRIRQITAVKTRESLQLSAQLTQVHEVDVTKIAKLRQRAKA-AFKEREGV 403
Cdd:PRK11854 383 GGGGPGLLPWPK---VDFSKFGEIEEVE-LGRIQKISGANLHRNWVMIPHVTQFDKADITELEAFRKQQNAeAEKRKLGV 458
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522119224 404 NLTFLPFFAKATVEALKQHPNVNASYNEDTKEITYHGAVHLGIAVDTEKGLLSVVIHDAGELSLAGLAHRIADLAGRARA 483
Cdd:PRK11854 459 KITPLVFIMKAVAAALEQMPRFNSSLSEDGQRLTLKKYVNIGIAVDTPNGLVVPVFKDVNKKGIIELSRELMDISKKARD 538
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522119224 484 GQIKPDELSGGTFTITNIGSNGALFDTPIIVQPQSGMLGTGAVVKRPVviadaDGNDTIAVRSMAFLPLTYDHRLVDGAD 563
Cdd:PRK11854 539 GKLTAGDMQGGCFTISSIGGLGTTHFTPIVNAPEVAILGVSKSAMEPV-----WNGKEFAPRLMLPLSLSYDHRVIDGAD 613
|
570
....*....|....*.
gi 522119224 564 AGRFVTTIKQRLEEGN 579
Cdd:PRK11854 614 GARFITIINDRLSDIR 629
|
|
| PRK11856 |
PRK11856 |
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed |
127-577 |
3.28e-133 |
|
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
Pssm-ID: 237001 [Multi-domain] Cd Length: 411 Bit Score: 394.93 E-value: 3.28e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522119224 127 TEVKLPELGESVTEGTVTRWLKQVGDSVEVDEPLLEISTDKVDTEVPSPVAGTVLEIRAGEDETVEVGGVLAVIGAAGSA 206
Cdd:PRK11856 3 FEFKMPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDVVPVGSVIAVIEEEGEA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522119224 207 PAPKAEPKPepkpepkpepkpepkpepkvEAAPAPKPVEAPKPVAQPAPKPAAASSDNGSDNAPyVTPLVRKLASEHGID 286
Cdd:PRK11856 83 EAAAAAEAA--------------------PEAPAPEPAPAAAAAAAAAPAAAAAPAAPAAAAAK-ASPAVRKLARELGVD 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522119224 287 LSSLTGSGVGGRIRKQDVLaaaeakqkaapapaaqPAAAAPAAAAPSAPRKAAVSPELAALRGTVQKASRIRQITAVKTR 366
Cdd:PRK11856 142 LSTVKGSGPGGRITKEDVE----------------AAAAAAAPAAAAAAAAAAAPPAAAAEGEERVPLSGMRKAIAKRMV 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522119224 367 ESLQLSAQLTQVHEVDVTKIAKLRQRAKAafkerEGVNLTFLPFFAKATVEALKQHPNVNASYNEDTkeITYHGAVHLGI 446
Cdd:PRK11856 206 ESKREIPHFTLTDEVDVTALLALRKQLKA-----IGVKLTVTDFLIKAVALALKKFPELNASWDDDA--IVLKKYVNIGI 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522119224 447 AVDTEKGLLSVVIHDAGELSLAGLAHRIADLAGRARAGQIKPDELSGGTFTITNIGSNGALFDTPIIVQPQSGMLGTGAV 526
Cdd:PRK11856 279 AVATDGGLIVPVIRDADKKSLFELAREIKDLAEKAREGKLKPEELQGGTFTISNLGMFGGDYFTPIINPPEVAILGVGAI 358
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 522119224 527 VKRPVVIadadgNDTIAVRSMAFLPLTYDHRLVDGADAGRFVTTIKQRLEE 577
Cdd:PRK11856 359 VERPVVV-----DGEIVVRKVMPLSLSFDHRVIDGADAARFLKALKELLEN 404
|
|
| PRK05704 |
PRK05704 |
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase; |
127-576 |
1.20e-119 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
Pssm-ID: 235571 [Multi-domain] Cd Length: 407 Bit Score: 359.92 E-value: 1.20e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522119224 127 TEVKLPELGESVTEGTVTRWLKQVGDSVEVDEPLLEISTDKVDTEVPSPVAGTVLEIRAGEDETVEVGGVLAVIGAAGsa 206
Cdd:PRK05704 3 VEIKVPTLPESVTEATIATWHKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGDTVTVGQVLGRIDEGA-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522119224 207 papkaepkpepkpepkpepkpepkpepkveAAPAPKPVEAPKPVAQPAPKPAAASSDNGSDNAPyVTPLVRKLASEHGID 286
Cdd:PRK05704 81 ------------------------------AAGAAAAAAAAAAAAAAAPAQAQAAAAAEQSNDA-LSPAARKLAAENGLD 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522119224 287 LSSLTGSGVGGRIRKQDVLAAAEAKQKAAPAPAAQPAAAapaaaapsaprkaaVSPELAALRGTVQKASRIRQITAVKTR 366
Cdd:PRK05704 130 ASAVKGTGKGGRVTKEDVLAALAAAAAAPAAPAAAAPAA--------------APAPLGARPEERVPMTRLRKTIAERLL 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522119224 367 ESLQLSAQLTQVHEVDVTKIAKLRQRAKAAFKEREGVNLTFLPFFAKATVEALKQHPNVNASYneDTKEITYHGAVHLGI 446
Cdd:PRK05704 196 EAQNTTAMLTTFNEVDMTPVMDLRKQYKDAFEKKHGVKLGFMSFFVKAVVEALKRYPEVNASI--DGDDIVYHNYYDIGI 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522119224 447 AVDTEKGLLSVVIHDAGELSLAGLAHRIADLAGRARAGQIKPDELSGGTFTITNIGSNGALFDTPIIVQPQSGMLGTGAV 526
Cdd:PRK05704 274 AVGTPRGLVVPVLRDADQLSFAEIEKKIAELAKKARDGKLSIEELTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHKI 353
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 522119224 527 VKRPVVIadadgNDTIAVRSMAFLPLTYDHRLVDGADAGRFVTTIKQRLE 576
Cdd:PRK05704 354 KERPVAV-----NGQIVIRPMMYLALSYDHRIIDGKEAVGFLVTIKELLE 398
|
|
| sucB |
TIGR01347 |
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ... |
127-577 |
1.92e-106 |
|
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: 325.92 E-value: 1.92e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522119224 127 TEVKLPELGESVTEGTVTRWLKQVGDSVEVDEPLLEISTDKVDTEVPSPVAGTVLEIRAGEDETVEVGGVLAVIGAAGSA 206
Cdd:TIGR01347 1 IEIKVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAILEEGNDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522119224 207 PapkaepkpepkpepkpepkpepkpepkvEAAPAPKPVEAPKpvaqpAPKPAAASSDNGSDNAPYVTPLVRKLASEHGID 286
Cdd:TIGR01347 81 T----------------------------AAPPAKSGEEKEE-----TPAASAAAAPTAAANRPSLSPAARRLAKEHGID 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522119224 287 LSSLTGSGVGGRIRKQDVLAAAEAKQKAAPAPAAQPAAaapaaaapsaprkaavSPELAALRGTVQKASRIRQITAVKTR 366
Cdd:TIGR01347 128 LSAVPGTGVTGRVTKEDIIKKTEAPASAQPPAAAAAAA----------------APAAATRPEERVKMTRLRQRIAERLK 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522119224 367 ESLQLSAQLTQVHEVDVTKIAKLRQRAKAAFKEREGVNLTFLPFFAKATVEALKQHPNVNASYneDTKEITYHGAVHLGI 446
Cdd:TIGR01347 192 EAQNSTAMLTTFNEVDMSAVMELRKRYKEEFEKKHGVKLGFMSFFVKAVVAALKRFPEVNAEI--DGDDIVYKDYYDISV 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522119224 447 AVDTEKGLLSVVIHDAGELSLAGLAHRIADLAGRARAGQIKPDELSGGTFTITNIGSNGALFDTPIIVQPQSGMLGTGAV 526
Cdd:TIGR01347 270 AVSTDRGLVVPVVRNADRMSFADIEKEIADLGKKARDGKLTLEDMTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHGI 349
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 522119224 527 VKRPVVIadadgNDTIAVRSMAFLPLTYDHRLVDGADAGRFVTTIKQRLEE 577
Cdd:TIGR01347 350 KERPVAV-----NGQIEIRPMMYLALSYDHRLIDGKEAVTFLVTIKELLED 395
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
367-577 |
1.01e-84 |
|
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: 262.86 E-value: 1.01e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522119224 367 ESLQLSAQLTQVHEVDVTKIAKLRQRAKAAFKEREGvNLTFLPFFAKATVEALKQHPNVNASYNEDTKEITYHGAVHLGI 446
Cdd:pfam00198 3 ESKQTIPHFTLTDEVDVTELLALREELKEDAADEET-KLTFLPFLVKAVALALKKFPELNASWDGEEGEIVYKKYVNIGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522119224 447 AVDTEKGLLSVVIHDAGELSLAGLAHRIADLAGRARAGQIKPDELSGGTFTITNIGSNGALFDTPIIVQPQSGMLGTGAV 526
Cdd:pfam00198 82 AVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVGRI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 522119224 527 VKRPVVIadadgNDTIAVRSMAFLPLTYDHRLVDGADAGRFVTTIKQRLEE 577
Cdd:pfam00198 162 RKRPVVV-----DGEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLEN 207
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
7-577 |
1.64e-84 |
|
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: 273.67 E-value: 1.64e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522119224 7 LPELGESvTEGTVTRWLKQEGDTVEVDEPLLEISTDKVDTEVPSPVAGKVVKISAQEDETVEVGGELAVIDDGTGGVPES 86
Cdd:TIGR01348 5 VPDIGDN-EEGEVIEVLVKPGDKVEAGQSLITLESDKASMEVPSSAAGIIKEIKVKVGDTLPVGGVIATLEVGAGAQAQA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522119224 87 SgsaapaaEEAQPEPEPEPVQEQASAPSQPAAAPASGGEGTEVKLPELGeSVTEGTVTRWLKQVGDSVEVDEPLLEISTD 166
Cdd:TIGR01348 84 E-------AKKEAAPAPTAGAPAPAAQAQAAPAAGQSSGVQEVTVPDIG-DIEKVTVIEVLVKVGDTVSADQSLITLESD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522119224 167 KVDTEVPSPVAGTVLEIRAGEDETVEVGGVLAVIGAAGSAPAPKAEPKPEPKPEPKpepkpepkpepkvEAAPAPKPVEA 246
Cdd:TIGR01348 156 KASMEVPAPASGVVKSVKVKVGDSVPTGDLILTLSVAGSTPATAPAPASAQPAAQS-------------PAATQPEPAAA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522119224 247 PKPVAQPAPKPAAASSDNGSdNAPYVTPLVRKLASEHGIDLSSLTGSGVGGRIRKQDVLAAAEAKQKAAPAPAAQPAAAA 326
Cdd:TIGR01348 223 PAAAKAQAPAPQQAGTQNPA-KVDHAAPAVRRLAREFGVDLSAVKGTGIKGRILREDVQRFVKEPSVRAQAAAASAAGGA 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522119224 327 PAAAAPsaprkaavsPELAALR-GTV--QKASRIRQITAVKTRESLQLSAQLTQVHEVDVTKIAKLRQRAKAAfKEREGV 403
Cdd:TIGR01348 302 PGALPW---------PNVDFSKfGEVeeVDMSRIRKISGANLTRNWTMIPHVTHFDKADITEMEAFRKQQNAA-VEKEGV 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522119224 404 NLTFLPFFAKATVEALKQHPNVNASYNEDTKEITYHGAVHLGIAVDTEKGLLSVVIHDAGELSLAGLAHRIADLAGRARA 483
Cdd:TIGR01348 372 KLTVLHILMKAVAAALKKFPKFNASLDLGGEQLILKKYVNIGVAVDTPNGLLVPVIKDVDRKGITELALELSDLAKKARD 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522119224 484 GQIKPDELSGGTFTITNIGSNGALFDTPIIVQPQSGMLGTGAVVKRPVviadADGNDtIAVRSMAFLPLTYDHRLVDGAD 563
Cdd:TIGR01348 452 GKLTPDEMQGACFTISSLGGIGGTAFTPIVNAPEVAILGVSKSGMEPV----WNGKE-FEPRLMLPLSLSYDHRVIDGAD 526
|
570
....*....|....
gi 522119224 564 AGRFVTTIKQRLEE 577
Cdd:TIGR01348 527 AARFTTYICESLAD 540
|
|
| PTZ00144 |
PTZ00144 |
dihydrolipoamide succinyltransferase; Provisional |
129-577 |
3.15e-81 |
|
dihydrolipoamide succinyltransferase; Provisional
Pssm-ID: 240289 [Multi-domain] Cd Length: 418 Bit Score: 261.16 E-value: 3.15e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522119224 129 VKLPELGESVTEGTVTRWLKQVGDSVEVDEPLLEISTDKVDTEVPSPVAGTVLEIRAGEDETVEVGGVLAVIGAAGSAPA 208
Cdd:PTZ00144 47 IKVPTMGDSISEGTVVEWKKKVGDYVKEDEVICIIETDKVSVDIRAPASGVITKIFAEEGDTVEVGAPLSEIDTGGAPPA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522119224 209 PKAEPKPEPKPEPKPEpkpepkpepkvEAAPAPKPVEAPKPVAQPAPKPAAASSDNGSDNAPYVTPLVRKLASEhgidls 288
Cdd:PTZ00144 127 AAPAAAAAAKAEKTTP-----------EKPKAAAPTPEPPAASKPTPPAAAKPPEPAPAAKPPPTPVARADPRE------ 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522119224 289 sltgsgvggrirkqdvlaaaeakqkaapapaaqpaaaapaaaapsaprkaavspelaalrgTVQKASRIRQITAVKTRES 368
Cdd:PTZ00144 190 -------------------------------------------------------------TRVPMSRMRQRIAERLKAS 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522119224 369 LQLSAQLTQVHEVDVTKIAKLRQRAKAAFKEREGVNLTFLPFFAKATVEALKQHPNVNASYneDTKEITYHGAVHLGIAV 448
Cdd:PTZ00144 209 QNTCAMLTTFNECDMSALMELRKEYKDDFQKKHGVKLGFMSAFVKASTIALKKMPIVNAYI--DGDEIVYRNYVDISVAV 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522119224 449 DTEKGLLSVVIHDAGELSLAGLAHRIADLAGRARAGQIKPDELSGGTFTITNIGSNGALFDTPIIVQPQSGMLGTGAVVK 528
Cdd:PTZ00144 287 ATPTGLVVPVIRNCENKSFAEIEKELADLAEKARNNKLTLEDMTGGTFTISNGGVFGSLMGTPIINPPQSAILGMHAIKK 366
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 522119224 529 RPVVIadadgNDTIAVRSMAFLPLTYDHRLVDGADAGRFVTTIKQRLEE 577
Cdd:PTZ00144 367 RPVVV-----GNEIVIRPIMYLALTYDHRLIDGRDAVTFLKKIKDLIED 410
|
|
| PRK11857 |
PRK11857 |
dihydrolipoamide acetyltransferase; Reviewed |
272-576 |
2.16e-66 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237002 [Multi-domain] Cd Length: 306 Bit Score: 218.51 E-value: 2.16e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522119224 272 VTPLVRKLASEHGIDLSSLTGSGVGGRIRKQDVLAAAEAKQKAAPAPAAQPAAAAPAAAAPSAPrkaavSPELAALRGTV 351
Cdd:PRK11857 4 ATPIARALAKKLGIDISLLKGSGRDGKILAEDVENFIKSLKSAPTPAEAASVSSAQQAAKTAAP-----AAAPPKLEGKR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522119224 352 QKASRIRQITAVKTRESLQLSAQLTQVHEVDVTKIAKLRQRAKAAFKEREGVNLTFLPFFAKATVEALKQHPNVNASYNE 431
Cdd:PRK11857 79 EKVAPIRKAIARAMTNSWSNVAYVNLVNEIDMTKLWDLRKSVKDPVLKTEGVKLTFLPFIAKAILIALKEFPIFAAKYDE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522119224 432 DTKEITYHGAVHLGIAVDTEKGLLSVVIHDAGELSLAGLAHRIADLAGRARAGQIKPDELSGGTFTITNIGSNGALFDTP 511
Cdd:PRK11857 159 ATSELVYPDTLNLGIAVDTEAGLMVPVIKNAQKLSIVEIAKEISRLAKAARERKIKPDEMKGGSFTITNYGSVGSLYGVP 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 522119224 512 IIVQPQSGMLGTGAVVKRPVVIadadgNDTIAVRSMAFLPLTYDHRLVDGADAGRFVTTIKQRLE 576
Cdd:PRK11857 239 VINYPELAIAGVGAIIDKAIVK-----NGQIVAGKVMHLTVAADHRWIDGATIGRFASRVKELLE 298
|
|
| PDHac_trf_mito |
TIGR01349 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
128-576 |
1.03e-61 |
|
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: 210.42 E-value: 1.03e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522119224 128 EVKLPELGESVTEGTVTRWLKQVGDSVEVDEPLLEISTDKVDTEVPSPVAGTVLEIRAGED-ETVEVGGVLAVIGAAGSA 206
Cdd:TIGR01349 1 KITMPALSPTMTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEGtKDVPVNKPIAVLVEEKED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522119224 207 PAPKAEPKPEPKPEPKPEPKPepkpepkvEAAPAPKPVEAPKPVAQPAPKPAAASSDNGSDNAP----YVTPLVRKLASE 282
Cdd:TIGR01349 81 VADAFKNYKLESSASPAPKPS--------EIAPTAPPSAPKPSPAPQKQSPEPSSPAPLSDKESgdriFASPLAKKLAKE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522119224 283 HGIDLSSLTGSGVGGRIRKQDVLAAAEAKQKAAPAPAAQPAAAAPAAAAPSAPRKAAVSPelaalrgtvqkASRIRQITA 362
Cdd:TIGR01349 153 KGIDLSAVAGSGPNGRIVKKDIESFVPQSPASANQQAAATTPATYPAAAPVSTGSYEDVP-----------LSNIRKIIA 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522119224 363 VKTRESLQLSAQLTQVHEVDVTKIAKLRQRAKAAFKERegVNLTFLPFFAKATVEALKQHPNVNASYNEDTkeITYHGAV 442
Cdd:TIGR01349 222 KRLLESKQTIPHYYVSIECNVDKLLALRKELNAMASEV--YKLSVNDFIIKASALALREVPEANSSWTDNF--IRRYKNV 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522119224 443 HLGIAVDTEKGLLSVVIHDAGELSLAGLAHRIADLAGRARAGQIKPDELSGGTFTITNIGSNGALFDTPIIVQPQSGMLG 522
Cdd:TIGR01349 298 DISVAVATPDGLITPIVRNADAKGLSTISNEIKDLAKRARNNKLKPEEFQGGTFTISNLGMFGIKDFTAIINPPQACILA 377
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 522119224 523 TGAVVKRPVVIADADgnDTIAVRSMAFLPLTYDHRLVDGADAGRFVTTIKQRLE 576
Cdd:TIGR01349 378 VGAVEDVAVVDNDEE--KGFAVASIMSVTLSCDHRVIDGAVGAEFLKSFKKYLE 429
|
|
| PLN02226 |
PLN02226 |
2-oxoglutarate dehydrogenase E2 component |
124-577 |
4.38e-54 |
|
2-oxoglutarate dehydrogenase E2 component
Pssm-ID: 177871 [Multi-domain] Cd Length: 463 Bit Score: 190.74 E-value: 4.38e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522119224 124 GEGTEVKLPELGESVTEGTVTRWLKQVGDSVEVDEPLLEISTDKVDTEVPSPVAGTVLEIRAGEDETVEVGGVLAVIG-A 202
Cdd:PLN02226 89 GDTVEAVVPHMGESITDGTLATFLKKPGERVQADEAIAQIETDKVTIDIASPASGVIQEFLVKEGDTVEPGTKVAIISkS 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522119224 203 AGSAPAPKAEPKPEPKPEPKPEPKPEPKPEPKVEAAPApkpVEAPKpvaqpapkpaaassdngsdnAPYVTPLVRKLASE 282
Cdd:PLN02226 169 EDAASQVTPSQKIPETTDPKPSPPAEDKQKPKVESAPV---AEKPK--------------------APSSPPPPKQSAKE 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522119224 283 hgidlssltgsgvggrirkqdvlaaaeakqkaapapaaqpaaaapaaaapsaprkaavsPELAAL-RGTVQKASRIRQIT 361
Cdd:PLN02226 226 -----------------------------------------------------------PQLPPKeRERRVPMTRLRKRV 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522119224 362 AVKTRESLQLSAQLTQVHEVDVTKIAKLRQRAKAAFKEREGVNLTFLPFFAKATVEALKQHPNVNASYNEDtkEITYHGA 441
Cdd:PLN02226 247 ATRLKDSQNTFALLTTFNEVDMTNLMKLRSQYKDAFYEKHGVKLGLMSGFIKAAVSALQHQPVVNAVIDGD--DIIYRDY 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522119224 442 VHLGIAVDTEKGLLSVVIHDAGELSLAGLAHRIADLAGRARAGQIKPDELSGGTFTITNIGSNGALFDTPIIVQPQSGML 521
Cdd:PLN02226 325 VDISIAVGTSKGLVVPVIRGADKMNFAEIEKTINGLAKKANEGTISIDEMAGGSFTVSNGGVYGSLISTPIINPPQSAIL 404
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 522119224 522 GTGAVVKRPVVIAdadgnDTIAVRSMAFLPLTYDHRLVDGADAGRFVTTIKQRLEE 577
Cdd:PLN02226 405 GMHSIVSRPMVVG-----GSVVPRPMMYVALTYDHRLIDGREAVYFLRRVKDVVED 455
|
|
| PLN02528 |
PLN02528 |
2-oxoisovalerate dehydrogenase E2 component |
129-576 |
1.32e-48 |
|
2-oxoisovalerate dehydrogenase E2 component
Pssm-ID: 215289 [Multi-domain] Cd Length: 416 Bit Score: 174.52 E-value: 1.32e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522119224 129 VKLPELGESVTEGTVTRWLKQVGDSVEVDEPLLEISTDKVDTEVPSPVAGTVLEIRAGEDETVEVGGVLAVIgaagsapa 208
Cdd:PLN02528 1 VPLAQTGEGIAECELLRWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGKVAQINFSPGDIVKVGETLLKI-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522119224 209 pkaepkpepkpepkpepkpepkpepKVEAAPAPKPVEAPKPVAQPAPKPAAASSDNGSDNAPYV-TPLVRKLASEHGIDL 287
Cdd:PLN02528 73 -------------------------MVEDSQHLRSDSLLLPTDSSNIVSLAESDERGSNLSGVLsTPAVRHLAKQYGIDL 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522119224 288 SSLTGSGVGGRIRKQDVLAAAEAKQKAAPAPAAQPAAAAPAAAAPSAprkaaVSPELAALRGTVQKASRIRQITAVKTre 367
Cdd:PLN02528 128 NDILGTGKDGRVLKEDVLKYAAQKGVVKDSSSAEEATIAEQEEFSTS-----VSTPTEQSYEDKTIPLRGFQRAMVKT-- 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522119224 368 sLQLSAQLTQVH---EVDVTKIAKLRQRAKAAfKEREGVNLTFLPFFAKATVEALKQHPNVNASYNEDTKEITYHGAVHL 444
Cdd:PLN02528 201 -MTAAAKVPHFHyveEINVDALVELKASFQEN-NTDPTVKHTFLPFLIKSLSMALSKYPLLNSCFNEETSEIRLKGSHNI 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522119224 445 GIAVDTEKGLLSVVIHDAGELSLAGLAHRIADLAGRARAGQIKPDELSGGTFTITNIGSNGALFDTPIIVQPQSGMLGTG 524
Cdd:PLN02528 279 GVAMATEHGLVVPNIKNVQSLSLLEITKELSRLQHLAAENKLNPEDITGGTITLSNIGAIGGKFGSPVLNLPEVAIIALG 358
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 522119224 525 AVVKRPVViadadgNDTIAVRSMAFLPLTY--DHRLVDGADAGRFVTTIKQRLE 576
Cdd:PLN02528 359 RIQKVPRF------VDDGNVYPASIMTVTIgaDHRVLDGATVARFCNEWKSYVE 406
|
|
| PRK14843 |
PRK14843 |
dihydrolipoamide acetyltransferase; Provisional |
272-576 |
5.68e-44 |
|
dihydrolipoamide acetyltransferase; Provisional
Pssm-ID: 184847 [Multi-domain] Cd Length: 347 Bit Score: 160.07 E-value: 5.68e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522119224 272 VTPLVRKLASEHGIDLSSLTGSGVGGRIRKQDVLAAAEAKQKAAPAPAAQPAAAAPaaaapsaprkaaVSPELAALRGTV 351
Cdd:PRK14843 51 ISPLAKRIALEHNIAWQEIQGTGHRGKIMKKDVLALLPENIENDSIKSPAQIEKVE------------EVPDNVTPYGEI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522119224 352 QK--ASRIRQITAVKTRESLQLSAQLTQVHEVDVTKIAKLRQRAKAAFKEREGVNLTFLPFFAKATVEALKQHPNVNASY 429
Cdd:PRK14843 119 ERipMTPMRKVIAQRMVESYLTAPTFTLNYEVDMTEMLALRKKVLEPIMEATGKKTTVTDLLSLAVVKTLMKHPYINASL 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522119224 430 NEDTKEITYHGAVHLGIAVDTEKGLLSVVIHDAGELSLAGLAHRIADLAGRARAGQIKPDELSGGTFTITNIGSNGALFD 509
Cdd:PRK14843 199 TEDGKTIITHNYVNLAMAVGMDNGLMTPVVYNAEKMSLSELVVAFKDVIGRTLDGKLAPSELQNSTFTISNLGMFGVQSF 278
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 522119224 510 TPIIVQPQSGMLGTGAVVKRPVVIadadgNDTIAVRSMAFLPLTYDHRLVDGADAGRFVTTIKQRLE 576
Cdd:PRK14843 279 GPIINQPNSAILGVSSTIEKPVVV-----NGEIVIRPIMSLGLTIDHRVVDGMAGAKFMKDLKELIE 340
|
|
| PLN02744 |
PLN02744 |
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex |
128-576 |
1.80e-41 |
|
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
Pssm-ID: 215397 [Multi-domain] Cd Length: 539 Bit Score: 157.32 E-value: 1.80e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522119224 128 EVKLPELGESVTEGTVTRWLKQVGDSVEVDEPLLEISTDKVDTEVPSPVAGTVLEIRAGE-DETVEVGGVLAVigaagsa 206
Cdd:PLN02744 114 EIGMPSLSPTMTEGNIARWLKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVKGDgAKEIKVGEVIAI------- 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522119224 207 pAPKAEPKPEPKPEPKPEPKPEPKPEPKVEAAPAPKPVEAPKPVAQPAPKPAAASSDNGSDNAPYVTPLVRKLASEHGID 286
Cdd:PLN02744 187 -TVEEEEDIGKFKDYKPSSSAAPAAPKAKPSPPPPKEEEVEKPASSPEPKASKPSAPPSSGDRIFASPLARKLAEDNNVP 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522119224 287 LSSLTGSGVGGRIRKQDVLAAAEAKQKAAPAPAAQPAaaapaaaapsaprkaavspELAALRGTVQKASRIRQITAVKTR 366
Cdd:PLN02744 266 LSSIKGTGPDGRIVKADIEDYLASGGKGATAPPSTDS-------------------KAPALDYTDIPNTQIRKVTASRLL 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522119224 367 ESLQLSAQLTQVHEVDVTKIAKLRQRAKAAFKEREGVNLTFLPFFAKATVEALKQHPNVNASYNEDTkeITYHGAVHLGI 446
Cdd:PLN02744 327 QSKQTIPHYYLTVDTRVDKLMALRSQLNSLQEASGGKKISVNDLVIKAAALALRKVPQCNSSWTDDY--IRQYHNVNINV 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522119224 447 AVDTEKGLLSVVIHDAGELSLAGLAHRIADLAGRARAGQIKPDELSGGTFTITNIGSN-GALFDTPIIVQPQSGMLGTGA 525
Cdd:PLN02744 405 AVQTENGLYVPVVKDADKKGLSTIAEEVKQLAQKARENSLKPEDYEGGTFTVSNLGGPfGIKQFCAIINPPQSAILAVGS 484
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 522119224 526 VVKRpVVIADADGNDTIAvrsmAFLPLTY--DHRLVDGADAGRFVTTIKQRLE 576
Cdd:PLN02744 485 AEKR-VIPGSGPDQYNFA----SFMSVTLscDHRVIDGAIGAEWLKAFKGYIE 532
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
127-200 |
4.11e-30 |
|
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: 112.85 E-value: 4.11e-30
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 522119224 127 TEVKLPELGESVTEGTVTRWLKQVGDSVEVDEPLLEISTDKVDTEVPSPVAGTVLEIRAGEDETVEVGGVLAVI 200
Cdd:COG0508 3 IEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
1-76 |
1.66e-29 |
|
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: 110.93 E-value: 1.66e-29
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 522119224 1 MAYSVTLPELGESVTEGTVTRWLKQEGDTVEVDEPLLEISTDKVDTEVPSPVAGKVVKISAQEDETVEVGGELAVI 76
Cdd:COG0508 1 MAIEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
127-200 |
1.54e-28 |
|
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: 108.26 E-value: 1.54e-28
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 522119224 127 TEVKLPELGESVTEGTVTRWLKQVGDSVEVDEPLLEISTDKVDTEVPSPVAGTVLEIRAGEDETVEVGGVLAVI 200
Cdd:cd06849 1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
5-76 |
4.24e-27 |
|
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: 104.41 E-value: 4.24e-27
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 522119224 5 VTLPELGESVTEGTVTRWLKQEGDTVEVDEPLLEISTDKVDTEVPSPVAGKVVKISAQEDETVEVGGELAVI 76
Cdd:cd06849 3 IKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
1-86 |
9.17e-20 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 91.16 E-value: 9.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522119224 1 MAYSVTLPELGESVTEGTVTRWLKQEGDTVEVDEPLLEISTDKVDTEVPSPVAGKVVKISAQEDETVEVGGELAVIDDgt 80
Cdd:PRK14875 1 SITPITMPKWGLSMTEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGETLPVGALLAVVAD-- 78
|
....*.
gi 522119224 81 GGVPES 86
Cdd:PRK14875 79 AEVSDA 84
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
127-204 |
1.92e-19 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 90.39 E-value: 1.92e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 522119224 127 TEVKLPELGESVTEGTVTRWLKQVGDSVEVDEPLLEISTDKVDTEVPSPVAGTVLEIRAGEDETVEVGGVLAVIGAAG 204
Cdd:PRK14875 3 TPITMPKWGLSMTEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGETLPVGALLAVVADAE 80
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
127-200 |
3.64e-19 |
|
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: 81.88 E-value: 3.64e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 522119224 127 TEVKLPELGESVTEGtVTRWLKQVGDSVEVDEPLLEISTDKVDTEVPSPVAGTVLEIRAGEDETVEVGGVLAVI 200
Cdd:pfam00364 1 TEIKSPMIGESVREG-VVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
|
|
| kgd |
PRK12270 |
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ... |
414-584 |
1.77e-18 |
|
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;
Pssm-ID: 237030 [Multi-domain] Cd Length: 1228 Bit Score: 89.95 E-value: 1.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522119224 414 ATVEALKQHPNVNASYNE-DTK-EITYHGAVHLGIAVDTEK-----GLLSVVIHDAGELSLAGLAHRIADLAGRARAGQI 486
Cdd:PRK12270 179 ALVQALKAFPNMNRHYAEvDGKpTLVTPAHVNLGLAIDLPKkdgsrQLVVPAIKGAETMDFAQFWAAYEDIVRRARDGKL 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522119224 487 KPDELSGGTFTITNIGSNGALFDTPIIVQPQSGMLGTGAVvKRPVVIADADgNDTIA---VRSMAFLPLTYDHRLVDGAD 563
Cdd:PRK12270 259 TADDFQGTTISLTNPGGIGTVHSVPRLMKGQGAIIGVGAM-EYPAEFQGAS-EERLAelgISKVMTLTSTYDHRIIQGAE 336
|
170 180
....*....|....*....|..
gi 522119224 564 AGRFVTTIKQRLE-EGNFEDEL 584
Cdd:PRK12270 337 SGEFLRTIHQLLLgEDGFYDEI 358
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
5-76 |
7.19e-18 |
|
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: 78.02 E-value: 7.19e-18
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 522119224 5 VTLPELGESVTEGtVTRWLKQEGDTVEVDEPLLEISTDKVDTEVPSPVAGKVVKISAQEDETVEVGGELAVI 76
Cdd:pfam00364 3 IKSPMIGESVREG-VVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
|
|
| PTZ00144 |
PTZ00144 |
dihydrolipoamide succinyltransferase; Provisional |
4-96 |
1.47e-15 |
|
dihydrolipoamide succinyltransferase; Provisional
Pssm-ID: 240289 [Multi-domain] Cd Length: 418 Bit Score: 78.96 E-value: 1.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522119224 4 SVTLPELGESVTEGTVTRWLKQEGDTVEVDEPLLEISTDKVDTEVPSPVAGKVVKISAQEDETVEVGGELAVIDdgTGGV 83
Cdd:PTZ00144 46 VIKVPTMGDSISEGTVVEWKKKVGDYVKEDEVICIIETDKVSVDIRAPASGVITKIFAEEGDTVEVGAPLSEID--TGGA 123
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 522119224 84 P------------------------------ESSGSAAPAAEE 96
Cdd:PTZ00144 124 PpaaapaaaaaakaekttpekpkaaaptpepPAASKPTPPAAA 166
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
128-351 |
6.44e-13 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 71.57 E-value: 6.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522119224 128 EVKLPELGesVTEGTVTRWLKQVGDSVEVDEPLLEISTDKVDTEVPSPVAGTVLEIRAGEDETVEVGGVLAVIGAAGSAP 207
Cdd:PRK11854 4 EIKVPDIG--ADEVEVTEILVKVGDKVEAEQSLITVEGDKASMEVPSPQAGVVKEIKVKVGDKVETGALIMIFESADGAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522119224 208 apkaepkpepkpepkpepkpepkpepkvEAAPAPKPVEAPKPvaqpapkpaaassdngsdnapyvtplvrklasehgidl 287
Cdd:PRK11854 82 ----------------------------DAAPAQAEEKKEAA-------------------------------------- 95
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 522119224 288 ssltgsgvggrirkqdvlaaaeakqkaapapaaqpaaaaPAAAAPSAPRKAAVSPELAALRGTV 351
Cdd:PRK11854 96 ---------------------------------------PAAAPAAAAAKDVHVPDIGSDEVEV 120
|
|
| E3_binding |
pfam02817 |
e3 binding domain; This family represents a small domain of the E2 subunit of 2-oxo-acid ... |
270-305 |
1.16e-12 |
|
e3 binding domain; This family represents a small domain of the E2 subunit of 2-oxo-acid dehydrogenases responsible for the binding of the E3 subunit.
Pssm-ID: 460710 [Multi-domain] Cd Length: 36 Bit Score: 62.32 E-value: 1.16e-12
10 20 30
....*....|....*....|....*....|....*.
gi 522119224 270 PYVTPLVRKLASEHGIDLSSLTGSGVGGRIRKQDVL 305
Cdd:pfam02817 1 VLASPAARKLARELGIDLSDVKGTGPGGRITKEDVE 36
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
128-200 |
8.53e-12 |
|
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: 60.92 E-value: 8.53e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 522119224 128 EVKLPELGESVTEGTVTRWLKQVGDSVEVDEPLLEISTDKVDTEVPSPVAGTVLEIRAGEDETVEVGGVLAVI 200
Cdd:cd06663 1 TILIPDLAQHLGDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKVEGDTPLVKI 73
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
5-76 |
2.16e-11 |
|
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: 59.76 E-value: 2.16e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 522119224 5 VTLPELGESVTEGTVTRWLKQEGDTVEVDEPLLEISTDKVDTEVPSPVAGKVVKISAQEDETVEVGGELAVI 76
Cdd:cd06663 2 ILIPDLAQHLGDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKVEGDTPLVKI 73
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
141-200 |
8.55e-11 |
|
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: 57.81 E-value: 8.55e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 522119224 141 GTVTRWLKQVGDSVEVDEPLLEISTDKVDTEVPSPVAGTVLEIRAGEDETVEVGGVLAVI 200
Cdd:cd06850 8 GTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
17-76 |
1.07e-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: 57.43 E-value: 1.07e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 522119224 17 GTVTRWLKQEGDTVEVDEPLLEISTDKVDTEVPSPVAGKVVKISAQEDETVEVGGELAVI 76
Cdd:cd06850 8 GTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
127-248 |
9.24e-09 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 58.01 E-value: 9.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522119224 127 TEVKLPELGESVTEGTVTRWLKQVGDSVEVDEPLLEISTDKVDTEVPSPVAGTVLEIRAGE-DETVEVGGVLAVIGAAG- 204
Cdd:PRK11892 3 IEILMPALSPTMEEGTLAKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKILVPEgTEGVKVNTPIAVLLEEGe 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 522119224 205 ---SAPAPKAEPKPEPKPEPKPEPKPEPKPEPKVEAAPAPKPVEAPK 248
Cdd:PRK11892 83 sasDAGAAPAAAAEAAAAAPAAAAAAAAKKAAPAPAAPAAPAAEVAA 129
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
1-76 |
7.91e-08 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 54.92 E-value: 7.91e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 522119224 1 MAYSVTLPELGESVTEGTVTRWLKQEGDTVEVDEPLLEISTDKVDTEVPSPVAGKVVKISAQE-DETVEVGGELAVI 76
Cdd:PRK11892 1 MAIEILMPALSPTMEEGTLAKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKILVPEgTEGVKVNTPIAVL 77
|
|
| PRK09282 |
PRK09282 |
pyruvate carboxylase subunit B; Validated |
141-200 |
2.66e-07 |
|
pyruvate carboxylase subunit B; Validated
Pssm-ID: 236449 [Multi-domain] Cd Length: 592 Bit Score: 53.31 E-value: 2.66e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 522119224 141 GTVTRWLKQVGDSVEVDEPLLEISTDKVDTEVPSPVAGTVLEIRAGEDETVEVGGVLAVI 200
Cdd:PRK09282 531 GTVVKVKVKEGDKVKAGDTVLVLEAMKMENEIQAPVDGTVKEILVKEGDRVNPGDVLMEI 590
|
|
| PRK09282 |
PRK09282 |
pyruvate carboxylase subunit B; Validated |
17-76 |
7.45e-07 |
|
pyruvate carboxylase subunit B; Validated
Pssm-ID: 236449 [Multi-domain] Cd Length: 592 Bit Score: 52.15 E-value: 7.45e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 522119224 17 GTVTRWLKQEGDTVEVDEPLLEISTDKVDTEVPSPVAGKVVKISAQEDETVEVGGELAVI 76
Cdd:PRK09282 531 GTVVKVKVKEGDKVKAGDTVLVLEAMKMENEIQAPVDGTVKEILVKEGDRVNPGDVLMEI 590
|
|
| AccB |
COG0511 |
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ... |
25-77 |
1.02e-06 |
|
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440277 [Multi-domain] Cd Length: 136 Bit Score: 48.35 E-value: 1.02e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 522119224 25 QEGDTVEVDEPLLEISTDKVDTEVPSPVAGKVVKISAQEDETVEVGGELAVID 77
Cdd:COG0511 84 KVGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVVEILVENGQPVEYGQPLFVIE 136
|
|
| AccB |
COG0511 |
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ... |
149-201 |
1.51e-06 |
|
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: 47.58 E-value: 1.51e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 522119224 149 QVGDSVEVDEPLLEISTDKVDTEVPSPVAGTVLEIRAGEDETVEVGGVLAVIG 201
Cdd:COG0511 84 KVGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVVEILVENGQPVEYGQPLFVIE 136
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
141-201 |
1.90e-04 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 44.74 E-value: 1.90e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 522119224 141 GTVTRWLKQVGDSVEVDEPLLEISTDKVDTEVPSPVAGTVLEIRAGEDETVEVGGVLAVIG 201
Cdd:PRK12999 1085 GSVVTVLVKEGDEVKAGDPLAVIEAMKMETTITAPVDGTVKRVLVKAGDQVEAGDLLVELE 1145
|
|
| PRK06549 |
PRK06549 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
141-201 |
2.01e-04 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235826 [Multi-domain] Cd Length: 130 Bit Score: 41.34 E-value: 2.01e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 522119224 141 GTVTRWLKQVGDSVEVDEPLLEISTDKVDTEVPSPVAGTVLEIRAGEDETVEVGGVLAVIG 201
Cdd:PRK06549 70 GTILKVLVAVGDQVTENQPLLILEAMKMENEIVASSAGTVTAIHVTPGQVVNPGDGLITIG 130
|
|
| GCS_H |
cd06848 |
Glycine cleavage H-protein. Glycine cleavage H-proteins are part of the glycine cleavage ... |
22-59 |
2.70e-04 |
|
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: 40.21 E-value: 2.70e-04
10 20 30
....*....|....*....|....*....|....*...
gi 522119224 22 WLKQEGDTVEVDEPLLEISTDKVDTEVPSPVAGKVVKI 59
Cdd:cd06848 35 ELPEVGTEVKKGDPFGSVESVKAASDLYSPVSGEVVEV 72
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
141-200 |
3.25e-04 |
|
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the Pathway/BioSystem: Urea cycle
Pssm-ID: 440660 [Multi-domain] Cd Length: 1144 Bit Score: 43.91 E-value: 3.25e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 522119224 141 GTVTRWLKQVGDSVEVDEPLLEISTDKVDTEVPSPVAGTVLEIRAGEDETVEVGGVLAVI 200
Cdd:COG1038 1085 GTVVKVLVKEGDEVKKGDPLLTIEAMKMETTITAPRDGTVKEVLVKEGDQVEAGDLLIEL 1144
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
17-76 |
3.31e-04 |
|
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the Pathway/BioSystem: Urea cycle
Pssm-ID: 440660 [Multi-domain] Cd Length: 1144 Bit Score: 43.91 E-value: 3.31e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 522119224 17 GTVTRWLKQEGDTVEVDEPLLEISTDKVDTEVPSPVAGKVVKISAQEDETVEVGGELAVI 76
Cdd:COG1038 1085 GTVVKVLVKEGDEVKKGDPLLTIEAMKMETTITAPRDGTVKEVLVKEGDQVEAGDLLIEL 1144
|
|
| GCS_H |
cd06848 |
Glycine cleavage H-protein. Glycine cleavage H-proteins are part of the glycine cleavage ... |
146-183 |
3.48e-04 |
|
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: 39.82 E-value: 3.48e-04
10 20 30
....*....|....*....|....*....|....*...
gi 522119224 146 WLKQVGDSVEVDEPLLEISTDKVDTEVPSPVAGTVLEI 183
Cdd:cd06848 35 ELPEVGTEVKKGDPFGSVESVKAASDLYSPVSGEVVEV 72
|
|
| PRK05641 |
PRK05641 |
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
17-73 |
4.77e-04 |
|
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235540 [Multi-domain] Cd Length: 153 Bit Score: 41.00 E-value: 4.77e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 522119224 17 GTVTRWLKQEGDTVEVDEPLLEISTDKVDTEVPSPVAGKVVKISAQEDETVEVGGEL 73
Cdd:PRK05641 93 GKILRILVREGQQVKVGQGLLILEAMKMENEIPAPKDGVVKKILVKEGDTVDTGQPL 149
|
|
| PRK07051 |
PRK07051 |
biotin carboxyl carrier domain-containing protein; |
148-202 |
5.39e-04 |
|
biotin carboxyl carrier domain-containing protein;
Pssm-ID: 180811 [Multi-domain] Cd Length: 80 Bit Score: 38.84 E-value: 5.39e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 522119224 148 KQVGDSVEVDEPLLEISTDKVDTEVPSPVAGTVLEIRAGEDETVEVGGVLAVIGA 202
Cdd:PRK07051 26 VEVGDAVAAGDVVGLIEVMKQFTEVEAEAAGRVVEFLVEDGEPVEAGQVLARIEE 80
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
17-78 |
5.97e-04 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 42.82 E-value: 5.97e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 522119224 17 GTVTRWLKQEGDTVEVDEPLLEISTDKVDTEVPSPVAGKVVKISAQEDETVEVGGELAVIDD 78
Cdd:PRK12999 1085 GSVVTVLVKEGDEVKAGDPLAVIEAMKMETTITAPVDGTVKRVLVKAGDQVEAGDLLVELEP 1146
|
|
| GcvH |
COG0509 |
Glycine cleavage system protein H (lipoate-binding) [Amino acid transport and metabolism]; ... |
147-183 |
1.09e-03 |
|
Glycine cleavage system protein H (lipoate-binding) [Amino acid transport and metabolism]; Glycine cleavage system protein H (lipoate-binding) is part of the Pathway/BioSystem: Glycine cleavage
Pssm-ID: 440275 Cd Length: 128 Bit Score: 39.34 E-value: 1.09e-03
10 20 30
....*....|....*....|....*....|....*..
gi 522119224 147 LKQVGDSVEVDEPLLEISTDKVDTEVPSPVAGTVLEI 183
Cdd:COG0509 44 LPEVGTEVEAGEPFGVVESVKAVSDLYAPVSGEVVEV 80
|
|
| PRK05641 |
PRK05641 |
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
141-201 |
2.48e-03 |
|
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235540 [Multi-domain] Cd Length: 153 Bit Score: 38.69 E-value: 2.48e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 522119224 141 GTVTRWLKQVGDSVEVDEPLLEISTDKVDTEVPSPVAGTVLEIRAGEDETVEVGGVLAVIG 201
Cdd:PRK05641 93 GKILRILVREGQQVKVGQGLLILEAMKMENEIPAPKDGVVKKILVKEGDTVDTGQPLIELG 153
|
|
| PRK07051 |
PRK07051 |
biotin carboxyl carrier domain-containing protein; |
24-78 |
5.73e-03 |
|
biotin carboxyl carrier domain-containing protein;
Pssm-ID: 180811 [Multi-domain] Cd Length: 80 Bit Score: 36.14 E-value: 5.73e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 522119224 24 KQEGDTVEVDEPLLEISTDKVDTEVPSPVAGKVVKISAQEDETVEVGGELAVIDD 78
Cdd:PRK07051 26 VEVGDAVAAGDVVGLIEVMKQFTEVEAEAAGRVVEFLVEDGEPVEAGQVLARIEE 80
|
|
| GcvH |
COG0509 |
Glycine cleavage system protein H (lipoate-binding) [Amino acid transport and metabolism]; ... |
23-59 |
7.61e-03 |
|
Glycine cleavage system protein H (lipoate-binding) [Amino acid transport and metabolism]; Glycine cleavage system protein H (lipoate-binding) is part of the Pathway/BioSystem: Glycine cleavage
Pssm-ID: 440275 Cd Length: 128 Bit Score: 37.03 E-value: 7.61e-03
10 20 30
....*....|....*....|....*....|....*..
gi 522119224 23 LKQEGDTVEVDEPLLEISTDKVDTEVPSPVAGKVVKI 59
Cdd:COG0509 44 LPEVGTEVEAGEPFGVVESVKAVSDLYAPVSGEVVEV 80
|
|
| |
