|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11856 |
PRK11856 |
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed |
1-369 |
5.70e-146 |
|
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
Pssm-ID: 237001 [Multi-domain] Cd Length: 411 Bit Score: 419.20 E-value: 5.70e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299066811 1 MIVFKLPDLGEGLQEAEIVQWHVQAGDTVEADQPLVSVETAKAIVEIPSPQAGRIARLFGQPGDIVHLGAPLVAF----- 75
Cdd:PRK11856 2 MFEFKMPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDVVPVGSVIAVIeeege 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299066811 76 --EGAGGGEADAGTVVGQMQVGQQVVREAPAVLAAAPGAAGGGIKATPAVRALARKLDVDLSMVTPSGPDGVITAADVER 153
Cdd:PRK11856 82 aeAAAAAEAAPEAPAPEPAPAAAAAAAAAPAAAAAPAAPAAAAAKASPAVRKLARELGVDLSTVKGSGPGGRITKEDVEA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299066811 154 VAK------------------VFAELGPPEVLRGVRRAMAQNMARAQSEVAAATVIDDADIHAW----------PPGTDV 205
Cdd:PRK11856 162 AAAaaapaaaaaaaaaaappaAAAEGEERVPLSGMRKAIAKRMVESKREIPHFTLTDEVDVTALlalrkqlkaiGVKLTV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299066811 206 TIRLIRALVAGCRAEPGLNAWFDGHAGRRHvlEKIDLGIAVDLPDGLFVPVLRNVAHRDAADLRAGLDRMRADIRARKIP 285
Cdd:PRK11856 242 TDFLIKAVALALKKFPELNASWDDDAIVLK--KYVNIGIAVATDGGLIVPVIRDADKKSLFELAREIKDLAEKAREGKLK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299066811 286 PEELRGNTITLSNFGMIAGKYAAPVVVPPTVAILGAGRIHEQVVAAGGVPAVHRVLPLSLTFDHRVVTGGEAARFLAATI 365
Cdd:PRK11856 320 PEELQGGTFTISNLGMFGGDYFTPIINPPEVAILGVGAIVERPVVVDGEIVVRKVMPLSLSFDHRVIDGADAARFLKALK 399
|
....
gi 299066811 366 ADLE 369
Cdd:PRK11856 400 ELLE 403
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
4-362 |
1.64e-72 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 235.49 E-value: 1.64e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299066811 4 FKLPDLGEgLQEAEIVQWHVQAGDTVEADQPLVSVETAKAIVEIPSPQAGRIARLFGQPGDIVHLGAPLVAFEGAGGGEA 83
Cdd:PRK11855 122 VKVPDIGE-ITEVEVIEWLVKVGDTVEEDQSLITVETDKATMEIPSPVAGVVKEIKVKVGDKVSVGSLLVVIEVAAAAPA 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299066811 84 DAGTVVGQMQVGQQVVREAPAVLAAAPGAAGGGIK---------ATPAVRALARKLDVDLSMVTPSGPDGVITAADVERV 154
Cdd:PRK11855 201 AAAAPAAAAPAAAAAAAPAPAPAAAAAPAAAAPAAaaapgkaphASPAVRRLARELGVDLSQVKGTGKKGRITKEDVQAF 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299066811 155 AKV-----------------------------FAELGPPEV--LRGVRRAMAQNMARAQSEVAAATVIDDADIhawppgT 203
Cdd:PRK11855 281 VKGamsaaaaaaaaaaaagggglgllpwpkvdFSKFGEIETkpLSRIKKISAANLHRSWVTIPHVTQFDEADI------T 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299066811 204 D-VTIR-------------------LIRALVAGCRAEPGLNAWFDGHAGRRHVLEKIDLGIAVDLPDGLFVPVLRNVAHR 263
Cdd:PRK11855 355 DlEALRkqlkkeaekagvkltmlpfFIKAVVAALKEFPVFNASLDEDGDELTYKKYFNIGFAVDTPNGLVVPVIKDVDKK 434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299066811 264 DAADLRAGLDRMRADIRARKIPPEELRGNTITLSNFGMIAGKYAAPVVVPPTVAILGAGRIHEQVVAAGGVPAVHRVLPL 343
Cdd:PRK11855 435 SLLEIAREIAELAKKARDGKLKPDDMQGGCFTISSLGGIGGTAFTPIINAPEVAILGVGKSQMKPVWDGKEFVPRLMLPL 514
|
410
....*....|....*....
gi 299066811 344 SLTFDHRVVTGGEAARFLA 362
Cdd:PRK11855 515 SLSYDHRVIDGATAARFTN 533
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
178-363 |
4.72e-55 |
|
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: 180.05 E-value: 4.72e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299066811 178 MARAQSEVAAATVIDDADI------------HAWPPGTDVTI--RLIRALVAGCRAEPGLNAWFDGHAGRRHVLEKIDLG 243
Cdd:pfam00198 1 MTESKQTIPHFTLTDEVDVtellalreelkeDAADEETKLTFlpFLVKAVALALKKFPELNASWDGEEGEIVYKKYVNIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299066811 244 IAVDLPDGLFVPVLRNVAHRDAADLRAGLDRMRADIRARKIPPEELRGNTITLSNFGMIAGKYAAPVVVPPTVAILGAGR 323
Cdd:pfam00198 81 IAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVGR 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 299066811 324 IHEQVVAAGGVPAVHRVLPLSLTFDHRVVTGGEAARFLAA 363
Cdd:pfam00198 161 IRKRPVVVDGEIVVRKVMPLSLSFDHRVIDGAEAARFLNT 200
|
|
| PLN02528 |
PLN02528 |
2-oxoisovalerate dehydrogenase E2 component |
4-360 |
7.84e-55 |
|
2-oxoisovalerate dehydrogenase E2 component
Pssm-ID: 215289 [Multi-domain] Cd Length: 416 Bit Score: 185.69 E-value: 7.84e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299066811 4 FKLPDLGEGLQEAEIVQWHVQAGDTVEADQPLVSVETAKAIVEIPSPQAGRIARLFGQPGDIVHLGAPLVaFEGAGGGEA 83
Cdd:PLN02528 1 VPLAQTGEGIAECELLRWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGKVAQINFSPGDIVKVGETLL-KIMVEDSQH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299066811 84 DAGTVVGQMQVGQQVVreaPAVLAAAPGAAGGGIKATPAVRALARKLDVDLSMVTPSGPDGVITAADVERVAKV------ 157
Cdd:PLN02528 80 LRSDSLLLPTDSSNIV---SLAESDERGSNLSGVLSTPAVRHLAKQYGIDLNDILGTGKDGRVLKEDVLKYAAQkgvvkd 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299066811 158 ---FAELGPPEV---------------------LRGVRRAMAQNMARAQS--------EVAA-ATVIDDADIHAWPpgTD 204
Cdd:PLN02528 157 sssAEEATIAEQeefstsvstpteqsyedktipLRGFQRAMVKTMTAAAKvphfhyveEINVdALVELKASFQENN--TD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299066811 205 VTIR------LIRALVAGCRAEPGLNAWFDGHAGRRHVLEKIDLGIAVDLPDGLFVPVLRNVAHRDAADLRAGLDRMRAD 278
Cdd:PLN02528 235 PTVKhtflpfLIKSLSMALSKYPLLNSCFNEETSEIRLKGSHNIGVAMATEHGLVVPNIKNVQSLSLLEITKELSRLQHL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299066811 279 IRARKIPPEELRGNTITLSNFGMIAGKYAAPVVVPPTVAILGAGRIHE--QVVAAGGVPAVhRVLPLSLTFDHRVVTGGE 356
Cdd:PLN02528 315 AAENKLNPEDITGGTITLSNIGAIGGKFGSPVLNLPEVAIIALGRIQKvpRFVDDGNVYPA-SIMTVTIGADHRVLDGAT 393
|
....
gi 299066811 357 AARF 360
Cdd:PLN02528 394 VARF 397
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
5-361 |
7.04e-49 |
|
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: 172.75 E-value: 7.04e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299066811 5 KLPDLGeGLQEAEIVQWHVQAGDTVEADQPLVSVETAKAIVEIPSPQAGRIARLFGQPGDIVHLGAPLVAFEGAGGGEAD 84
Cdd:TIGR01348 120 TVPDIG-DIEKVTVIEVLVKVGDTVSADQSLITLESDKASMEVPAPASGVVKSVKVKVGDSVPTGDLILTLSVAGSTPAT 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299066811 85 AGTVVGQMQVGQQVVREAPAVLAAAPGAAGGG--------------IKATPAVRALARKLDVDLSMVTPSGPDGVITAAD 150
Cdd:TIGR01348 199 APAPASAQPAAQSPAATQPEPAAAPAAAKAQApapqqagtqnpakvDHAAPAVRRLAREFGVDLSAVKGTGIKGRILRED 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299066811 151 VERVAK---VFAELGP-------------PEV------------LRGVRRAMAQNMARAQSEVAAATVIDDADI------ 196
Cdd:TIGR01348 279 VQRFVKepsVRAQAAAasaaggapgalpwPNVdfskfgeveevdMSRIRKISGANLTRNWTMIPHVTHFDKADItemeaf 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299066811 197 ----HAWPPGTDVTIR----LIRALVAGCRAEPGLNAWFDGHAGRRHVLEKIDLGIAVDLPDGLFVPVLRNVAHRDAADL 268
Cdd:TIGR01348 359 rkqqNAAVEKEGVKLTvlhiLMKAVAAALKKFPKFNASLDLGGEQLILKKYVNIGVAVDTPNGLLVPVIKDVDRKGITEL 438
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299066811 269 RAGLDRMRADIRARKIPPEELRGNTITLSNFGMIAGKYAAPVVVPPTVAILGAGRIHEQVVAAGGVPAVHRVLPLSLTFD 348
Cdd:TIGR01348 439 ALELSDLAKKARDGKLTPDEMQGACFTISSLGGIGGTAFTPIVNAPEVAILGVSKSGMEPVWNGKEFEPRLMLPLSLSYD 518
|
410
....*....|...
gi 299066811 349 HRVVTGGEAARFL 361
Cdd:TIGR01348 519 HRVIDGADAARFT 531
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
5-362 |
2.28e-45 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 164.41 E-value: 2.28e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299066811 5 KLPDLGEGlqEAEIVQWHVQAGDTVEADQPLVSVETAKAIVEIPSPQAGRIARLFGQPGDIVHLGAPLVAFEGAGGGEAD 84
Cdd:PRK11854 210 NVPDIGGD--EVEVTEVMVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVKTGSLIMRFEVEGAAPAA 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299066811 85 AGTVVGQMQVGQQVVREAPAVLAAAPGAAGGG--------IKATPAVRALARKLDVDLSMVTPSGPDGVITAADVERVAK 156
Cdd:PRK11854 288 APAKQEAAAPAPAAAKAEAPAAAPAAKAEGKSefaendayVHATPLVRRLAREFGVNLAKVKGTGRKGRILKEDVQAYVK 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299066811 157 V-------------------------------FAELGPPEVLRgVRRAMAQNMARAQSEVAAATVIDDADI--------- 196
Cdd:PRK11854 368 DavkraeaapaaaaaggggpgllpwpkvdfskFGEIEEVELGR-IQKISGANLHRNWVMIPHVTQFDKADIteleafrkq 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299066811 197 ---HAWPPGTDVTIR----LIRALVAGCRAEPGLNAWFDgHAGRRHVLEK-IDLGIAVDLPDGLFVPVLRNVAHRDAADL 268
Cdd:PRK11854 447 qnaEAEKRKLGVKITplvfIMKAVAAALEQMPRFNSSLS-EDGQRLTLKKyVNIGIAVDTPNGLVVPVFKDVNKKGIIEL 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299066811 269 RAGLDRMRADIRARKIPPEELRGNTITLSNFGMIAGKYAAPVVVPPTVAILGAGRIHEQVVAAGGVPAVHRVLPLSLTFD 348
Cdd:PRK11854 526 SRELMDISKKARDGKLTAGDMQGGCFTISSIGGLGTTHFTPIVNAPEVAILGVSKSAMEPVWNGKEFAPRLMLPLSLSYD 605
|
410
....*....|....
gi 299066811 349 HRVVTGGEAARFLA 362
Cdd:PRK11854 606 HRVIDGADGARFIT 619
|
|
| sucB |
TIGR01347 |
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ... |
5-361 |
2.71e-41 |
|
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: 149.50 E-value: 2.71e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299066811 5 KLPDLGEGLQEAEIVQWHVQAGDTVEADQPLVSVETAKAIVEIPSPQAGRIARLFGQPGDIVHLGAPLvafegagGGEAD 84
Cdd:TIGR01347 4 KVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVL-------AILEE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299066811 85 AGTVVGQMQVGQQVVREAPAVLAAAPGAAGGGIK--ATPAVRALARKLDVDLSMVTPSGPDGVITAADVERVAKVFAELG 162
Cdd:TIGR01347 77 GNDATAAPPAKSGEEKEETPAASAAAAPTAAANRpsLSPAARRLAKEHGIDLSAVPGTGVTGRVTKEDIIKKTEAPASAQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299066811 163 PP------------------EVLRGVRRAMAQNMARAQSEVAAATVIDDADIHA-----------WPPGTDVTIRL---- 209
Cdd:TIGR01347 157 PPaaaaaaaapaaatrpeerVKMTRLRQRIAERLKEAQNSTAMLTTFNEVDMSAvmelrkrykeeFEKKHGVKLGFmsff 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299066811 210 IRALVAGCRAEPGLNAWFDGhagrRHVLEK--IDLGIAVDLPDGLFVPVLRNVAHRDAADLRAGLDRMRADIRARKIPPE 287
Cdd:TIGR01347 237 VKAVVAALKRFPEVNAEIDG----DDIVYKdyYDISVAVSTDRGLVVPVVRNADRMSFADIEKEIADLGKKARDGKLTLE 312
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 299066811 288 ELRGNTITLSNFGMIAGKYAAPVVVPPTVAILGAGRIHEQVVAAGGVPAVHRVLPLSLTFDHRVVTGGEAARFL 361
Cdd:TIGR01347 313 DMTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHGIKERPVAVNGQIEIRPMMYLALSYDHRLIDGKEAVTFL 386
|
|
| PRK05704 |
PRK05704 |
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase; |
1-361 |
6.41e-37 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
Pssm-ID: 235571 [Multi-domain] Cd Length: 407 Bit Score: 137.66 E-value: 6.41e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299066811 1 MIVFKLPDLGEGLQEAEIVQWHVQAGDTVEADQPLVSVETAKAIVEIPSPQAGRIARLFGQPGDIVHLGAPLVAFEGAGG 80
Cdd:PRK05704 2 MVEIKVPTLPESVTEATIATWHKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGDTVTVGQVLGRIDEGAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299066811 81 GEADAGTvvgqmQVGQQVVREAPAVLAAAPGAAGGGIKATPAVRALARKLDVDLSMVTPSGPDGVITAADVE-------- 152
Cdd:PRK05704 82 AGAAAAA-----AAAAAAAAAAPAQAQAAAAAEQSNDALSPAARKLAAENGLDASAVKGTGKGGRVTKEDVLaalaaaaa 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299066811 153 RVAKVFAELGPPEVLR-GVRRAMAQNMAR-----------AQSEVAAATVIDDADIhawppgTDV--------------- 205
Cdd:PRK05704 157 APAAPAAAAPAAAPAPlGARPEERVPMTRlrktiaerlleAQNTTAMLTTFNEVDM------TPVmdlrkqykdafekkh 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299066811 206 TIRL------IRALVAGCRAEPGLNAWFDGhagrrhvlEKI------DLGIAVDLPDGLFVPVLRNVAHRDAADLRAGLD 273
Cdd:PRK05704 231 GVKLgfmsffVKAVVEALKRYPEVNASIDG--------DDIvyhnyyDIGIAVGTPRGLVVPVLRDADQLSFAEIEKKIA 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299066811 274 RMRADIRARKIPPEELRGNTITLSNFGMIAGKYAAPVVVPPTVAILGAGRIHEQVVAAGGVPAVHRVLPLSLTFDHRVVT 353
Cdd:PRK05704 303 ELAKKARDGKLSIEELTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHKIKERPVAVNGQIVIRPMMYLALSYDHRIID 382
|
....*...
gi 299066811 354 GGEAARFL 361
Cdd:PRK05704 383 GKEAVGFL 390
|
|
| PTZ00144 |
PTZ00144 |
dihydrolipoamide succinyltransferase; Provisional |
2-368 |
5.98e-34 |
|
dihydrolipoamide succinyltransferase; Provisional
Pssm-ID: 240289 [Multi-domain] Cd Length: 418 Bit Score: 129.80 E-value: 5.98e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299066811 2 IVFKLPDLGEGLQEAEIVQWHVQAGDTVEADQPLVSVETAKAIVEIPSPQAGRIARLFGQPGDIVHLGAPLVAFEGAGGG 81
Cdd:PTZ00144 45 KVIKVPTMGDSISEGTVVEWKKKVGDYVKEDEVICIIETDKVSVDIRAPASGVITKIFAEEGDTVEVGAPLSEIDTGGAP 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299066811 82 EADAGTVVGQMQVGQQVVREAPAVLAAAPGAAGGGIKATPAVRAlarkldvdlsmvtpsgpdgVITAADVERVAKVFAEL 161
Cdd:PTZ00144 125 PAAAPAAAAAAKAEKTTPEKPKAAAPTPEPPAASKPTPPAAAKP-------------------PEPAPAAKPPPTPVARA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299066811 162 GPPEV---LRGVRRAMAQNMARAQSEVAAATVIDDADIhawPPGTDVTIRL------------------IRALVAGCRAE 220
Cdd:PTZ00144 186 DPRETrvpMSRMRQRIAERLKASQNTCAMLTTFNECDM---SALMELRKEYkddfqkkhgvklgfmsafVKASTIALKKM 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299066811 221 PGLNAWFDGHAGRRHvlEKIDLGIAVDLPDGLFVPVLRNVAHRDAADLRAGLDRMRADIRARKIPPEELRGNTITLSNFG 300
Cdd:PTZ00144 263 PIVNAYIDGDEIVYR--NYVDISVAVATPTGLVVPVIRNCENKSFAEIEKELADLAEKARNNKLTLEDMTGGTFTISNGG 340
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 299066811 301 MIAGKYAAPVVVPPTVAILGAGRIHEQVVAAGGVPAVHRVLPLSLTFDHRVVTGGEAARFLaATIADL 368
Cdd:PTZ00144 341 VFGSLMGTPIINPPQSAILGMHAIKKRPVVVGNEIVIRPIMYLALTYDHRLIDGRDAVTFL-KKIKDL 407
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
1-73 |
2.91e-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: 102.84 E-value: 2.91e-27
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 299066811 1 MIVFKLPDLGEGLQEAEIVQWHVQAGDTVEADQPLVSVETAKAIVEIPSPQAGRIARLFGQPGDIVHLGAPLV 73
Cdd:COG0508 2 AIEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIA 74
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
2-72 |
4.59e-26 |
|
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: 99.40 E-value: 4.59e-26
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 299066811 2 IVFKLPDLGEGLQEAEIVQWHVQAGDTVEADQPLVSVETAKAIVEIPSPQAGRIARLFGQPGDIVHLGAPL 72
Cdd:cd06849 1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVI 71
|
|
| PRK11857 |
PRK11857 |
dihydrolipoamide acetyltransferase; Reviewed |
117-362 |
4.82e-26 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237002 [Multi-domain] Cd Length: 306 Bit Score: 106.03 E-value: 4.82e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299066811 117 IKATPAVRALARKLDVDLSMVTPSGPDGVITAADVER----------------------VAKVFAELGPPEVLRG----- 169
Cdd:PRK11857 2 ILATPIARALAKKLGIDISLLKGSGRDGKILAEDVENfikslksaptpaeaasvssaqqAAKTAAPAAAPPKLEGkrekv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299066811 170 --VRRAMAQNMARAQSEVAAATVIDDADIHA-WP----------PGTDVTIR----LIRALVAGCRAEPGLNAWFDGHAG 232
Cdd:PRK11857 82 apIRKAIARAMTNSWSNVAYVNLVNEIDMTKlWDlrksvkdpvlKTEGVKLTflpfIAKAILIALKEFPIFAAKYDEATS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299066811 233 RRHVLEKIDLGIAVDLPDGLFVPVLRNVAHRDAADLRAGLDRMRADIRARKIPPEELRGNTITLSNFGMIAGKYAAPVVV 312
Cdd:PRK11857 162 ELVYPDTLNLGIAVDTEAGLMVPVIKNAQKLSIVEIAKEISRLAKAARERKIKPDEMKGGSFTITNYGSVGSLYGVPVIN 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 299066811 313 PPTVAILGAGRIHEQVVAAGGVPAVHRVLPLSLTFDHRVVTGGEAARFLA 362
Cdd:PRK11857 242 YPELAIAGVGAIIDKAIVKNGQIVAGKVMHLTVAADHRWIDGATIGRFAS 291
|
|
| SucB_Actino |
TIGR02927 |
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model ... |
5-371 |
3.90e-22 |
|
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: 97.78 E-value: 3.90e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299066811 5 KLPDLGEGLQEAEIVQWHVQAGDTVEADQPLVSVETAKAIVEIPSPQAGRIARLFGQPGDIVHLGAPLV----------- 73
Cdd:TIGR02927 6 KMPALGESVTEGTVTSWLKAVGDTVEADEPLLEVSTDKVDTEIPSPAAGVLLEIRAPEDDTVEVGGVLAiigepgeagse 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299066811 74 ----------------------------AFEGAGGGEADAGTVVGQMQVGQQVV-------------------------- 99
Cdd:TIGR02927 86 papaapepeaapepeapapaptpaaeapAPAAPQAGGSGEATEVKMPELGESVTegtvtswlkavgdtvevdepllevst 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299066811 100 ------------------------------------------------------------------REAPAVLAAAPGAA 113
Cdd:TIGR02927 166 dkvdteipspvagtlleirapeddtvevgtvlaiigdanaapaepaeeeapapseagsepapdpaaRAPHAAPDPPAPAP 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299066811 114 GGGIKA-----------------TPAVRALARKLDVDLSMVTPSGPDGVITAADVERVAK-------------------- 156
Cdd:TIGR02927 246 APAKTAapaaaapvssgdsgpyvTPLVRKLAKDKGVDLSTVKGTGVGGRIRKQDVLAAAKaaeearaaaaapaaaaapaa 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299066811 157 VFAELGPPEV----LRG-------VRRAMAQNMARAQSEVAAATVIDDADI-------------HAWPPGTDVTIR--LI 210
Cdd:TIGR02927 326 PAAAAKPAEPdtakLRGttqkmnrIRQITADKTIESLQTSAQLTQVHEVDMtrvaalrarakndFLEKNGVNLTFLpfFV 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299066811 211 RALVAGCRAEPGLNAWFDGHAGRRHVLEKIDLGIAVDLPDGLFVPVLRNvahrdAADLR-AGLDRMRADIRAR----KIP 285
Cdd:TIGR02927 406 QAVTEALKAHPNVNASYNAETKEVTYHDVEHVGIAVDTPRGLLVPVIHN-----AGDLSlPGLAKAINDLAARardnKLK 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299066811 286 PEELRGNTITLSNFGMIAGKYAAPVVVPPTVAILGAGRIHEQVVA-----AGGVPAVHRVLPLSLTFDHRVVTGGEAARF 360
Cdd:TIGR02927 481 PDELSGGTFTITNIGSGGALFDTPILNPPQAAILGTGAIVKRPRVikdedGGESIAIRSVCYLPLTYDHRLVDGADAGRF 560
|
570
....*....|.
gi 299066811 361 LAATIADLEAA 371
Cdd:TIGR02927 561 LTTIKKRLEEG 571
|
|
| PLN02226 |
PLN02226 |
2-oxoglutarate dehydrogenase E2 component |
6-361 |
2.91e-20 |
|
2-oxoglutarate dehydrogenase E2 component
Pssm-ID: 177871 [Multi-domain] Cd Length: 463 Bit Score: 91.74 E-value: 2.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299066811 6 LPDLGEGLQEAEIVQWHVQAGDTVEADQPLVSVETAKAIVEIPSPQAGRIARLFGQPGDIVHLGAPLvafegagGGEADA 85
Cdd:PLN02226 96 VPHMGESITDGTLATFLKKPGERVQADEAIAQIETDKVTIDIASPASGVIQEFLVKEGDTVEPGTKV-------AIISKS 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299066811 86 GTVVGQMQVGQQVVREAPAVlaaapgaagggiKATPAVRALARKLDVDLSMVTPSGPDgviTAADVERVAKVfAELGPPE 165
Cdd:PLN02226 169 EDAASQVTPSQKIPETTDPK------------PSPPAEDKQKPKVESAPVAEKPKAPS---SPPPPKQSAKE-PQLPPKE 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299066811 166 VLRGV-----RRAMAQNMARAQSEVAAATVIDDADI-----------HAWPPGTDVTIRL----IRALVAGCRAEPGLNA 225
Cdd:PLN02226 233 RERRVpmtrlRKRVATRLKDSQNTFALLTTFNEVDMtnlmklrsqykDAFYEKHGVKLGLmsgfIKAAVSALQHQPVVNA 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299066811 226 WFDGHAGRRHvlEKIDLGIAVDLPDGLFVPVLRNVAHRDAADLRAGLDRMRADIRARKIPPEELRGNTITLSNFGMIAGK 305
Cdd:PLN02226 313 VIDGDDIIYR--DYVDISIAVGTSKGLVVPVIRGADKMNFAEIEKTINGLAKKANEGTISIDEMAGGSFTVSNGGVYGSL 390
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 299066811 306 YAAPVVVPPTVAILGAGRIHEQVVAAGGVPAVHRVLPLSLTFDHRVVTGGEAARFL 361
Cdd:PLN02226 391 ISTPIINPPQSAILGMHSIVSRPMVVGGSVVPRPMMYVALTYDHRLIDGREAVYFL 446
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
3-73 |
9.61e-16 |
|
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue binds biotin in one group and lipoic acid in the other. Note that the HMM does not currently recognize the Glycine cleavage system H proteins.
Pssm-ID: 395290 [Multi-domain] Cd Length: 73 Bit Score: 71.09 E-value: 9.61e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 299066811 3 VFKLPDLGEGLQEAeIVQWHVQAGDTVEADQPLVSVETAKAIVEIPSPQAGRIARLFGQPGDIVHLGAPLV 73
Cdd:pfam00364 2 EIKSPMIGESVREG-VVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLA 71
|
|
| PLN02744 |
PLN02744 |
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex |
6-363 |
1.28e-15 |
|
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
Pssm-ID: 215397 [Multi-domain] Cd Length: 539 Bit Score: 77.97 E-value: 1.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299066811 6 LPDLGEGLQEAEIVQWHVQAGDTVEADQPLVSVETAKAIVEIPSPQAGRIARLF----------GQ--------PGDIVH 67
Cdd:PLN02744 117 MPSLSPTMTEGNIARWLKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVkgdgakeikvGEviaitveeEEDIGK 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299066811 68 LG---APLVAFEGAGGGEADAGTVVGQMQVGQQVVREAPAVLAAAPGAAGGGIKATPAVRALARKLDVDLSMVTPSGPDG 144
Cdd:PLN02744 197 FKdykPSSSAAPAAPKAKPSPPPPKEEEVEKPASSPEPKASKPSAPPSSGDRIFASPLARKLAEDNNVPLSSIKGTGPDG 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299066811 145 VITAADVER-VAKVFAELGPPEVLRG--------------VRRAMAQNMARAQSEV-----AAATVIDD-----ADIHAW 199
Cdd:PLN02744 277 RIVKADIEDyLASGGKGATAPPSTDSkapaldytdipntqIRKVTASRLLQSKQTIphyylTVDTRVDKlmalrSQLNSL 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299066811 200 ---PPGTDVTIR--LIRALVAGCRAEPGLNA-WFDGHAGRRHvleKIDLGIAVDLPDGLFVPVLRNvahrdaADlRAGLD 273
Cdd:PLN02744 357 qeaSGGKKISVNdlVIKAAALALRKVPQCNSsWTDDYIRQYH---NVNINVAVQTENGLYVPVVKD------AD-KKGLS 426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299066811 274 RMRADIR--ARK-----IPPEELRGNTITLSNFGMIAG-KYAAPVVVPPTVAILGAGRIHEQVVaAGGVPAVHRV---LP 342
Cdd:PLN02744 427 TIAEEVKqlAQKarensLKPEDYEGGTFTVSNLGGPFGiKQFCAIINPPQSAILAVGSAEKRVI-PGSGPDQYNFasfMS 505
|
410 420
....*....|....*....|.
gi 299066811 343 LSLTFDHRVVTGGEAARFLAA 363
Cdd:PLN02744 506 VTLSCDHRVIDGAIGAEWLKA 526
|
|
| PRK14843 |
PRK14843 |
dihydrolipoamide acetyltransferase; Provisional |
240-361 |
3.83e-15 |
|
dihydrolipoamide acetyltransferase; Provisional
Pssm-ID: 184847 [Multi-domain] Cd Length: 347 Bit Score: 75.71 E-value: 3.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299066811 240 IDLGIAVDLPDGLFVPVLRNVAHRDAADLRAGLDRMRADIRARKIPPEELRGNTITLSNFGMIAGKYAAPVVVPPTVAIL 319
Cdd:PRK14843 211 VNLAMAVGMDNGLMTPVVYNAEKMSLSELVVAFKDVIGRTLDGKLAPSELQNSTFTISNLGMFGVQSFGPIINQPNSAIL 290
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 299066811 320 GAGRIHEQVVAAGGVPAVHRVLPLSLTFDHRVVTGGEAARFL 361
Cdd:PRK14843 291 GVSSTIEKPVVVNGEIVIRPIMSLGLTIDHRVVDGMAGAKFM 332
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
2-75 |
1.70e-12 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 68.49 E-value: 1.70e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 299066811 2 IVFKLPDLGEGlqEAEIVQWHVQAGDTVEADQPLVSVETAKAIVEIPSPQAGRIARLFGQPGDIVHLGAPLVAF 75
Cdd:PRK11854 3 IEIKVPDIGAD--EVEVTEILVKVGDKVEAEQSLITVEGDKASMEVPSPQAGVVKEIKVKVGDKVETGALIMIF 74
|
|
| E3_binding |
pfam02817 |
e3 binding domain; This family represents a small domain of the E2 subunit of 2-oxo-acid ... |
117-152 |
1.69e-11 |
|
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: 58.08 E-value: 1.69e-11
10 20 30
....*....|....*....|....*....|....*.
gi 299066811 117 IKATPAVRALARKLDVDLSMVTPSGPDGVITAADVE 152
Cdd:pfam02817 1 VLASPAARKLARELGIDLSDVKGTGPGGRITKEDVE 36
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
18-75 |
1.35e-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: 56.66 E-value: 1.35e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 299066811 18 IVQWHVQAGDTVEADQPLVSVETAKAIVEIPSPQAGRIARLFGQPGDIVHLGAPLVAF 75
Cdd:cd06850 10 VVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| kgd |
PRK12270 |
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ... |
212-368 |
6.62e-10 |
|
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;
Pssm-ID: 237030 [Multi-domain] Cd Length: 1228 Bit Score: 60.67 E-value: 6.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299066811 212 ALVAGCRAEPGLNAWFDGHAGRRHVL--EKIDLGIAVDL--PDG---LFVPVLRNVAHRDAAD-LRAGLDRMRadiRAR- 282
Cdd:PRK12270 179 ALVQALKAFPNMNRHYAEVDGKPTLVtpAHVNLGLAIDLpkKDGsrqLVVPAIKGAETMDFAQfWAAYEDIVR---RARd 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299066811 283 -KIPPEELRGNTITLSNFGMIAGKYAAPVVVPPTVAILGAGRIHEQVVAAGGVP------AVHRVLPLSLTFDHRVVTGG 355
Cdd:PRK12270 256 gKLTADDFQGTTISLTNPGGIGTVHSVPRLMKGQGAIIGVGAMEYPAEFQGASEerlaelGISKVMTLTSTYDHRIIQGA 335
|
170
....*....|...
gi 299066811 356 EAARFLaATIADL 368
Cdd:PRK12270 336 ESGEFL-RTIHQL 347
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
5-72 |
2.42e-09 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 58.42 E-value: 2.42e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 299066811 5 KLPDLGEGLQEAEIVQWHVQAGDTVEADQPLVSVETAKAIVEIPSPQAGRIARLFGQPGDIVHLGAPL 72
Cdd:PRK14875 6 TMPKWGLSMTEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGETLPVGALL 73
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
6-75 |
8.68e-09 |
|
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases, and the H-protein of the glycine cleavage system (GCS). These domains transport CO2, acyl, or methylamine, respectively, between components of the complex/protein via a biotinyl or lipoyl group, which is covalently attached to a highly conserved lysine residue.
Pssm-ID: 133456 [Multi-domain] Cd Length: 73 Bit Score: 51.67 E-value: 8.68e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299066811 6 LPDLGEGLQEAEIVQWHVQAGDTVEADQPLVSVETAKAIVEIPSPQAGRIARLFGQPGDIVHLGAPLVAF 75
Cdd:cd06663 4 IPDLAQHLGDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKVEGDTPLVKI 73
|
|
| AccB |
COG0511 |
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ... |
23-73 |
6.21e-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: 45.27 E-value: 6.21e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 299066811 23 VQAGDTVEADQPLVSVETAKAIVEIPSPQAGRIARLFGQPGDIVHLGAPLV 73
Cdd:COG0511 83 VKVGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVVEILVENGQPVEYGQPLF 133
|
|
| PRK14040 |
PRK14040 |
oxaloacetate decarboxylase subunit alpha; |
18-74 |
2.90e-04 |
|
oxaloacetate decarboxylase subunit alpha;
Pssm-ID: 237592 [Multi-domain] Cd Length: 593 Bit Score: 42.61 E-value: 2.90e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 299066811 18 IVQWHVQAGDTVEADQPLVSVETAKAIVEIPSPQAGRIARLFGQPGDIVHLGAPLVA 74
Cdd:PRK14040 535 IFKVIVTEGQTVAEGDVLLILEAMKMETEIRAAQAGTVRGIAVKEGDAVAVGDTLLT 591
|
|
| PRK05641 |
PRK05641 |
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
23-73 |
7.10e-04 |
|
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235540 [Multi-domain] Cd Length: 153 Bit Score: 39.85 E-value: 7.10e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 299066811 23 VQAGDTVEADQPLVSVETAKAIVEIPSPQAGRIARLFGQPGDIVHLGAPLV 73
Cdd:PRK05641 100 VREGQQVKVGQGLLILEAMKMENEIPAPKDGVVKKILVKEGDTVDTGQPLI 150
|
|
| GCS_H |
cd06848 |
Glycine cleavage H-protein. Glycine cleavage H-proteins are part of the glycine cleavage ... |
26-55 |
7.41e-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: 38.28 E-value: 7.41e-04
10 20 30
....*....|....*....|....*....|
gi 299066811 26 GDTVEADQPLVSVETAKAIVEIPSPQAGRI 55
Cdd:cd06848 40 GTEVKKGDPFGSVESVKAASDLYSPVSGEV 69
|
|
| PRK14042 |
PRK14042 |
pyruvate carboxylase subunit B; Provisional |
18-73 |
2.19e-03 |
|
pyruvate carboxylase subunit B; Provisional
Pssm-ID: 172536 [Multi-domain] Cd Length: 596 Bit Score: 40.09 E-value: 2.19e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 299066811 18 IVQWHVQAGDTVEADQPLVSVETAKAIVEIPSPQAGRIARLFGQPGDIVHLGAPLV 73
Cdd:PRK14042 536 IIAIHVSAGDEVKAGQAVLVIEAMKMETEIKAPANGVVAEILCQKGDKVTPGQVLI 591
|
|
| PRK09282 |
PRK09282 |
pyruvate carboxylase subunit B; Validated |
18-73 |
2.30e-03 |
|
pyruvate carboxylase subunit B; Validated
Pssm-ID: 236449 [Multi-domain] Cd Length: 592 Bit Score: 39.83 E-value: 2.30e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 299066811 18 IVQWHVQAGDTVEADQPLVSVETAKAIVEIPSPQAGRIARLFGQPGDIVHLGAPLV 73
Cdd:PRK09282 533 VVKVKVKEGDKVKAGDTVLVLEAMKMENEIQAPVDGTVKEILVKEGDRVNPGDVLM 588
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
18-66 |
4.70e-03 |
|
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the Pathway/BioSystem: Urea cycle
Pssm-ID: 440660 [Multi-domain] Cd Length: 1144 Bit Score: 39.29 E-value: 4.70e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 299066811 18 IVQWHVQAGDTVEADQPLVSVETAKAIVEIPSPQAGRIARLFGQPGDIV 66
Cdd:COG1038 1087 VVKVLVKEGDEVKKGDPLLTIEAMKMETTITAPRDGTVKEVLVKEGDQV 1135
|
|
| PRK06549 |
PRK06549 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
23-73 |
6.23e-03 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235826 [Multi-domain] Cd Length: 130 Bit Score: 36.71 E-value: 6.23e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 299066811 23 VQAGDTVEADQPLVSVETAKAIVEIPSPQAGRIARLFGQPGDIVHLGAPLV 73
Cdd:PRK06549 77 VAVGDQVTENQPLLILEAMKMENEIVASSAGTVTAIHVTPGQVVNPGDGLI 127
|
|
| |
