|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11856 |
PRK11856 |
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed |
1-504 |
2.59e-136 |
|
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
Pssm-ID: 237001 [Multi-domain] Cd Length: 411 Bit Score: 399.94 E-value: 2.59e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490254044 1 MSEIKtleMPKWGLSMEEGLLARWAIQEGDDFTRGQEICEIETSKIVNVLEAPFAGTLRRILAREGETLQVGAVLA-LAA 79
Cdd:PRK11856 2 MFEFK---MPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDVVPVGSVIAvIEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490254044 80 DASVSDAELDEfvarlatakpaapgpeaaapDVAAQAGAKPASVVsppsnspeppvgqtvipvslqgvtdvtqvnatpha 159
Cdd:PRK11856 79 EGEAEAAAAAE--------------------AAPEAPAPEPAPAA----------------------------------- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490254044 160 lrlsarwgvdlkkvrgsgrgdrisvsdlesaivaaggrlASPTPPVRRSKAPRSHADDSQVSATPLARRLAGKLGINLHD 239
Cdd:PRK11856 104 ---------------------------------------AAAAAAAPAAAAAPAAPAAAAAKASPAVRKLARELGVDLST 144
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490254044 240 CRSSGSRGRVSRDDVLAAA-----LLLDEHPQTSPVQESAPAPFESIPMSGMRRAIASRLQTSKQQSPHFRLSVDLDLER 314
Cdd:PRK11856 145 VKGSGPGGRITKEDVEAAAaaaapAAAAAAAAAAAPPAAAAEGEERVPLSGMRKAIAKRMVESKREIPHFTLTDEVDVTA 224
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490254044 315 LLALRQDINREvpGVKISVNDLLVKACALALVAVPDVNIQFDEAAqsIRRFTDADISVAVALPAGLITPIVRSANRKSIS 394
Cdd:PRK11856 225 LLALRKQLKAI--GVKLTVTDFLIKAVALALKKFPELNASWDDDA--IVLKKYVNIGIAVATDGGLIVPVIRDADKKSLF 300
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490254044 395 DISNEIHSLVTRAKAGTLKPEEFQGGTFSLSNLGMLGVRQFDAIINPPQSAILAIGAGEVRAVVRDGQIVARQQMTVSLS 474
Cdd:PRK11856 301 ELAREIKDLAEKAREGKLKPEELQGGTFTISNLGMFGGDYFTPIINPPEVAILGVGAIVERPVVVDGEIVVRKVMPLSLS 380
|
490 500 510
....*....|....*....|....*....|
gi 490254044 475 CDHRVIDGAAGAAFLRELKRLIETPTLMFI 504
Cdd:PRK11856 381 FDHRVIDGADAARFLKALKELLENPALLLL 410
|
|
| PDHac_trf_mito |
TIGR01349 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
7-504 |
2.06e-120 |
|
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: 360.26 E-value: 2.06e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490254044 7 LEMPKWGLSMEEGLLARWAIQEGDDFTRGQEICEIETSKIVNVLEAPFAGTLRRILAREG-ETLQVGAVLALaadaSVSD 85
Cdd:TIGR01349 2 ITMPALSPTMTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEGtKDVPVNKPIAV----LVEE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490254044 86 AELDEFVARLATAKPAAPGPEAAAPDVAAQAGAKPASvvsppsnsPEPPVGQTVIPVSLQGVTDV---TQVNATPHALRL 162
Cdd:TIGR01349 78 KEDVADAFKNYKLESSASPAPKPSEIAPTAPPSAPKP--------SPAPQKQSPEPSSPAPLSDKesgDRIFASPLAKKL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490254044 163 SARWGVDLKKVRGSGRGDRISVSDLESAIvaaggrlasptppvrrSKAPRShADDSQVSATPLArrlagklginlhdcrs 242
Cdd:TIGR01349 150 AKEKGIDLSAVAGSGPNGRIVKKDIESFV----------------PQSPAS-ANQQAAATTPAT---------------- 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490254044 243 sgsrgrvsrddvlaaallldeHPQTSPVQesaPAPFESIPMSGMRRAIASRLQTSKQQSPHFRLSVDLDLERLLALRQDI 322
Cdd:TIGR01349 197 ---------------------YPAAAPVS---TGSYEDVPLSNIRKIIAKRLLESKQTIPHYYVSIECNVDKLLALRKEL 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490254044 323 NREVPGV-KISVNDLLVKACALALVAVPDVNIQFDEaaQSIRRFTDADISVAVALPAGLITPIVRSANRKSISDISNEIH 401
Cdd:TIGR01349 253 NAMASEVyKLSVNDFIIKASALALREVPEANSSWTD--NFIRRYKNVDISVAVATPDGLITPIVRNADAKGLSTISNEIK 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490254044 402 SLVTRAKAGTLKPEEFQGGTFSLSNLGMLGVRQFDAIINPPQSAILAIGAGEVRAVVRDGQ---IVARQQMTVSLSCDHR 478
Cdd:TIGR01349 331 DLAKRARNNKLKPEEFQGGTFTISNLGMFGIKDFTAIINPPQACILAVGAVEDVAVVDNDEekgFAVASIMSVTLSCDHR 410
|
490 500
....*....|....*....|....*.
gi 490254044 479 VIDGAAGAAFLRELKRLIETPTLMFI 504
Cdd:TIGR01349 411 VIDGAVGAEFLKSFKKYLENPIEMLL 436
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
294-503 |
5.61e-99 |
|
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: 297.15 E-value: 5.61e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490254044 294 LQTSKQQSPHFRLSVDLDLERLLALRQDINREV--PGVKISVNDLLVKACALALVAVPDVNIQFDEAAQSIRRFTDADIS 371
Cdd:pfam00198 1 MTESKQTIPHFTLTDEVDVTELLALREELKEDAadEETKLTFLPFLVKAVALALKKFPELNASWDGEEGEIVYKKYVNIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490254044 372 VAVALPAGLITPIVRSANRKSISDISNEIHSLVTRAKAGTLKPEEFQGGTFSLSNLGMLGVRQFDAIINPPQSAILAIGA 451
Cdd:pfam00198 81 IAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVGR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490254044 452 GEVRAVVRDGQIVARQQMTVSLSCDHRVIDGAAGAAFLRELKRLIETPTLMF 503
Cdd:pfam00198 161 IRKRPVVVDGEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELLL 212
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
5-77 |
9.50e-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: 100.17 E-value: 9.50e-26
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490254044 5 KTLEMPKWGLSMEEGLLARWAIQEGDDFTRGQEICEIETSKIVNVLEAPFAGTLRRILAREGETLQVGAVLAL 77
Cdd:cd06849 1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAV 73
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
1-79 |
1.36e-23 |
|
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: 93.98 E-value: 1.36e-23
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490254044 1 MSEIKtleMPKWGLSMEEGLLARWAIQEGDDFTRGQEICEIETSKIVNVLEAPFAGTLRRILAREGETLQVGAVLALAA 79
Cdd:COG0508 2 AIEIK---MPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVIA 77
|
|
| E3_binding |
pfam02817 |
e3 binding domain; This family represents a small domain of the E2 subunit of 2-oxo-acid ... |
153-188 |
9.20e-05 |
|
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: 39.59 E-value: 9.20e-05
10 20 30
....*....|....*....|....*....|....*.
gi 490254044 153 VNATPHALRLSARWGVDLKKVRGSGRGDRISVSDLE 188
Cdd:pfam02817 1 VLASPAARKLARELGIDLSDVKGTGPGGRITKEDVE 36
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11856 |
PRK11856 |
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed |
1-504 |
2.59e-136 |
|
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
Pssm-ID: 237001 [Multi-domain] Cd Length: 411 Bit Score: 399.94 E-value: 2.59e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490254044 1 MSEIKtleMPKWGLSMEEGLLARWAIQEGDDFTRGQEICEIETSKIVNVLEAPFAGTLRRILAREGETLQVGAVLA-LAA 79
Cdd:PRK11856 2 MFEFK---MPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDVVPVGSVIAvIEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490254044 80 DASVSDAELDEfvarlatakpaapgpeaaapDVAAQAGAKPASVVsppsnspeppvgqtvipvslqgvtdvtqvnatpha 159
Cdd:PRK11856 79 EGEAEAAAAAE--------------------AAPEAPAPEPAPAA----------------------------------- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490254044 160 lrlsarwgvdlkkvrgsgrgdrisvsdlesaivaaggrlASPTPPVRRSKAPRSHADDSQVSATPLARRLAGKLGINLHD 239
Cdd:PRK11856 104 ---------------------------------------AAAAAAAPAAAAAPAAPAAAAAKASPAVRKLARELGVDLST 144
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490254044 240 CRSSGSRGRVSRDDVLAAA-----LLLDEHPQTSPVQESAPAPFESIPMSGMRRAIASRLQTSKQQSPHFRLSVDLDLER 314
Cdd:PRK11856 145 VKGSGPGGRITKEDVEAAAaaaapAAAAAAAAAAAPPAAAAEGEERVPLSGMRKAIAKRMVESKREIPHFTLTDEVDVTA 224
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490254044 315 LLALRQDINREvpGVKISVNDLLVKACALALVAVPDVNIQFDEAAqsIRRFTDADISVAVALPAGLITPIVRSANRKSIS 394
Cdd:PRK11856 225 LLALRKQLKAI--GVKLTVTDFLIKAVALALKKFPELNASWDDDA--IVLKKYVNIGIAVATDGGLIVPVIRDADKKSLF 300
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490254044 395 DISNEIHSLVTRAKAGTLKPEEFQGGTFSLSNLGMLGVRQFDAIINPPQSAILAIGAGEVRAVVRDGQIVARQQMTVSLS 474
Cdd:PRK11856 301 ELAREIKDLAEKAREGKLKPEELQGGTFTISNLGMFGGDYFTPIINPPEVAILGVGAIVERPVVVDGEIVVRKVMPLSLS 380
|
490 500 510
....*....|....*....|....*....|
gi 490254044 475 CDHRVIDGAAGAAFLRELKRLIETPTLMFI 504
Cdd:PRK11856 381 FDHRVIDGADAARFLKALKELLENPALLLL 410
|
|
| PDHac_trf_mito |
TIGR01349 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
7-504 |
2.06e-120 |
|
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: 360.26 E-value: 2.06e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490254044 7 LEMPKWGLSMEEGLLARWAIQEGDDFTRGQEICEIETSKIVNVLEAPFAGTLRRILAREG-ETLQVGAVLALaadaSVSD 85
Cdd:TIGR01349 2 ITMPALSPTMTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEGtKDVPVNKPIAV----LVEE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490254044 86 AELDEFVARLATAKPAAPGPEAAAPDVAAQAGAKPASvvsppsnsPEPPVGQTVIPVSLQGVTDV---TQVNATPHALRL 162
Cdd:TIGR01349 78 KEDVADAFKNYKLESSASPAPKPSEIAPTAPPSAPKP--------SPAPQKQSPEPSSPAPLSDKesgDRIFASPLAKKL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490254044 163 SARWGVDLKKVRGSGRGDRISVSDLESAIvaaggrlasptppvrrSKAPRShADDSQVSATPLArrlagklginlhdcrs 242
Cdd:TIGR01349 150 AKEKGIDLSAVAGSGPNGRIVKKDIESFV----------------PQSPAS-ANQQAAATTPAT---------------- 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490254044 243 sgsrgrvsrddvlaaallldeHPQTSPVQesaPAPFESIPMSGMRRAIASRLQTSKQQSPHFRLSVDLDLERLLALRQDI 322
Cdd:TIGR01349 197 ---------------------YPAAAPVS---TGSYEDVPLSNIRKIIAKRLLESKQTIPHYYVSIECNVDKLLALRKEL 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490254044 323 NREVPGV-KISVNDLLVKACALALVAVPDVNIQFDEaaQSIRRFTDADISVAVALPAGLITPIVRSANRKSISDISNEIH 401
Cdd:TIGR01349 253 NAMASEVyKLSVNDFIIKASALALREVPEANSSWTD--NFIRRYKNVDISVAVATPDGLITPIVRNADAKGLSTISNEIK 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490254044 402 SLVTRAKAGTLKPEEFQGGTFSLSNLGMLGVRQFDAIINPPQSAILAIGAGEVRAVVRDGQ---IVARQQMTVSLSCDHR 478
Cdd:TIGR01349 331 DLAKRARNNKLKPEEFQGGTFTISNLGMFGIKDFTAIINPPQACILAVGAVEDVAVVDNDEekgFAVASIMSVTLSCDHR 410
|
490 500
....*....|....*....|....*.
gi 490254044 479 VIDGAAGAAFLRELKRLIETPTLMFI 504
Cdd:TIGR01349 411 VIDGAVGAEFLKSFKKYLENPIEMLL 436
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
294-503 |
5.61e-99 |
|
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: 297.15 E-value: 5.61e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490254044 294 LQTSKQQSPHFRLSVDLDLERLLALRQDINREV--PGVKISVNDLLVKACALALVAVPDVNIQFDEAAQSIRRFTDADIS 371
Cdd:pfam00198 1 MTESKQTIPHFTLTDEVDVTELLALREELKEDAadEETKLTFLPFLVKAVALALKKFPELNASWDGEEGEIVYKKYVNIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490254044 372 VAVALPAGLITPIVRSANRKSISDISNEIHSLVTRAKAGTLKPEEFQGGTFSLSNLGMLGVRQFDAIINPPQSAILAIGA 451
Cdd:pfam00198 81 IAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVGR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490254044 452 GEVRAVVRDGQIVARQQMTVSLSCDHRVIDGAAGAAFLRELKRLIETPTLMF 503
Cdd:pfam00198 161 IRKRPVVVDGEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELLL 212
|
|
| PLN02744 |
PLN02744 |
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex |
9-504 |
1.58e-82 |
|
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
Pssm-ID: 215397 [Multi-domain] Cd Length: 539 Bit Score: 265.95 E-value: 1.58e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490254044 9 MPKWGLSMEEGLLARWAIQEGDDFTRGQEICEIETSKIVNVLEAPFAGTLRRILAREG-ETLQVGAVLALAADasvSDAE 87
Cdd:PLN02744 117 MPSLSPTMTEGNIARWLKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVKGDGaKEIKVGEVIAITVE---EEED 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490254044 88 LDEFvarlatakpaapgpeAAAPDVAAQAGAKPASvvsppsnspeppvgqtvipvslqgvtdvTQVNATPHAlrlsarwg 167
Cdd:PLN02744 194 IGKF---------------KDYKPSSSAAPAAPKA----------------------------KPSPPPPKE-------- 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490254044 168 vdlKKVRGSgrgdrisvsdlesaivaaggrlaSPTPPVRRSKAPRSHADDSQVSATPLARRLAGKLGINLHDCRSSGSRG 247
Cdd:PLN02744 223 ---EEVEKP-----------------------ASSPEPKASKPSAPPSSGDRIFASPLARKLAEDNNVPLSSIKGTGPDG 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490254044 248 RVSRDDVLA-AALLLDEHPQTSPVQESAPA-PFESIPMSGMRRAIASRLQTSKQQSPHFRLSVDLDLERLLALRQDIN-- 323
Cdd:PLN02744 277 RIVKADIEDyLASGGKGATAPPSTDSKAPAlDYTDIPNTQIRKVTASRLLQSKQTIPHYYLTVDTRVDKLMALRSQLNsl 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490254044 324 -REVPGVKISVNDLLVKACALALVAVPDVNIQFDEaaQSIRRFTDADISVAVALPAGLITPIVRSANRKSISDISNEIHS 402
Cdd:PLN02744 357 qEASGGKKISVNDLVIKAAALALRKVPQCNSSWTD--DYIRQYHNVNINVAVQTENGLYVPVVKDADKKGLSTIAEEVKQ 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490254044 403 LVTRAKAGTLKPEEFQGGTFSLSNL-GMLGVRQFDAIINPPQSAILAIGAGEVRAV--VRDGQIVARQQMTVSLSCDHRV 479
Cdd:PLN02744 435 LAQKARENSLKPEDYEGGTFTVSNLgGPFGIKQFCAIINPPQSAILAVGSAEKRVIpgSGPDQYNFASFMSVTLSCDHRV 514
|
490 500
....*....|....*....|....*
gi 490254044 480 IDGAAGAAFLRELKRLIETPTLMFI 504
Cdd:PLN02744 515 IDGAIGAEWLKAFKGYIENPESMLL 539
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
1-502 |
3.21e-75 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 247.04 E-value: 3.21e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490254044 1 MSEIKtleMPKWGlSMEEGLLARWAIQEGDDFTRGQEICEIETSKIVNVLEAPFAGTLRRILAREGETLQVGAVLALAAD 80
Cdd:PRK11855 2 AIEFK---VPDIG-EVVEVEVIEWLVKEGDTVEEDQPLVTVETDKATMEIPSPAAGVVKEIKVKVGDTVSVGGLLAVIEA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490254044 81 ASVSDAELDEfvARLATAKPAAPGPEAAAPDVAAQAGAKPAS------------VVSPPSNSPEPPVG------QTVIPV 142
Cdd:PRK11855 78 AGAAAAAAAP--AAAAAPAAAAAAAPAPAAAAPAAAAAAAGGgvvevkvpdigeITEVEVIEWLVKVGdtveedQSLITV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490254044 143 SlqgvTD--VTQVNAtPHAlrlsarwGVDLK-KVRgsgRGDRISVSDLESAIVAAGGRLASPTPPVRRSKAPRSHA---- 215
Cdd:PRK11855 156 E----TDkaTMEIPS-PVA-------GVVKEiKVK---VGDKVSVGSLLVVIEVAAAAPAAAAAPAAAAPAAAAAAapap 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490254044 216 -----------------DDSQVS-ATPLARRLAGKLGINLHDCRSSGSRGRVSRDDVLAAAllldEHPQTSPVQESAPAP 277
Cdd:PRK11855 221 apaaaaapaaaapaaaaAPGKAPhASPAVRRLARELGVDLSQVKGTGKKGRITKEDVQAFV----KGAMSAAAAAAAAAA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490254044 278 ----------------------FESIPMSGMRRAIASRLQTSKQQSPHFRLSVDLDLERLLALRQDINR--EVPGVKISV 333
Cdd:PRK11855 297 aagggglgllpwpkvdfskfgeIETKPLSRIKKISAANLHRSWVTIPHVTQFDEADITDLEALRKQLKKeaEKAGVKLTM 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490254044 334 NDLLVKACALALVAVPDVNIQFDEAAQSIRRFTDADISVAVALPAGLITPIVRSANRKSISDISNEIHSLVTRAKAGTLK 413
Cdd:PRK11855 377 LPFFIKAVVAALKEFPVFNASLDEDGDELTYKKYFNIGFAVDTPNGLVVPVIKDVDKKSLLEIAREIAELAKKARDGKLK 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490254044 414 PEEFQGGTFSLSNLGMLGVRQFDAIINPPQSAILAIGAGEVRAVVRDGQIVARQQMTVSLSCDHRVIDGAAGAAFLRELK 493
Cdd:PRK11855 457 PDDMQGGCFTISSLGGIGGTAFTPIINAPEVAILGVGKSQMKPVWDGKEFVPRLMLPLSLSYDHRVIDGATAARFTNYLK 536
|
....*....
gi 490254044 494 RLIETPTLM 502
Cdd:PRK11855 537 QLLADPRRM 545
|
|
| PRK14843 |
PRK14843 |
dihydrolipoamide acetyltransferase; Provisional |
155-504 |
5.57e-69 |
|
dihydrolipoamide acetyltransferase; Provisional
Pssm-ID: 184847 [Multi-domain] Cd Length: 347 Bit Score: 224.78 E-value: 5.57e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490254044 155 ATPHALRLSARWGVDLKKVRGSGRGDRISVSDLESaivaaggrlasptppvrrskaprsHADDSQVSATPLARRLAGKLG 234
Cdd:PRK14843 8 ATPAARKLADDLGINLYDVSGSGANGRVHKEDVET------------------------YKDTNVVRISPLAKRIALEHN 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490254044 235 INLHDCRSSGSRGRVSRDDVLAaalLLDEHPQTSPVQESAP--------------APFESIPMSGMRRAIASRLQTSKQQ 300
Cdd:PRK14843 64 IAWQEIQGTGHRGKIMKKDVLA---LLPENIENDSIKSPAQiekveevpdnvtpyGEIERIPMTPMRKVIAQRMVESYLT 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490254044 301 SPHFRLSVDLDLERLLALRQDINR---EVPGVKISVNDLLVKACALALVAVPDVNIQFDEAAQSIRRFTDADISVAVALP 377
Cdd:PRK14843 141 APTFTLNYEVDMTEMLALRKKVLEpimEATGKKTTVTDLLSLAVVKTLMKHPYINASLTEDGKTIITHNYVNLAMAVGMD 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490254044 378 AGLITPIVRSANRKSISDISNEIHSLVTRAKAGTLKPEEFQGGTFSLSNLGMLGVRQFDAIINPPQSAILAIGAGEVRAV 457
Cdd:PRK14843 221 NGLMTPVVYNAEKMSLSELVVAFKDVIGRTLDGKLAPSELQNSTFTISNLGMFGVQSFGPIINQPNSAILGVSSTIEKPV 300
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 490254044 458 VRDGQIVARQQMTVSLSCDHRVIDGAAGAAFLRELKRLIETPTLMFI 504
Cdd:PRK14843 301 VVNGEIVIRPIMSLGLTIDHRVVDGMAGAKFMKDLKELIETPISMLI 347
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
2-498 |
6.98e-63 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 216.41 E-value: 6.98e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490254044 2 SEIKTLEMPKWGlsMEEGLLARWAIQEGDDFTRGQEICEIETSKIVNVLEAPFAGTLRRILAREGETLQVGAVLALAADA 81
Cdd:PRK11854 103 AAAKDVHVPDIG--SDEVEVTEILVKVGDTVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVSTGSLIMVFEVA 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490254044 82 SVSDAELDEfVARLATAKPAAPGPEAAAPDVAAQAGAKPASVVSPPSNspeppVGQTV------IPVSLQGVTdvTQVNA 155
Cdd:PRK11854 181 GEAPAAAPA-AAEAAAPAAAPAAAAGVKDVNVPDIGGDEVEVTEVMVK-----VGDKVeaeqslITVEGDKAS--MEVPA 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490254044 156 tPHAlrlsarwGVdLKKVRGSgRGDRISVSDL-------ESAIVAAGGRLASPTPPVRRSKAPRSHA------------- 215
Cdd:PRK11854 253 -PFA-------GT-VKEIKVN-VGDKVKTGSLimrfeveGAAPAAAPAKQEAAAPAPAAAKAEAPAAapaakaegksefa 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490254044 216 -DDSQVSATPLARRLAGKLGINLHDCRSSGSRGRVSRDDVLAAALLLDEHPQTSPVQESA--------------PAPFES 280
Cdd:PRK11854 323 eNDAYVHATPLVRRLAREFGVNLAKVKGTGRKGRILKEDVQAYVKDAVKRAEAAPAAAAAggggpgllpwpkvdFSKFGE 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490254044 281 I---PMSGMRRAIASRLQTSKQQSPHFRLSVDLDLERLLALRQDIN----REVPGVKISVNDLLVKACALALVAVPDVNI 353
Cdd:PRK11854 403 IeevELGRIQKISGANLHRNWVMIPHVTQFDKADITELEAFRKQQNaeaeKRKLGVKITPLVFIMKAVAAALEQMPRFNS 482
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490254044 354 QFDEAAQSIRRFTDADISVAVALPAGLITPIVRSANRKSISDISNEIHSLVTRAKAGTLKPEEFQGGTFSLSNLGMLGVR 433
Cdd:PRK11854 483 SLSEDGQRLTLKKYVNIGIAVDTPNGLVVPVFKDVNKKGIIELSRELMDISKKARDGKLTAGDMQGGCFTISSIGGLGTT 562
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490254044 434 QFDAIINPPQSAILAIGAGEVRAVVRDGQIVARQQMTVSLSCDHRVIDGAAGAAFLRELKRLIET 498
Cdd:PRK11854 563 HFTPIVNAPEVAILGVSKSAMEPVWNGKEFAPRLMLPLSLSYDHRVIDGADGARFITIINDRLSD 627
|
|
| PRK05704 |
PRK05704 |
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase; |
1-499 |
2.21e-62 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
Pssm-ID: 235571 [Multi-domain] Cd Length: 407 Bit Score: 209.31 E-value: 2.21e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490254044 1 MSEIKTlemPKWGLSMEEGLLARWAIQEGDDFTRGQEICEIETSKIVNVLEAPFAGTLRRILAREGETLQVGAVLAlaad 80
Cdd:PRK05704 2 MVEIKV---PTLPESVTEATIATWHKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGDTVTVGQVLG---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490254044 81 asvsdaELDEfvarlatakpaapgpeaaapdvaaqaGAKPASVvsppsnspeppvgqtvipvslqgvtdvtqvNATPHAl 160
Cdd:PRK05704 75 ------RIDE--------------------------GAAAGAA------------------------------AAAAAA- 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490254044 161 rlsarwgvdlkkvrgsgrgdrisvsdlesaivaaggrlASPTPPVRRSKAPRSHADDSQVSATPLARRLAGKLGINLHDC 240
Cdd:PRK05704 92 --------------------------------------AAAAAAAPAQAQAAAAAEQSNDALSPAARKLAAENGLDASAV 133
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490254044 241 RSSGSRGRVSRDDVLAAALLLDEHPQTSPVQESAPAPF-------ESIPMSGMRRAIASRLQTSKQQSPHFRLSVDLDLE 313
Cdd:PRK05704 134 KGTGKGGRVTKEDVLAALAAAAAAPAAPAAAAPAAAPAplgarpeERVPMTRLRKTIAERLLEAQNTTAMLTTFNEVDMT 213
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490254044 314 RLLALR---QDINREVPGVKISVNDLLVKACALALVAVPDVN--IQFDEAAqsIRRFtdADISVAVALPAGLITPIVRSA 388
Cdd:PRK05704 214 PVMDLRkqyKDAFEKKHGVKLGFMSFFVKAVVEALKRYPEVNasIDGDDIV--YHNY--YDIGIAVGTPRGLVVPVLRDA 289
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490254044 389 NRKSISDISNEIHSLVTRAKAGTLKPEEFQGGTFSLSNLGMLGVRQFDAIINPPQSAILAIGAGEVRAVVRDGQIVARQQ 468
Cdd:PRK05704 290 DQLSFAEIEKKIAELAKKARDGKLSIEELTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHKIKERPVAVNGQIVIRPM 369
|
490 500 510
....*....|....*....|....*....|.
gi 490254044 469 MTVSLSCDHRVIDGAAGAAFLRELKRLIETP 499
Cdd:PRK05704 370 MYLALSYDHRIIDGKEAVGFLVTIKELLEDP 400
|
|
| sucB |
TIGR01347 |
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ... |
3-504 |
5.14e-62 |
|
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: 208.43 E-value: 5.14e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490254044 3 EIKTLEMPKwglSMEEGLLARWAIQEGDDFTRGQEICEIETSKIVNVLEAPFAGTLRRILAREGETLQVGAVLALAADAS 82
Cdd:TIGR01347 2 EIKVPELAE---SITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAILEEGN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490254044 83 VSDAELDEfvarlatakpaapgpeaaapdvaaqaGAKPAsvvsppsnspeppvgqtvipvslqgvtdvtqvnatphalrl 162
Cdd:TIGR01347 79 DATAAPPA--------------------------KSGEE----------------------------------------- 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490254044 163 sarwgvdlkkvrgsgrgdrisvsdlesaivaaggrlASPTPPVRRSKAPRshADDSQVSATPLARRLAGKLGINLHDCRS 242
Cdd:TIGR01347 92 ------------------------------------KEETPAASAAAAPT--AAANRPSLSPAARRLAKEHGIDLSAVPG 133
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490254044 243 SGSRGRVSRDDVLAAALLLDEHPQTSPVQESA-----PAPFESIPMSGMRRAIASRLQTSKQQSPHFRLSVDLDLERLLA 317
Cdd:TIGR01347 134 TGVTGRVTKEDIIKKTEAPASAQPPAAAAAAAapaaaTRPEERVKMTRLRQRIAERLKEAQNSTAMLTTFNEVDMSAVME 213
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490254044 318 LR---QDINREVPGVKISVNDLLVKACALALVAVPDVNIQFDEAAQSIRRFTDadISVAVALPAGLITPIVRSANRKSIS 394
Cdd:TIGR01347 214 LRkryKEEFEKKHGVKLGFMSFFVKAVVAALKRFPEVNAEIDGDDIVYKDYYD--ISVAVSTDRGLVVPVVRNADRMSFA 291
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490254044 395 DISNEIHSLVTRAKAGTLKPEEFQGGTFSLSNLGMLGVRQFDAIINPPQSAILAIGAGEVRAVVRDGQIVARQQMTVSLS 474
Cdd:TIGR01347 292 DIEKEIADLGKKARDGKLTLEDMTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHGIKERPVAVNGQIEIRPMMYLALS 371
|
490 500 510
....*....|....*....|....*....|
gi 490254044 475 CDHRVIDGAAGAAFLRELKRLIETPTLMFI 504
Cdd:TIGR01347 372 YDHRLIDGKEAVTFLVTIKELLEDPRRLLL 401
|
|
| PTZ00144 |
PTZ00144 |
dihydrolipoamide succinyltransferase; Provisional |
3-504 |
2.77e-57 |
|
dihydrolipoamide succinyltransferase; Provisional
Pssm-ID: 240289 [Multi-domain] Cd Length: 418 Bit Score: 196.06 E-value: 2.77e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490254044 3 EIKTLEMPKWGLSMEEGLLARWAIQEGDDFTRGQEICEIETSKiVNV-LEAPFAGTLRRILAREGETLQVGAVLAlaada 81
Cdd:PTZ00144 43 SIKVIKVPTMGDSISEGTVVEWKKKVGDYVKEDEVICIIETDK-VSVdIRAPASGVITKIFAEEGDTVEVGAPLS----- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490254044 82 svsdaELDEfvarlatakpaapgpeaaapdvaaqAGAKPASvvsppsnspeppvgqtvIPVSLQGVTDVTQVNATPHAlr 161
Cdd:PTZ00144 117 -----EIDT-------------------------GGAPPAA-----------------APAAAAAAKAEKTTPEKPKA-- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490254044 162 lsarwgvdlkkvrgsgrgdrisvsdlesaivaaggrlASPTPPVRRSKAPRSHADDSQVSATPLARRLAgklginlhdcr 241
Cdd:PTZ00144 148 -------------------------------------AAPTPEPPAASKPTPPAAAKPPEPAPAAKPPP----------- 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490254044 242 ssgsrgrvsrddvlaaallldehpqtSPVQESAPaPFESIPMSGMRRAIASRLQTSKQQSPHFRLSVDLDLERLLALR-- 319
Cdd:PTZ00144 180 --------------------------TPVARADP-RETRVPMSRMRQRIAERLKASQNTCAMLTTFNECDMSALMELRke 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490254044 320 -QDINREVPGVKISVNDLLVKACALALVAVPDVNIQFDEAAQSIRRFTDadISVAVALPAGLITPIVRSANRKSISDISN 398
Cdd:PTZ00144 233 yKDDFQKKHGVKLGFMSAFVKASTIALKKMPIVNAYIDGDEIVYRNYVD--ISVAVATPTGLVVPVIRNCENKSFAEIEK 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490254044 399 EIHSLVTRAKAGTLKPEEFQGGTFSLSNLGMLGVRQFDAIINPPQSAILAIGAGEVRAVVRDGQIVARQQMTVSLSCDHR 478
Cdd:PTZ00144 311 ELADLAEKARNNKLTLEDMTGGTFTISNGGVFGSLMGTPIINPPQSAILGMHAIKKRPVVVGNEIVIRPIMYLALTYDHR 390
|
490 500
....*....|....*....|....*.
gi 490254044 479 VIDGAAGAAFLRELKRLIETPTLMFI 504
Cdd:PTZ00144 391 LIDGRDAVTFLKKIKDLIEDPARMLL 416
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
17-502 |
3.19e-57 |
|
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: 199.33 E-value: 3.19e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490254044 17 EEGLLARWAIQEGDDFTRGQEICEIETSKIVNVLEAPFAGTLRRILAREGETLQVGAVLALAADASVSDAELDEfvARLA 96
Cdd:TIGR01348 12 EEGEVIEVLVKPGDKVEAGQSLITLESDKASMEVPSSAAGIIKEIKVKVGDTLPVGGVIATLEVGAGAQAQAEA--KKEA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490254044 97 TAKPAAPGPEAAAPDVAAQAGAKPASVVSPPSNSPEPPVGQTVIPVsLQGVTD-------VTQVNATPHALRLSARWGVD 169
Cdd:TIGR01348 90 APAPTAGAPAPAAQAQAAPAAGQSSGVQEVTVPDIGDIEKVTVIEV-LVKVGDtvsadqsLITLESDKASMEVPAPASGV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490254044 170 LKKVRgSGRGDRISVSDL-----------------ESAIVAAGGRLASPTPPVRRSKAPRSHA---------DDSQVS-A 222
Cdd:TIGR01348 169 VKSVK-VKVGDSVPTGDLiltlsvagstpatapapASAQPAAQSPAATQPEPAAAPAAAKAQApapqqagtqNPAKVDhA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490254044 223 TPLARRLAGKLGINLHDCRSSGSRGRVSRDDVLAAALLLDEHPQTSPVQESAPAP---------------FESIPMSGMR 287
Cdd:TIGR01348 248 APAVRRLAREFGVDLSAVKGTGIKGRILREDVQRFVKEPSVRAQAAAASAAGGAPgalpwpnvdfskfgeVEEVDMSRIR 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490254044 288 RAIASRLQTSKQQSPHFRLSVDLDLERLLALRQDIN--REVPGVKISVNDLLVKACALALVAVPDVNIQFDEAAQSIRRF 365
Cdd:TIGR01348 328 KISGANLTRNWTMIPHVTHFDKADITEMEAFRKQQNaaVEKEGVKLTVLHILMKAVAAALKKFPKFNASLDLGGEQLILK 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490254044 366 TDADISVAVALPAGLITPIVRSANRKSISDISNEIHSLVTRAKAGTLKPEEFQGGTFSLSNLGMLGVRQFDAIINPPQSA 445
Cdd:TIGR01348 408 KYVNIGVAVDTPNGLLVPVIKDVDRKGITELALELSDLAKKARDGKLTPDEMQGACFTISSLGGIGGTAFTPIVNAPEVA 487
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 490254044 446 ILAIGAGEVRAVVRDGQIVARQQMTVSLSCDHRVIDGAAGAAFLRELKRLIETPTLM 502
Cdd:TIGR01348 488 ILGVSKSGMEPVWNGKEFEPRLMLPLSLSYDHRVIDGADAARFTTYICESLADIRRL 544
|
|
| PLN02528 |
PLN02528 |
2-oxoisovalerate dehydrogenase E2 component |
187-505 |
3.51e-53 |
|
2-oxoisovalerate dehydrogenase E2 component
Pssm-ID: 215289 [Multi-domain] Cd Length: 416 Bit Score: 185.31 E-value: 3.51e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490254044 187 LESAIVAAGGRLASPTPPVRRSKAPRSHADDSQVS---ATPLARRLAGKLGINLHDCRSSGSRGRVSRDDVLAAA----- 258
Cdd:PLN02528 74 VEDSQHLRSDSLLLPTDSSNIVSLAESDERGSNLSgvlSTPAVRHLAKQYGIDLNDILGTGKDGRVLKEDVLKYAaqkgv 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490254044 259 ------LLLDEHPQTSPVQESAPAPFES------IPMSGMRRAIASRLqTSKQQSPHFRLSVDLDLERLLALRQDI--NR 324
Cdd:PLN02528 154 vkdsssAEEATIAEQEEFSTSVSTPTEQsyedktIPLRGFQRAMVKTM-TAAAKVPHFHYVEEINVDALVELKASFqeNN 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490254044 325 EVPGVKISVNDLLVKACALALVAVPDVNIQFDEAAQSIRRFTDADISVAVALPAGLITPIVRSANRKSISDISNEIHSLV 404
Cdd:PLN02528 233 TDPTVKHTFLPFLIKSLSMALSKYPLLNSCFNEETSEIRLKGSHNIGVAMATEHGLVVPNIKNVQSLSLLEITKELSRLQ 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490254044 405 TRAKAGTLKPEEFQGGTFSLSNLGMLGVRQFDAIINPPQSAILAIgaGEVRAVVR---DGQIVARQQMTVSLSCDHRVID 481
Cdd:PLN02528 313 HLAAENKLNPEDITGGTITLSNIGAIGGKFGSPVLNLPEVAIIAL--GRIQKVPRfvdDGNVYPASIMTVTIGADHRVLD 390
|
330 340
....*....|....*....|....
gi 490254044 482 GAAGAAFLRELKRLIETPTLMFIQ 505
Cdd:PLN02528 391 GATVARFCNEWKSYVEKPELLMLH 414
|
|
| SucB_Actino |
TIGR02927 |
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model ... |
6-498 |
1.12e-48 |
|
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: 176.74 E-value: 1.12e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490254044 6 TLEMPKWGLSMEEGLLARWAIQEGDDFTRGQEICEIETSKIVNVLEAPFAGTLRRILAREGETLQVGAVLALAADASVSD 85
Cdd:TIGR02927 4 SVKMPALGESVTEGTVTSWLKAVGDTVEADEPLLEVSTDKVDTEIPSPAAGVLLEIRAPEDDTVEVGGVLAIIGEPGEAG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490254044 86 AELDEFVAR-LATAKPAAPGPEAAAPDVAAQAGAKPASVVSPPSNSPEPPVGQTV----IPVSLQGVTDVTQVNatpHAL 160
Cdd:TIGR02927 84 SEPAPAAPEpEAAPEPEAPAPAPTPAAEAPAPAAPQAGGSGEATEVKMPELGESVtegtVTSWLKAVGDTVEVD---EPL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490254044 161 RLSARWGVDlKKVRGSGRGDRISVSDLESAIVAAGGRLA----------------------------------------S 200
Cdd:TIGR02927 161 LEVSTDKVD-TEIPSPVAGTLLEIRAPEDDTVEVGTVLAiigdanaapaepaeeeapapseagsepapdpaaraphaapD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490254044 201 PTPPVRRSKAPRSHADDSQVSA-------TPLARRLAGKLGINLHDCRSSGSRGRVSRDDVLAAALLLDEHPQ------- 266
Cdd:TIGR02927 240 PPAPAPAPAKTAAPAAAAPVSSgdsgpyvTPLVRKLAKDKGVDLSTVKGTGVGGRIRKQDVLAAAKAAEEARAaaaapaa 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490254044 267 ----TSPVQESAPAPFESIPMSG-------MRRAIASRLQTSKQQSPHFRLSVDLDLERLLALRQDIN---REVPGVKIS 332
Cdd:TIGR02927 320 aaapAAPAAAAKPAEPDTAKLRGttqkmnrIRQITADKTIESLQTSAQLTQVHEVDMTRVAALRARAKndfLEKNGVNLT 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490254044 333 VNDLLVKACALALVAVPDVNIQFDEAAQSIRRFTDADISVAVALPAGLITPIVRSANRKSISDISNEIHSLVTRAKAGTL 412
Cdd:TIGR02927 400 FLPFFVQAVTEALKAHPNVNASYNAETKEVTYHDVEHVGIAVDTPRGLLVPVIHNAGDLSLPGLAKAINDLAARARDNKL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490254044 413 KPEEFQGGTFSLSNLGMLGVRQFDAIINPPQSAILAIGAGEVRAVV---RDG--QIVARQQMTVSLSCDHRVIDGAAGAA 487
Cdd:TIGR02927 480 KPDELSGGTFTITNIGSGGALFDTPILNPPQAAILGTGAIVKRPRVikdEDGgeSIAIRSVCYLPLTYDHRLVDGADAGR 559
|
570
....*....|.
gi 490254044 488 FLRELKRLIET 498
Cdd:TIGR02927 560 FLTTIKKRLEE 570
|
|
| PRK11857 |
PRK11857 |
dihydrolipoamide acetyltransferase; Reviewed |
219-504 |
2.39e-45 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237002 [Multi-domain] Cd Length: 306 Bit Score: 161.11 E-value: 2.39e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490254044 219 QVSATPLARRLAGKLGINLHDCRSSGSRGRVSRDDVLAAALLLDEHP------QTSPVQESAPAPF----------ESIP 282
Cdd:PRK11857 1 KILATPIARALAKKLGIDISLLKGSGRDGKILAEDVENFIKSLKSAPtpaeaaSVSSAQQAAKTAApaaappklegKREK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490254044 283 MSGMRRAIASRLQTSKQQSPHFRLSVDLDLERLLALRQDINREV---PGVKISVNDLLVKACALALVAVPDVNIQFDEAA 359
Cdd:PRK11857 81 VAPIRKAIARAMTNSWSNVAYVNLVNEIDMTKLWDLRKSVKDPVlktEGVKLTFLPFIAKAILIALKEFPIFAAKYDEAT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490254044 360 QSIRRFTDADISVAVALPAGLITPIVRSANRKSISDISNEIHSLVTRAKAGTLKPEEFQGGTFSLSNLGMLGVRQFDAII 439
Cdd:PRK11857 161 SELVYPDTLNLGIAVDTEAGLMVPVIKNAQKLSIVEIAKEISRLAKAARERKIKPDEMKGGSFTITNYGSVGSLYGVPVI 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490254044 440 NPPQSAILAIGAGEVRAVVRDGQIVARQQMTVSLSCDHRVIDGAAGAAFLRELKRLIETPTLMFI 504
Cdd:PRK11857 241 NYPELAIAGVGAIIDKAIVKNGQIVAGKVMHLTVAADHRWIDGATIGRFASRVKELLEKPEILGV 305
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
4-97 |
4.01e-37 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 140.46 E-value: 4.01e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490254044 4 IKTLEMPKWGLSMEEGLLARWAIQEGDDFTRGQEICEIETSKIVNVLEAPFAGTLRRILAREGETLQVGAVLALAADASV 83
Cdd:PRK14875 2 ITPITMPKWGLSMTEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGETLPVGALLAVVADAEV 81
|
90
....*....|....
gi 490254044 84 SDAELDEFVARLAT 97
Cdd:PRK14875 82 SDAEIDAFIAPFAR 95
|
|
| PLN02226 |
PLN02226 |
2-oxoglutarate dehydrogenase E2 component |
263-504 |
1.21e-34 |
|
2-oxoglutarate dehydrogenase E2 component
Pssm-ID: 177871 [Multi-domain] Cd Length: 463 Bit Score: 135.65 E-value: 1.21e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490254044 263 EHPQTSPVQESapapfESIPMSGMRRAIASRLQTSKQQSPHFRLSVDLDLERLLALR---QDINREVPGVKISVNDLLVK 339
Cdd:PLN02226 224 KEPQLPPKERE-----RRVPMTRLRKRVATRLKDSQNTFALLTTFNEVDMTNLMKLRsqyKDAFYEKHGVKLGLMSGFIK 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490254044 340 ACALALVAVPDVNIQFDEAAQSIRRFTDadISVAVALPAGLITPIVRSANRKSISDISNEIHSLVTRAKAGTLKPEEFQG 419
Cdd:PLN02226 299 AAVSALQHQPVVNAVIDGDDIIYRDYVD--ISIAVGTSKGLVVPVIRGADKMNFAEIEKTINGLAKKANEGTISIDEMAG 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490254044 420 GTFSLSNLGMLGVRQFDAIINPPQSAILAIGAGEVRAVVRDGQIVARQQMTVSLSCDHRVIDGAAGAAFLRELKRLIETP 499
Cdd:PLN02226 377 GSFTVSNGGVYGSLISTPIINPPQSAILGMHSIVSRPMVVGGSVVPRPMMYVALTYDHRLIDGREAVYFLRRVKDVVEDP 456
|
....*
gi 490254044 500 TLMFI 504
Cdd:PLN02226 457 QRLLL 461
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
5-77 |
9.50e-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: 100.17 E-value: 9.50e-26
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490254044 5 KTLEMPKWGLSMEEGLLARWAIQEGDDFTRGQEICEIETSKIVNVLEAPFAGTLRRILAREGETLQVGAVLAL 77
Cdd:cd06849 1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAV 73
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
1-79 |
1.36e-23 |
|
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: 93.98 E-value: 1.36e-23
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490254044 1 MSEIKtleMPKWGLSMEEGLLARWAIQEGDDFTRGQEICEIETSKIVNVLEAPFAGTLRRILAREGETLQVGAVLALAA 79
Cdd:COG0508 2 AIEIK---MPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVIA 77
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
5-76 |
2.34e-12 |
|
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: 62.23 E-value: 2.34e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490254044 5 KTLEMPKWGLSMEEGLlARWAIQEGDDFTRGQEICEIETSKIVNVLEAPFAGTLRRILAREGETLQVGAVLA 76
Cdd:pfam00364 1 TEIKSPMIGESVREGV-VEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLA 71
|
|
| kgd |
PRK12270 |
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ... |
265-495 |
3.62e-12 |
|
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;
Pssm-ID: 237030 [Multi-domain] Cd Length: 1228 Bit Score: 69.15 E-value: 3.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490254044 265 PQTSPVQESAPAPFESIPMSGMRRAIASRLQTSkqqsphfrLSV-------DLDLERLLALRQDIN---REVPGVKISVN 334
Cdd:PRK12270 102 AAAAAAPAAAAVEDEVTPLRGAAAAVAKNMDAS--------LEVptatsvrAVPAKLLIDNRIVINnhlKRTRGGKVSFT 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490254044 335 DLLVKACALALVAVPDVNIQFDEAAQSIRRFTDADISVAVAL----PAG---LITPIVRSANRKSISDISNEIHSLVTRA 407
Cdd:PRK12270 174 HLIGYALVQALKAFPNMNRHYAEVDGKPTLVTPAHVNLGLAIdlpkKDGsrqLVVPAIKGAETMDFAQFWAAYEDIVRRA 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490254044 408 KAGTLKPEEFQGGTFSLSNLGMLGVRQFDAIINPPQSAILAIGAGEVRA------VVRDGQIVARQQMTVSLSCDHRVID 481
Cdd:PRK12270 254 RDGKLTADDFQGTTISLTNPGGIGTVHSVPRLMKGQGAIIGVGAMEYPAefqgasEERLAELGISKVMTLTSTYDHRIIQ 333
|
250
....*....|....
gi 490254044 482 GAAGAAFLRELKRL 495
Cdd:PRK12270 334 GAESGEFLRTIHQL 347
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
19-76 |
9.38e-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: 57.43 E-value: 9.38e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 490254044 19 GLLARWAIQEGDDFTRGQEICEIETSKIVNVLEAPFAGTLRRILAREGETLQVGAVLA 76
Cdd:cd06850 8 GTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLV 65
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
9-86 |
6.17e-09 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 58.01 E-value: 6.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490254044 9 MPKWGLSMEEGLLARWAIQEGDDFTRGQEICEIETSKIVNVLEAPFAGTLRRILAREG-ETLQVGAVLA-LAADA-SVSD 85
Cdd:PRK11892 7 MPALSPTMEEGTLAKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKILVPEGtEGVKVNTPIAvLLEEGeSASD 86
|
.
gi 490254044 86 A 86
Cdd:PRK11892 87 A 87
|
|
| E3_binding |
pfam02817 |
e3 binding domain; This family represents a small domain of the E2 subunit of 2-oxo-acid ... |
220-255 |
3.15e-08 |
|
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: 49.22 E-value: 3.15e-08
10 20 30
....*....|....*....|....*....|....*.
gi 490254044 220 VSATPLARRLAGKLGINLHDCRSSGSRGRVSRDDVL 255
Cdd:pfam02817 1 VLASPAARKLARELGIDLSDVKGTGPGGRITKEDVE 36
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
10-75 |
5.76e-07 |
|
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: 47.05 E-value: 5.76e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490254044 10 PKWGLSMEEGLLARWAIQEGDDFTRGQEICEIETSKIVNVLEAPFAGTLRRILAREGETLQVGAVL 75
Cdd:cd06663 5 PDLAQHLGDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKVEGDTPL 70
|
|
| AccB |
COG0511 |
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ... |
26-77 |
1.93e-05 |
|
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: 44.50 E-value: 1.93e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 490254044 26 IQEGDDFTRGQEICEIETSKIVNVLEAPFAGTLRRILAREGETLQVGAVLAL 77
Cdd:COG0511 83 VKVGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVVEILVENGQPVEYGQPLFV 134
|
|
| E3_binding |
pfam02817 |
e3 binding domain; This family represents a small domain of the E2 subunit of 2-oxo-acid ... |
153-188 |
9.20e-05 |
|
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: 39.59 E-value: 9.20e-05
10 20 30
....*....|....*....|....*....|....*.
gi 490254044 153 VNATPHALRLSARWGVDLKKVRGSGRGDRISVSDLE 188
Cdd:pfam02817 1 VLASPAARKLARELGIDLSDVKGTGPGGRITKEDVE 36
|
|
| PRK09282 |
PRK09282 |
pyruvate carboxylase subunit B; Validated |
26-77 |
5.27e-04 |
|
pyruvate carboxylase subunit B; Validated
Pssm-ID: 236449 [Multi-domain] Cd Length: 592 Bit Score: 42.52 E-value: 5.27e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 490254044 26 IQEGDDFTRGQEICEIETSKIVNVLEAPFAGTLRRILAREGETLQVGAVLAL 77
Cdd:PRK09282 538 VKEGDKVKAGDTVLVLEAMKMENEIQAPVDGTVKEILVKEGDRVNPGDVLME 589
|
|
| PRK05641 |
PRK05641 |
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
19-75 |
9.18e-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: 9.18e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 490254044 19 GLLARWAIQEGDDFTRGQEICEIETSKIVNVLEAPFAGTLRRILAREGETLQVGAVL 75
Cdd:PRK05641 93 GKILRILVREGQQVKVGQGLLILEAMKMENEIPAPKDGVVKKILVKEGDTVDTGQPL 149
|
|
| |
