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Conserved domains on  [gi|686543092|gb|AIQ53789|]
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branched-chain alpha-keto acid dehydrogenase subunit E2 [Paenibacillus sp. FSL R7-0331]

Protein Classification

dihydrolipoamide acetyltransferase family protein( domain architecture ID 11485570)

dihydrolipoamide acetyltransferase family protein is the acetyltransferase (E2) subunit of a 2-oxo acid dehydrogenase multienzyme complex, such as Pseudomonas putida lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex

EC:  2.3.-.-
Gene Ontology:  GO:0016407|GO:0045240
PubMed:  3332999|24077172
SCOP:  4000430

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
PRK11856 PRK11856
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
8-469 3.57e-140

branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed


:

Pssm-ID: 237001 [Multi-domain]  Cd Length: 411  Bit Score: 408.80  E-value: 3.57e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092   8 TDVVMPQLAESLVSATIGKWLKQPGDRVEEYEPICELITDKVNAELPSTVEGTLVELLAEEGQVISVGEIIARIAVAAPA 87
Cdd:PRK11856   3 FEFKMPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDVVPVGSVIAVIEEEGEA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092  88 GASAGSSAPAAGTAPQAAAAAPAPGTPAAPVRPAapslSAADAPMRSRYSPAVQTLAAEHRIDLSAVPGTGLGGRITRKD 167
Cdd:PRK11856  83 EAAAAAEAAPEAPAPEPAPAAAAAAAAAPAAAAA----PAAPAAAAAKASPAVRKLARELGVDLSTVKGSGPGGRITKED 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092 168 VLAYLENGGAAAGQTVPAhpgaagagqagrqvpealqqPALQVIQAEAQEQLEPVRnsglhlsespriptievegglgss 247
Cdd:PRK11856 159 VEAAAAAAAPAAAAAAAA--------------------AAAPPAAAAEGEERVPLS------------------------ 194
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092 248 seylidvtPIRNTIATRMRQSVSEIPHAWTMIEVDVTNLVVLRNKLKDEFKRkeginLTYLAFMMKAVVSAIKDYPIMNS 327
Cdd:PRK11856 195 --------GMRKAIAKRMVESKREIPHFTLTDEVDVTALLALRKQLKAIGVK-----LTVTDFLIKAVALALKKFPELNA 261
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092 328 VWAVDKIIVKRDINIALAVGTEDSVMTPVIKKADQKNIAGLAREIDELAQKTREGKLRLDDMQGGTFTVNNTGSFGSILS 407
Cdd:PRK11856 262 SWDDDAIVLKKYVNIGIAVATDGGLIVPVIRDADKKSLFELAREIKDLAEKAREGKLKPEELQGGTFTISNLGMFGGDYF 341
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 686543092 408 YPIINYPQAAILTFESIVKKPVVINDMIAVRSMANICLSLDHRILDGVICGRFLQRVKDNLE 469
Cdd:PRK11856 342 TPIINPPEVAILGVGAIVERPVVVDGEIVVRKVMPLSLSFDHRVIDGADAARFLKALKELLE 403
 
Name Accession Description Interval E-value
PRK11856 PRK11856
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
8-469 3.57e-140

branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed


Pssm-ID: 237001 [Multi-domain]  Cd Length: 411  Bit Score: 408.80  E-value: 3.57e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092   8 TDVVMPQLAESLVSATIGKWLKQPGDRVEEYEPICELITDKVNAELPSTVEGTLVELLAEEGQVISVGEIIARIAVAAPA 87
Cdd:PRK11856   3 FEFKMPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDVVPVGSVIAVIEEEGEA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092  88 GASAGSSAPAAGTAPQAAAAAPAPGTPAAPVRPAapslSAADAPMRSRYSPAVQTLAAEHRIDLSAVPGTGLGGRITRKD 167
Cdd:PRK11856  83 EAAAAAEAAPEAPAPEPAPAAAAAAAAAPAAAAA----PAAPAAAAAKASPAVRKLARELGVDLSTVKGSGPGGRITKED 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092 168 VLAYLENGGAAAGQTVPAhpgaagagqagrqvpealqqPALQVIQAEAQEQLEPVRnsglhlsespriptievegglgss 247
Cdd:PRK11856 159 VEAAAAAAAPAAAAAAAA--------------------AAAPPAAAAEGEERVPLS------------------------ 194
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092 248 seylidvtPIRNTIATRMRQSVSEIPHAWTMIEVDVTNLVVLRNKLKDEFKRkeginLTYLAFMMKAVVSAIKDYPIMNS 327
Cdd:PRK11856 195 --------GMRKAIAKRMVESKREIPHFTLTDEVDVTALLALRKQLKAIGVK-----LTVTDFLIKAVALALKKFPELNA 261
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092 328 VWAVDKIIVKRDINIALAVGTEDSVMTPVIKKADQKNIAGLAREIDELAQKTREGKLRLDDMQGGTFTVNNTGSFGSILS 407
Cdd:PRK11856 262 SWDDDAIVLKKYVNIGIAVATDGGLIVPVIRDADKKSLFELAREIKDLAEKAREGKLKPEELQGGTFTISNLGMFGGDYF 341
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 686543092 408 YPIINYPQAAILTFESIVKKPVVINDMIAVRSMANICLSLDHRILDGVICGRFLQRVKDNLE 469
Cdd:PRK11856 342 TPIINPPEVAILGVGAIVERPVVVDGEIVVRKVMPLSLSFDHRVIDGADAARFLKALKELLE 403
sucB TIGR01347
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ...
8-469 9.91e-97

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: 297.42  E-value: 9.91e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092    8 TDVVMPQLAESLVSATIGKWLKQPGDRVEEYEPICELITDKVNAELPSTVEGTLVELLAEEGQVISVGEIIARIAVAAPA 87
Cdd:TIGR01347   1 IEIKVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAILEEGNDA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092   88 GASAGSSAPAAGTAPQAAAAAPapgtpaapvrpaapslSAADAPMRSRYSPAVQTLAAEHRIDLSAVPGTGLGGRITRKD 167
Cdd:TIGR01347  81 TAAPPAKSGEEKEETPAASAAA----------------APTAAANRPSLSPAARRLAKEHGIDLSAVPGTGVTGRVTKED 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092  168 VLAYLENGGAAagqtvpahpgaagagqagrqvpealQQPALQVIQAEAQEQLEPVRnsglhlsespRIPtievegglgss 247
Cdd:TIGR01347 145 IIKKTEAPASA-------------------------QPPAAAAAAAAPAAATRPEE----------RVK----------- 178
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092  248 seylidVTPIRNTIATRMRQSVSEIPHAWTMIEVDVTNLVVLRNKLKDEFKRKEGINLTYLAFMMKAVVSAIKDYPIMNS 327
Cdd:TIGR01347 179 ------MTRLRQRIAERLKEAQNSTAMLTTFNEVDMSAVMELRKRYKEEFEKKHGVKLGFMSFFVKAVVAALKRFPEVNA 252
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092  328 VWAVDKIIVKRDINIALAVGTEDSVMTPVIKKADQKNIAGLAREIDELAQKTREGKLRLDDMQGGTFTVNNTGSFGSILS 407
Cdd:TIGR01347 253 EIDGDDIVYKDYYDISVAVSTDRGLVVPVVRNADRMSFADIEKEIADLGKKARDGKLTLEDMTGGTFTITNGGVFGSLMS 332
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 686543092  408 YPIINYPQAAILTFESIVKKPVVINDMIAVRSMANICLSLDHRILDGVICGRFLQRVKDNLE 469
Cdd:TIGR01347 333 TPIINPPQSAILGMHGIKERPVAVNGQIEIRPMMYLALSYDHRLIDGKEAVTFLVTIKELLE 394
2-oxoacid_dh pfam00198
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ...
265-469 3.23e-87

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: 265.95  E-value: 3.23e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092  265 MRQSVSEIPHAWTMIEVDVTNLVVLRNKLKDEFKrKEGINLTYLAFMMKAVVSAIKDYPIMNSVWAVDK--IIVKRDINI 342
Cdd:pfam00198   1 MTESKQTIPHFTLTDEVDVTELLALREELKEDAA-DEETKLTFLPFLVKAVALALKKFPELNASWDGEEgeIVYKKYVNI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092  343 ALAVGTEDSVMTPVIKKADQKNIAGLAREIDELAQKTREGKLRLDDMQGGTFTVNNTGSFGSILSYPIINYPQAAILTFE 422
Cdd:pfam00198  80 GIAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVG 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 686543092  423 SIVKKPVVINDMIAVRSMANICLSLDHRILDGVICGRFLQRVKDNLE 469
Cdd:pfam00198 160 RIRKRPVVVDGEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLE 206
AceF COG0508
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ...
8-82 3.39e-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: 103.99  E-value: 3.39e-27
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 686543092   8 TDVVMPQLAESLVSATIGKWLKQPGDRVEEYEPICELITDKVNAELPSTVEGTLVELLAEEGQVISVGEIIARIA 82
Cdd:COG0508    3 IEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVIA 77
lipoyl_domain cd06849
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ...
8-81 4.10e-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: 100.94  E-value: 4.10e-26
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 686543092   8 TDVVMPQLAESLVSATIGKWLKQPGDRVEEYEPICELITDKVNAELPSTVEGTLVELLAEEGQVISVGEIIARI 81
Cdd:cd06849    1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
 
Name Accession Description Interval E-value
PRK11856 PRK11856
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
8-469 3.57e-140

branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed


Pssm-ID: 237001 [Multi-domain]  Cd Length: 411  Bit Score: 408.80  E-value: 3.57e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092   8 TDVVMPQLAESLVSATIGKWLKQPGDRVEEYEPICELITDKVNAELPSTVEGTLVELLAEEGQVISVGEIIARIAVAAPA 87
Cdd:PRK11856   3 FEFKMPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDVVPVGSVIAVIEEEGEA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092  88 GASAGSSAPAAGTAPQAAAAAPAPGTPAAPVRPAapslSAADAPMRSRYSPAVQTLAAEHRIDLSAVPGTGLGGRITRKD 167
Cdd:PRK11856  83 EAAAAAEAAPEAPAPEPAPAAAAAAAAAPAAAAA----PAAPAAAAAKASPAVRKLARELGVDLSTVKGSGPGGRITKED 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092 168 VLAYLENGGAAAGQTVPAhpgaagagqagrqvpealqqPALQVIQAEAQEQLEPVRnsglhlsespriptievegglgss 247
Cdd:PRK11856 159 VEAAAAAAAPAAAAAAAA--------------------AAAPPAAAAEGEERVPLS------------------------ 194
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092 248 seylidvtPIRNTIATRMRQSVSEIPHAWTMIEVDVTNLVVLRNKLKDEFKRkeginLTYLAFMMKAVVSAIKDYPIMNS 327
Cdd:PRK11856 195 --------GMRKAIAKRMVESKREIPHFTLTDEVDVTALLALRKQLKAIGVK-----LTVTDFLIKAVALALKKFPELNA 261
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092 328 VWAVDKIIVKRDINIALAVGTEDSVMTPVIKKADQKNIAGLAREIDELAQKTREGKLRLDDMQGGTFTVNNTGSFGSILS 407
Cdd:PRK11856 262 SWDDDAIVLKKYVNIGIAVATDGGLIVPVIRDADKKSLFELAREIKDLAEKAREGKLKPEELQGGTFTISNLGMFGGDYF 341
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 686543092 408 YPIINYPQAAILTFESIVKKPVVINDMIAVRSMANICLSLDHRILDGVICGRFLQRVKDNLE 469
Cdd:PRK11856 342 TPIINPPEVAILGVGAIVERPVVVDGEIVVRKVMPLSLSFDHRVIDGADAARFLKALKELLE 403
PRK05704 PRK05704
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
8-469 3.03e-105

2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;


Pssm-ID: 235571 [Multi-domain]  Cd Length: 407  Bit Score: 319.47  E-value: 3.03e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092   8 TDVVMPQLAESLVSATIGKWLKQPGDRVEEYEPICELITDKVNAELPSTVEGTLVELLAEEGQVISVGEIIARIAvaapa 87
Cdd:PRK05704   3 VEIKVPTLPESVTEATIATWHKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGDTVTVGQVLGRID----- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092  88 gasagssapaaGTAPQAAAAAPAPGTPAAPVRPAAPSLSAADAPMRSRYSPAVQTLAAEHRIDLSAVPGTGLGGRITRKD 167
Cdd:PRK05704  78 -----------EGAAAGAAAAAAAAAAAAAAAPAQAQAAAAAEQSNDALSPAARKLAAENGLDASAVKGTGKGGRVTKED 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092 168 VLAYLENGGAAAGQtvpahpgaagagqagrqvPEALQQPALQVIQAEAQEQLEPVrnsglhlsespriptievegglgss 247
Cdd:PRK05704 147 VLAALAAAAAAPAA------------------PAAAAPAAAPAPLGARPEERVPM------------------------- 183
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092 248 seylidvTPIRNTIATRMRQSVSEIPHAWTMIEVDVTNLVVLRNKLKDEFKRKEGINLTYLAFMMKAVVSAIKDYPIMNS 327
Cdd:PRK05704 184 -------TRLRKTIAERLLEAQNTTAMLTTFNEVDMTPVMDLRKQYKDAFEKKHGVKLGFMSFFVKAVVEALKRYPEVNA 256
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092 328 VWAVDKIIVKRDINIALAVGTEDSVMTPVIKKADQKNIAGLAREIDELAQKTREGKLRLDDMQGGTFTVNNTGSFGSILS 407
Cdd:PRK05704 257 SIDGDDIVYHNYYDIGIAVGTPRGLVVPVLRDADQLSFAEIEKKIAELAKKARDGKLSIEELTGGTFTITNGGVFGSLMS 336
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 686543092 408 YPIINYPQAAILTFESIVKKPVVINDMIAVRSMANICLSLDHRILDGVICGRFLQRVKDNLE 469
Cdd:PRK05704 337 TPIINPPQSAILGMHKIKERPVAVNGQIVIRPMMYLALSYDHRIIDGKEAVGFLVTIKELLE 398
PRK11855 PRK11855
dihydrolipoamide acetyltransferase; Reviewed
8-469 7.13e-102

dihydrolipoamide acetyltransferase; Reviewed


Pssm-ID: 237000 [Multi-domain]  Cd Length: 547  Bit Score: 315.22  E-value: 7.13e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092   8 TDVVMPQLAEsLVSATIGKWLKQPGDRVEEYEPICELITDKVNAELPSTVEGTLVELLAEEGQVISVGEIIARIAVAAPA 87
Cdd:PRK11855 120 VEVKVPDIGE-ITEVEVIEWLVKVGDTVEEDQSLITVETDKATMEIPSPVAGVVKEIKVKVGDKVSVGSLLVVIEVAAAA 198
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092  88 GASAGSSAPAAGTAPQAAAAAPAPGTPAAPVRPAApslSAADAPMRSRY-SPAVQTLAAEHRIDLSAVPGTGLGGRITRK 166
Cdd:PRK11855 199 PAAAAAPAAAAPAAAAAAAPAPAPAAAAAPAAAAP---AAAAAPGKAPHaSPAVRRLARELGVDLSQVKGTGKKGRITKE 275
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092 167 DVLAYLEngGAAAGQTVPAhpgaagagqagrqvpealqqpALQVIQAEAqeqlepvrnsGLHLSESPRIP-----TIEVE 241
Cdd:PRK11855 276 DVQAFVK--GAMSAAAAAA---------------------AAAAAAGGG----------GLGLLPWPKVDfskfgEIETK 322
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092 242 gglgssseyliDVTPIRNTIATRMRQSVSEIPHAWTMIEVDVTNLVVLRNKLKDEFKrKEGINLTYLAFMMKAVVSAIKD 321
Cdd:PRK11855 323 -----------PLSRIKKISAANLHRSWVTIPHVTQFDEADITDLEALRKQLKKEAE-KAGVKLTMLPFFIKAVVAALKE 390
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092 322 YPIMNSV--WAVDKIIVKRDINIALAVGTEDSVMTPVIKKADQKNIAGLAREIDELAQKTREGKLRLDDMQGGTFTVNNT 399
Cdd:PRK11855 391 FPVFNASldEDGDELTYKKYFNIGFAVDTPNGLVVPVIKDVDKKSLLEIAREIAELAKKARDGKLKPDDMQGGCFTISSL 470
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092 400 GSFGSILSYPIINYPQAAILTFESIVKKPVVINDMIAVRSMANICLSLDHRILDGVICGRFLQRVKDNLE 469
Cdd:PRK11855 471 GGIGGTAFTPIINAPEVAILGVGKSQMKPVWDGKEFVPRLMLPLSLSYDHRVIDGATAARFTNYLKQLLA 540
sucB TIGR01347
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ...
8-469 9.91e-97

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: 297.42  E-value: 9.91e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092    8 TDVVMPQLAESLVSATIGKWLKQPGDRVEEYEPICELITDKVNAELPSTVEGTLVELLAEEGQVISVGEIIARIAVAAPA 87
Cdd:TIGR01347   1 IEIKVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAILEEGNDA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092   88 GASAGSSAPAAGTAPQAAAAAPapgtpaapvrpaapslSAADAPMRSRYSPAVQTLAAEHRIDLSAVPGTGLGGRITRKD 167
Cdd:TIGR01347  81 TAAPPAKSGEEKEETPAASAAA----------------APTAAANRPSLSPAARRLAKEHGIDLSAVPGTGVTGRVTKED 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092  168 VLAYLENGGAAagqtvpahpgaagagqagrqvpealQQPALQVIQAEAQEQLEPVRnsglhlsespRIPtievegglgss 247
Cdd:TIGR01347 145 IIKKTEAPASA-------------------------QPPAAAAAAAAPAAATRPEE----------RVK----------- 178
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092  248 seylidVTPIRNTIATRMRQSVSEIPHAWTMIEVDVTNLVVLRNKLKDEFKRKEGINLTYLAFMMKAVVSAIKDYPIMNS 327
Cdd:TIGR01347 179 ------MTRLRQRIAERLKEAQNSTAMLTTFNEVDMSAVMELRKRYKEEFEKKHGVKLGFMSFFVKAVVAALKRFPEVNA 252
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092  328 VWAVDKIIVKRDINIALAVGTEDSVMTPVIKKADQKNIAGLAREIDELAQKTREGKLRLDDMQGGTFTVNNTGSFGSILS 407
Cdd:TIGR01347 253 EIDGDDIVYKDYYDISVAVSTDRGLVVPVVRNADRMSFADIEKEIADLGKKARDGKLTLEDMTGGTFTITNGGVFGSLMS 332
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 686543092  408 YPIINYPQAAILTFESIVKKPVVINDMIAVRSMANICLSLDHRILDGVICGRFLQRVKDNLE 469
Cdd:TIGR01347 333 TPIINPPQSAILGMHGIKERPVAVNGQIEIRPMMYLALSYDHRLIDGKEAVTFLVTIKELLE 394
SucB_Actino TIGR02927
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model ...
8-469 2.38e-89

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: 283.83  E-value: 2.38e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092    8 TDVVMPQLAESLVSATIGKWLKQPGDRVEEYEPICELITDKVNAELPSTVEGTLVELLAEEGQVISVGEIIARIAVAAPA 87
Cdd:TIGR02927 127 TEVKMPELGESVTEGTVTSWLKAVGDTVEVDEPLLEVSTDKVDTEIPSPVAGTLLEIRAPEDDTVEVGTVLAIIGDANAA 206
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092   88 GASAGSSAPAA--------GTAPQAAAAAPAPGTPAAPVRPAAPSLSAADAPMRSRYS-----PAVQTLAAEHRIDLSAV 154
Cdd:TIGR02927 207 PAEPAEEEAPApseagsepAPDPAARAPHAAPDPPAPAPAPAKTAAPAAAAPVSSGDSgpyvtPLVRKLAKDKGVDLSTV 286
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092  155 PGTGLGGRITRKDVLAylenggAAAGQTVPAhpgaagagqagrqvpEALQQPALQVIQAEAQEQLEPVRNSGLHLSespr 234
Cdd:TIGR02927 287 KGTGVGGRIRKQDVLA------AAKAAEEAR---------------AAAAAPAAAAAPAAPAAAAKPAEPDTAKLR---- 341
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092  235 iptievegglGSSSEylidVTPIRNTIATRMRQSVSEIPHAWTMIEVDVTNLVVLRNKLKDEFKRKEGINLTYLAFMMKA 314
Cdd:TIGR02927 342 ----------GTTQK----MNRIRQITADKTIESLQTSAQLTQVHEVDMTRVAALRARAKNDFLEKNGVNLTFLPFFVQA 407
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092  315 VVSAIKDYPIMNSVWAVD-KIIVKRDI-NIALAVGTEDSVMTPVIKKADQKNIAGLAREIDELAQKTREGKLRLDDMQGG 392
Cdd:TIGR02927 408 VTEALKAHPNVNASYNAEtKEVTYHDVeHVGIAVDTPRGLLVPVIHNAGDLSLPGLAKAINDLAARARDNKLKPDELSGG 487
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092  393 TFTVNNTGSFGSILSYPIINYPQAAILTFESIVKKPVVI-----NDMIAVRSMANICLSLDHRILDGVICGRFLQRVKDN 467
Cdd:TIGR02927 488 TFTITNIGSGGALFDTPILNPPQAAILGTGAIVKRPRVIkdedgGESIAIRSVCYLPLTYDHRLVDGADAGRFLTTIKKR 567

                  ..
gi 686543092  468 LE 469
Cdd:TIGR02927 568 LE 569
2-oxoacid_dh pfam00198
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ...
265-469 3.23e-87

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: 265.95  E-value: 3.23e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092  265 MRQSVSEIPHAWTMIEVDVTNLVVLRNKLKDEFKrKEGINLTYLAFMMKAVVSAIKDYPIMNSVWAVDK--IIVKRDINI 342
Cdd:pfam00198   1 MTESKQTIPHFTLTDEVDVTELLALREELKEDAA-DEETKLTFLPFLVKAVALALKKFPELNASWDGEEgeIVYKKYVNI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092  343 ALAVGTEDSVMTPVIKKADQKNIAGLAREIDELAQKTREGKLRLDDMQGGTFTVNNTGSFGSILSYPIINYPQAAILTFE 422
Cdd:pfam00198  80 GIAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVG 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 686543092  423 SIVKKPVVINDMIAVRSMANICLSLDHRILDGVICGRFLQRVKDNLE 469
Cdd:pfam00198 160 RIRKRPVVVDGEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLE 206
aceF PRK11854
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
8-469 2.26e-80

pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated


Pssm-ID: 236999 [Multi-domain]  Cd Length: 633  Bit Score: 261.86  E-value: 2.26e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092   8 TDVVMPQLAESlvSATIGKWLKQPGDRVEEYEPICELITDKVNAELPSTVEGTLVELLAEEGQVISVGEIIARIAVAAPA 87
Cdd:PRK11854 207 KDVNVPDIGGD--EVEVTEVMVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVKTGSLIMRFEVEGAA 284
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092  88 GASAGSSAPAAGTAPQAAAAAPAPGTPAAPVRPAAPSLSAADAPmrsRYSPAVQTLAAEHRIDLSAVPGTGLGGRITRKD 167
Cdd:PRK11854 285 PAAAPAKQEAAAPAPAAAKAEAPAAAPAAKAEGKSEFAENDAYV---HATPLVRRLAREFGVNLAKVKGTGRKGRILKED 361
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092 168 VLAYlenggaaagqtvpahpgaagagqagrqVPEALQQpalqviqAEAQEQLEPVRNSGLHLsesPRIPTIEVegglgsS 247
Cdd:PRK11854 362 VQAY---------------------------VKDAVKR-------AEAAPAAAAAGGGGPGL---LPWPKVDF------S 398
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092 248 SEYLIDVTP---IRNTIATRMRQSVSEIPHAWTMIEVDVTNLVVLRN-KLKDEFKRKEGINLTYLAFMMKAVVSAIKDYP 323
Cdd:PRK11854 399 KFGEIEEVElgrIQKISGANLHRNWVMIPHVTQFDKADITELEAFRKqQNAEAEKRKLGVKITPLVFIMKAVAAALEQMP 478
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092 324 IMNSVWAVD--KIIVKRDINIALAVGTEDSVMTPVIKKADQKNIAGLAREIDELAQKTREGKLRLDDMQGGTFTVNNTGS 401
Cdd:PRK11854 479 RFNSSLSEDgqRLTLKKYVNIGIAVDTPNGLVVPVFKDVNKKGIIELSRELMDISKKARDGKLTAGDMQGGCFTISSIGG 558
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 686543092 402 FGSILSYPIINYPQAAILTFESIVKKPVVINDMIAVRSMANICLSLDHRILDGVICGRFLQRVKDNLE 469
Cdd:PRK11854 559 LGTTHFTPIVNAPEVAILGVSKSAMEPVWNGKEFAPRLMLPLSLSYDHRVIDGADGARFITIINDRLS 626
PTZ00144 PTZ00144
dihydrolipoamide succinyltransferase; Provisional
13-469 1.21e-74

dihydrolipoamide succinyltransferase; Provisional


Pssm-ID: 240289 [Multi-domain]  Cd Length: 418  Bit Score: 240.74  E-value: 1.21e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092  13 PQLAESLVSATIGKWLKQPGDRVEEYEPICELITDKVNAELPSTVEGTLVELLAEEGQVISVGeiiariavaapagasag 92
Cdd:PTZ00144  50 PTMGDSISEGTVVEWKKKVGDYVKEDEVICIIETDKVSVDIRAPASGVITKIFAEEGDTVEVG----------------- 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092  93 ssapaagtapqaaaaapapgtpaapvrpaapslsaadAPMrsryspavqtlaaeHRIDLSAVPGTGlggritrkdvlayl 172
Cdd:PTZ00144 113 -------------------------------------APL--------------SEIDTGGAPPAA-------------- 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092 173 engGAAAGQTVPAHPGAAGAGQAGRQVPEALQQPAlqviqAEAQEQLEPVRNSglhlSESPRIPTIEVEGGlgsSSEYLI 252
Cdd:PTZ00144 128 ---APAAAAAAKAEKTTPEKPKAAAPTPEPPAASK-----PTPPAAAKPPEPA----PAAKPPPTPVARAD---PRETRV 192
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092 253 DVTPIRNTIATRMRQSVSEIPHAWTMIEVDVTNLVVLRNKLKDEFKRKEGINLTYLAFMMKAVVSAIKDYPIMNSVWAVD 332
Cdd:PTZ00144 193 PMSRMRQRIAERLKASQNTCAMLTTFNECDMSALMELRKEYKDDFQKKHGVKLGFMSAFVKASTIALKKMPIVNAYIDGD 272
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092 333 KIIVKRDINIALAVGTEDSVMTPVIKKADQKNIAGLAREIDELAQKTREGKLRLDDMQGGTFTVNNTGSFGSILSYPIIN 412
Cdd:PTZ00144 273 EIVYRNYVDISVAVATPTGLVVPVIRNCENKSFAEIEKELADLAEKARNNKLTLEDMTGGTFTISNGGVFGSLMGTPIIN 352
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 686543092 413 YPQAAILTFESIVKKPVVINDMIAVRSMANICLSLDHRILDGVICGRFLQRVKDNLE 469
Cdd:PTZ00144 353 PPQSAILGMHAIKKRPVVVGNEIVIRPIMYLALTYDHRLIDGRDAVTFLKKIKDLIE 409
PDHac_trf_mito TIGR01349
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
10-469 1.62e-66

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: 220.05  E-value: 1.62e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092   10 VVMPQLAESLVSATIGKWLKQPGDRVEEYEPICELITDKVNAELPSTVEGTLVELLAEEG-QVISVGEIIARIAVAAPAG 88
Cdd:TIGR01349   2 ITMPALSPTMTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEGtKDVPVNKPIAVLVEEKEDV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092   89 ASAGSSAPAAGTAPQAAAAAPAPGTPAAPVRPAAPS-------------LSAADAPMRSRYSPAVQTLAAEHRIDLSAVP 155
Cdd:TIGR01349  82 ADAFKNYKLESSASPAPKPSEIAPTAPPSAPKPSPApqkqspepsspapLSDKESGDRIFASPLAKKLAKEKGIDLSAVA 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092  156 GTGLGGRITRKDVLAYLEnggaaagqtvpahpgaagagqagrQVPEALQQPALQVIQAEAQEqLEPVrnsglhlsespri 235
Cdd:TIGR01349 162 GSGPNGRIVKKDIESFVP------------------------QSPASANQQAAATTPATYPA-AAPV------------- 203
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092  236 ptievegglgSSSEY-LIDVTPIRNTIATRMRQSVSEIPHAWTMIEVDVTNLVVLRNKLKDEFkrKEGINLTYLAFMMKA 314
Cdd:TIGR01349 204 ----------STGSYeDVPLSNIRKIIAKRLLESKQTIPHYYVSIECNVDKLLALRKELNAMA--SEVYKLSVNDFIIKA 271
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092  315 VVSAIKDYPIMNSVWAVDKIIVKRDINIALAVGTEDSVMTPVIKKADQKNIAGLAREIDELAQKTREGKLRLDDMQGGTF 394
Cdd:TIGR01349 272 SALALREVPEANSSWTDNFIRRYKNVDISVAVATPDGLITPIVRNADAKGLSTISNEIKDLAKRARNNKLKPEEFQGGTF 351
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 686543092  395 TVNNTGSFGSILSYPIINYPQAAILTFESIVKKPVVINDMIAVRSMANIC---LSLDHRILDGVICGRFLQRVKDNLE 469
Cdd:TIGR01349 352 TISNLGMFGIKDFTAIINPPQACILAVGAVEDVAVVDNDEEKGFAVASIMsvtLSCDHRVIDGAVGAEFLKSFKKYLE 429
PRK11857 PRK11857
dihydrolipoamide acetyltransferase; Reviewed
137-469 3.59e-62

dihydrolipoamide acetyltransferase; Reviewed


Pssm-ID: 237002 [Multi-domain]  Cd Length: 306  Bit Score: 204.64  E-value: 3.59e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092 137 SPAVQTLAAEHRIDLSAVPGTGLGGRITRKDVLAYLENGGAAAGQTVPAhpgaagagqagrQVPeALQQPALQVIQAEAQ 216
Cdd:PRK11857   5 TPIARALAKKLGIDISLLKGSGRDGKILAEDVENFIKSLKSAPTPAEAA------------SVS-SAQQAAKTAAPAAAP 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092 217 EQLEPVRNSglhlsespriptievegglgssseylidVTPIRNTIATRMRQSVSEIPHAWTMIEVDVTNLVVLRNKLKDE 296
Cdd:PRK11857  72 PKLEGKREK----------------------------VAPIRKAIARAMTNSWSNVAYVNLVNEIDMTKLWDLRKSVKDP 123
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092 297 FKRKEGINLTYLAFMMKAVVSAIKDYPIMNSVW--AVDKIIVKRDINIALAVGTEDSVMTPVIKKADQKNIAGLAREIDE 374
Cdd:PRK11857 124 VLKTEGVKLTFLPFIAKAILIALKEFPIFAAKYdeATSELVYPDTLNLGIAVDTEAGLMVPVIKNAQKLSIVEIAKEISR 203
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092 375 LAQKTREGKLRLDDMQGGTFTVNNTGSFGSILSYPIINYPQAAILTFESIVKKPVVINDMIAVRSMANICLSLDHRILDG 454
Cdd:PRK11857 204 LAKAARERKIKPDEMKGGSFTITNYGSVGSLYGVPVINYPELAIAGVGAIIDKAIVKNGQIVAGKVMHLTVAADHRWIDG 283
                        330
                 ....*....|....*
gi 686543092 455 VICGRFLQRVKDNLE 469
Cdd:PRK11857 284 ATIGRFASRVKELLE 298
PLN02226 PLN02226
2-oxoglutarate dehydrogenase E2 component
2-469 1.66e-61

2-oxoglutarate dehydrogenase E2 component


Pssm-ID: 177871 [Multi-domain]  Cd Length: 463  Bit Score: 207.69  E-value: 1.66e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092   2 SDNTKLTDVVMPQLAESLVSATIGKWLKQPGDRVEEYEPICELITDKVNAELPSTVEGTLVELLAEEGQVISVGEIIARI 81
Cdd:PLN02226  86 SESGDTVEAVVPHMGESITDGTLATFLKKPGERVQADEAIAQIETDKVTIDIASPASGVIQEFLVKEGDTVEPGTKVAII 165
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092  82 AvaapagasagssapaagtapqaaaaapapgtpaapvrpaapslSAADAPmrSRYSPAvqtlaaehridlSAVPGTGlgg 161
Cdd:PLN02226 166 S-------------------------------------------KSEDAA--SQVTPS------------QKIPETT--- 185
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092 162 ritrkdvlaylenggaaagQTVPAHPGAAGAGQAGRQVPEAlQQPalqviqaEAQEQLEPVRNSglhlSESPRIPTIEve 241
Cdd:PLN02226 186 -------------------DPKPSPPAEDKQKPKVESAPVA-EKP-------KAPSSPPPPKQS----AKEPQLPPKE-- 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092 242 gglgssSEYLIDVTPIRNTIATRMRQSVSEIPHAWTMIEVDVTNLVVLRNKLKDEFKRKEGINLTYLAFMMKAVVSAIKD 321
Cdd:PLN02226 233 ------RERRVPMTRLRKRVATRLKDSQNTFALLTTFNEVDMTNLMKLRSQYKDAFYEKHGVKLGLMSGFIKAAVSALQH 306
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092 322 YPIMNSVWAVDKIIVKRDINIALAVGTEDSVMTPVIKKADQKNIAGLAREIDELAQKTREGKLRLDDMQGGTFTVNNTGS 401
Cdd:PLN02226 307 QPVVNAVIDGDDIIYRDYVDISIAVGTSKGLVVPVIRGADKMNFAEIEKTINGLAKKANEGTISIDEMAGGSFTVSNGGV 386
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 686543092 402 FGSILSYPIINYPQAAILTFESIVKKPVVINDMIAVRSMANICLSLDHRILDGVICGRFLQRVKDNLE 469
Cdd:PLN02226 387 YGSLISTPIINPPQSAILGMHSIVSRPMVVGGSVVPRPMMYVALTYDHRLIDGREAVYFLRRVKDVVE 454
PLN02744 PLN02744
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
12-477 3.88e-55

dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex


Pssm-ID: 215397 [Multi-domain]  Cd Length: 539  Bit Score: 192.76  E-value: 3.88e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092  12 MPQLAESLVSATIGKWLKQPGDRVEEYEPICELITDKVNAELPSTVEGTLVELLAEEG-QVISVGEIIArIAVAA----- 85
Cdd:PLN02744 117 MPSLSPTMTEGNIARWLKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVKGDGaKEIKVGEVIA-ITVEEeedig 195
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092  86 -----PAGASAGSSAPAAGTAPQAAAAAPAPGTPAAPVRPAAPSLSAADAPMRSRYSPAVQTLAAEHRIDLSAVPGTGLG 160
Cdd:PLN02744 196 kfkdyKPSSSAAPAAPKAKPSPPPPKEEEVEKPASSPEPKASKPSAPPSSGDRIFASPLARKLAEDNNVPLSSIKGTGPD 275
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092 161 GRITRKDVLAYLENGGAAAGQTVPAHPGAagagqagrqvpealqqPALQVIQaeaqeqlepvrnsglhlsesprIPTiev 240
Cdd:PLN02744 276 GRIVKADIEDYLASGGKGATAPPSTDSKA----------------PALDYTD----------------------IPN--- 314
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092 241 egglgssseylidvTPIRNTIATRMRQSVSEIPHAWTMIEVDVTNLVVLRNKLKDEFKRKEGINLTYLAFMMKAVVSAIK 320
Cdd:PLN02744 315 --------------TQIRKVTASRLLQSKQTIPHYYLTVDTRVDKLMALRSQLNSLQEASGGKKISVNDLVIKAAALALR 380
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092 321 DYPIMNSVWAVDKIIVKRDINIALAVGTEDSVMTPVIKKADQKNIAGLAREIDELAQKTREGKLRLDDMQGGTFTVNNTG 400
Cdd:PLN02744 381 KVPQCNSSWTDDYIRQYHNVNINVAVQTENGLYVPVVKDADKKGLSTIAEEVKQLAQKARENSLKPEDYEGGTFTVSNLG 460
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092 401 S-FGSILSYPIINYPQAAILTFESIVKK--PVVINDMIAVRSMANICLSLDHRILDGVICGRFLQRVKDNLEgyTPDTKL 477
Cdd:PLN02744 461 GpFGIKQFCAIINPPQSAILAVGSAEKRviPGSGPDQYNFASFMSVTLSCDHRVIDGAIGAEWLKAFKGYIE--NPESML 538
PDHac_trf_long TIGR01348
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
32-469 1.58e-53

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: 188.55  E-value: 1.58e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092   32 GDRVEEYEPICELITDKVNAELPSTVEGTLVELLAEEGQVISVGEIIARIAVAAPAGASAGSSAPAAGTAPQAAAAAPAP 111
Cdd:TIGR01348 140 GDTVSADQSLITLESDKASMEVPAPASGVVKSVKVKVGDSVPTGDLILTLSVAGSTPATAPAPASAQPAAQSPAATQPEP 219
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092  112 GTPAAPVRPAAPSLSAADAPMRSRY---SPAVQTLAAEHRIDLSAVPGTGLGGRITRKDVLAYLENggaaagqtvpahpg 188
Cdd:TIGR01348 220 AAAPAAAKAQAPAPQQAGTQNPAKVdhaAPAVRRLAREFGVDLSAVKGTGIKGRILREDVQRFVKE-------------- 285
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092  189 aagagqagrqvpealqqpalQVIQAEAQeqlePVRNSGLHLSESPrIPTIEVEGgLGSSSEylIDVTPIRNTIATRMRQS 268
Cdd:TIGR01348 286 --------------------PSVRAQAA----AASAAGGAPGALP-WPNVDFSK-FGEVEE--VDMSRIRKISGANLTRN 337
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092  269 VSEIPHAWTMIEVDVTNLVVLRNKLKDEfKRKEGINLTYLAFMMKAVVSAIKDYPIMNSVWAVD--KIIVKRDINIALAV 346
Cdd:TIGR01348 338 WTMIPHVTHFDKADITEMEAFRKQQNAA-VEKEGVKLTVLHILMKAVAAALKKFPKFNASLDLGgeQLILKKYVNIGVAV 416
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092  347 GTEDSVMTPVIKKADQKNIAGLAREIDELAQKTREGKLRLDDMQGGTFTVNNTGSFGSILSYPIINYPQAAILTFESIVK 426
Cdd:TIGR01348 417 DTPNGLLVPVIKDVDRKGITELALELSDLAKKARDGKLTPDEMQGACFTISSLGGIGGTAFTPIVNAPEVAILGVSKSGM 496
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|...
gi 686543092  427 KPVVINDMIAVRSMANICLSLDHRILDGVICGRFLQRVKDNLE 469
Cdd:TIGR01348 497 EPVWNGKEFEPRLMLPLSLSYDHRVIDGADAARFTTYICESLA 539
PLN02528 PLN02528
2-oxoisovalerate dehydrogenase E2 component
10-469 1.55e-51

2-oxoisovalerate dehydrogenase E2 component


Pssm-ID: 215289 [Multi-domain]  Cd Length: 416  Bit Score: 179.92  E-value: 1.55e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092  10 VVMPQLAESLVSATIGKWLKQPGDRVEEYEPICELITDKVNAELPSTVEGTLVELLAEEGQVISVGEIIARIAVAAPAGA 89
Cdd:PLN02528   1 VPLAQTGEGIAECELLRWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGKVAQINFSPGDIVKVGETLLKIMVEDSQHL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092  90 SAGSSAPAAGTAPQAAAAAPAPGTPaapvrpaapSLSAADApmrsrySPAVQTLAAEHRIDLSAVPGTGLGGRITRKDVL 169
Cdd:PLN02528  81 RSDSLLLPTDSSNIVSLAESDERGS---------NLSGVLS------TPAVRHLAKQYGIDLNDILGTGKDGRVLKEDVL 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092 170 AYLenggaaagqtvpahpgaagagqagrqvpealqqpalqvIQAEAQEQlepvrNSGLHLSESPRIPTIEVEGGLGSSSE 249
Cdd:PLN02528 146 KYA--------------------------------------AQKGVVKD-----SSSAEEATIAEQEEFSTSVSTPTEQS 182
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092 250 YLIDVTPIRN---TIATRMRQSVSeIPHAWTMIEVDVTNLVVLRNKLKDEfKRKEGINLTYLAFMMKAVVSAIKDYPIMN 326
Cdd:PLN02528 183 YEDKTIPLRGfqrAMVKTMTAAAK-VPHFHYVEEINVDALVELKASFQEN-NTDPTVKHTFLPFLIKSLSMALSKYPLLN 260
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092 327 SVWAVD--KIIVKRDINIALAVGTEDSVMTPVIKKADQKNIAGLAREIDELAQKTREGKLRLDDMQGGTFTVNNTGSFGS 404
Cdd:PLN02528 261 SCFNEEtsEIRLKGSHNIGVAMATEHGLVVPNIKNVQSLSLLEITKELSRLQHLAAENKLNPEDITGGTITLSNIGAIGG 340
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 686543092 405 ILSYPIINYPQAAILTFESIVKKPVVIND--MIAVRSMaNICLSLDHRILDGVICGRFLQRVKDNLE 469
Cdd:PLN02528 341 KFGSPVLNLPEVAIIALGRIQKVPRFVDDgnVYPASIM-TVTIGADHRVLDGATVARFCNEWKSYVE 406
PRK14843 PRK14843
dihydrolipoamide acetyltransferase; Provisional
135-469 1.43e-45

dihydrolipoamide acetyltransferase; Provisional


Pssm-ID: 184847 [Multi-domain]  Cd Length: 347  Bit Score: 162.38  E-value: 1.43e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092 135 RYSPAVQTLAAEHRIDLSAVPGTGLGGRITRKDVLAYLenggaaagqtvpAHPGAAGAGQAGRQVPEALQQPAlqviQAE 214
Cdd:PRK14843  50 RISPLAKRIALEHNIAWQEIQGTGHRGKIMKKDVLALL------------PENIENDSIKSPAQIEKVEEVPD----NVT 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092 215 AQEQLEpvrnsglhlsespRIPtievegglgssseylidVTPIRNTIATRMRQSVSEIPHAWTMIEVDVTNLVVLRNKLK 294
Cdd:PRK14843 114 PYGEIE-------------RIP-----------------MTPMRKVIAQRMVESYLTAPTFTLNYEVDMTEMLALRKKVL 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092 295 DEFKRKEGINLTYLAFMMKAVVSAIKDYPIMNSVWAVD--KIIVKRDINIALAVGTEDSVMTPVIKKADQKNIAGLAREI 372
Cdd:PRK14843 164 EPIMEATGKKTTVTDLLSLAVVKTLMKHPYINASLTEDgkTIITHNYVNLAMAVGMDNGLMTPVVYNAEKMSLSELVVAF 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092 373 DELAQKTREGKLRLDDMQGGTFTVNNTGSFGSILSYPIINYPQAAILTFESIVKKPVVINDMIAVRSMANICLSLDHRIL 452
Cdd:PRK14843 244 KDVIGRTLDGKLAPSELQNSTFTISNLGMFGVQSFGPIINQPNSAILGVSSTIEKPVVVNGEIVIRPIMSLGLTIDHRVV 323
                        330
                 ....*....|....*..
gi 686543092 453 DGVICGRFLQRVKDNLE 469
Cdd:PRK14843 324 DGMAGAKFMKDLKELIE 340
AceF COG0508
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ...
8-82 3.39e-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: 103.99  E-value: 3.39e-27
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 686543092   8 TDVVMPQLAESLVSATIGKWLKQPGDRVEEYEPICELITDKVNAELPSTVEGTLVELLAEEGQVISVGEIIARIA 82
Cdd:COG0508    3 IEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVIA 77
lipoyl_domain cd06849
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ...
8-81 4.10e-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: 100.94  E-value: 4.10e-26
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 686543092   8 TDVVMPQLAESLVSATIGKWLKQPGDRVEEYEPICELITDKVNAELPSTVEGTLVELLAEEGQVISVGEIIARI 81
Cdd:cd06849    1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
Biotin_lipoyl pfam00364
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ...
8-81 3.61e-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: 73.02  E-value: 3.61e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 686543092    8 TDVVMPQLAESlVSATIGKWLKQPGDRVEEYEPICELITDKVNAELPSTVEGTLVELLAEEGQVISVGEIIARI 81
Cdd:pfam00364   1 TEIKSPMIGES-VREGVVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
kgd PRK12270
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ...
175-470 4.58e-16

multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;


Pssm-ID: 237030 [Multi-domain]  Cd Length: 1228  Bit Score: 81.09  E-value: 4.58e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092  175 GGAAAGQTVPAHPGAAGAGQAGRQVPEALQQPALQVIQAEAQEQLEPVRNSGLHLSESPRIPTIEVEGGLGSsseyliDV 254
Cdd:PRK12270   44 PTAAAAAAAAAASAPAAAPAAKAPAAPAPAPPAAAAPAAPPKPAAAAAAAAAPAAPPAAAAAAAPAAAAVED------EV 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092  255 TPIR---NTIATRMRQSVsEIPHAWTMIEVDVTNLVVLRNKLKDEFKRKEG--INLTYL-AFmmkAVVSAIKDYPIMNSV 328
Cdd:PRK12270  118 TPLRgaaAAVAKNMDASL-EVPTATSVRAVPAKLLIDNRIVINNHLKRTRGgkVSFTHLiGY---ALVQALKAFPNMNRH 193
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092  329 WAVDK---IIVKR-DINIALAV------GTEdSVMTPVIKKADQKNIAGLAREIDELAQKTREGKLRLDDMQGGTFTVNN 398
Cdd:PRK12270  194 YAEVDgkpTLVTPaHVNLGLAIdlpkkdGSR-QLVVPAIKGAETMDFAQFWAAYEDIVRRARDGKLTADDFQGTTISLTN 272
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092  399 TGSFGSILSYP--------II-----NYP---QAAiltfesivkKPVVINDMiAVRSMANICLSLDHRILDGVICGRFLQ 462
Cdd:PRK12270  273 PGGIGTVHSVPrlmkgqgaIIgvgamEYPaefQGA---------SEERLAEL-GISKVMTLTSTYDHRIIQGAESGEFLR 342

                  ....*...
gi 686543092  463 RVKDNLEG 470
Cdd:PRK12270  343 TIHQLLLG 350
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
8-82 1.21e-13

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 72.28  E-value: 1.21e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 686543092   8 TDVVMPQLAESLVSATIGKWLKQPGDRVEEYEPICELITDKVNAELPSTVEGTLVELLAEEGQVISVGEIIARIA 82
Cdd:PRK14875   3 TPITMPKWGLSMTEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGETLPVGALLAVVA 77
E3_binding pfam02817
e3 binding domain; This family represents a small domain of the E2 subunit of 2-oxo-acid ...
135-169 3.29e-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: 57.70  E-value: 3.29e-11
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 686543092  135 RYSPAVQTLAAEHRIDLSAVPGTGLGGRITRKDVL 169
Cdd:pfam02817   2 LASPAARKLARELGIDLSDVKGTGPGGRITKEDVE 36
Biotinyl_lipoyl_domains cd06663
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ...
9-81 6.41e-10

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: 55.14  E-value: 6.41e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 686543092   9 DVVMPQLAESLVSATIGKWLKQPGDRVEEYEPICELITDKVNAELPSTVEGTLVELLAEEGQVISVGEIIARI 81
Cdd:cd06663    1 TILIPDLAQHLGDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKVEGDTPLVKI 73
PRK11892 PRK11892
pyruvate dehydrogenase subunit beta; Provisional
8-82 3.17e-08

pyruvate dehydrogenase subunit beta; Provisional


Pssm-ID: 237011 [Multi-domain]  Cd Length: 464  Bit Score: 55.69  E-value: 3.17e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 686543092   8 TDVVMPQLAESLVSATIGKWLKQPGDRVEEYEPICELITDKVNAELPSTVEGTLVELLAEEG-QVISVGEIIARIA 82
Cdd:PRK11892   3 IEILMPALSPTMEEGTLAKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKILVPEGtEGVKVNTPIAVLL 78
biotinyl_domain cd06850
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ...
20-81 4.95e-07

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: 47.03  E-value: 4.95e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 686543092  20 VSATIGKWLKQPGDRVEEYEPICELITDKVNAELPSTVEGTLVELLAEEGQVISVGEIIARI 81
Cdd:cd06850    6 MPGTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
PRK09282 PRK09282
pyruvate carboxylase subunit B; Validated
23-81 1.83e-04

pyruvate carboxylase subunit B; Validated


Pssm-ID: 236449 [Multi-domain]  Cd Length: 592  Bit Score: 44.06  E-value: 1.83e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 686543092  23 TIGKWLKQPGDRVEEYEPICELITDKVNAELPSTVEGTLVELLAEEGQVISVGEIIARI 81
Cdd:PRK09282 532 TVVKVKVKEGDKVKAGDTVLVLEAMKMENEIQAPVDGTVKEILVKEGDRVNPGDVLMEI 590
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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