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Conserved domains on  [gi|2481688347|ref|XP_054901164|]
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lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial [Poeciliopsis prolifica]

Protein Classification

lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex( domain architecture ID 1003376)

lipoamide acyltransferase component (E2) of branched-chain alpha-keto acid dehydrogenase complex that catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2)

CATH:  3.30.559.10
EC:  2.3.1.168
Gene Ontology:  GO:0043754|GO:0016407|GO:0031625|GO:0031405|GO:0009083

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN02528 super family cl33511
2-oxoisovalerate dehydrogenase E2 component
 67-490 1.32e-167

2-oxoisovalerate dehydrogenase E2 component


The actual alignment was detected with superfamily member PLN02528:

Pssm-ID: 215289 [Multi-domain]  Cd Length: 416  Bit Score: 479.22  E-value: 1.32e-167
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2481688347  67 FKLSDIGEGIMEVTVKEWYVKEGDRVSQFDSICEVQSDKASVTITSRYDGVIRRLYYEADATALVGKPLVDIETESA--- 143
Cdd:PLN02528    1 VPLAQTGEGIAECELLRWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGKVAQINFSPGDIVKVGETLLKIMVEDSqhl 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2481688347 144 ---SELSQEDVVETPAMAREEHTHQEIKGhkTQATPAVRRLAMENNIKLSEVVGTGKDGRILKEDILNFLAkQTGAILPP 220
Cdd:PLN02528   81 rsdSLLLPTDSSNIVSLAESDERGSNLSG--VLSTPAVRHLAKQYGIDLNDILGTGKDGRVLKEDVLKYAA-QKGVVKDS 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2481688347 221 APLfqeiqtpgpaptppLSAPAGVRPPPATPRPDFTG---KDVTEPLKGFHKAMVKTMTAALKIPHFGYCDEVDLSRLVL 297
Cdd:PLN02528  158 SSA--------------EEATIAEQEEFSTSVSTPTEqsyEDKTIPLRGFQRAMVKTMTAAAKVPHFHYVEEINVDALVE 223

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2481688347 298 LRSELKPVAERRGVRLSYLPFFIKAASLSLLRFPILNSTLDESCQNITFKASHNIGVAMDTSLGLLVPSVKSVQLLSVFQ 377
Cdd:PLN02528  224 LKASFQENNTDPTVKHTFLPFLIKSLSMALSKYPLLNSCFNEETSEIRLKGSHNIGVAMATEHGLVVPNIKNVQSLSLLE 303

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2481688347 378 VAQELTRLQTLGAAGQLGTAELSGGTFTLSNIGSIGGTYAKPVILPPEVAIGALGKIQVLPRFGPDGQVKAAHIMKVSWS 457
Cdd:PLN02528  304 ITKELSRLQHLAAENKLNPEDITGGTITLSNIGAIGGKFGSPVLNLPEVAIIALGRIQKVPRFVDDGNVYPASIMTVTIG 383

                         410       420       430
                  ....*....|....*....|....*....|...
gi 2481688347 458 ADHRLIDGATMCRFSNLWREYLENPASMLLDLK 490
Cdd:PLN02528  384 ADHRVLDGATVARFCNEWKSYVEKPELLMLHMR 416
 
Name Accession Description Interval E-value
PLN02528 PLN02528
2-oxoisovalerate dehydrogenase E2 component
 67-490 1.32e-167

2-oxoisovalerate dehydrogenase E2 component


Pssm-ID: 215289 [Multi-domain]  Cd Length: 416  Bit Score: 479.22  E-value: 1.32e-167
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2481688347  67 FKLSDIGEGIMEVTVKEWYVKEGDRVSQFDSICEVQSDKASVTITSRYDGVIRRLYYEADATALVGKPLVDIETESA--- 143
Cdd:PLN02528    1 VPLAQTGEGIAECELLRWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGKVAQINFSPGDIVKVGETLLKIMVEDSqhl 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2481688347 144 ---SELSQEDVVETPAMAREEHTHQEIKGhkTQATPAVRRLAMENNIKLSEVVGTGKDGRILKEDILNFLAkQTGAILPP 220
Cdd:PLN02528   81 rsdSLLLPTDSSNIVSLAESDERGSNLSG--VLSTPAVRHLAKQYGIDLNDILGTGKDGRVLKEDVLKYAA-QKGVVKDS 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2481688347 221 APLfqeiqtpgpaptppLSAPAGVRPPPATPRPDFTG---KDVTEPLKGFHKAMVKTMTAALKIPHFGYCDEVDLSRLVL 297
Cdd:PLN02528  158 SSA--------------EEATIAEQEEFSTSVSTPTEqsyEDKTIPLRGFQRAMVKTMTAAAKVPHFHYVEEINVDALVE 223

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2481688347 298 LRSELKPVAERRGVRLSYLPFFIKAASLSLLRFPILNSTLDESCQNITFKASHNIGVAMDTSLGLLVPSVKSVQLLSVFQ 377
Cdd:PLN02528  224 LKASFQENNTDPTVKHTFLPFLIKSLSMALSKYPLLNSCFNEETSEIRLKGSHNIGVAMATEHGLVVPNIKNVQSLSLLE 303

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2481688347 378 VAQELTRLQTLGAAGQLGTAELSGGTFTLSNIGSIGGTYAKPVILPPEVAIGALGKIQVLPRFGPDGQVKAAHIMKVSWS 457
Cdd:PLN02528  304 ITKELSRLQHLAAENKLNPEDITGGTITLSNIGAIGGKFGSPVLNLPEVAIIALGRIQKVPRFVDDGNVYPASIMTVTIG 383

                         410       420       430
                  ....*....|....*....|....*....|...
gi 2481688347 458 ADHRLIDGATMCRFSNLWREYLENPASMLLDLK 490
Cdd:PLN02528  384 ADHRVLDGATVARFCNEWKSYVEKPELLMLHMR 416
2-oxoacid_dh pfam00198
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ...
 275-486 1.71e-90

2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to three copies of a lipoyl binding domain followed by the catalytic domain.


Pssm-ID: 425518 [Multi-domain]  Cd Length: 212  Bit Score: 274.81  E-value: 1.71e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2481688347 275 MTAAL-KIPHFGYCDEVDLSRLVLLRSELKPVAERRGVRLSYLPFFIKAASLSLLRFPILNSTLDESCQNITFKASHNIG 353
Cdd:pfam00198   1 MTESKqTIPHFTLTDEVDVTELLALREELKEDAADEETKLTFLPFLVKAVALALKKFPELNASWDGEEGEIVYKKYVNIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2481688347 354 VAMDTSLGLLVPSVKSVQLLSVFQVAQELTRLQTLGAAGQLGTAELSGGTFTLSNIGSIGGTYAKPVILPPEVAIGALGK 433
Cdd:pfam00198  81 IAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVGR 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2481688347 434 IQVLPRFgPDGQVKAAHIMKVSWSADHRLIDGATMCRFSNLWREYLENPASML 486
Cdd:pfam00198 161 IRKRPVV-VDGEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELLL 212
sucB TIGR01347
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ...
 65-489 6.48e-72

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: 233.47  E-value: 6.48e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2481688347  65 VQFKLSDIGEGIMEVTVKEWYVKEGDRVSQFDSICEVQSDKASVTITSRYDGVIRRLYYEADATALVGKPLVDIE----- 139
Cdd:TIGR01347   1 IEIKVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAILEegnda 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2481688347 140 TESASELSQEDVVETPAMAREehTHQEIKGHKTQATPAVRRLAMENNIKLSEVVGTGKDGRILKEDILNFLAKqtgailp 219
Cdd:TIGR01347  81 TAAPPAKSGEEKEETPAASAA--AAPTAAANRPSLSPAARRLAKEHGIDLSAVPGTGVTGRVTKEDIIKKTEA------- 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2481688347 220 paplfqeiqtpgPAPTPPLSAPAGVRPPPATPRPDFTGK------DVTEPLKgfhkaMVKTMTAALKIPHfgycdEVDLS 293
Cdd:TIGR01347 152 ------------PASAQPPAAAAAAAAPAAATRPEERVKmtrlrqRIAERLK-----EAQNSTAMLTTFN-----EVDMS 209

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2481688347 294 RLVLLRSELKPVAERR-GVRLSYLPFFIKAASLSLLRFPILNSTLDEscQNITFKASHNIGVAMDTSLGLLVPSVKSVQL 372
Cdd:TIGR01347 210 AVMELRKRYKEEFEKKhGVKLGFMSFFVKAVVAALKRFPEVNAEIDG--DDIVYKDYYDISVAVSTDRGLVVPVVRNADR 287

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2481688347 373 LSVFQVAQELTRLQTLGAAGQLGTAELSGGTFTLSNIGSIGGTYAKPVILPPEVAIGALGKIQVLPrFGPDGQVKAAHIM 452
Cdd:TIGR01347 288 MSFADIEKEIADLGKKARDGKLTLEDMTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHGIKERP-VAVNGQIEIRPMM 366

                         410       420       430
                  ....*....|....*....|....*....|....*..
gi 2481688347 453 KVSWSADHRLIDGATMCRFSNLWREYLENPASMLLDL 489
Cdd:TIGR01347 367 YLALSYDHRLIDGKEAVTFLVTIKELLEDPRRLLLDL 403
lipoyl_domain cd06849
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ...
 65-138 3.44e-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: 101.33  E-value: 3.44e-26
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2481688347  65 VQFKLSDIGEGIMEVTVKEWYVKEGDRVSQFDSICEVQSDKASVTITSRYDGVIRRLYYEADATALVGKPLVDI 138
Cdd:cd06849     1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
AceF COG0508
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ...
 65-138 9.90e-22

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: 88.97  E-value: 9.90e-22
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2481688347  65 VQFKLSDIGEGIMEVTVKEWYVKEGDRVSQFDSICEVQSDKASVTITSRYDGVIRRLYYEADATALVGKPLVDI 138
Cdd:COG0508     3 IEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
 
Name Accession Description Interval E-value
PLN02528 PLN02528
2-oxoisovalerate dehydrogenase E2 component
 67-490 1.32e-167

2-oxoisovalerate dehydrogenase E2 component


Pssm-ID: 215289 [Multi-domain]  Cd Length: 416  Bit Score: 479.22  E-value: 1.32e-167
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2481688347  67 FKLSDIGEGIMEVTVKEWYVKEGDRVSQFDSICEVQSDKASVTITSRYDGVIRRLYYEADATALVGKPLVDIETESA--- 143
Cdd:PLN02528    1 VPLAQTGEGIAECELLRWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGKVAQINFSPGDIVKVGETLLKIMVEDSqhl 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2481688347 144 ---SELSQEDVVETPAMAREEHTHQEIKGhkTQATPAVRRLAMENNIKLSEVVGTGKDGRILKEDILNFLAkQTGAILPP 220
Cdd:PLN02528   81 rsdSLLLPTDSSNIVSLAESDERGSNLSG--VLSTPAVRHLAKQYGIDLNDILGTGKDGRVLKEDVLKYAA-QKGVVKDS 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2481688347 221 APLfqeiqtpgpaptppLSAPAGVRPPPATPRPDFTG---KDVTEPLKGFHKAMVKTMTAALKIPHFGYCDEVDLSRLVL 297
Cdd:PLN02528  158 SSA--------------EEATIAEQEEFSTSVSTPTEqsyEDKTIPLRGFQRAMVKTMTAAAKVPHFHYVEEINVDALVE 223

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2481688347 298 LRSELKPVAERRGVRLSYLPFFIKAASLSLLRFPILNSTLDESCQNITFKASHNIGVAMDTSLGLLVPSVKSVQLLSVFQ 377
Cdd:PLN02528  224 LKASFQENNTDPTVKHTFLPFLIKSLSMALSKYPLLNSCFNEETSEIRLKGSHNIGVAMATEHGLVVPNIKNVQSLSLLE 303

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2481688347 378 VAQELTRLQTLGAAGQLGTAELSGGTFTLSNIGSIGGTYAKPVILPPEVAIGALGKIQVLPRFGPDGQVKAAHIMKVSWS 457
Cdd:PLN02528  304 ITKELSRLQHLAAENKLNPEDITGGTITLSNIGAIGGKFGSPVLNLPEVAIIALGRIQKVPRFVDDGNVYPASIMTVTIG 383

                         410       420       430
                  ....*....|....*....|....*....|...
gi 2481688347 458 ADHRLIDGATMCRFSNLWREYLENPASMLLDLK 490
Cdd:PLN02528  384 ADHRVLDGATVARFCNEWKSYVEKPELLMLHMR 416
PRK11855 PRK11855
dihydrolipoamide acetyltransferase; Reviewed
 64-487 4.27e-152

dihydrolipoamide acetyltransferase; Reviewed


Pssm-ID: 237000 [Multi-domain]  Cd Length: 547  Bit Score: 444.65  E-value: 4.27e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2481688347  64 VVQFKLSDIGEgIMEVTVKEWYVKEGDRVSQFDSICEVQSDKASVTITSRYDGVIRRLYYEADATALVGKPLVDIETE-- 141
Cdd:PRK11855  119 VVEVKVPDIGE-ITEVEVIEWLVKVGDTVEEDQSLITVETDKATMEIPSPVAGVVKEIKVKVGDKVSVGSLLVVIEVAaa 197

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2481688347 142 -------SASELSQEDVVETPAMAREEHTHQEIK--------GHKTQATPAVRRLAMENNIKLSEVVGTGKDGRILKEDI 206
Cdd:PRK11855  198 apaaaaaPAAAAPAAAAAAAPAPAPAAAAAPAAAapaaaaapGKAPHASPAVRRLARELGVDLSQVKGTGKKGRITKEDV 277

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2481688347 207 LNFL-AKQTGAILPPAPlfqeiqtPGPAPTPPLSAPAgvrpppaTPRPDFT--GKDVTEPLKGFHKAMVKTMTAAL-KIP 282
Cdd:PRK11855  278 QAFVkGAMSAAAAAAAA-------AAAAGGGGLGLLP-------WPKVDFSkfGEIETKPLSRIKKISAANLHRSWvTIP 343

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2481688347 283 HFGYCDEVDLSRLVLLRSELKPVAERRGVRLSYLPFFIKAASLSLLRFPILNSTLDESCQNITFKASHNIGVAMDTSLGL 362
Cdd:PRK11855  344 HVTQFDEADITDLEALRKQLKKEAEKAGVKLTMLPFFIKAVVAALKEFPVFNASLDEDGDELTYKKYFNIGFAVDTPNGL 423

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2481688347 363 LVPSVKSVQLLSVFQVAQELTRLQTLGAAGQLGTAELSGGTFTLSNIGSIGGTYAKPVILPPEVAIGALGKIQVLPRFGp 442
Cdd:PRK11855  424 VVPVIKDVDKKSLLEIAREIAELAKKARDGKLKPDDMQGGCFTISSLGGIGGTAFTPIINAPEVAILGVGKSQMKPVWD- 502

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*
gi 2481688347 443 DGQVKAAHIMKVSWSADHRLIDGATMCRFSNLWREYLENPASMLL 487
Cdd:PRK11855  503 GKEFVPRLMLPLSLSYDHRVIDGATAARFTNYLKQLLADPRRMLL 547
PRK11856 PRK11856
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
 64-488 1.17e-119

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


Pssm-ID: 237001 [Multi-domain]  Cd Length: 411  Bit Score: 356.79  E-value: 1.17e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2481688347  64 VVQFKLSDIGEGIMEVTVKEWYVKEGDRVSQFDSICEVQSDKASVTITSRYDGVIRRLYYEADATALVGKPLVDIETE-- 141
Cdd:PRK11856    2 MFEFKMPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDVVPVGSVIAVIEEEge 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2481688347 142 -------------SASELSQEDVVETPAMAREEHTHQEIKGHKTQATPAVRRLAMENNIKLSEVVGTGKDGRILKEDILN 208
Cdd:PRK11856   82 aeaaaaaeaapeaPAPEPAPAAAAAAAAAPAAAAAPAAPAAAAAKASPAVRKLARELGVDLSTVKGSGPGGRITKEDVEA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2481688347 209 FLAKQtgailppaplfqeiQTPGPAPTPPLSAPAGVRPPPATprpdftgkdvTEPLKGFHKAMVKTMTAA-LKIPHFGYC 287
Cdd:PRK11856  162 AAAAA--------------APAAAAAAAAAAAPPAAAAEGEE----------RVPLSGMRKAIAKRMVESkREIPHFTLT 217

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2481688347 288 DEVDLSRLVLLRSELKPVAerrgVRLSYLPFFIKAASLSLLRFPILNSTLDEscQNITFKASHNIGVAMDTSLGLLVPSV 367
Cdd:PRK11856  218 DEVDVTALLALRKQLKAIG----VKLTVTDFLIKAVALALKKFPELNASWDD--DAIVLKKYVNIGIAVATDGGLIVPVI 291

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2481688347 368 KSVQLLSVFQVAQELTRLQTLGAAGQLGTAELSGGTFTLSNIGSIGGTYAKPVILPPEVAIGALGKIQVLPRFGpDGQVK 447
Cdd:PRK11856  292 RDADKKSLFELAREIKDLAEKAREGKLKPEELQGGTFTISNLGMFGGDYFTPIINPPEVAILGVGAIVERPVVV-DGEIV 370

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|.
gi 2481688347 448 AAHIMKVSWSADHRLIDGATMCRFSNLWREYLENPASMLLD 488
Cdd:PRK11856  371 VRKVMPLSLSFDHRVIDGADAARFLKALKELLENPALLLLE 411
2-oxoacid_dh pfam00198
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ...
 275-486 1.71e-90

2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to three copies of a lipoyl binding domain followed by the catalytic domain.


Pssm-ID: 425518 [Multi-domain]  Cd Length: 212  Bit Score: 274.81  E-value: 1.71e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2481688347 275 MTAAL-KIPHFGYCDEVDLSRLVLLRSELKPVAERRGVRLSYLPFFIKAASLSLLRFPILNSTLDESCQNITFKASHNIG 353
Cdd:pfam00198   1 MTESKqTIPHFTLTDEVDVTELLALREELKEDAADEETKLTFLPFLVKAVALALKKFPELNASWDGEEGEIVYKKYVNIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2481688347 354 VAMDTSLGLLVPSVKSVQLLSVFQVAQELTRLQTLGAAGQLGTAELSGGTFTLSNIGSIGGTYAKPVILPPEVAIGALGK 433
Cdd:pfam00198  81 IAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVGR 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2481688347 434 IQVLPRFgPDGQVKAAHIMKVSWSADHRLIDGATMCRFSNLWREYLENPASML 486
Cdd:pfam00198 161 IRKRPVV-VDGEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELLL 212
aceF PRK11854
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
 71-481 3.13e-75

pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated


Pssm-ID: 236999 [Multi-domain]  Cd Length: 633  Bit Score: 248.76  E-value: 3.13e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2481688347  71 DIGEGimEVTVKEWYVKEGDRVSQFDSICEVQSDKASVTITSRYDGVIRRLYYEADATALVGKPLVDIETE----SASEL 146
Cdd:PRK11854  213 DIGGD--EVEVTEVMVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVKTGSLIMRFEVEgaapAAAPA 290

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2481688347 147 SQEDVVETPAMAREEHTHQEIK------------GHKTQATPAVRRLAMENNIKLSEVVGTGKDGRILKEDILNFlAKQT 214
Cdd:PRK11854  291 KQEAAAPAPAAAKAEAPAAAPAakaegksefaenDAYVHATPLVRRLAREFGVNLAKVKGTGRKGRILKEDVQAY-VKDA 369

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2481688347 215 GAilppaplfqeiqtpgPAPTPPLSAPAGVRPPPATPRP--DFT--GKDVTEPLKGFHKAMVKTMTAAL-KIPHFGYCDE 289
Cdd:PRK11854  370 VK---------------RAEAAPAAAAAGGGGPGLLPWPkvDFSkfGEIEEVELGRIQKISGANLHRNWvMIPHVTQFDK 434

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2481688347 290 VDLSRLVLLRSELKPVAERR--GVRLSYLPFFIKAASLSLLRFPILNSTLDESCQNITFKASHNIGVAMDTSLGLLVPSV 367
Cdd:PRK11854  435 ADITELEAFRKQQNAEAEKRklGVKITPLVFIMKAVAAALEQMPRFNSSLSEDGQRLTLKKYVNIGIAVDTPNGLVVPVF 514

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2481688347 368 KSVQLLSVFQVAQELTRLQTLGAAGQLGTAELSGGTFTLSNIGSIGGTYAKPVILPPEVAIGALGKIQVLPRFgpDGQVK 447
Cdd:PRK11854  515 KDVNKKGIIELSRELMDISKKARDGKLTAGDMQGGCFTISSIGGLGTTHFTPIVNAPEVAILGVSKSAMEPVW--NGKEF 592

                         410       420       430
                  ....*....|....*....|....*....|....*
gi 2481688347 448 AAHIM-KVSWSADHRLIDGATMCRFSNLWREYLEN 481
Cdd:PRK11854  593 APRLMlPLSLSYDHRVIDGADGARFITIINDRLSD 627
sucB TIGR01347
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ...
 65-489 6.48e-72

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: 233.47  E-value: 6.48e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2481688347  65 VQFKLSDIGEGIMEVTVKEWYVKEGDRVSQFDSICEVQSDKASVTITSRYDGVIRRLYYEADATALVGKPLVDIE----- 139
Cdd:TIGR01347   1 IEIKVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAILEegnda 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2481688347 140 TESASELSQEDVVETPAMAREehTHQEIKGHKTQATPAVRRLAMENNIKLSEVVGTGKDGRILKEDILNFLAKqtgailp 219
Cdd:TIGR01347  81 TAAPPAKSGEEKEETPAASAA--AAPTAAANRPSLSPAARRLAKEHGIDLSAVPGTGVTGRVTKEDIIKKTEA------- 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2481688347 220 paplfqeiqtpgPAPTPPLSAPAGVRPPPATPRPDFTGK------DVTEPLKgfhkaMVKTMTAALKIPHfgycdEVDLS 293
Cdd:TIGR01347 152 ------------PASAQPPAAAAAAAAPAAATRPEERVKmtrlrqRIAERLK-----EAQNSTAMLTTFN-----EVDMS 209

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2481688347 294 RLVLLRSELKPVAERR-GVRLSYLPFFIKAASLSLLRFPILNSTLDEscQNITFKASHNIGVAMDTSLGLLVPSVKSVQL 372
Cdd:TIGR01347 210 AVMELRKRYKEEFEKKhGVKLGFMSFFVKAVVAALKRFPEVNAEIDG--DDIVYKDYYDISVAVSTDRGLVVPVVRNADR 287

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2481688347 373 LSVFQVAQELTRLQTLGAAGQLGTAELSGGTFTLSNIGSIGGTYAKPVILPPEVAIGALGKIQVLPrFGPDGQVKAAHIM 452
Cdd:TIGR01347 288 MSFADIEKEIADLGKKARDGKLTLEDMTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHGIKERP-VAVNGQIEIRPMM 366

                         410       420       430
                  ....*....|....*....|....*....|....*..
gi 2481688347 453 KVSWSADHRLIDGATMCRFSNLWREYLENPASMLLDL 489
Cdd:TIGR01347 367 YLALSYDHRLIDGKEAVTFLVTIKELLEDPRRLLLDL 403
PDHac_trf_long TIGR01348
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
 64-487 9.85e-70

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: 232.07  E-value: 9.85e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2481688347  64 VVQFKLSDIGeGIMEVTVKEWYVKEGDRVSQFDSICEVQSDKASVTITSRYDGVIRRLYYEADATALVGKPLVDIETESA 143
Cdd:TIGR01348 116 VQEVTVPDIG-DIEKVTVIEVLVKVGDTVSADQSLITLESDKASMEVPAPASGVVKSVKVKVGDSVPTGDLILTLSVAGS 194

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2481688347 144 SELSQEDVVETPAMAREEHTHQE---------------IKGHKTQ-------ATPAVRRLAMENNIKLSEVVGTGKDGRI 201
Cdd:TIGR01348 195 TPATAPAPASAQPAAQSPAATQPepaaapaaakaqapaPQQAGTQnpakvdhAAPAVRRLAREFGVDLSAVKGTGIKGRI 274

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2481688347 202 LKEDILNFLAKQTGAilppaplfqeiqtpgpAPTPPLSAPAGVRPPPATPRPDFT--GKDVTEPLKGFHKAMVKTMTAA- 278
Cdd:TIGR01348 275 LREDVQRFVKEPSVR----------------AQAAAASAAGGAPGALPWPNVDFSkfGEVEEVDMSRIRKISGANLTRNw 338

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2481688347 279 LKIPHFGYCDEVDLSRLVLLRSELKPVAERRGVRLSYLPFFIKAASLSLLRFPILNSTLDESCQNITFKASHNIGVAMDT 358
Cdd:TIGR01348 339 TMIPHVTHFDKADITEMEAFRKQQNAAVEKEGVKLTVLHILMKAVAAALKKFPKFNASLDLGGEQLILKKYVNIGVAVDT 418

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2481688347 359 SLGLLVPSVKSVQLLSVFQVAQELTRLQTLGAAGQLGTAELSGGTFTLSNIGSIGGTYAKPVILPPEVAIGALGKIQVLP 438
Cdd:TIGR01348 419 PNGLLVPVIKDVDRKGITELALELSDLAKKARDGKLTPDEMQGACFTISSLGGIGGTAFTPIVNAPEVAILGVSKSGMEP 498

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|
gi 2481688347 439 RFgpDGQVKAAHIM-KVSWSADHRLIDGATMCRFSNLWREYLENPASMLL 487
Cdd:TIGR01348 499 VW--NGKEFEPRLMlPLSLSYDHRVIDGADAARFTTYICESLADIRRLLL 546
PRK11857 PRK11857
dihydrolipoamide acetyltransferase; Reviewed
 171-482 2.86e-68

dihydrolipoamide acetyltransferase; Reviewed


Pssm-ID: 237002 [Multi-domain]  Cd Length: 306  Bit Score: 220.82  E-value: 2.86e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2481688347 171 KTQATPAVRRLAMENNIKLSEVVGTGKDGRILKEDILNFLAKQTGAilppaplfqeiQTPGPAPTPPLSAPAGVRPPPAT 250
Cdd:PRK11857    1 KILATPIARALAKKLGIDISLLKGSGRDGKILAEDVENFIKSLKSA-----------PTPAEAASVSSAQQAAKTAAPAA 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2481688347 251 PRPDFTGKdvTEPLKGFHKAMVKTMTAALK-IPHFGYCDEVDLSRLVLLRSELK-PVAERRGVRLSYLPFFIKAASLSLL 328
Cdd:PRK11857   70 APPKLEGK--REKVAPIRKAIARAMTNSWSnVAYVNLVNEIDMTKLWDLRKSVKdPVLKTEGVKLTFLPFIAKAILIALK 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2481688347 329 RFPILNSTLDESCQNITFKASHNIGVAMDTSLGLLVPSVKSVQLLSVFQVAQELTRLQTLGAAGQLGTAELSGGTFTLSN 408
Cdd:PRK11857  148 EFPIFAAKYDEATSELVYPDTLNLGIAVDTEAGLMVPVIKNAQKLSIVEIAKEISRLAKAARERKIKPDEMKGGSFTITN 227

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2481688347 409 IGSIGGTYAKPVILPPEVAIGALGKIQVLPRFgPDGQVKAAHIMKVSWSADHRLIDGATMCRFSNLWREYLENP 482
Cdd:PRK11857  228 YGSVGSLYGVPVINYPELAIAGVGAIIDKAIV-KNGQIVAGKVMHLTVAADHRWIDGATIGRFASRVKELLEKP 300
PRK05704 PRK05704
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
68-489 8.62e-65

2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;


Pssm-ID: 235571 [Multi-domain]  Cd Length: 407  Bit Score: 215.08  E-value: 8.62e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2481688347  68 KLSDIGEGIMEVTVKEWYVKEGDRVSQFDSICEVQSDKASVTITSRYDGVIRRLYYEADATALVGKPLVDIETE---SAS 144
Cdd:PRK05704    6 KVPTLPESVTEATIATWHKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGDTVTVGQVLGRIDEGaaaGAA 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2481688347 145 ELSQEDVVETPAMAREEHTHQEIKGHKTQATPAVRRLAMENNIKLSEVVGTGKDGRILKEDILNFLAKQTGAILPPAPlf 224
Cdd:PRK05704   86 AAAAAAAAAAAAAPAQAQAAAAAEQSNDALSPAARKLAAENGLDASAVKGTGKGGRVTKEDVLAALAAAAAAPAAPAA-- 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2481688347 225 qeiqtPGPAPTPPLSAPAGVRPPPATPRPdftgKDVTEPLKgfhkaMVKTMTAALKIphFgycDEVDLSRLVLLRSELKP 304
Cdd:PRK05704  164 -----AAPAAAPAPLGARPEERVPMTRLR----KTIAERLL-----EAQNTTAMLTT--F---NEVDMTPVMDLRKQYKD 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2481688347 305 VAERR-GVRLSYLPFFIKAASLSLLRFPILNSTLDEScqNITFKASHNIGVAMDTSLGLLVPSVKSVQLLSVFQVAQELT 383
Cdd:PRK05704  225 AFEKKhGVKLGFMSFFVKAVVEALKRYPEVNASIDGD--DIVYHNYYDIGIAVGTPRGLVVPVLRDADQLSFAEIEKKIA 302

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2481688347 384 RLQTLGAAGQLGTAELSGGTFTLSNigsiGGTY----AKPVILPPEVAIgaLG--KIQVLPrFGPDGQVKAAHIMKVSWS 457
Cdd:PRK05704  303 ELAKKARDGKLSIEELTGGTFTITN----GGVFgslmSTPIINPPQSAI--LGmhKIKERP-VAVNGQIVIRPMMYLALS 375

                         410       420       430
                  ....*....|....*....|....*....|..
gi 2481688347 458 ADHRLIDGATMCRFSNLWREYLENPASMLLDL 489
Cdd:PRK05704  376 YDHRIIDGKEAVGFLVTIKELLEDPERLLLDL 407
PDHac_trf_mito TIGR01349
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
 77-487 2.60e-59

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: 201.56  E-value: 2.60e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2481688347  77 MEV-TVKEWYVKEGDRVSQFDSICEVQSDKASVTITSRYDGVIRRLYYEADATAL-VGKPLV-------DIET------- 140
Cdd:TIGR01349  11 MTTgNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEGTKDVpVNKPIAvlveekeDVADafknykl 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2481688347 141 -ESASELSQ--------EDVVETPAMAREEHTHQEI---------KGHKTQATPAVRRLAMENNIKLSEVVGTGKDGRIL 202
Cdd:TIGR01349  91 eSSASPAPKpseiaptaPPSAPKPSPAPQKQSPEPSspaplsdkeSGDRIFASPLAKKLAKEKGIDLSAVAGSGPNGRIV 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2481688347 203 KEDILNFlakqtgaiLPPAPlfQEIQTPGPAPTPPLSapagvrpPPATPRPdfTGKDVTEPLKGFHKAMVKTMTAALK-I 281
Cdd:TIGR01349 171 KKDIESF--------VPQSP--ASANQQAAATTPATY-------PAAAPVS--TGSYEDVPLSNIRKIIAKRLLESKQtI 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2481688347 282 PHFGYCDEVDLSRLVLLRSELKPVAERRgVRLSYLPFFIKAASLSLLRFPILNSTLDEscQNITFKASHNIGVAMDTSLG 361
Cdd:TIGR01349 232 PHYYVSIECNVDKLLALRKELNAMASEV-YKLSVNDFIIKASALALREVPEANSSWTD--NFIRRYKNVDISVAVATPDG 308

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2481688347 362 LLVPSVKSVQLLSVFQVAQELTRLQTLGAAGQLGTAELSGGTFTLSNIGSIGGTYAKPVILPPEVAIGALG--KIQVLPR 439
Cdd:TIGR01349 309 LITPIVRNADAKGLSTISNEIKDLAKRARNNKLKPEEFQGGTFTISNLGMFGIKDFTAIINPPQACILAVGavEDVAVVD 388

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*...
gi 2481688347 440 FGPDGQVKAAHIMKVSWSADHRLIDGATMCRFSNLWREYLENPASMLL 487
Cdd:TIGR01349 389 NDEEKGFAVASIMSVTLSCDHRVIDGAVGAEFLKSFKKYLENPIEMLL 436
PTZ00144 PTZ00144
dihydrolipoamide succinyltransferase; Provisional
 68-489 4.07e-59

dihydrolipoamide succinyltransferase; Provisional


Pssm-ID: 240289 [Multi-domain]  Cd Length: 418  Bit Score: 200.29  E-value: 4.07e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2481688347  68 KLSDIGEGIMEVTVKEWYVKEGDRVSQFDSICEVQSDKASVTITSRYDGVIRRLYYEADATALVGKPLVDIETesaSELS 147
Cdd:PTZ00144   48 KVPTMGDSISEGTVVEWKKKVGDYVKEDEVICIIETDKVSVDIRAPASGVITKIFAEEGDTVEVGAPLSEIDT---GGAP 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2481688347 148 QEDVVETPAMAREEHTHQEikghktqatpavrrlamenniklsevvgtgkdgrilkedilnflAKQTGAILPPAPlfqEI 227
Cdd:PTZ00144  125 PAAAPAAAAAAKAEKTTPE--------------------------------------------KPKAAAPTPEPP---AA 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2481688347 228 QTPGPAPTPPLSAPAGVRPPPATP--RPDFTGKDV---------TEPLKGFHK--AMVKTMTaalkiphfgycdEVDLSR 294
Cdd:PTZ00144  158 SKPTPPAAAKPPEPAPAAKPPPTPvaRADPRETRVpmsrmrqriAERLKASQNtcAMLTTFN------------ECDMSA 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2481688347 295 LVLLRSELKPVAERR-GVRLSYLPFFIKAASLSLLRFPILNSTLDESCqnITFKASHNIGVAMDTSLGLLVPSVKSVQLL 373
Cdd:PTZ00144  226 LMELRKEYKDDFQKKhGVKLGFMSAFVKASTIALKKMPIVNAYIDGDE--IVYRNYVDISVAVATPTGLVVPVIRNCENK 303

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2481688347 374 SVFQVAQELTRLQTLGAAGQLGTAELSGGTFTLSNIGSIGGTYAKPVILPPEVAIGALGKIQVLPrFGPDGQVKAAHIMK 453
Cdd:PTZ00144  304 SFAEIEKELADLAEKARNNKLTLEDMTGGTFTISNGGVFGSLMGTPIINPPQSAILGMHAIKKRP-VVVGNEIVIRPIMY 382

                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 2481688347 454 VSWSADHRLIDGATMCRFSNLWREYLENPASMLLDL 489
Cdd:PTZ00144  383 LALTYDHRLIDGRDAVTFLKKIKDLIEDPARMLLDL 418
SucB_Actino TIGR02927
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model ...
 27-480 5.08e-59

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: 204.09  E-value: 5.08e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2481688347  27 PQNLRLSRTEPAPPRWAASLQSSCRRTlqtaverrrpvvQFKLSDIGEGIMEVTVKEWYVKEGDRVSQFDSICEVQSDKA 106
Cdd:TIGR02927 101 APAPAPTPAAEAPAPAAPQAGGSGEAT------------EVKMPELGESVTEGTVTSWLKAVGDTVEVDEPLLEVSTDKV 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2481688347 107 SVTITSRYDGVIRRLYYEADATALVGKPLVDI-ETESASELSQEDVVETPAMAREEHTHQEIKGHKTQA----------- 174
Cdd:TIGR02927 169 DTEIPSPVAGTLLEIRAPEDDTVEVGTVLAIIgDANAAPAEPAEEEAPAPSEAGSEPAPDPAARAPHAApdppapapapa 248

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2481688347 175 --------------------TPAVRRLAMENNIKLSEVVGTGKDGRILKEDILnflAKQTGAILPPAplfqeiqtpGPAP 234
Cdd:TIGR02927 249 ktaapaaaapvssgdsgpyvTPLVRKLAKDKGVDLSTVKGTGVGGRIRKQDVL---AAAKAAEEARA---------AAAA 316

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2481688347 235 TPPLSAPAGVRPPPATPRPDFTG-KDVTEPLKGFHKAMVKTMTAALKI-PHFGYCDEVDLSRLVLLRSELKP-VAERRGV 311
Cdd:TIGR02927 317 PAAAAAPAAPAAAAKPAEPDTAKlRGTTQKMNRIRQITADKTIESLQTsAQLTQVHEVDMTRVAALRARAKNdFLEKNGV 396

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2481688347 312 RLSYLPFFIKAASLSLLRFPILNSTLDESCQNITFKASHNIGVAMDTSLGLLVPSVKSVQLLSVFQVAQELTRLQTLGAA 391
Cdd:TIGR02927 397 NLTFLPFFVQAVTEALKAHPNVNASYNAETKEVTYHDVEHVGIAVDTPRGLLVPVIHNAGDLSLPGLAKAINDLAARARD 476

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2481688347 392 GQLGTAELSGGTFTLSNIGSIGGTYAKPVILPPEVAIGALGKIQVLPRFGPD---GQVKAAHIM-KVSWSADHRLIDGAT 467
Cdd:TIGR02927 477 NKLKPDELSGGTFTITNIGSGGALFDTPILNPPQAAILGTGAIVKRPRVIKDedgGESIAIRSVcYLPLTYDHRLVDGAD 556

                         490
                  ....*....|...
gi 2481688347 468 MCRFSNLWREYLE 480
Cdd:TIGR02927 557 AGRFLTTIKKRLE 569
PLN02744 PLN02744
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
 78-487 6.30e-50

dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex


Pssm-ID: 215397 [Multi-domain]  Cd Length: 539  Bit Score: 178.89  E-value: 6.30e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2481688347  78 EVTVKEWYVKEGDRVSQFDSICEVQSDKASVTITSRYDGVIRRLY-----------------------------YEADAT 128
Cdd:PLN02744  126 EGNIARWLKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVkgdgakeikvgeviaitveeeedigkfkdYKPSSS 205

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2481688347 129 ALVGKPlvdiETESASELSQEDVVETPAMAREEHTHQE----IKGHKTQATPAVRRLAMENNIKLSEVVGTGKDGRILKE 204
Cdd:PLN02744  206 AAPAAP----KAKPSPPPPKEEEVEKPASSPEPKASKPsappSSGDRIFASPLARKLAEDNNVPLSSIKGTGPDGRIVKA 281

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2481688347 205 DILNFLAKQ-TGAILPPaplfqeiqtPGPAPTPPLSApagvrpppaTPRPDFTGKDVTEPLKGFHKAMvktmtaalkIPH 283
Cdd:PLN02744  282 DIEDYLASGgKGATAPP---------STDSKAPALDY---------TDIPNTQIRKVTASRLLQSKQT---------IPH 334

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2481688347 284 FGYCDEVDLSRLVLLRSELKPVAER-RGVRLSYLPFFIKAASLSLLRFPILNStldeSCQNITFKASHN--IGVAMDTSL 360
Cdd:PLN02744  335 YYLTVDTRVDKLMALRSQLNSLQEAsGGKKISVNDLVIKAAALALRKVPQCNS----SWTDDYIRQYHNvnINVAVQTEN 410

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2481688347 361 GLLVPSVKSVQLLSVFQVAQELTRLQTLGAAGQLGTAELSGGTFTLSNIGS-IGGTYAKPVILPPEVAIGALGKIQ--VL 437
Cdd:PLN02744  411 GLYVPVVKDADKKGLSTIAEEVKQLAQKARENSLKPEDYEGGTFTVSNLGGpFGIKQFCAIINPPQSAILAVGSAEkrVI 490

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|
gi 2481688347 438 PRFGPDgQVKAAHIMKVSWSADHRLIDGATMCRFSNLWREYLENPASMLL 487
Cdd:PLN02744  491 PGSGPD-QYNFASFMSVTLSCDHRVIDGAIGAEWLKAFKGYIENPESMLL 539
PRK14843 PRK14843
dihydrolipoamide acetyltransferase; Provisional
 140-487 6.04e-35

dihydrolipoamide acetyltransferase; Provisional


Pssm-ID: 184847 [Multi-domain]  Cd Length: 347  Bit Score: 133.49  E-value: 6.04e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2481688347 140 TESASELSQE---DVVETPAMAREEHTHQE-IKGHKTQA----TPAVRRLAMENNIKLSEVVGTGKDGRILKEDILNFLA 211
Cdd:PRK14843    9 TPAARKLADDlgiNLYDVSGSGANGRVHKEdVETYKDTNvvriSPLAKRIALEHNIAWQEIQGTGHRGKIMKKDVLALLP 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2481688347 212 K--QTGAILPPAplfqEIQTpgpaptpplsapAGVRPPPATPRpdftGKDVTEPLKGFHKAMVKTMTAA-LKIPHFGYCD 288
Cdd:PRK14843   89 EniENDSIKSPA----QIEK------------VEEVPDNVTPY----GEIERIPMTPMRKVIAQRMVESyLTAPTFTLNY 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2481688347 289 EVDLSRLVLLRSE-LKPVAERRGVRLSYLPFFIKAASLSLLRFPILNSTLDESCQNITFKASHNIGVAMDTSLGLLVPSV 367
Cdd:PRK14843  149 EVDMTEMLALRKKvLEPIMEATGKKTTVTDLLSLAVVKTLMKHPYINASLTEDGKTIITHNYVNLAMAVGMDNGLMTPVV 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2481688347 368 KSVQLLSVFQVAQELTRLQTLGAAGQLGTAELSGGTFTLSNIGSIGGTYAKPVILPPEVAIgaLGKIQVLPRfgP---DG 444
Cdd:PRK14843  229 YNAEKMSLSELVVAFKDVIGRTLDGKLAPSELQNSTFTISNLGMFGVQSFGPIINQPNSAI--LGVSSTIEK--PvvvNG 304

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 2481688347 445 QVKAAHIMKVSWSADHRLIDGATMCRFSNLWREYLENPASMLL 487
Cdd:PRK14843  305 EIVIRPIMSLGLTIDHRVVDGMAGAKFMKDLKELIETPISMLI 347
PLN02226 PLN02226
2-oxoglutarate dehydrogenase E2 component
 3-489 1.56e-32

2-oxoglutarate dehydrogenase E2 component


Pssm-ID: 177871 [Multi-domain]  Cd Length: 463  Bit Score: 129.10  E-value: 1.56e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2481688347   3 AVTRGSFSALRVLLTQQYRRRSFGPQNLRLSRTEPAPPR--WAASLQ-------SSCRRTLQ---TAVER-RRP------ 63
Cdd:PLN02226   10 ASTRGSSPSLFGKSLQSSRVAASSPSLLSGSETGALLHRgnHAHSFHnlalpgnSGISRSASlvsSTLQRwVRPfssesg 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2481688347  64 -VVQFKLSDIGEGIMEVTVKEWYVKEGDRVSQFDSICEVQSDKASVTITSRYDGVIRRLYYEADATALVGKPLVDIET-- 140
Cdd:PLN02226   90 dTVEAVVPHMGESITDGTLATFLKKPGERVQADEAIAQIETDKVTIDIASPASGVIQEFLVKEGDTVEPGTKVAIISKse 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2481688347 141 ESASELS-QEDVVETPAmareehthqeikghkTQATPAVrrlamENNIKLSevvgtgkdgrilkedilnflakqtgaiLP 219
Cdd:PLN02226  170 DAASQVTpSQKIPETTD---------------PKPSPPA-----EDKQKPK---------------------------VE 202

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2481688347 220 PAPLFQEIQTPGPAPTPPLSAPAGVRPPPATPRpdftgkdvTEPLKGFHKAMVKTM-----TAALkiphFGYCDEVDLSR 294
Cdd:PLN02226  203 SAPVAEKPKAPSSPPPPKQSAKEPQLPPKERER--------RVPMTRLRKRVATRLkdsqnTFAL----LTTFNEVDMTN 270

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2481688347 295 LVLLRSELK-PVAERRGVRLSYLPFFIKAASLSLLRFPILNSTLDEScqNITFKASHNIGVAMDTSLGLLVPSVKSVQLL 373
Cdd:PLN02226  271 LMKLRSQYKdAFYEKHGVKLGLMSGFIKAAVSALQHQPVVNAVIDGD--DIIYRDYVDISIAVGTSKGLVVPVIRGADKM 348

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2481688347 374 SVFQVAQELTRLQTLGAAGQLGTAELSGGTFTLSNIGSIGGTYAKPVILPPEVAIGALGKIQVLPRFgPDGQVKAAHIMK 453
Cdd:PLN02226  349 NFAEIEKTINGLAKKANEGTISIDEMAGGSFTVSNGGVYGSLISTPIINPPQSAILGMHSIVSRPMV-VGGSVVPRPMMY 427

                         490       500       510
                  ....*....|....*....|....*....|....*.
gi 2481688347 454 VSWSADHRLIDGATMCRFSNLWREYLENPASMLLDL 489
Cdd:PLN02226  428 VALTYDHRLIDGREAVYFLRRVKDVVEDPQRLLLDI 463
lipoyl_domain cd06849
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ...
 65-138 3.44e-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: 101.33  E-value: 3.44e-26
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2481688347  65 VQFKLSDIGEGIMEVTVKEWYVKEGDRVSQFDSICEVQSDKASVTITSRYDGVIRRLYYEADATALVGKPLVDI 138
Cdd:cd06849     1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
AceF COG0508
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ...
 65-138 9.90e-22

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: 88.97  E-value: 9.90e-22
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2481688347  65 VQFKLSDIGEGIMEVTVKEWYVKEGDRVSQFDSICEVQSDKASVTITSRYDGVIRRLYYEADATALVGKPLVDI 138
Cdd:COG0508     3 IEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
Biotin_lipoyl pfam00364
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ...
 65-138 2.19e-18

Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue binds biotin in one group and lipoic acid in the other. Note that the HMM does not currently recognize the Glycine cleavage system H proteins.


Pssm-ID: 395290 [Multi-domain]  Cd Length: 73  Bit Score: 79.18  E-value: 2.19e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2481688347  65 VQFKLSDIGEGIMEVtVKEWYVKEGDRVSQFDSICEVQSDKASVTITSRYDGVIRRLYYEADATALVGKPLVDI 138
Cdd:pfam00364   1 TEIKSPMIGESVREG-VVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
E3_binding pfam02817
e3 binding domain; This family represents a small domain of the E2 subunit of 2-oxo-acid ...
 174-207 1.58e-13

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: 64.24  E-value: 1.58e-13
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2481688347 174 ATPAVRRLAMENNIKLSEVVGTGKDGRILKEDIL 207
Cdd:pfam02817   3 ASPAARKLARELGIDLSDVKGTGPGGRITKEDVE 36
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 73-219 2.18e-08

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 56.11  E-value: 2.18e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2481688347  73 GEGIMEVTVKEWYVKEGDRVSQFDSICEVQSDKASVTITSRYDGVIRRLYYEADATALVGKPLVDIETESASELSQEDVV 152
Cdd:PRK14875   11 GLSMTEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGETLPVGALLAVVADAEVSDAEIDAFI 90

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2481688347 153 etpamareehthqeikghktqaTPAVRRLAMEnNIKLSEVVGTGKDGRILKEDIlNFLAKQTGAILP 219
Cdd:PRK14875   91 ----------------------APFARRFAPE-GIDEEDAGPAPRKARIGGRTV-RYLRLGEGDGTP 133
kgd PRK12270
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ...
 211-471 3.76e-08

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


Pssm-ID: 237030 [Multi-domain]  Cd Length: 1228  Bit Score: 56.05  E-value: 3.76e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2481688347  211 AKQTGAILPPAPlfqeiQTPGPAPTPPLSAPAGVRPPPATPRPDFTGKDVTEPLKGFHKAMVKTMTAALKIPHFGYCDEV 290
Cdd:PRK12270    72 PAPPAAAAPAAP-----PKPAAAAAAAAAPAAPPAAAAAAAPAAAAVEDEVTPLRGAAAAVAKNMDASLEVPTATSVRAV 146

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2481688347  291 -----DLSRLVlLRSELKpvaERRGVRLSY---LPF-FIKAaslsLLRFPILNSTLDEscqnITFKASH------NIGVA 355
Cdd:PRK12270   147 pakllIDNRIV-INNHLK---RTRGGKVSFthlIGYaLVQA----LKAFPNMNRHYAE----VDGKPTLvtpahvNLGLA 214

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2481688347  356 MDT-----SLGLLVPSVKSVQLLSVFQVAQELTRLQTLGAAGQLGTAELSGGTFTLSNIGSIGGTYAKPVILPPEVAIGA 430
Cdd:PRK12270   215 IDLpkkdgSRQLVVPAIKGAETMDFAQFWAAYEDIVRRARDGKLTADDFQGTTISLTNPGGIGTVHSVPRLMKGQGAIIG 294

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 2481688347  431 LGKIQVLPRFGPDGQVKAAH-----IMKVSWSADHRLIDGATMCRF 471
Cdd:PRK12270   295 VGAMEYPAEFQGASEERLAElgiskVMTLTSTYDHRIIQGAESGEF 340
Biotinyl_lipoyl_domains cd06663
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ...
 69-138 3.55e-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: 47.44  E-value: 3.55e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2481688347  69 LSDIGEGIMEVTVKEWYVKEGDRVSQFDSICEVQSDKASVTITSRYDGVIRRLYYEADATALVGKPLVDI 138
Cdd:cd06663     4 IPDLAQHLGDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKVEGDTPLVKI 73
biotinyl_domain cd06850
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ...
 80-138 5.41e-05

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: 41.25  E-value: 5.41e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2481688347  80 TVKEWYVKEGDRVSQFDSICEVQSDKASVTITSRYDGVIRRLYYEADATALVGKPLVDI 138
Cdd:cd06850     9 TVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
PHA01732 PHA01732
proline-rich protein
 219-282 1.67e-03

proline-rich protein


Pssm-ID: 222828 [Multi-domain]  Cd Length: 94  Bit Score: 37.80  E-value: 1.67e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2481688347 219 PPAPLfqeiqTPGPAPTPPLSAPAGVRPPPATPRPDFTGKDVTEPLKGFHKAMVKTMTAALKIP 282
Cdd:PHA01732   12 PPAPL-----PPAPVPPPPPAPPAPVPEPTVKPVNAEAPKIREAQSKRGQKQQKAGGTASLRIP 70
PRK11892 PRK11892
pyruvate dehydrogenase subunit beta; Provisional
 78-178 3.51e-03

pyruvate dehydrogenase subunit beta; Provisional


Pssm-ID: 237011 [Multi-domain]  Cd Length: 464  Bit Score: 39.90  E-value: 3.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2481688347  78 EVTVKEWYVKEGDRVSQFDSICEVQSDKASVTITSRYDGVIRRLYYEADATAL-VGKPLVDI--ETESASELS------Q 148
Cdd:PRK11892   16 EGTLAKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKILVPEGTEGVkVNTPIAVLleEGESASDAGaapaaaA 95

                          90       100       110
                  ....*....|....*....|....*....|
gi 2481688347 149 EDVVETPAMAREEHTHQEIKGHKTQATPAV 178
Cdd:PRK11892   96 EAAAAAPAAAAAAAAKKAAPAPAAPAAPAA 125
PRK05641 PRK05641
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
 191-266 8.95e-03

putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated


Pssm-ID: 235540 [Multi-domain]  Cd Length: 153  Bit Score: 36.76  E-value: 8.95e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2481688347 191 EVVGTGKDGRILKEDILNFLAKQTGAILPPAPLFQEIQTPGPAPTPPlSAPAGVRPPPATPRPDFTGKD-VTEPLKG 266
Cdd:PRK05641   18 EELGPGKFRVSFEGKTYEVEAKGLGIDLSAVQEQVPTPAPAPAPAVP-SAPTPVAPAAPAPAPASAGENvVTAPMPG 93
 
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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