|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02528 |
PLN02528 |
2-oxoisovalerate dehydrogenase E2 component |
33-448 |
1.89e-177 |
|
2-oxoisovalerate dehydrogenase E2 component
Pssm-ID: 215289 [Multi-domain] Cd Length: 416 Bit Score: 502.33 E-value: 1.89e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537937 33 FKLSDIGEGIAEVQVKEWYVKEGDTISQFDKVCEVQSDKAAVTISCRYDGIVKKLYHEVDGMARVGQALIDVEIE-GNVE 111
Cdd:PLN02528 1 VPLAQTGEGIAECELLRWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGKVAQINFSPGDIVKVGETLLKIMVEdSQHL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537937 112 EPEQPKKEAASSspEAPKSSAPKAPESAHSEgkVLATPAVRRIAIENKIKLAEVRGTGKDGRVLKEDVLKFL---GQVPA 188
Cdd:PLN02528 81 RSDSLLLPTDSS--NIVSLAESDERGSNLSG--VLSTPAVRHLAKQYGIDLNDILGTGKDGRVLKEDVLKYAaqkGVVKD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537937 189 DHTSGSTNIRTTHQAPQPSSKSYEPLKEDVAVPIRGYTRAMVKTMTEALKIPHFGYNDEINVDSLVKYRAELKEFAKERH 268
Cdd:PLN02528 157 SSSAEEATIAEQEEFSTSVSTPTEQSYEDKTIPLRGFQRAMVKTMTAAAKVPHFHYVEEINVDALVELKASFQENNTDPT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537937 269 IKLSYMPFFIKAASLALLEYPSLNSTTDEKMENVIHKASHNICLAMDTPGGLVVPNIKNCEQRSIFEIAQELNRLLEAGK 348
Cdd:PLN02528 237 VKHTFLPFLIKSLSMALSKYPLLNSCFNEETSEIRLKGSHNIGVAMATEHGLVVPNIKNVQSLSLLEITKELSRLQHLAA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537937 349 KQQIKREDLIDGTFSLSNIGNIGGTYASPVVFPPQVAIGAIGKIEKLPRFDKHDNVIPVNIMKVSWCADHRVVDGATMAR 428
Cdd:PLN02528 317 ENKLNPEDITGGTITLSNIGAIGGKFGSPVLNLPEVAIIALGRIQKVPRFVDDGNVYPASIMTVTIGADHRVLDGATVAR 396
|
410 420
....*....|....*....|
gi 17537937 429 FSNRWKFYLEHPSAMLAQLK 448
Cdd:PLN02528 397 FCNEWKSYVEKPELLMLHMR 416
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
233-444 |
1.15e-92 |
|
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: 279.04 E-value: 1.15e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537937 233 MTEAL-KIPHFGYNDEINVDSLVKYRAELKEFAKERHIKLSYMPFFIKAASLALLEYPSLNSTTDEKMENVIHKASHNIC 311
Cdd:pfam00198 1 MTESKqTIPHFTLTDEVDVTELLALREELKEDAADEETKLTFLPFLVKAVALALKKFPELNASWDGEEGEIVYKKYVNIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537937 312 LAMDTPGGLVVPNIKNCEQRSIFEIAQELNRLLEAGKKQQIKREDLIDGTFSLSNIGNIGGTYASPVVFPPQVAIGAIGK 391
Cdd:pfam00198 81 IAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVGR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 17537937 392 IEKLPRFdKHDNVIPVNIMKVSWCADHRVVDGATMARFSNRWKFYLEHPSAML 444
Cdd:pfam00198 161 IRKRPVV-VDGEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELLL 212
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
30-444 |
1.87e-72 |
|
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: 237.85 E-value: 1.87e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537937 30 VVQFKLSDIGeGIAEVQVKEWYVKEGDTISQFDKVCEVQSDKAAVTISCRYDGIVKKLYHEVDGMARVGQALIDVEIEGN 109
Cdd:TIGR01348 116 VQEVTVPDIG-DIEKVTVIEVLVKVGDTVSADQSLITLESDKASMEVPAPASGVVKSVKVKVGDSVPTGDLILTLSVAGS 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537937 110 VE-EPEQPKK-EAASSSPEAPKSSAPKAPESAHSEGKVL-------------ATPAVRRIAIENKIKLAEVRGTGKDGRV 174
Cdd:TIGR01348 195 TPaTAPAPASaQPAAQSPAATQPEPAAAPAAAKAQAPAPqqagtqnpakvdhAAPAVRRLAREFGVDLSAVKGTGIKGRI 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537937 175 LKEDVLKFLGQ--VPADHTSGSTNIRTTHQAPQPSSkSYEPLKEDVAVPIRGYTRAMVKTMTEA-LKIPHFGYNDEINVD 251
Cdd:TIGR01348 275 LREDVQRFVKEpsVRAQAAAASAAGGAPGALPWPNV-DFSKFGEVEEVDMSRIRKISGANLTRNwTMIPHVTHFDKADIT 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537937 252 SLVKYRAELKEFAKERHIKLSYMPFFIKAASLALLEYPSLNSTTDEKMENVIHKASHNICLAMDTPGGLVVPNIKNCEQR 331
Cdd:TIGR01348 354 EMEAFRKQQNAAVEKEGVKLTVLHILMKAVAAALKKFPKFNASLDLGGEQLILKKYVNIGVAVDTPNGLLVPVIKDVDRK 433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537937 332 SIFEIAQELNRLLEAGKKQQIKREDLIDGTFSLSNIGNIGGTYASPVVFPPQVAIGAIGKIEKLPRFDKHDNViPVNIMK 411
Cdd:TIGR01348 434 GITELALELSDLAKKARDGKLTPDEMQGACFTISSLGGIGGTAFTPIVNAPEVAILGVSKSGMEPVWNGKEFE-PRLMLP 512
|
410 420 430
....*....|....*....|....*....|...
gi 17537937 412 VSWCADHRVVDGATMARFSNRWKFYLEHPSAML 444
Cdd:TIGR01348 513 LSLSYDHRVIDGADAARFTTYICESLADIRRLL 545
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
31-104 |
5.83e-21 |
|
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: 86.30 E-value: 5.83e-21
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17537937 31 VQFKLSDIGEGIAEVQVKEWYVKEGDTISQFDKVCEVQSDKAAVTISCRYDGIVKKLYHEVDGMARVGQALIDV 104
Cdd:cd06849 1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
31-104 |
4.82e-17 |
|
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: 75.49 E-value: 4.82e-17
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17537937 31 VQFKLSDIGEGIAEVQVKEWYVKEGDTISQFDKVCEVQSDKAAVTISCRYDGIVKKLYHEVDGMARVGQALIDV 104
Cdd:COG0508 3 IEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02528 |
PLN02528 |
2-oxoisovalerate dehydrogenase E2 component |
33-448 |
1.89e-177 |
|
2-oxoisovalerate dehydrogenase E2 component
Pssm-ID: 215289 [Multi-domain] Cd Length: 416 Bit Score: 502.33 E-value: 1.89e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537937 33 FKLSDIGEGIAEVQVKEWYVKEGDTISQFDKVCEVQSDKAAVTISCRYDGIVKKLYHEVDGMARVGQALIDVEIE-GNVE 111
Cdd:PLN02528 1 VPLAQTGEGIAECELLRWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGKVAQINFSPGDIVKVGETLLKIMVEdSQHL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537937 112 EPEQPKKEAASSspEAPKSSAPKAPESAHSEgkVLATPAVRRIAIENKIKLAEVRGTGKDGRVLKEDVLKFL---GQVPA 188
Cdd:PLN02528 81 RSDSLLLPTDSS--NIVSLAESDERGSNLSG--VLSTPAVRHLAKQYGIDLNDILGTGKDGRVLKEDVLKYAaqkGVVKD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537937 189 DHTSGSTNIRTTHQAPQPSSKSYEPLKEDVAVPIRGYTRAMVKTMTEALKIPHFGYNDEINVDSLVKYRAELKEFAKERH 268
Cdd:PLN02528 157 SSSAEEATIAEQEEFSTSVSTPTEQSYEDKTIPLRGFQRAMVKTMTAAAKVPHFHYVEEINVDALVELKASFQENNTDPT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537937 269 IKLSYMPFFIKAASLALLEYPSLNSTTDEKMENVIHKASHNICLAMDTPGGLVVPNIKNCEQRSIFEIAQELNRLLEAGK 348
Cdd:PLN02528 237 VKHTFLPFLIKSLSMALSKYPLLNSCFNEETSEIRLKGSHNIGVAMATEHGLVVPNIKNVQSLSLLEITKELSRLQHLAA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537937 349 KQQIKREDLIDGTFSLSNIGNIGGTYASPVVFPPQVAIGAIGKIEKLPRFDKHDNVIPVNIMKVSWCADHRVVDGATMAR 428
Cdd:PLN02528 317 ENKLNPEDITGGTITLSNIGAIGGKFGSPVLNLPEVAIIALGRIQKVPRFVDDGNVYPASIMTVTIGADHRVLDGATVAR 396
|
410 420
....*....|....*....|
gi 17537937 429 FSNRWKFYLEHPSAMLAQLK 448
Cdd:PLN02528 397 FCNEWKSYVEKPELLMLHMR 416
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
30-444 |
8.61e-132 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 391.11 E-value: 8.61e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537937 30 VVQFKLSDIGEgIAEVQVKEWYVKEGDTISQFDKVCEVQSDKAAVTISCRYDGIVKKLYHEVDGMARVGQALIDVEIEGN 109
Cdd:PRK11855 119 VVEVKVPDIGE-ITEVEVIEWLVKVGDTVEEDQSLITVETDKATMEIPSPVAGVVKEIKVKVGDKVSVGSLLVVIEVAAA 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537937 110 ------VEEPEQPKKEAASSSPEAPKSSAPKAP----ESAHSEGKVLATPAVRRIAIENKIKLAEVRGTGKDGRVLKEDV 179
Cdd:PRK11855 198 apaaaaAPAAAAPAAAAAAAPAPAPAAAAAPAAaapaAAAAPGKAPHASPAVRRLARELGVDLSQVKGTGKKGRITKEDV 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537937 180 LKFL-----GQVPADHTSGSTNIRTTHQAPQP---SSKSYEplKEdvAVPIRGYTRAMVKTMTEAL-KIPHFGYNDEINV 250
Cdd:PRK11855 278 QAFVkgamsAAAAAAAAAAAAGGGGLGLLPWPkvdFSKFGE--IE--TKPLSRIKKISAANLHRSWvTIPHVTQFDEADI 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537937 251 DSLVKYRAELKEFAKERHIKLSYMPFFIKAASLALLEYPSLNSTTDEKMENVIHKASHNICLAMDTPGGLVVPNIKNCEQ 330
Cdd:PRK11855 354 TDLEALRKQLKKEAEKAGVKLTMLPFFIKAVVAALKEFPVFNASLDEDGDELTYKKYFNIGFAVDTPNGLVVPVIKDVDK 433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537937 331 RSIFEIAQELNRLLEAGKKQQIKREDLIDGTFSLSNIGNIGGTYASPVVFPPQVAIGAIGKIEKLPRFDKhDNVIPVNIM 410
Cdd:PRK11855 434 KSLLEIAREIAELAKKARDGKLKPDDMQGGCFTISSLGGIGGTAFTPIINAPEVAILGVGKSQMKPVWDG-KEFVPRLML 512
|
410 420 430
....*....|....*....|....*....|....
gi 17537937 411 KVSWCADHRVVDGATMARFSNRWKFYLEHPSAML 444
Cdd:PRK11855 513 PLSLSYDHRVIDGATAARFTNYLKQLLADPRRML 546
|
|
| PRK11856 |
PRK11856 |
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed |
30-445 |
1.63e-127 |
|
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
Pssm-ID: 237001 [Multi-domain] Cd Length: 411 Bit Score: 375.28 E-value: 1.63e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537937 30 VVQFKLSDIGEGIAEVQVKEWYVKEGDTISQFDKVCEVQSDKAAVTISCRYDGIVKKLYHEVDGMARVGQALIDVEIEGN 109
Cdd:PRK11856 2 MFEFKMPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDVVPVGSVIAVIEEEGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537937 110 VEEPEQPKKEAASSSPEAPKSSAPKAPESAHSE--------GKVLATPAVRRIAIENKIKLAEVRGTGKDGRVLKEDVLK 181
Cdd:PRK11856 82 AEAAAAAEAAPEAPAPEPAPAAAAAAAAAPAAAaapaapaaAAAKASPAVRKLARELGVDLSTVKGSGPGGRITKEDVEA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537937 182 FLGQVPADHTSGSTNIRTTHQAPQPSSKsyeplkedvAVPIRGYTRAMVKTMTEA-LKIPHFGYNDEINVDSLVKYRAEL 260
Cdd:PRK11856 162 AAAAAAPAAAAAAAAAAAPPAAAAEGEE---------RVPLSGMRKAIAKRMVESkREIPHFTLTDEVDVTALLALRKQL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537937 261 KEFAkerhIKLSYMPFFIKAASLALLEYPSLNSTTDEkmENVIHKASHNICLAMDTPGGLVVPNIKNCEQRSIFEIAQEL 340
Cdd:PRK11856 233 KAIG----VKLTVTDFLIKAVALALKKFPELNASWDD--DAIVLKKYVNIGIAVATDGGLIVPVIRDADKKSLFELAREI 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537937 341 NRLLEAGKKQQIKREDLIDGTFSLSNIGNIGGTYASPVVFPPQVAIGAIGKIEKLPRFdKHDNVIPVNIMKVSWCADHRV 420
Cdd:PRK11856 307 KDLAEKAREGKLKPEELQGGTFTISNLGMFGGDYFTPIINPPEVAILGVGAIVERPVV-VDGEIVVRKVMPLSLSFDHRV 385
|
410 420
....*....|....*....|....*
gi 17537937 421 VDGATMARFSNRWKFYLEHPSAMLA 445
Cdd:PRK11856 386 IDGADAARFLKALKELLENPALLLL 410
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
233-444 |
1.15e-92 |
|
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: 279.04 E-value: 1.15e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537937 233 MTEAL-KIPHFGYNDEINVDSLVKYRAELKEFAKERHIKLSYMPFFIKAASLALLEYPSLNSTTDEKMENVIHKASHNIC 311
Cdd:pfam00198 1 MTESKqTIPHFTLTDEVDVTELLALREELKEDAADEETKLTFLPFLVKAVALALKKFPELNASWDGEEGEIVYKKYVNIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537937 312 LAMDTPGGLVVPNIKNCEQRSIFEIAQELNRLLEAGKKQQIKREDLIDGTFSLSNIGNIGGTYASPVVFPPQVAIGAIGK 391
Cdd:pfam00198 81 IAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVGR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 17537937 392 IEKLPRFdKHDNVIPVNIMKVSWCADHRVVDGATMARFSNRWKFYLEHPSAML 444
Cdd:pfam00198 161 IRKRPVV-VDGEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELLL 212
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
30-444 |
1.87e-72 |
|
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: 237.85 E-value: 1.87e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537937 30 VVQFKLSDIGeGIAEVQVKEWYVKEGDTISQFDKVCEVQSDKAAVTISCRYDGIVKKLYHEVDGMARVGQALIDVEIEGN 109
Cdd:TIGR01348 116 VQEVTVPDIG-DIEKVTVIEVLVKVGDTVSADQSLITLESDKASMEVPAPASGVVKSVKVKVGDSVPTGDLILTLSVAGS 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537937 110 VE-EPEQPKK-EAASSSPEAPKSSAPKAPESAHSEGKVL-------------ATPAVRRIAIENKIKLAEVRGTGKDGRV 174
Cdd:TIGR01348 195 TPaTAPAPASaQPAAQSPAATQPEPAAAPAAAKAQAPAPqqagtqnpakvdhAAPAVRRLAREFGVDLSAVKGTGIKGRI 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537937 175 LKEDVLKFLGQ--VPADHTSGSTNIRTTHQAPQPSSkSYEPLKEDVAVPIRGYTRAMVKTMTEA-LKIPHFGYNDEINVD 251
Cdd:TIGR01348 275 LREDVQRFVKEpsVRAQAAAASAAGGAPGALPWPNV-DFSKFGEVEEVDMSRIRKISGANLTRNwTMIPHVTHFDKADIT 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537937 252 SLVKYRAELKEFAKERHIKLSYMPFFIKAASLALLEYPSLNSTTDEKMENVIHKASHNICLAMDTPGGLVVPNIKNCEQR 331
Cdd:TIGR01348 354 EMEAFRKQQNAAVEKEGVKLTVLHILMKAVAAALKKFPKFNASLDLGGEQLILKKYVNIGVAVDTPNGLLVPVIKDVDRK 433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537937 332 SIFEIAQELNRLLEAGKKQQIKREDLIDGTFSLSNIGNIGGTYASPVVFPPQVAIGAIGKIEKLPRFDKHDNViPVNIMK 411
Cdd:TIGR01348 434 GITELALELSDLAKKARDGKLTPDEMQGACFTISSLGGIGGTAFTPIVNAPEVAILGVSKSGMEPVWNGKEFE-PRLMLP 512
|
410 420 430
....*....|....*....|....*....|...
gi 17537937 412 VSWCADHRVVDGATMARFSNRWKFYLEHPSAML 444
Cdd:TIGR01348 513 LSLSYDHRVIDGADAARFTTYICESLADIRRLL 545
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
37-438 |
5.85e-71 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 236.05 E-value: 5.85e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537937 37 DIGEGiaEVQVKEWYVKEGDTISQFDKVCEVQSDKAAVTISCRYDGIVKKLYHEVDGMARVGQALIDVEIEGNVEEPEQP 116
Cdd:PRK11854 213 DIGGD--EVEVTEVMVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVKTGSLIMRFEVEGAAPAAAPA 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537937 117 KKEAASSSPEAPKSSAPKAPESAHSEGK---------VLATPAVRRIAIENKIKLAEVRGTGKDGRVLKEDVLKFLGQVP 187
Cdd:PRK11854 291 KQEAAAPAPAAAKAEAPAAAPAAKAEGKsefaendayVHATPLVRRLAREFGVNLAKVKGTGRKGRILKEDVQAYVKDAV 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537937 188 ADHTSGSTNIRTTHQAPQ--PSSK-SYEPLKEDVAVPIRGYTRAMVKTMTEAL-KIPHFGYNDEINVDSLVKYRAELKEF 263
Cdd:PRK11854 371 KRAEAAPAAAAAGGGGPGllPWPKvDFSKFGEIEEVELGRIQKISGANLHRNWvMIPHVTQFDKADITELEAFRKQQNAE 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537937 264 A-KERH-IKLSYMPFFIKAASLALLEYPSLNSTTDEKMENVIHKASHNICLAMDTPGGLVVPNIKNCEQRSIFEIAQELN 341
Cdd:PRK11854 451 AeKRKLgVKITPLVFIMKAVAAALEQMPRFNSSLSEDGQRLTLKKYVNIGIAVDTPNGLVVPVFKDVNKKGIIELSRELM 530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537937 342 RLLEAGKKQQIKREDLIDGTFSLSNIGNIGGTYASPVVFPPQVAIGAIGKIEKLPRFDKhDNVIPVNIMKVSWCADHRVV 421
Cdd:PRK11854 531 DISKKARDGKLTAGDMQGGCFTISSIGGLGTTHFTPIVNAPEVAILGVSKSAMEPVWNG-KEFAPRLMLPLSLSYDHRVI 609
|
410
....*....|....*..
gi 17537937 422 DGATMARFSNRWKFYLE 438
Cdd:PRK11854 610 DGADGARFITIINDRLS 626
|
|
| PDHac_trf_mito |
TIGR01349 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
50-444 |
6.56e-68 |
|
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: 222.75 E-value: 6.56e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537937 50 WYVKEGDTISQFDKVCEVQSDKAAVTISCRYDGIVKKLYHE---------------VDGMARVGQALIDVEIEGNVEEPE 114
Cdd:TIGR01349 19 WLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPegtkdvpvnkpiavlVEEKEDVADAFKNYKLESSASPAP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537937 115 QPKKEAASSSPEAPK---SSAPKAPESA--------HSEGKVLATPAVRRIAIENKIKLAEVRGTGKDGRVLKEDVLKFL 183
Cdd:TIGR01349 99 KPSEIAPTAPPSAPKpspAPQKQSPEPSspaplsdkESGDRIFASPLAKKLAKEKGIDLSAVAGSGPNGRIVKKDIESFV 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537937 184 --GQVPADHTSGSTNIRTTHQAPQPSSKSYEplkedvAVPIRGYTRAMVKTMTEALK-IPHFGYNDEINVDSLVKYRAEL 260
Cdd:TIGR01349 179 pqSPASANQQAAATTPATYPAAAPVSTGSYE------DVPLSNIRKIIAKRLLESKQtIPHYYVSIECNVDKLLALRKEL 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537937 261 KEFAKERhIKLSYMPFFIKAASLALLEYPSLNSTTdekMENVIHKASH-NICLAMDTPGGLVVPNIKNCEQRSIFEIAQE 339
Cdd:TIGR01349 253 NAMASEV-YKLSVNDFIIKASALALREVPEANSSW---TDNFIRRYKNvDISVAVATPDGLITPIVRNADAKGLSTISNE 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537937 340 LNRLLEAGKKQQIKREDLIDGTFSLSNIGNIGGTYASPVVFPPQVAIGAIGKIEK--LPRFDKHDNVIPVNIMKVSWCAD 417
Cdd:TIGR01349 329 IKDLAKRARNNKLKPEEFQGGTFTISNLGMFGIKDFTAIINPPQACILAVGAVEDvaVVDNDEEKGFAVASIMSVTLSCD 408
|
410 420
....*....|....*....|....*..
gi 17537937 418 HRVVDGATMARFSNRWKFYLEHPSAML 444
Cdd:TIGR01349 409 HRVIDGAVGAEFLKSFKKYLENPIEML 435
|
|
| sucB |
TIGR01347 |
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ... |
31-444 |
4.58e-63 |
|
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: 209.20 E-value: 4.58e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537937 31 VQFKLSDIGEGIAEVQVKEWYVKEGDTISQFDKVCEVQSDKAAVTISCRYDGIVKKLYHEVDGMARVGQALIDVEiEGNV 110
Cdd:TIGR01347 1 IEIKVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAILE-EGND 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537937 111 EEPEQPKKeAASSSPEAPKSSAPKAPESAhsEGKVLATPAVRRIAIENKIKLAEVRGTGKDGRVLKEDVLKFLGQVPADh 190
Cdd:TIGR01347 80 ATAAPPAK-SGEEKEETPAASAAAAPTAA--ANRPSLSPAARRLAKEHGIDLSAVPGTGVTGRVTKEDIIKKTEAPASA- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537937 191 tsgstnirtthQAPQPSSKSYEPLKEDVAVPIRGYTRaMVKTMTEALK--------IPHFgynDEINVDSLVKYRAELKE 262
Cdd:TIGR01347 156 -----------QPPAAAAAAAAPAAATRPEERVKMTR-LRQRIAERLKeaqnstamLTTF---NEVDMSAVMELRKRYKE 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537937 263 -FAKERHIKLSYMPFFIKAASLALLEYPSLNSTTDEKmeNVIHKASHNICLAMDTPGGLVVPNIKNCEQRSIFEIAQELN 341
Cdd:TIGR01347 221 eFEKKHGVKLGFMSFFVKAVVAALKRFPEVNAEIDGD--DIVYKDYYDISVAVSTDRGLVVPVVRNADRMSFADIEKEIA 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537937 342 RLLEAGKKQQIKREDLIDGTFSLSNIGNIGGTYASPVVFPPQVAIGAIGKIEKLP-RFDKHDNVIPvnIMKVSWCADHRV 420
Cdd:TIGR01347 299 DLGKKARDGKLTLEDMTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHGIKERPvAVNGQIEIRP--MMYLALSYDHRL 376
|
410 420
....*....|....*....|....
gi 17537937 421 VDGATMARFSNRWKFYLEHPSAML 444
Cdd:TIGR01347 377 IDGKEAVTFLVTIKELLEDPRRLL 400
|
|
| PLN02744 |
PLN02744 |
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex |
44-444 |
1.40e-62 |
|
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
Pssm-ID: 215397 [Multi-domain] Cd Length: 539 Bit Score: 211.64 E-value: 1.40e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537937 44 EVQVKEWYVKEGDTISQFDKVCEVQSDKAAVTISCRYDGIVKKLYHEvDGMA--RVGQAL-IDVEIEGNVE--------- 111
Cdd:PLN02744 126 EGNIARWLKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVKG-DGAKeiKVGEVIaITVEEEEDIGkfkdykpss 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537937 112 -----------EPEQPKKEAASSSPEAPKSSAPKAPESAHSEGKVLATPAVRRIAIENKIKLAEVRGTGKDGRVLKEDVL 180
Cdd:PLN02744 205 saapaapkakpSPPPPKEEEVEKPASSPEPKASKPSAPPSSGDRIFASPLARKLAEDNNVPLSSIKGTGPDGRIVKADIE 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537937 181 KFLGQvpadhtsgstniRTTHQAPQPSSKSYEPLKEDVAVP---IRGYT--RAMVKTMTealkIPHFGYNDEINVDSLVK 255
Cdd:PLN02744 285 DYLAS------------GGKGATAPPSTDSKAPALDYTDIPntqIRKVTasRLLQSKQT----IPHYYLTVDTRVDKLMA 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537937 256 YRAELKEFA-KERHIKLSYMPFFIKAASLALLEYPSLNST-TDE---KMENVihkashNICLAMDTPGGLVVPNIKNCEQ 330
Cdd:PLN02744 349 LRSQLNSLQeASGGKKISVNDLVIKAAALALRKVPQCNSSwTDDyirQYHNV------NINVAVQTENGLYVPVVKDADK 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537937 331 RSIFEIAQELNRLLEAGKKQQIKREDLIDGTFSLSNIGN-IGGTYASPVVFPPQVAIGAIGKIEKlprfdkhdNVIPVN- 408
Cdd:PLN02744 423 KGLSTIAEEVKQLAQKARENSLKPEDYEGGTFTVSNLGGpFGIKQFCAIINPPQSAILAVGSAEK--------RVIPGSg 494
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 17537937 409 --------IMKVSWCADHRVVDGATMARFSNRWKFYLEHPSAML 444
Cdd:PLN02744 495 pdqynfasFMSVTLSCDHRVIDGAIGAEWLKAFKGYIENPESML 538
|
|
| PRK11857 |
PRK11857 |
dihydrolipoamide acetyltransferase; Reviewed |
144-440 |
5.42e-59 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237002 [Multi-domain] Cd Length: 306 Bit Score: 195.78 E-value: 5.42e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537937 144 KVLATPAVRRIAIENKIKLAEVRGTGKDGRVLKEDVLKFL-----GQVPADHTSGSTNIRTTHQA-PQPSSKSYEPLKED 217
Cdd:PRK11857 1 KILATPIARALAKKLGIDISLLKGSGRDGKILAEDVENFIkslksAPTPAEAASVSSAQQAAKTAaPAAAPPKLEGKREK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537937 218 VAvPIRgytRAMVKTMTEALK-IPHFGYNDEINVDSLVKYRAELKE-FAKERHIKLSYMPFFIKAASLALLEYPSLNSTT 295
Cdd:PRK11857 81 VA-PIR---KAIARAMTNSWSnVAYVNLVNEIDMTKLWDLRKSVKDpVLKTEGVKLTFLPFIAKAILIALKEFPIFAAKY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537937 296 DEKMENVIHKASHNICLAMDTPGGLVVPNIKNCEQRSIFEIAQELNRLLEAGKKQQIKREDLIDGTFSLSNIGNIGGTYA 375
Cdd:PRK11857 157 DEATSELVYPDTLNLGIAVDTEAGLMVPVIKNAQKLSIVEIAKEISRLAKAARERKIKPDEMKGGSFTITNYGSVGSLYG 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17537937 376 SPVVFPPQVAIGAIGKIEKLPRFdKHDNVIPVNIMKVSWCADHRVVDGATMARFSNRWKFYLEHP 440
Cdd:PRK11857 237 VPVINYPELAIAGVGAIIDKAIV-KNGQIVAGKVMHLTVAADHRWIDGATIGRFASRVKELLEKP 300
|
|
| PRK05704 |
PRK05704 |
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase; |
34-444 |
5.82e-58 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
Pssm-ID: 235571 [Multi-domain] Cd Length: 407 Bit Score: 195.82 E-value: 5.82e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537937 34 KLSDIGEGIAEVQVKEWYVKEGDTISQFDKVCEVQSDKAAVTISCRYDGIVKKLYHEVDGMARVGQALIDVEiEGNVEEP 113
Cdd:PRK05704 6 KVPTLPESVTEATIATWHKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGDTVTVGQVLGRID-EGAAAGA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537937 114 EQPKKEAASSSPEAPkssAPKAPESAHSEGKVLATPAVRRIAIENKIKLAEVRGTGKDGRVLKEDVLKFLGQVPADHTsg 193
Cdd:PRK05704 85 AAAAAAAAAAAAAAP---AQAQAAAAAEQSNDALSPAARKLAAENGLDASAVKGTGKGGRVTKEDVLAALAAAAAAPA-- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537937 194 stnirTTHQAPQPSSKSYEPLKEDVAVPIrgyTR----------------AMVKTmtealkiphfgYNdEINVDSLVKYR 257
Cdd:PRK05704 160 -----APAAAAPAAAPAPLGARPEERVPM---TRlrktiaerlleaqnttAMLTT-----------FN-EVDMTPVMDLR 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537937 258 AELKE-FAKERHIKLSYMPFFIKAASLALLEYPSLNSTTDEKmENVIHKASHnICLAMDTPGGLVVPNIKNCEQRSIFEI 336
Cdd:PRK05704 220 KQYKDaFEKKHGVKLGFMSFFVKAVVEALKRYPEVNASIDGD-DIVYHNYYD-IGIAVGTPRGLVVPVLRDADQLSFAEI 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537937 337 AQELNRLLEAGKKQQIKREDLIDGTFSLSNigniGGTYAS----PVVFPPQVAIGAIGKIEKLPRFDKHDNVI-PVNIMK 411
Cdd:PRK05704 298 EKKIAELAKKARDGKLSIEELTGGTFTITN----GGVFGSlmstPIINPPQSAILGMHKIKERPVAVNGQIVIrPMMYLA 373
|
410 420 430
....*....|....*....|....*....|...
gi 17537937 412 VSWcaDHRVVDGATMARFSNRWKFYLEHPSAML 444
Cdd:PRK05704 374 LSY--DHRIIDGKEAVGFLVTIKELLEDPERLL 404
|
|
| SucB_Actino |
TIGR02927 |
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model ... |
34-438 |
9.96e-57 |
|
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: 196.77 E-value: 9.96e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537937 34 KLSDIGEGIAEVQVKEWYVKEGDTISQFDKVCEVQSDKAAVTISCRYDGIVKKLYHEVDG-------MARVGQALIDVEI 106
Cdd:TIGR02927 130 KMPELGESVTEGTVTSWLKAVGDTVEVDEPLLEVSTDKVDTEIPSPVAGTLLEIRAPEDDtvevgtvLAIIGDANAAPAE 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537937 107 ----------EGNVEEPEQPKKEAASSSPE-------APKSSAPKA-PESAHSEGKVLATPAVRRIAIENKIKLAEVRGT 168
Cdd:TIGR02927 210 paeeeapapsEAGSEPAPDPAARAPHAAPDppapapaPAKTAAPAAaAPVSSGDSGPYVTPLVRKLAKDKGVDLSTVKGT 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537937 169 GKDGRVLKEDVLKFL-GQVPADHTSGSTNIRTTHQAPQPSSKSYEPLKedvaVPIRGYTRAM-------VKTMTEALKI- 239
Cdd:TIGR02927 290 GVGGRIRKQDVLAAAkAAEEARAAAAAPAAAAAPAAPAAAAKPAEPDT----AKLRGTTQKMnrirqitADKTIESLQTs 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537937 240 PHFGYNDEINVDSLVKYRAELK-EFAKERHIKLSYMPFFIKAASLALLEYPSLNSTTDEKMENVIHKASHNICLAMDTPG 318
Cdd:TIGR02927 366 AQLTQVHEVDMTRVAALRARAKnDFLEKNGVNLTFLPFFVQAVTEALKAHPNVNASYNAETKEVTYHDVEHVGIAVDTPR 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537937 319 GLVVPNIKNCEQRSIFEIAQELNRLLEAGKKQQIKREDLIDGTFSLSNIGNIGGTYASPVVFPPQVAIGAIGKIEKLPRF 398
Cdd:TIGR02927 446 GLLVPVIHNAGDLSLPGLAKAINDLAARARDNKLKPDELSGGTFTITNIGSGGALFDTPILNPPQAAILGTGAIVKRPRV 525
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 17537937 399 DK-HDNVIPVNIMKVSWCA---DHRVVDGATMARFSNRWKFYLE 438
Cdd:TIGR02927 526 IKdEDGGESIAIRSVCYLPltyDHRLVDGADAGRFLTTIKKRLE 569
|
|
| PTZ00144 |
PTZ00144 |
dihydrolipoamide succinyltransferase; Provisional |
7-447 |
1.70e-50 |
|
dihydrolipoamide succinyltransferase; Provisional
Pssm-ID: 240289 [Multi-domain] Cd Length: 418 Bit Score: 176.41 E-value: 1.70e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537937 7 LGTSSRIFKLNKHL-----HTSKVAFMPVVqFKLSDIGEGIAEVQVKEWYVKEGDTISQFDKVCEVQSDKAAVTISCRYD 81
Cdd:PTZ00144 17 VKGMFRRFSLRKLQpacsaHFSKSYFSIKV-IKVPTMGDSISEGTVVEWKKKVGDYVKEDEVICIIETDKVSVDIRAPAS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537937 82 GIVKKLYHEVDGMARVGQAL--IDVEIEGNVEEPEQP-----------KKEAASSSPEAPKSSAPKAPESAHSE-----G 143
Cdd:PTZ00144 96 GVITKIFAEEGDTVEVGAPLseIDTGGAPPAAAPAAAaaakaekttpeKPKAAAPTPEPPAASKPTPPAAAKPPepapaA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537937 144 KVLATPAVRRIAIENKIKLAEVRgtgkdgrvlkedvlkflgQVPADHTSGSTNirtthqapqpssksyeplkedvavpir 223
Cdd:PTZ00144 176 KPPPTPVARADPRETRVPMSRMR------------------QRIAERLKASQN--------------------------- 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537937 224 gyTRAMVKTMTEalkiphfgyndeINVDSLVKYRAELKE-FAKERHIKLSYMPFFIKAASLALLEYPSLNSTTDEKmeNV 302
Cdd:PTZ00144 211 --TCAMLTTFNE------------CDMSALMELRKEYKDdFQKKHGVKLGFMSAFVKASTIALKKMPIVNAYIDGD--EI 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537937 303 IHKASHNICLAMDTPGGLVVPNIKNCEQRSIFEIAQELNRLLEAGKKQQIKREDLIDGTFSLSNIGNIGGTYASPVVFPP 382
Cdd:PTZ00144 275 VYRNYVDISVAVATPTGLVVPVIRNCENKSFAEIEKELADLAEKARNNKLTLEDMTGGTFTISNGGVFGSLMGTPIINPP 354
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17537937 383 QVAIGAIGKIEKLPrFDKHDNVIPVNIMKVSWCADHRVVDGATMARFSNRWKFYLEHPSAMLAQL 447
Cdd:PTZ00144 355 QSAILGMHAIKKRP-VVVGNEIVIRPIMYLALTYDHRLIDGRDAVTFLKKIKDLIEDPARMLLDL 418
|
|
| PRK14843 |
PRK14843 |
dihydrolipoamide acetyltransferase; Provisional |
137-444 |
3.97e-31 |
|
dihydrolipoamide acetyltransferase; Provisional
Pssm-ID: 184847 [Multi-domain] Cd Length: 347 Bit Score: 122.32 E-value: 3.97e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537937 137 ESAHSEGKVLATPAVRRIAIENKIKLAEVRGTGKDGRVLKEDVLKFLgqvPADHTSGSTNIRTTHQAPQPSSKSYEPLKE 216
Cdd:PRK14843 41 ETYKDTNVVRISPLAKRIALEHNIAWQEIQGTGHRGKIMKKDVLALL---PENIENDSIKSPAQIEKVEEVPDNVTPYGE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537937 217 DVAVPIRGYTRAMVKTMTEA-LKIPHFGYNDEINVDSLVKYRAELKEFAKERHIKLSYMPFFIKAASL-ALLEYPSLNST 294
Cdd:PRK14843 118 IERIPMTPMRKVIAQRMVESyLTAPTFTLNYEVDMTEMLALRKKVLEPIMEATGKKTTVTDLLSLAVVkTLMKHPYINAS 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537937 295 TDEKMENVIHKASHNICLAMDTPGGLVVPNIKNCEQRSIFEIAQELNRLLEAGKKQQIKREDLIDGTFSLSNIGNIGGTY 374
Cdd:PRK14843 198 LTEDGKTIITHNYVNLAMAVGMDNGLMTPVVYNAEKMSLSELVVAFKDVIGRTLDGKLAPSELQNSTFTISNLGMFGVQS 277
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17537937 375 ASPVVFPPQVAI-GAIGKIEKLPRFDKHDNVIPvnIMKVSWCADHRVVDGATMARFSNRWKFYLEHPSAML 444
Cdd:PRK14843 278 FGPIINQPNSAIlGVSSTIEKPVVVNGEIVIRP--IMSLGLTIDHRVVDGMAGAKFMKDLKELIETPISML 346
|
|
| PLN02226 |
PLN02226 |
2-oxoglutarate dehydrogenase E2 component |
30-444 |
5.20e-26 |
|
2-oxoglutarate dehydrogenase E2 component
Pssm-ID: 177871 [Multi-domain] Cd Length: 463 Bit Score: 109.84 E-value: 5.20e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537937 30 VVQFKLSDIGEGIAEVQVKEWYVKEGDTISQFDKVCEVQSDKAAVTISCRYDGIVKKLyhevdgmarvgqaLIDveiEGN 109
Cdd:PLN02226 91 TVEAVVPHMGESITDGTLATFLKKPGERVQADEAIAQIETDKVTIDIASPASGVIQEF-------------LVK---EGD 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537937 110 VEEPEQP----KKEAASSSPEAPKSSAPKAPESAHSE-GKVLATPAVRRIAIENKIKLAevrgtgkdgrvlkedvlkflg 184
Cdd:PLN02226 155 TVEPGTKvaiiSKSEDAASQVTPSQKIPETTDPKPSPpAEDKQKPKVESAPVAEKPKAP--------------------- 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537937 185 qvpadhtSGSTNIRTTHQAPQPSSKSYEPLKEDVAVPIRGYTRAMVKTMTEALkIPHFgynDEINVDSLVKYRAELKEFA 264
Cdd:PLN02226 214 -------SSPPPPKQSAKEPQLPPKERERRVPMTRLRKRVATRLKDSQNTFAL-LTTF---NEVDMTNLMKLRSQYKDAF 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537937 265 KERH-IKLSYMPFFIKAASLALLEYPSLNSTTDEkmENVIHKASHNICLAMDTPGGLVVPNIKNCEQRSIFEIAQELNRL 343
Cdd:PLN02226 283 YEKHgVKLGLMSGFIKAAVSALQHQPVVNAVIDG--DDIIYRDYVDISIAVGTSKGLVVPVIRGADKMNFAEIEKTINGL 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537937 344 LEAGKKQQIKREDLIDGTFSLSNIGNIGGTYASPVVFPPQVAIGAIGKIEKLPRFdKHDNVIPVNIMKVSWCADHRVVDG 423
Cdd:PLN02226 361 AKKANEGTISIDEMAGGSFTVSNGGVYGSLISTPIINPPQSAILGMHSIVSRPMV-VGGSVVPRPMMYVALTYDHRLIDG 439
|
410 420
....*....|....*....|.
gi 17537937 424 ATMARFSNRWKFYLEHPSAML 444
Cdd:PLN02226 440 REAVYFLRRVKDVVEDPQRLL 460
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
31-104 |
5.83e-21 |
|
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: 86.30 E-value: 5.83e-21
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17537937 31 VQFKLSDIGEGIAEVQVKEWYVKEGDTISQFDKVCEVQSDKAAVTISCRYDGIVKKLYHEVDGMARVGQALIDV 104
Cdd:cd06849 1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
31-104 |
4.82e-17 |
|
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: 75.49 E-value: 4.82e-17
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17537937 31 VQFKLSDIGEGIAEVQVKEWYVKEGDTISQFDKVCEVQSDKAAVTISCRYDGIVKKLYHEVDGMARVGQALIDV 104
Cdd:COG0508 3 IEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
|
|
| E3_binding |
pfam02817 |
e3 binding domain; This family represents a small domain of the E2 subunit of 2-oxo-acid ... |
145-180 |
4.69e-14 |
|
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: 65.79 E-value: 4.69e-14
10 20 30
....*....|....*....|....*....|....*.
gi 17537937 145 VLATPAVRRIAIENKIKLAEVRGTGKDGRVLKEDVL 180
Cdd:pfam02817 1 VLASPAARKLARELGIDLSDVKGTGPGGRITKEDVE 36
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
31-104 |
6.25e-14 |
|
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: 66.47 E-value: 6.25e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17537937 31 VQFKLSDIGEGIAEVqVKEWYVKEGDTISQFDKVCEVQSDKAAVTISCRYDGIVKKLYHEVDGMARVGQALIDV 104
Cdd:pfam00364 1 TEIKSPMIGESVREG-VVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
|
|
| kgd |
PRK12270 |
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ... |
203-429 |
7.70e-13 |
|
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;
Pssm-ID: 237030 [Multi-domain] Cd Length: 1228 Bit Score: 70.69 E-value: 7.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537937 203 APQPSSKSYEPLKEDVAVPIRGYTRAMVKTMTEALKIPHFGYNDEINVDSLVKYRAELKEF-AKERHIKLSYMPFFIKAA 281
Cdd:PRK12270 101 AAAAAAAPAAAAVEDEVTPLRGAAAAVAKNMDASLEVPTATSVRAVPAKLLIDNRIVINNHlKRTRGGKVSFTHLIGYAL 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537937 282 SLALLEYPSLNSTTDEK--MENVIHKASHNICLAMDTPG-----GLVVPNIKNCEQRSIFEIAQELNRLLEAGKKQQIKR 354
Cdd:PRK12270 181 VQALKAFPNMNRHYAEVdgKPTLVTPAHVNLGLAIDLPKkdgsrQLVVPAIKGAETMDFAQFWAAYEDIVRRARDGKLTA 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537937 355 EDLIDGTFSLSNIGNIGGTYASPVVFPPQVAIGAIGKIEKLPRF----DKHDNVIPVN-IMKVSWCADHRVVDGATMARF 429
Cdd:PRK12270 261 DDFQGTTISLTNPGGIGTVHSVPRLMKGQGAIIGVGAMEYPAEFqgasEERLAELGISkVMTLTSTYDHRIIQGAESGEF 340
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
39-179 |
4.11e-07 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 51.87 E-value: 4.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537937 39 GEGIAEVQVKEWYVKEGDTISQFDKVCEVQSDKAAVTISCRYDGIVKKLYHEVDGMARVGqALIDVeiegnveepeqpkk 118
Cdd:PRK14875 11 GLSMTEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGETLPVG-ALLAV-------------- 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17537937 119 EAASSSPEApkssapkapesahsEGKVLATPAVRRIAIENkIKLAEVRGTGKDGRVLKEDV 179
Cdd:PRK14875 76 VADAEVSDA--------------EIDAFIAPFARRFAPEG-IDEEDAGPAPRKARIGGRTV 121
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
35-102 |
1.83e-05 |
|
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: 42.43 E-value: 1.83e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17537937 35 LSDIGEGIAEVQVKEWYVKEGDTISQFDKVCEVQSDKAAVTISCRYDGIVKKLYHEVDGMARVGQALI 102
Cdd:cd06663 4 IPDLAQHLGDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKVEGDTPLV 71
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
50-151 |
8.96e-04 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 41.44 E-value: 8.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537937 50 WYVKEGDTISQFDKVCEVQSDKAAVTISCRYDGIVKKLYHE--VDGMArVGQ--ALIDVEIEGNVEEPEQPKKEAASSSP 125
Cdd:PRK11892 22 WLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKILVPegTEGVK-VNTpiAVLLEEGESASDAGAAPAAAAEAAAA 100
|
90 100
....*....|....*....|....*.
gi 17537937 126 EAPKSSAPKAPESAHSEgKVLATPAV 151
Cdd:PRK11892 101 APAAAAAAAAKKAAPAP-AAPAAPAA 125
|
|
| |
