|
Name |
Accession |
Description |
Interval |
E-value |
| sucB |
TIGR01347 |
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ... |
74-460 |
0e+00 |
|
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: 579.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935098744 74 ITINTPAFAESVTEGDV-RWEKAVGDTVAEDEVVCEIETDKTSVQVPSPAAGVIEALLVPDGGKVEGGTPLFKLRKSGAA 152
Cdd:TIGR01347 1 IEIKVPELAESITEGTVaEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAILEEGNDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935098744 153 PTKAKPAVAPPAAAPAPEPVAAAVAPPAEPIPTMMPPVPPVSTQPIDTKPVSAVKPT-----------------AAPVAA 215
Cdd:TIGR01347 81 TAAPPAKSGEEKEETPAASAAAAPTAAANRPSLSPAARRLAKEHGIDLSAVPGTGVTgrvtkediikkteapasAQPPAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935098744 216 PGVEPGASKGARSEHRVKMNRMRQRIAQRLKEAQNTCAMLTTFNEIDMSNIQEMRARHRDSFQKKHNLKLGFMSAFVKAA 295
Cdd:TIGR01347 161 AAAAAAPAAATRPEERVKMTRLRQRIAERLKEAQNSTAMLTTFNEVDMSAVMELRKRYKEEFEKKHGVKLGFMSFFVKAV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935098744 296 AFALQEQPIVNAVIDDTtkEMVYRDYVDISVAVATPRGLVVPVIRNVETMNFADIERTINELGEKARKNELAIEDMDGGT 375
Cdd:TIGR01347 241 VAALKRFPEVNAEIDGD--DIVYKDYYDISVAVSTDRGLVVPVVRNADRMSFADIEKEIADLGKKARDGKLTLEDMTGGT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935098744 376 FTISNGGVFGSLFGTPIINPPQSAILGMHGIFDRPVAVGGKVEVRPMMYVALTYDHRLIDGREAVTFLRKIKAVVEDPRV 455
Cdd:TIGR01347 319 FTITNGGVFGSLMSTPIINPPQSAILGMHGIKERPVAVNGQIEIRPMMYLALSYDHRLIDGKEAVTFLVTIKELLEDPRR 398
|
....*
gi 1935098744 456 MLLDL 460
Cdd:TIGR01347 399 LLLDL 403
|
|
| PTZ00144 |
PTZ00144 |
dihydrolipoamide succinyltransferase; Provisional |
45-460 |
0e+00 |
|
dihydrolipoamide succinyltransferase; Provisional
Pssm-ID: 240289 [Multi-domain] Cd Length: 418 Bit Score: 546.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935098744 45 TNSSKLVVNTSSVFSVRYFRITAVCRD-------DVITINTPAFAESVTEGDV-RWEKAVGDTVAEDEVVCEIETDKTSV 116
Cdd:PTZ00144 9 LNKPLLSSVKGMFRRFSLRKLQPACSAhfsksyfSIKVIKVPTMGDSISEGTVvEWKKKVGDYVKEDEVICIIETDKVSV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935098744 117 QVPSPAAGVIEALLVPDGGKVEGGTPLFKLRKSGAAPtkakpavappaaapAPEPVAAAVAPPAEPIPTMMPPVPPVSTQ 196
Cdd:PTZ00144 89 DIRAPASGVITKIFAEEGDTVEVGAPLSEIDTGGAPP--------------AAAPAAAAAAKAEKTTPEKPKAAAPTPEP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935098744 197 PIDTKPVSA--VKPTAAPVAAPGVEPGASKGARSEHRVKMNRMRQRIAQRLKEAQNTCAMLTTFNEIDMSNIQEMRARHR 274
Cdd:PTZ00144 155 PAASKPTPPaaAKPPEPAPAAKPPPTPVARADPRETRVPMSRMRQRIAERLKASQNTCAMLTTFNECDMSALMELRKEYK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935098744 275 DSFQKKHNLKLGFMSAFVKAAAFALQEQPIVNAVIDdtTKEMVYRDYVDISVAVATPRGLVVPVIRNVETMNFADIERTI 354
Cdd:PTZ00144 235 DDFQKKHGVKLGFMSAFVKASTIALKKMPIVNAYID--GDEIVYRNYVDISVAVATPTGLVVPVIRNCENKSFAEIEKEL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935098744 355 NELGEKARKNELAIEDMDGGTFTISNGGVFGSLFGTPIINPPQSAILGMHGIFDRPVAVGGKVEVRPMMYVALTYDHRLI 434
Cdd:PTZ00144 313 ADLAEKARNNKLTLEDMTGGTFTISNGGVFGSLMGTPIINPPQSAILGMHAIKKRPVVVGNEIVIRPIMYLALTYDHRLI 392
|
410 420
....*....|....*....|....*.
gi 1935098744 435 DGREAVTFLRKIKAVVEDPRVMLLDL 460
Cdd:PTZ00144 393 DGRDAVTFLKKIKDLIEDPARMLLDL 418
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
245-457 |
1.99e-96 |
|
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: 289.06 E-value: 1.99e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935098744 245 LKEAQNTCAMLTTFNEIDMSNIQEMRARHRDSFQKKHNlKLGFMSAFVKAAAFALQEQPIVNAVIDDTTKEMVYRDYVDI 324
Cdd:pfam00198 1 MTESKQTIPHFTLTDEVDVTELLALREELKEDAADEET-KLTFLPFLVKAVALALKKFPELNASWDGEEGEIVYKKYVNI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935098744 325 SVAVATPRGLVVPVIRNVETMNFADIERTINELGEKARKNELAIEDMDGGTFTISNGGVFGSLFGTPIINPPQSAILGMH 404
Cdd:pfam00198 80 GIAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVG 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1935098744 405 GIFDRPVAVGGKVEVRPMMYVALTYDHRLIDGREAVTFLRKIKAVVEDPRVML 457
Cdd:pfam00198 160 RIRKRPVVVDGEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELLL 212
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
74-146 |
3.08e-24 |
|
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: 95.55 E-value: 3.08e-24
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1935098744 74 ITINTPAFAESVTEGDV-RWEKAVGDTVAEDEVVCEIETDKTSVQVPSPAAGVIEALLVPDGGKVEGGTPLFKL 146
Cdd:cd06849 1 TEIKMPDLGESMTEGTIvEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
74-146 |
9.27e-23 |
|
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component [Energy production and conversion]; Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component is part of the Pathway/BioSystem: Pyruvate oxidation
Pssm-ID: 440274 [Multi-domain] Cd Length: 77 Bit Score: 91.67 E-value: 9.27e-23
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1935098744 74 ITINTPAFAESVTEGDV-RWEKAVGDTVAEDEVVCEIETDKTSVQVPSPAAGVIEALLVPDGGKVEGGTPLFKL 146
Cdd:COG0508 3 IEIKMPDLGESMTEGTIvEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| sucB |
TIGR01347 |
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ... |
74-460 |
0e+00 |
|
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: 579.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935098744 74 ITINTPAFAESVTEGDV-RWEKAVGDTVAEDEVVCEIETDKTSVQVPSPAAGVIEALLVPDGGKVEGGTPLFKLRKSGAA 152
Cdd:TIGR01347 1 IEIKVPELAESITEGTVaEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAILEEGNDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935098744 153 PTKAKPAVAPPAAAPAPEPVAAAVAPPAEPIPTMMPPVPPVSTQPIDTKPVSAVKPT-----------------AAPVAA 215
Cdd:TIGR01347 81 TAAPPAKSGEEKEETPAASAAAAPTAAANRPSLSPAARRLAKEHGIDLSAVPGTGVTgrvtkediikkteapasAQPPAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935098744 216 PGVEPGASKGARSEHRVKMNRMRQRIAQRLKEAQNTCAMLTTFNEIDMSNIQEMRARHRDSFQKKHNLKLGFMSAFVKAA 295
Cdd:TIGR01347 161 AAAAAAPAAATRPEERVKMTRLRQRIAERLKEAQNSTAMLTTFNEVDMSAVMELRKRYKEEFEKKHGVKLGFMSFFVKAV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935098744 296 AFALQEQPIVNAVIDDTtkEMVYRDYVDISVAVATPRGLVVPVIRNVETMNFADIERTINELGEKARKNELAIEDMDGGT 375
Cdd:TIGR01347 241 VAALKRFPEVNAEIDGD--DIVYKDYYDISVAVSTDRGLVVPVVRNADRMSFADIEKEIADLGKKARDGKLTLEDMTGGT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935098744 376 FTISNGGVFGSLFGTPIINPPQSAILGMHGIFDRPVAVGGKVEVRPMMYVALTYDHRLIDGREAVTFLRKIKAVVEDPRV 455
Cdd:TIGR01347 319 FTITNGGVFGSLMSTPIINPPQSAILGMHGIKERPVAVNGQIEIRPMMYLALSYDHRLIDGKEAVTFLVTIKELLEDPRR 398
|
....*
gi 1935098744 456 MLLDL 460
Cdd:TIGR01347 399 LLLDL 403
|
|
| PTZ00144 |
PTZ00144 |
dihydrolipoamide succinyltransferase; Provisional |
45-460 |
0e+00 |
|
dihydrolipoamide succinyltransferase; Provisional
Pssm-ID: 240289 [Multi-domain] Cd Length: 418 Bit Score: 546.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935098744 45 TNSSKLVVNTSSVFSVRYFRITAVCRD-------DVITINTPAFAESVTEGDV-RWEKAVGDTVAEDEVVCEIETDKTSV 116
Cdd:PTZ00144 9 LNKPLLSSVKGMFRRFSLRKLQPACSAhfsksyfSIKVIKVPTMGDSISEGTVvEWKKKVGDYVKEDEVICIIETDKVSV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935098744 117 QVPSPAAGVIEALLVPDGGKVEGGTPLFKLRKSGAAPtkakpavappaaapAPEPVAAAVAPPAEPIPTMMPPVPPVSTQ 196
Cdd:PTZ00144 89 DIRAPASGVITKIFAEEGDTVEVGAPLSEIDTGGAPP--------------AAAPAAAAAAKAEKTTPEKPKAAAPTPEP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935098744 197 PIDTKPVSA--VKPTAAPVAAPGVEPGASKGARSEHRVKMNRMRQRIAQRLKEAQNTCAMLTTFNEIDMSNIQEMRARHR 274
Cdd:PTZ00144 155 PAASKPTPPaaAKPPEPAPAAKPPPTPVARADPRETRVPMSRMRQRIAERLKASQNTCAMLTTFNECDMSALMELRKEYK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935098744 275 DSFQKKHNLKLGFMSAFVKAAAFALQEQPIVNAVIDdtTKEMVYRDYVDISVAVATPRGLVVPVIRNVETMNFADIERTI 354
Cdd:PTZ00144 235 DDFQKKHGVKLGFMSAFVKASTIALKKMPIVNAYID--GDEIVYRNYVDISVAVATPTGLVVPVIRNCENKSFAEIEKEL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935098744 355 NELGEKARKNELAIEDMDGGTFTISNGGVFGSLFGTPIINPPQSAILGMHGIFDRPVAVGGKVEVRPMMYVALTYDHRLI 434
Cdd:PTZ00144 313 ADLAEKARNNKLTLEDMTGGTFTISNGGVFGSLMGTPIINPPQSAILGMHAIKKRPVVVGNEIVIRPIMYLALTYDHRLI 392
|
410 420
....*....|....*....|....*.
gi 1935098744 435 DGREAVTFLRKIKAVVEDPRVMLLDL 460
Cdd:PTZ00144 393 DGRDAVTFLKKIKDLIEDPARMLLDL 418
|
|
| PRK05704 |
PRK05704 |
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase; |
74-460 |
2.95e-177 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
Pssm-ID: 235571 [Multi-domain] Cd Length: 407 Bit Score: 502.06 E-value: 2.95e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935098744 74 ITINTPAFAESVTEGDV-RWEKAVGDTVAEDEVVCEIETDKTSVQVPSPAAGVIEALLVPDGGKVEGGTPLFKLRKSGAA 152
Cdd:PRK05704 3 VEIKVPTLPESVTEATIaTWHKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGDTVTVGQVLGRIDEGAAA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935098744 153 PTKAKPAVAPPAAAPAPEPVAAAVAPPAEPIPTMMPPVPPVSTQPID-------------TKP--VSAVKPTAAPVAAPG 217
Cdd:PRK05704 83 GAAAAAAAAAAAAAAAPAQAQAAAAAEQSNDALSPAARKLAAENGLDasavkgtgkggrvTKEdvLAALAAAAAAPAAPA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935098744 218 VEPGASK----GARSEHRVKMNRMRQRIAQRLKEAQNTCAMLTTFNEIDMSNIQEMRARHRDSFQKKHNLKLGFMSAFVK 293
Cdd:PRK05704 163 AAAPAAApaplGARPEERVPMTRLRKTIAERLLEAQNTTAMLTTFNEVDMTPVMDLRKQYKDAFEKKHGVKLGFMSFFVK 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935098744 294 AAAFALQEQPIVNAVIDDTtkEMVYRDYVDISVAVATPRGLVVPVIRNVETMNFADIERTINELGEKARKNELAIEDMDG 373
Cdd:PRK05704 243 AVVEALKRYPEVNASIDGD--DIVYHNYYDIGIAVGTPRGLVVPVLRDADQLSFAEIEKKIAELAKKARDGKLSIEELTG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935098744 374 GTFTISNGGVFGSLFGTPIINPPQSAILGMHGIFDRPVAVGGKVEVRPMMYVALTYDHRLIDGREAVTFLRKIKAVVEDP 453
Cdd:PRK05704 321 GTFTITNGGVFGSLMSTPIINPPQSAILGMHKIKERPVAVNGQIVIRPMMYLALSYDHRIIDGKEAVGFLVTIKELLEDP 400
|
....*..
gi 1935098744 454 RVMLLDL 460
Cdd:PRK05704 401 ERLLLDL 407
|
|
| PLN02226 |
PLN02226 |
2-oxoglutarate dehydrogenase E2 component |
34-460 |
2.59e-128 |
|
2-oxoglutarate dehydrogenase E2 component
Pssm-ID: 177871 [Multi-domain] Cd Length: 463 Bit Score: 379.87 E-value: 2.59e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935098744 34 SGVSRSQGLAYTNSSklvvntssvfsvRYFRITAVCRDDVITINTPAFAESVTEGDV-RWEKAVGDTVAEDEVVCEIETD 112
Cdd:PLN02226 64 SGISRSASLVSSTLQ------------RWVRPFSSESGDTVEAVVPHMGESITDGTLaTFLKKPGERVQADEAIAQIETD 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935098744 113 KTSVQVPSPAAGVIEALLVPDGGKVEGGTPLFKLRKSGAAPTKAKPAVAPPAAAPAPEPVAAAVAPPAEPiptmmppvpp 192
Cdd:PLN02226 132 KVTIDIASPASGVIQEFLVKEGDTVEPGTKVAIISKSEDAASQVTPSQKIPETTDPKPSPPAEDKQKPKV---------- 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935098744 193 vSTQPIDTKPVSAVKPtaAPVAAPGVEPGASKGARsEHRVKMNRMRQRIAQRLKEAQNTCAMLTTFNEIDMSNIQEMRAR 272
Cdd:PLN02226 202 -ESAPVAEKPKAPSSP--PPPKQSAKEPQLPPKER-ERRVPMTRLRKRVATRLKDSQNTFALLTTFNEVDMTNLMKLRSQ 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935098744 273 HRDSFQKKHNLKLGFMSAFVKAAAFALQEQPIVNAVIDDttKEMVYRDYVDISVAVATPRGLVVPVIRNVETMNFADIER 352
Cdd:PLN02226 278 YKDAFYEKHGVKLGLMSGFIKAAVSALQHQPVVNAVIDG--DDIIYRDYVDISIAVGTSKGLVVPVIRGADKMNFAEIEK 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935098744 353 TINELGEKARKNELAIEDMDGGTFTISNGGVFGSLFGTPIINPPQSAILGMHGIFDRPVAVGGKVEVRPMMYVALTYDHR 432
Cdd:PLN02226 356 TINGLAKKANEGTISIDEMAGGSFTVSNGGVYGSLISTPIINPPQSAILGMHSIVSRPMVVGGSVVPRPMMYVALTYDHR 435
|
410 420
....*....|....*....|....*...
gi 1935098744 433 LIDGREAVTFLRKIKAVVEDPRVMLLDL 460
Cdd:PLN02226 436 LIDGREAVYFLRRVKDVVEDPQRLLLDI 463
|
|
| PRK11856 |
PRK11856 |
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed |
73-459 |
8.62e-111 |
|
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
Pssm-ID: 237001 [Multi-domain] Cd Length: 411 Bit Score: 332.91 E-value: 8.62e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935098744 73 VITINTPAFAESVTEGD-VRWEKAVGDTVAEDEVVCEIETDKTSVQVPSPAAGVIEALLVPDGGKVEGGTPLFKLRKSGA 151
Cdd:PRK11856 2 MFEFKMPDLGEGMTEGEiVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDVVPVGSVIAVIEEEGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935098744 152 APTKAKPAVAPPAAAPAPEPVAAAVAPPAEPIPTMMPPVPPVSTQ--P----------IDtkpVSAVKPT---------- 209
Cdd:PRK11856 82 AEAAAAAEAAPEAPAPEPAPAAAAAAAAAPAAAAAPAAPAAAAAKasPavrklarelgVD---LSTVKGSgpggritked 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935098744 210 ----------AAPVAAPGVEPGASKGARSEHRVKMNRMRQRIAQRLKEAQNTCAMLTTFNEIDMSNIQEMRARHrdsfqK 279
Cdd:PRK11856 159 veaaaaaaapAAAAAAAAAAAPPAAAAEGEERVPLSGMRKAIAKRMVESKREIPHFTLTDEVDVTALLALRKQL-----K 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935098744 280 KHNLKLGFMSAFVKAAAFALQEQPIVNAVIDDTTkeMVYRDYVDISVAVATPRGLVVPVIRNVETMNFADIERTINELGE 359
Cdd:PRK11856 234 AIGVKLTVTDFLIKAVALALKKFPELNASWDDDA--IVLKKYVNIGIAVATDGGLIVPVIRDADKKSLFELAREIKDLAE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935098744 360 KARKNELAIEDMDGGTFTISNGGVFGSLFGTPIINPPQSAILGMHGIFDRPVAVGGKVEVRPMMYVALTYDHRLIDGREA 439
Cdd:PRK11856 312 KAREGKLKPEELQGGTFTISNLGMFGGDYFTPIINPPEVAILGVGAIVERPVVVDGEIVVRKVMPLSLSFDHRVIDGADA 391
|
410 420
....*....|....*....|
gi 1935098744 440 VTFLRKIKAVVEDPRVMLLD 459
Cdd:PRK11856 392 ARFLKALKELLENPALLLLE 411
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
245-457 |
1.99e-96 |
|
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: 289.06 E-value: 1.99e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935098744 245 LKEAQNTCAMLTTFNEIDMSNIQEMRARHRDSFQKKHNlKLGFMSAFVKAAAFALQEQPIVNAVIDDTTKEMVYRDYVDI 324
Cdd:pfam00198 1 MTESKQTIPHFTLTDEVDVTELLALREELKEDAADEET-KLTFLPFLVKAVALALKKFPELNASWDGEEGEIVYKKYVNI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935098744 325 SVAVATPRGLVVPVIRNVETMNFADIERTINELGEKARKNELAIEDMDGGTFTISNGGVFGSLFGTPIINPPQSAILGMH 404
Cdd:pfam00198 80 GIAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVG 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1935098744 405 GIFDRPVAVGGKVEVRPMMYVALTYDHRLIDGREAVTFLRKIKAVVEDPRVML 457
Cdd:pfam00198 160 RIRKRPVVVDGEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELLL 212
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
84-458 |
2.21e-92 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 290.19 E-value: 2.21e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935098744 84 SVTEGDV-RWEKAVGDTVAEDEVVCEIETDKTSVQVPSPAAGVIEALLVPDGGKVEGGTPLFKLRKSGAAPTKAKPAVAP 162
Cdd:PRK11855 129 EITEVEViEWLVKVGDTVEEDQSLITVETDKATMEIPSPVAGVVKEIKVKVGDKVSVGSLLVVIEVAAAAPAAAAAPAAA 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935098744 163 PAAAPAPEPVAAAVAPPAEPIPTMMPPVPPVSTQPIDTKPV-----------SAVK------------------------ 207
Cdd:PRK11855 209 APAAAAAAAPAPAPAAAAAPAAAAPAAAAAPGKAPHASPAVrrlarelgvdlSQVKgtgkkgritkedvqafvkgamsaa 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935098744 208 --PTAAPVAAPGVEPGA--------SKGARSEhRVKMNRMRQRIAQRLKEAQNTCAMLTTFNEIDMSNIQEMRARHRDSF 277
Cdd:PRK11855 289 aaAAAAAAAAGGGGLGLlpwpkvdfSKFGEIE-TKPLSRIKKISAANLHRSWVTIPHVTQFDEADITDLEALRKQLKKEA 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935098744 278 QKKhNLKLGFMSAFVKAAAFALQEQPIVNAVIDDTTKEMVYRDYVDISVAVATPRGLVVPVIRNVETMNFADIERTINEL 357
Cdd:PRK11855 368 EKA-GVKLTMLPFFIKAVVAALKEFPVFNASLDEDGDELTYKKYFNIGFAVDTPNGLVVPVIKDVDKKSLLEIAREIAEL 446
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935098744 358 GEKARKNELAIEDMDGGTFTISNGGVFGSLFGTPIINPPQSAILGMHGIFDRPVAVGGKVEVRPMMYVALTYDHRLIDGR 437
Cdd:PRK11855 447 AKKARDGKLKPDDMQGGCFTISSLGGIGGTAFTPIINAPEVAILGVGKSQMKPVWDGKEFVPRLMLPLSLSYDHRVIDGA 526
|
410 420
....*....|....*....|.
gi 1935098744 438 EAVTFLRKIKAVVEDPRVMLL 458
Cdd:PRK11855 527 TAARFTNYLKQLLADPRRMLL 547
|
|
| SucB_Actino |
TIGR02927 |
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model ... |
76-452 |
1.28e-81 |
|
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: 263.03 E-value: 1.28e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935098744 76 INTPAFAESVTEGDV-RWEKAVGDTVAEDEVVCEIETDKTSVQVPSPAAGVIEALLVPDGGKVEGGTPLFKLRKSGAAPT 154
Cdd:TIGR02927 129 VKMPELGESVTEGTVtSWLKAVGDTVEVDEPLLEVSTDKVDTEIPSPVAGTLLEIRAPEDDTVEVGTVLAIIGDANAAPA 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935098744 155 KAKPAVAPPAAAPAPEPVAAAVAPPAEPI--PTMMPPVPPVSTQPIDTKPVS---------------------------- 204
Cdd:TIGR02927 209 EPAEEEAPAPSEAGSEPAPDPAARAPHAApdPPAPAPAPAKTAAPAAAAPVSsgdsgpyvtplvrklakdkgvdlstvkg 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935098744 205 ------------------AVKPTAAPVA-APGVEPGASKGARSEHRV----------KMNRMRQRIAQRLKEAQNTCAML 255
Cdd:TIGR02927 289 tgvggrirkqdvlaaakaAEEARAAAAApAAAAAPAAPAAAAKPAEPdtaklrgttqKMNRIRQITADKTIESLQTSAQL 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935098744 256 TTFNEIDMSNIQEMRARHRDSFQKKHNLKLGFMSAFVKAAAFALQEQPIVNAVIDDTTKEMVYRDYVDISVAVATPRGLV 335
Cdd:TIGR02927 369 TQVHEVDMTRVAALRARAKNDFLEKNGVNLTFLPFFVQAVTEALKAHPNVNASYNAETKEVTYHDVEHVGIAVDTPRGLL 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935098744 336 VPVIRNVETMNFADIERTINELGEKARKNELAIEDMDGGTFTISNGGVFGSLFGTPIINPPQSAILGMHGIFDRPVAV-- 413
Cdd:TIGR02927 449 VPVIHNAGDLSLPGLAKAINDLAARARDNKLKPDELSGGTFTITNIGSGGALFDTPILNPPQAAILGTGAIVKRPRVIkd 528
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1935098744 414 ---GGKVEVRPMMYVALTYDHRLIDGREAVTFLRKIKAVVED 452
Cdd:TIGR02927 529 edgGESIAIRSVCYLPLTYDHRLVDGADAGRFLTTIKKRLEE 570
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
85-458 |
3.07e-71 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 237.21 E-value: 3.07e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935098744 85 VTEGDV-RWEKAVGDTVAEDEVVCEIETDKTSVQVPSPAAGVIEALLVPDGGKVEGGTPLFKLRKSGAAPTKAKPAVAPP 163
Cdd:PRK11854 216 GDEVEVtEVMVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVKTGSLIMRFEVEGAAPAAAPAKQEAA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935098744 164 AAAPAPEPVAAAVAPPAEPIPTMMPPVPPVSTqpIDTKPV------------SAVKPT-------------AAPVAAPGV 218
Cdd:PRK11854 296 APAPAAAKAEAPAAAPAAKAEGKSEFAENDAY--VHATPLvrrlarefgvnlAKVKGTgrkgrilkedvqaYVKDAVKRA 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935098744 219 EPGASKGARSEHR-------------------VKMNRMRQRIAQRLKEAQNTCAMLTTFNEIDMSNIQEMR-ARHRDSFQ 278
Cdd:PRK11854 374 EAAPAAAAAGGGGpgllpwpkvdfskfgeieeVELGRIQKISGANLHRNWVMIPHVTQFDKADITELEAFRkQQNAEAEK 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935098744 279 KKHNLKLGFMSAFVKAAAFALQEQPIVNAVIDDTTKEMVYRDYVDISVAVATPRGLVVPVIRNVETMNFADIERTINELG 358
Cdd:PRK11854 454 RKLGVKITPLVFIMKAVAAALEQMPRFNSSLSEDGQRLTLKKYVNIGIAVDTPNGLVVPVFKDVNKKGIIELSRELMDIS 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935098744 359 EKARKNELAIEDMDGGTFTISNGGVFGSLFGTPIINPPQSAILGMHGIFDRPVAVGGKVEVRPMMYVALTYDHRLIDGRE 438
Cdd:PRK11854 534 KKARDGKLTAGDMQGGCFTISSIGGLGTTHFTPIVNAPEVAILGVSKSAMEPVWNGKEFAPRLMLPLSLSYDHRVIDGAD 613
|
410 420
....*....|....*....|
gi 1935098744 439 AVTFLRKIKAVVEDPRVMLL 458
Cdd:PRK11854 614 GARFITIINDRLSDIRRLVL 633
|
|
| PDHac_trf_mito |
TIGR01349 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
76-458 |
4.00e-58 |
|
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: 197.71 E-value: 4.00e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935098744 76 INTPAFAESVTEGD-VRWEKAVGDTVAEDEVVCEIETDKTSVQVPSPAAGVIEALLVPDGGK-VEGGTPLFKLRKSGAAP 153
Cdd:TIGR01349 2 ITMPALSPTMTTGNlAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEGTKdVPVNKPIAVLVEEKEDV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935098744 154 TKAKPAVAPPAAAPAPEPVAAAVAPPAEPIPTMMPPVPPVSTQPIDTKPVS----------------------------- 204
Cdd:TIGR01349 82 ADAFKNYKLESSASPAPKPSEIAPTAPPSAPKPSPAPQKQSPEPSSPAPLSdkesgdrifasplakklakekgidlsava 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935098744 205 -----------------AVKPTAAPVAAPGVEPGASKGAR-----SEHRVKMNRMRQRIAQRLKEAQNTCAMLTTFNEID 262
Cdd:TIGR01349 162 gsgpngrivkkdiesfvPQSPASANQQAAATTPATYPAAApvstgSYEDVPLSNIRKIIAKRLLESKQTIPHYYVSIECN 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935098744 263 MSNIQEMRARHRDSFQKKHnlKLGFMSAFVKAAAFALQEQPIVNAVIDDTTkeMVYRDYVDISVAVATPRGLVVPVIRNV 342
Cdd:TIGR01349 242 VDKLLALRKELNAMASEVY--KLSVNDFIIKASALALREVPEANSSWTDNF--IRRYKNVDISVAVATPDGLITPIVRNA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935098744 343 ETMNFADIERTINELGEKARKNELAIEDMDGGTFTISNGGVFGSLFGTPIINPPQSAILGMHGIFDRPVAVGGK---VEV 419
Cdd:TIGR01349 318 DAKGLSTISNEIKDLAKRARNNKLKPEEFQGGTFTISNLGMFGIKDFTAIINPPQACILAVGAVEDVAVVDNDEekgFAV 397
|
410 420 430
....*....|....*....|....*....|....*....
gi 1935098744 420 RPMMYVALTYDHRLIDGREAVTFLRKIKAVVEDPRVMLL 458
Cdd:TIGR01349 398 ASIMSVTLSCDHRVIDGAVGAEFLKSFKKYLENPIEMLL 436
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
96-458 |
7.08e-58 |
|
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model describes a subset of pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase specifically close by both phylogenetic and per cent identity (UPGMA) trees. Members of this set include two or three copies of the lipoyl-binding domain. E. coli AceF is a member of this model, while mitochondrial and some other bacterial forms belong to a separate model. [Energy metabolism, Pyruvate dehydrogenase]
Pssm-ID: 273566 [Multi-domain] Cd Length: 546 Bit Score: 199.72 E-value: 7.08e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935098744 96 VGDTVAEDEVVCEIETDKTSVQVPSPAAGVIEALLVPDGGKVEGGTPLFKLRKSGAAPTKAKPAVAPPAAAPAPEPVAAA 175
Cdd:TIGR01348 139 VGDTVSADQSLITLESDKASMEVPAPASGVVKSVKVKVGDSVPTGDLILTLSVAGSTPATAPAPASAQPAAQSPAATQPE 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935098744 176 VAPPAEPIPTMMPPVPPVSTQPIDTKP----------------VSAVKPT-----------------------AAPVAAP 216
Cdd:TIGR01348 219 PAAAPAAAKAQAPAPQQAGTQNPAKVDhaapavrrlarefgvdLSAVKGTgikgrilredvqrfvkepsvraqAAAASAA 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935098744 217 GVEPGA--------SKGARSEhRVKMNRMRQRIAQRLKEAQNTCAMLTTFNEIDMSNIQEMRARhRDSFQKKHNLKLGFM 288
Cdd:TIGR01348 299 GGAPGAlpwpnvdfSKFGEVE-EVDMSRIRKISGANLTRNWTMIPHVTHFDKADITEMEAFRKQ-QNAAVEKEGVKLTVL 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935098744 289 SAFVKAAAFALQEQPIVNAVIDDTTKEMVYRDYVDISVAVATPRGLVVPVIRNVETMNFADIERTINELGEKARKNELAI 368
Cdd:TIGR01348 377 HILMKAVAAALKKFPKFNASLDLGGEQLILKKYVNIGVAVDTPNGLLVPVIKDVDRKGITELALELSDLAKKARDGKLTP 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935098744 369 EDMDGGTFTISN-GGVFGSLFgTPIINPPQSAILGMHGIFDRPVAVGGKVEVRPMMYVALTYDHRLIDGREAVTFLRKIK 447
Cdd:TIGR01348 457 DEMQGACFTISSlGGIGGTAF-TPIVNAPEVAILGVSKSGMEPVWNGKEFEPRLMLPLSLSYDHRVIDGADAARFTTYIC 535
|
410
....*....|.
gi 1935098744 448 AVVEDPRVMLL 458
Cdd:TIGR01348 536 ESLADIRRLLL 546
|
|
| PRK11857 |
PRK11857 |
dihydrolipoamide acetyltransferase; Reviewed |
194-456 |
3.49e-56 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237002 [Multi-domain] Cd Length: 306 Bit Score: 188.46 E-value: 3.49e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935098744 194 STQPIDTKPVSAVKPTAAPVAAPgvepgASKGARSEhrvKMNRMRQRIAQRLKEAQNTCAMLTTFNEIDMSNIQEMRARH 273
Cdd:PRK11857 49 PAEAASVSSAQQAAKTAAPAAAP-----PKLEGKRE---KVAPIRKAIARAMTNSWSNVAYVNLVNEIDMTKLWDLRKSV 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935098744 274 RDSFQKKHNLKLGFMSAFVKAAAFALQEQPIVNAVIDDTTKEMVYRDYVDISVAVATPRGLVVPVIRNVETMNFADIERT 353
Cdd:PRK11857 121 KDPVLKTEGVKLTFLPFIAKAILIALKEFPIFAAKYDEATSELVYPDTLNLGIAVDTEAGLMVPVIKNAQKLSIVEIAKE 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935098744 354 INELGEKARKNELAIEDMDGGTFTISNGGVFGSLFGTPIINPPQSAILGMHGIFDRPVAVGGKVEVRPMMYVALTYDHRL 433
Cdd:PRK11857 201 ISRLAKAARERKIKPDEMKGGSFTITNYGSVGSLYGVPVINYPELAIAGVGAIIDKAIVKNGQIVAGKVMHLTVAADHRW 280
|
250 260
....*....|....*....|...
gi 1935098744 434 IDGREAVTFLRKIKAVVEDPRVM 456
Cdd:PRK11857 281 IDGATIGRFASRVKELLEKPEIL 303
|
|
| PRK14843 |
PRK14843 |
dihydrolipoamide acetyltransferase; Provisional |
204-458 |
7.44e-42 |
|
dihydrolipoamide acetyltransferase; Provisional
Pssm-ID: 184847 [Multi-domain] Cd Length: 347 Bit Score: 151.98 E-value: 7.44e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935098744 204 SAVKPTAAPVAAPGVEPGASKGARSEhRVKMNRMRQRIAQRLKEAQNTCAMLTTFNEIDMSNIQEMRARHRDSFQKKHNL 283
Cdd:PRK14843 94 DSIKSPAQIEKVEEVPDNVTPYGEIE-RIPMTPMRKVIAQRMVESYLTAPTFTLNYEVDMTEMLALRKKVLEPIMEATGK 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935098744 284 KLGFMSAFVKAAAFALQEQPIVNAVIDDTTKEMVYRDYVDISVAVATPRGLVVPVIRNVETMNFADIERTINELGEKARK 363
Cdd:PRK14843 173 KTTVTDLLSLAVVKTLMKHPYINASLTEDGKTIITHNYVNLAMAVGMDNGLMTPVVYNAEKMSLSELVVAFKDVIGRTLD 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935098744 364 NELAIEDMDGGTFTISNGGVFG-SLFGtPIINPPQSAILGMHGIFDRPVAVGGKVEVRPMMYVALTYDHRLIDGREAVTF 442
Cdd:PRK14843 253 GKLAPSELQNSTFTISNLGMFGvQSFG-PIINQPNSAILGVSSTIEKPVVVNGEIVIRPIMSLGLTIDHRVVDGMAGAKF 331
|
250
....*....|....*.
gi 1935098744 443 LRKIKAVVEDPRVMLL 458
Cdd:PRK14843 332 MKDLKELIETPISMLI 347
|
|
| PLN02744 |
PLN02744 |
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex |
76-458 |
4.83e-41 |
|
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
Pssm-ID: 215397 [Multi-domain] Cd Length: 539 Bit Score: 153.86 E-value: 4.83e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935098744 76 INTPAFAESVTEGDV-RWEKAVGDTVAEDEVVCEIETDKTSVQVPSPAAGVIEALLVPDGGK-----------VEGGTPL 143
Cdd:PLN02744 115 IGMPSLSPTMTEGNIaRWLKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVKGDGAKeikvgeviaitVEEEEDI 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935098744 144 FKLR-----KSGAAPTKAKPAVAPPAAAPAPEPVAAAVAPPAEPIPTMMPPVPPVSTQPIDTK-------PVSAVKPTA- 210
Cdd:PLN02744 195 GKFKdykpsSSAAPAAPKAKPSPPPPKEEEVEKPASSPEPKASKPSAPPSSGDRIFASPLARKlaednnvPLSSIKGTGp 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935098744 211 ----------APVAAPGVEPGASKGARSEH------RVKMNRMRQRIAQRLKEAQNTCA--MLTTFNEIDmsNIQEMRAR 272
Cdd:PLN02744 275 dgrivkadieDYLASGGKGATAPPSTDSKApaldytDIPNTQIRKVTASRLLQSKQTIPhyYLTVDTRVD--KLMALRSQ 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935098744 273 HRDSFQKKHNLKLGFMSAFVKAAAFALQEQPIVNAvidDTTKEMVyRDY--VDISVAVATPRGLVVPVIRNVETMNFADI 350
Cdd:PLN02744 353 LNSLQEASGGKKISVNDLVIKAAALALRKVPQCNS---SWTDDYI-RQYhnVNINVAVQTENGLYVPVVKDADKKGLSTI 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935098744 351 ERTINELGEKARKNELAIEDMDGGTFTISN-GGVFGSLFGTPIINPPQSAILGMhGIFDRPVAVG---GKVEVRPMMYVA 426
Cdd:PLN02744 429 AEEVKQLAQKARENSLKPEDYEGGTFTVSNlGGPFGIKQFCAIINPPQSAILAV-GSAEKRVIPGsgpDQYNFASFMSVT 507
|
410 420 430
....*....|....*....|....*....|..
gi 1935098744 427 LTYDHRLIDGREAVTFLRKIKAVVEDPRVMLL 458
Cdd:PLN02744 508 LSCDHRVIDGAIGAEWLKAFKGYIENPESMLL 539
|
|
| PLN02528 |
PLN02528 |
2-oxoisovalerate dehydrogenase E2 component |
260-460 |
4.32e-39 |
|
2-oxoisovalerate dehydrogenase E2 component
Pssm-ID: 215289 [Multi-domain] Cd Length: 416 Bit Score: 146.02 E-value: 4.32e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935098744 260 EIDMSNIQEMRaRHRDSFQKKHNLKLGFMSAFVKAAAFALQEQPIVNAVIDDTTKEMVYRDYVDISVAVATPRGLVVPVI 339
Cdd:PLN02528 215 EINVDALVELK-ASFQENNTDPTVKHTFLPFLIKSLSMALSKYPLLNSCFNEETSEIRLKGSHNIGVAMATEHGLVVPNI 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935098744 340 RNVETMNFADIERTINELGEKARKNELAIEDMDGGTFTISNGGVFGSLFGTPIINPPQSAILGMHGIFDRPVAVG-GKVE 418
Cdd:PLN02528 294 KNVQSLSLLEITKELSRLQHLAAENKLNPEDITGGTITLSNIGAIGGKFGSPVLNLPEVAIIALGRIQKVPRFVDdGNVY 373
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1935098744 419 VRPMMYVALTYDHRLIDGREAVTFLRKIKAVVEDPRVMLLDL 460
Cdd:PLN02528 374 PASIMTVTIGADHRVLDGATVARFCNEWKSYVEKPELLMLHM 415
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
74-146 |
3.08e-24 |
|
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: 95.55 E-value: 3.08e-24
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1935098744 74 ITINTPAFAESVTEGDV-RWEKAVGDTVAEDEVVCEIETDKTSVQVPSPAAGVIEALLVPDGGKVEGGTPLFKL 146
Cdd:cd06849 1 TEIKMPDLGESMTEGTIvEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
74-146 |
9.27e-23 |
|
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component [Energy production and conversion]; Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component is part of the Pathway/BioSystem: Pyruvate oxidation
Pssm-ID: 440274 [Multi-domain] Cd Length: 77 Bit Score: 91.67 E-value: 9.27e-23
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1935098744 74 ITINTPAFAESVTEGDV-RWEKAVGDTVAEDEVVCEIETDKTSVQVPSPAAGVIEALLVPDGGKVEGGTPLFKL 146
Cdd:COG0508 3 IEIKMPDLGESMTEGTIvEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
75-146 |
1.09e-22 |
|
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: 91.12 E-value: 1.09e-22
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1935098744 75 TINTPAFAESVTEGDVRWEKAVGDTVAEDEVVCEIETDKTSVQVPSPAAGVIEALLVPDGGKVEGGTPLFKL 146
Cdd:pfam00364 2 EIKSPMIGESVREGVVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
|
|
| kgd |
PRK12270 |
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ... |
194-446 |
4.31e-18 |
|
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;
Pssm-ID: 237030 [Multi-domain] Cd Length: 1228 Bit Score: 87.25 E-value: 4.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935098744 194 STQPIDTKPVSAVKPTAAPVAAPGVEPGASKGARSEHRVkmnrMRQrIAQRLkeAQNTCAML-----TTFNEIDMS---- 264
Cdd:PRK12270 81 AAPPKPAAAAAAAAAPAAPPAAAAAAAPAAAAVEDEVTP----LRG-AAAAV--AKNMDASLevptaTSVRAVPAKllid 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935098744 265 N---IQEMRARHRD---SFQkkHnlKLGFmsAFVKAaafaLQEQPIVNAVID--DTTKEMVYRDYVDISVAVATP----- 331
Cdd:PRK12270 154 NrivINNHLKRTRGgkvSFT--H--LIGY--ALVQA----LKAFPNMNRHYAevDGKPTLVTPAHVNLGLAIDLPkkdgs 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935098744 332 RGLVVPVIRNVETMNFADIERTINELGEKARKNELAIEDMDGGTFTISNGGVFGSLFGTPIINPPQSAILGMhGIFDRPV 411
Cdd:PRK12270 224 RQLVVPAIKGAETMDFAQFWAAYEDIVRRARDGKLTADDFQGTTISLTNPGGIGTVHSVPRLMKGQGAIIGV-GAMEYPA 302
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1935098744 412 AVGGKVE-------VRPMMYVALTYDHRLIDGREAVTFLRKI 446
Cdd:PRK12270 303 EFQGASEerlaelgISKVMTLTSTYDHRIIQGAESGEFLRTI 344
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
75-146 |
2.74e-16 |
|
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: 73.24 E-value: 2.74e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1935098744 75 TINTPAFAESVTEGDV-RWEKAVGDTVAEDEVVCEIETDKTSVQVPSPAAGVIEALLVPDGGKVEGGTPLFKL 146
Cdd:cd06663 1 TILIPDLAQHLGDGTVvKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKVEGDTPLVKI 73
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
74-153 |
4.85e-12 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 68.11 E-value: 4.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935098744 74 ITINTPAFAesVTEGDV-RWEKAVGDTVAEDEVVCEIETDKTSVQVPSPAAGVIEALLVPDGGKVEGGTPLFKLRKSGAA 152
Cdd:PRK11854 3 IEIKVPDIG--ADEVEVtEILVKVGDKVEAEQSLITVEGDKASMEVPSPQAGVVKEIKVKVGDKVETGALIMIFESADGA 80
|
.
gi 1935098744 153 P 153
Cdd:PRK11854 81 A 81
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
90-146 |
6.64e-11 |
|
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all biotin-dependent enzymes, such as acetyl-CoA carboxylase, pyruvate carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA carboxylase, geranyl-CoA carboxylase, oxaloacetate decarboxylase, methylmalonyl-CoA decarboxylase, transcarboxylase and urea amidolyase. This domain functions in transferring CO2 from one subsite to another, allowing carboxylation, decarboxylation, or transcarboxylation. During this process, biotin is covalently attached to a specific lysine.
Pssm-ID: 133459 [Multi-domain] Cd Length: 67 Bit Score: 57.81 E-value: 6.64e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1935098744 90 VRWEKAVGDTVAEDEVVCEIETDKTSVQVPSPAAGVIEALLVPDGGKVEGGTPLFKL 146
Cdd:cd06850 11 VKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| AccB |
COG0511 |
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ... |
96-147 |
3.42e-10 |
|
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440277 [Multi-domain] Cd Length: 136 Bit Score: 57.98 E-value: 3.42e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1935098744 96 VGDTVAEDEVVCEIETDKTSVQVPSPAAGVIEALLVPDGGKVEGGTPLFKLR 147
Cdd:COG0511 85 VGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVVEILVENGQPVEYGQPLFVIE 136
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
72-143 |
3.63e-09 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 58.42 E-value: 3.63e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1935098744 72 DVITINTPAFAESVTEGDV-RWEKAVGDTVAEDEVVCEIETDKTSVQVPSPAAGVIEALLVPDGGKVEGGTPL 143
Cdd:PRK14875 1 SITPITMPKWGLSMTEGKVaGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGETLPVGALL 73
|
|
| PRK07051 |
PRK07051 |
biotin carboxyl carrier domain-containing protein; |
94-146 |
1.98e-06 |
|
biotin carboxyl carrier domain-containing protein;
Pssm-ID: 180811 [Multi-domain] Cd Length: 80 Bit Score: 45.39 E-value: 1.98e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1935098744 94 KAVGDTVAEDEVVCEIETDKTSVQVPSPAAGVIEALLVPDGGKVEGGTPLFKL 146
Cdd:PRK07051 26 VEVGDAVAAGDVVGLIEVMKQFTEVEAEAAGRVVEFLVEDGEPVEAGQVLARI 78
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
74-142 |
2.57e-06 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 49.53 E-value: 2.57e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1935098744 74 ITINTPAFAESVTEGDV-RWEKAVGDTVAEDEVVCEIETDKTSVQVPSPAAGVIEALLVPDGGK-VEGGTP 142
Cdd:PRK11892 3 IEILMPALSPTMEEGTLaKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKILVPEGTEgVKVNTP 73
|
|
| PRK09282 |
PRK09282 |
pyruvate carboxylase subunit B; Validated |
96-148 |
3.40e-05 |
|
pyruvate carboxylase subunit B; Validated
Pssm-ID: 236449 [Multi-domain] Cd Length: 592 Bit Score: 46.37 E-value: 3.40e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1935098744 96 VGDTVAEDEVVCEIETDKTSVQVPSPAAGVIEALLVPDGGKVEGGTPLFKLRK 148
Cdd:PRK09282 540 EGDKVKAGDTVLVLEAMKMENEIQAPVDGTVKEILVKEGDRVNPGDVLMEIEP 592
|
|
| GCS_H |
cd06848 |
Glycine cleavage H-protein. Glycine cleavage H-proteins are part of the glycine cleavage ... |
94-128 |
8.04e-04 |
|
Glycine cleavage H-protein. Glycine cleavage H-proteins are part of the glycine cleavage system (GCS) found in bacteria, archea and the mitochondria of eukaryotes. GCS is a multienzyme complex consisting of 4 different components (P-, H-, T- and L-proteins) which catalyzes the oxidative cleavage of glycine. The H-protein shuttles the methylamine group of glycine from the P-protein (glycine dehydrogenase) to the T-protein (aminomethyltransferase) via a lipoyl group, attached to a completely conserved lysine residue.
Pssm-ID: 133457 [Multi-domain] Cd Length: 96 Bit Score: 38.67 E-value: 8.04e-04
10 20 30
....*....|....*....|....*....|....*
gi 1935098744 94 KAVGDTVAEDEVVCEIETDKTSVQVPSPAAGVIEA 128
Cdd:cd06848 37 PEVGTEVKKGDPFGSVESVKAASDLYSPVSGEVVE 71
|
|
| |
