|
Name |
Accession |
Description |
Interval |
E-value |
| PDHac_trf_mito |
TIGR01349 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
1-440 |
2.28e-138 |
|
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: 403.79 E-value: 2.28e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 1 MPSLSPTMEEGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEGSKNIRLGALIGLLVEEGED--- 77
Cdd:TIGR01349 4 MPALSPTMTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEGTKDVPVNKPIAVLVEEKEDvad 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 78 ----------WKHVEIPKDVGPPSPASKPSVPcPSPEPQI---STAVEKEHIPGKLQFRLSPAARNILEKHSLDASQGTA 144
Cdd:TIGR01349 84 afknyklessASPAPKPSEIAPTAPPSAPKPS-PAPQKQSpepSSPAPLSDKESGDRIFASPLAKKLAKEKGIDLSAVAG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 145 TGPRGIFTKEDALKLVqlketgkitESRPTPAPlatpavplpPQAMATPPYTRPMIPPVSTpgqpnvvGTFTEIPASNIR 224
Cdd:TIGR01349 163 SGPNGRIVKKDIESFV---------PQSPASAN---------QQAAATTPATYPAAAPVST-------GSYEDVPLSNIR 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 225 RVIAKRLTESKSTVPHAYATTDCDLGAVLKARQSL---VRDDIKVSVNDFIIKAAAVTLKQMPDVNVSWDGEGPKQLPFI 301
Cdd:TIGR01349 218 KIIAKRLLESKQTIPHYYVSIECNVDKLLALRKELnamASEVYKLSVNDFIIKASALALREVPEANSSWTDNFIRRYKNV 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 302 DISVAVATDKGLITPIIKDAAAKGIREIADSVKALSKKARDGKLLPEEYQGGSFSISNLGMFGIDEFTAVINPPQACILA 381
Cdd:TIGR01349 298 DISVAVATPDGLITPIVRNADAKGLSTISNEIKDLAKRARNNKLKPEEFQGGTFTISNLGMFGIKDFTAIINPPQACILA 377
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1435033878 382 VGRFRPVLKLTRDEEgnAQLQRHQLITVTMSSDSRVVDDELATRFLESFKANLENPIRL 440
Cdd:TIGR01349 378 VGAVEDVAVVDNDEE--KGFAVASIMSVTLSCDHRVIDGAVGAEFLKSFKKYLENPIEM 434
|
|
| PRK11856 |
PRK11856 |
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed |
1-440 |
4.09e-134 |
|
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
Pssm-ID: 237001 [Multi-domain] Cd Length: 411 Bit Score: 391.85 E-value: 4.09e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 1 MPSLSPTMEEGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEGSKnIRLGALIGLLVEEGEdwKH 80
Cdd:PRK11856 7 MPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDV-VPVGSVIAVIEEEGE--AE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 81 VEIPKDVGPPSPASKPSVPCPSPEPQISTAVEKEHIPGKLQFRLSPAARNILEKHSLDASQGTATGPRGIFTKEDALKLV 160
Cdd:PRK11856 84 AAAAAEAAPEAPAPEPAPAAAAAAAAAPAAAAAPAAPAAAAAKASPAVRKLARELGVDLSTVKGSGPGGRITKEDVEAAA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 161 qlketgkiteSRPTPAPLATPAVPLPPQAMATPPYTRpmippvstpgqpnvvgtfteIPASNIRRVIAKRLTESKSTVPH 240
Cdd:PRK11856 164 ----------AAAAPAAAAAAAAAAAPPAAAAEGEER--------------------VPLSGMRKAIAKRMVESKREIPH 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 241 AYATTDCDLGAVLKARQSLVRDDIKVSVNDFIIKAAAVTLKQMPDVNVSWDGEGPKQLPFIDISVAVATDKGLITPIIKD 320
Cdd:PRK11856 214 FTLTDEVDVTALLALRKQLKAIGVKLTVTDFLIKAVALALKKFPELNASWDDDAIVLKKYVNIGIAVATDGGLIVPVIRD 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 321 AAAKGIREIADSVKALSKKARDGKLLPEEYQGGSFSISNLGMFGIDEFTAVINPPQACILAVGRF--RPVLKltrdeegN 398
Cdd:PRK11856 294 ADKKSLFELAREIKDLAEKAREGKLKPEELQGGTFTISNLGMFGGDYFTPIINPPEVAILGVGAIveRPVVV-------D 366
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1435033878 399 AQLQRHQLITVTMSSDSRVVDDELATRFLESFKANLENPIRL 440
Cdd:PRK11856 367 GEIVVRKVMPLSLSFDHRVIDGADAARFLKALKELLENPALL 408
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
231-440 |
3.42e-82 |
|
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: 252.08 E-value: 3.42e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 231 LTESKSTVPHAYATTDCDLGAVLKARQSL----VRDDIKVSVNDFIIKAAAVTLKQMPDVNVSWDGEGPK--QLPFIDIS 304
Cdd:pfam00198 1 MTESKQTIPHFTLTDEVDVTELLALREELkedaADEETKLTFLPFLVKAVALALKKFPELNASWDGEEGEivYKKYVNIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 305 VAVATDKGLITPIIKDAAAKGIREIADSVKALSKKARDGKLLPEEYQGGSFSISNLGMFGIDEFTAVINPPQACILAVGR 384
Cdd:pfam00198 81 IAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVGR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1435033878 385 --FRPVLKltrdeegNAQLQRHQLITVTMSSDSRVVDDELATRFLESFKANLENPIRL 440
Cdd:pfam00198 161 irKRPVVV-------DGEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELL 211
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
1-71 |
4.07e-26 |
|
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. 2-oxo acid dehydrogenase multienzyme complexes, like pyruvate dehydrogenase (PDH), 2-oxoglutarate dehydrogenase (OGDH) and branched-chain 2-oxo acid dehydrogenase (BCDH), contain at least three different enzymes, 2-oxo acid dehydrogenase (E1), dihydrolipoyl acyltransferase (E2) and dihydrolipoamide dehydrogenase (E3) and play a key role in redox regulation. E2, the central component of the complex, catalyzes the transfer of the acyl group of CoA from E1 to E3 via reductive acetylation of a lipoyl group covalently attached to a lysine residue.
Pssm-ID: 133458 [Multi-domain] Cd Length: 74 Bit Score: 100.56 E-value: 4.07e-26
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1435033878 1 MPSLSPTMEEGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEGSKnIRLGALIGLL 71
Cdd:cd06849 5 MPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDT-VPVGQVIAVI 74
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
1-72 |
2.82e-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: 92.82 E-value: 2.82e-23
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1435033878 1 MPSLSPTMEEGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEGSKnIRLGALIGLLV 72
Cdd:COG0508 7 MPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDT-VPVGAVIAVIA 77
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| PDHac_trf_mito |
TIGR01349 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
1-440 |
2.28e-138 |
|
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: 403.79 E-value: 2.28e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 1 MPSLSPTMEEGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEGSKNIRLGALIGLLVEEGED--- 77
Cdd:TIGR01349 4 MPALSPTMTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEGTKDVPVNKPIAVLVEEKEDvad 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 78 ----------WKHVEIPKDVGPPSPASKPSVPcPSPEPQI---STAVEKEHIPGKLQFRLSPAARNILEKHSLDASQGTA 144
Cdd:TIGR01349 84 afknyklessASPAPKPSEIAPTAPPSAPKPS-PAPQKQSpepSSPAPLSDKESGDRIFASPLAKKLAKEKGIDLSAVAG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 145 TGPRGIFTKEDALKLVqlketgkitESRPTPAPlatpavplpPQAMATPPYTRPMIPPVSTpgqpnvvGTFTEIPASNIR 224
Cdd:TIGR01349 163 SGPNGRIVKKDIESFV---------PQSPASAN---------QQAAATTPATYPAAAPVST-------GSYEDVPLSNIR 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 225 RVIAKRLTESKSTVPHAYATTDCDLGAVLKARQSL---VRDDIKVSVNDFIIKAAAVTLKQMPDVNVSWDGEGPKQLPFI 301
Cdd:TIGR01349 218 KIIAKRLLESKQTIPHYYVSIECNVDKLLALRKELnamASEVYKLSVNDFIIKASALALREVPEANSSWTDNFIRRYKNV 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 302 DISVAVATDKGLITPIIKDAAAKGIREIADSVKALSKKARDGKLLPEEYQGGSFSISNLGMFGIDEFTAVINPPQACILA 381
Cdd:TIGR01349 298 DISVAVATPDGLITPIVRNADAKGLSTISNEIKDLAKRARNNKLKPEEFQGGTFTISNLGMFGIKDFTAIINPPQACILA 377
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1435033878 382 VGRFRPVLKLTRDEEgnAQLQRHQLITVTMSSDSRVVDDELATRFLESFKANLENPIRL 440
Cdd:TIGR01349 378 VGAVEDVAVVDNDEE--KGFAVASIMSVTLSCDHRVIDGAVGAEFLKSFKKYLENPIEM 434
|
|
| PRK11856 |
PRK11856 |
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed |
1-440 |
4.09e-134 |
|
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
Pssm-ID: 237001 [Multi-domain] Cd Length: 411 Bit Score: 391.85 E-value: 4.09e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 1 MPSLSPTMEEGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEGSKnIRLGALIGLLVEEGEdwKH 80
Cdd:PRK11856 7 MPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDV-VPVGSVIAVIEEEGE--AE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 81 VEIPKDVGPPSPASKPSVPCPSPEPQISTAVEKEHIPGKLQFRLSPAARNILEKHSLDASQGTATGPRGIFTKEDALKLV 160
Cdd:PRK11856 84 AAAAAEAAPEAPAPEPAPAAAAAAAAAPAAAAAPAAPAAAAAKASPAVRKLARELGVDLSTVKGSGPGGRITKEDVEAAA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 161 qlketgkiteSRPTPAPLATPAVPLPPQAMATPPYTRpmippvstpgqpnvvgtfteIPASNIRRVIAKRLTESKSTVPH 240
Cdd:PRK11856 164 ----------AAAAPAAAAAAAAAAAPPAAAAEGEER--------------------VPLSGMRKAIAKRMVESKREIPH 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 241 AYATTDCDLGAVLKARQSLVRDDIKVSVNDFIIKAAAVTLKQMPDVNVSWDGEGPKQLPFIDISVAVATDKGLITPIIKD 320
Cdd:PRK11856 214 FTLTDEVDVTALLALRKQLKAIGVKLTVTDFLIKAVALALKKFPELNASWDDDAIVLKKYVNIGIAVATDGGLIVPVIRD 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 321 AAAKGIREIADSVKALSKKARDGKLLPEEYQGGSFSISNLGMFGIDEFTAVINPPQACILAVGRF--RPVLKltrdeegN 398
Cdd:PRK11856 294 ADKKSLFELAREIKDLAEKAREGKLKPEELQGGTFTISNLGMFGGDYFTPIINPPEVAILGVGAIveRPVVV-------D 366
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1435033878 399 AQLQRHQLITVTMSSDSRVVDDELATRFLESFKANLENPIRL 440
Cdd:PRK11856 367 GEIVVRKVMPLSLSFDHRVIDGADAARFLKALKELLENPALL 408
|
|
| PLN02744 |
PLN02744 |
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex |
1-437 |
2.32e-111 |
|
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
Pssm-ID: 215397 [Multi-domain] Cd Length: 539 Bit Score: 338.37 E-value: 2.32e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 1 MPSLSPTMEEGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEGSKNIRLGALIGLLVEEGED--- 77
Cdd:PLN02744 117 MPSLSPTMTEGNIARWLKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVKGDGAKEIKVGEVIAITVEEEEDigk 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 78 WKHVEIPKDVGPPSPASKPSVPCP----------SPEPQISTAVEKEHiPGKLQFRlSPAARNILEKHSLDASQGTATGP 147
Cdd:PLN02744 197 FKDYKPSSSAAPAAPKAKPSPPPPkeeevekpasSPEPKASKPSAPPS-SGDRIFA-SPLARKLAEDNNVPLSSIKGTGP 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 148 RGIFTKEDALKLVQLKETGkitESRPTPAPLATPAVplppqamatppytrpmippvstpgqpnvvgTFTEIPASNIRRVI 227
Cdd:PLN02744 275 DGRIVKADIEDYLASGGKG---ATAPPSTDSKAPAL------------------------------DYTDIPNTQIRKVT 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 228 AKRLTESKSTVPHAYATTDCDLGAVLKARQSL-----VRDDIKVSVNDFIIKAAAVTLKQMPDVNVSWDGEGPKQLPFID 302
Cdd:PLN02744 322 ASRLLQSKQTIPHYYLTVDTRVDKLMALRSQLnslqeASGGKKISVNDLVIKAAALALRKVPQCNSSWTDDYIRQYHNVN 401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 303 ISVAVATDKGLITPIIKDAAAKGIREIADSVKALSKKARDGKLLPEEYQGGSFSISNL-GMFGIDEFTAVINPPQACILA 381
Cdd:PLN02744 402 INVAVQTENGLYVPVVKDADKKGLSTIAEEVKQLAQKARENSLKPEDYEGGTFTVSNLgGPFGIKQFCAIINPPQSAILA 481
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 382 VG----RFRPvlkltrdEEGNAQLQRHQLITVTMSSDSRVVDDELATRFLESFKANLENP 437
Cdd:PLN02744 482 VGsaekRVIP-------GSGPDQYNFASFMSVTLSCDHRVIDGAIGAEWLKAFKGYIENP 534
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
231-440 |
3.42e-82 |
|
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: 252.08 E-value: 3.42e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 231 LTESKSTVPHAYATTDCDLGAVLKARQSL----VRDDIKVSVNDFIIKAAAVTLKQMPDVNVSWDGEGPK--QLPFIDIS 304
Cdd:pfam00198 1 MTESKQTIPHFTLTDEVDVTELLALREELkedaADEETKLTFLPFLVKAVALALKKFPELNASWDGEEGEivYKKYVNIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 305 VAVATDKGLITPIIKDAAAKGIREIADSVKALSKKARDGKLLPEEYQGGSFSISNLGMFGIDEFTAVINPPQACILAVGR 384
Cdd:pfam00198 81 IAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVGR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1435033878 385 --FRPVLKltrdeegNAQLQRHQLITVTMSSDSRVVDDELATRFLESFKANLENPIRL 440
Cdd:pfam00198 161 irKRPVVV-------DGEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELL 211
|
|
| sucB |
TIGR01347 |
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ... |
2-441 |
3.52e-73 |
|
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: 235.40 E-value: 3.52e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 2 PSLSPTMEEGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEGSKnirlgaligllVEEGEDWKHV 81
Cdd:TIGR01347 6 PELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDT-----------VESGQVLAIL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 82 EIPKDVGPPSPA----SKPSVPCPSPEPQISTAVEKEHipgklqfrLSPAARNILEKHSLDASQGTATGPRGIFTKEDAL 157
Cdd:TIGR01347 75 EEGNDATAAPPAksgeEKEETPAASAAAAPTAAANRPS--------LSPAARRLAKEHGIDLSAVPGTGVTGRVTKEDII 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 158 KLvqlketgkiTESRPTPAPLATPAVPLPPQAmatppYTRPMippvstpgqpnvvgtfTEIPASNIRRVIAKRLTESKST 237
Cdd:TIGR01347 147 KK---------TEAPASAQPPAAAAAAAAPAA-----ATRPE----------------ERVKMTRLRQRIAERLKEAQNS 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 238 VphAYATT--DCDLGAVLKAR-----QSLVRDDIKVSVNDFIIKAAAVTLKQMPDVNVSWDGEGPKQLPFIDISVAVATD 310
Cdd:TIGR01347 197 T--AMLTTfnEVDMSAVMELRkrykeEFEKKHGVKLGFMSFFVKAVVAALKRFPEVNAEIDGDDIVYKDYYDISVAVSTD 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 311 KGLITPIIKDAAAKGIREIADSVKALSKKARDGKLLPEEYQGGSFSISNLGMFGIDEFTAVINPPQACILAVGRF--RPV 388
Cdd:TIGR01347 275 RGLVVPVVRNADRMSFADIEKEIADLGKKARDGKLTLEDMTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHGIkeRPV 354
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1435033878 389 LKltrdeegNAQLQRHQLITVTMSSDSRVVDDELATRFLESFKANLENPIRLA 441
Cdd:TIGR01347 355 AV-------NGQIEIRPMMYLALSYDHRLIDGKEAVTFLVTIKELLEDPRRLL 400
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
10-441 |
4.67e-73 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 238.95 E-value: 4.67e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 10 EGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEGSKnIRLGALIGLLVEEGEDWKHVEIPKDVGP 89
Cdd:PRK11855 132 EVEVIEWLVKVGDTVEEDQSLITVETDKATMEIPSPVAGVVKEIKVKVGDK-VSVGSLLVVIEVAAAAPAAAAAPAAAAP 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 90 PSPASKPSVPCPSPEPQISTAVEKEHIPGKLQFRLSPAARNILEKHSLDASQGTATGPRGIFTKEDALKLVQLKETGKIT 169
Cdd:PRK11855 211 AAAAAAAPAPAPAAAAAPAAAAPAAAAAPGKAPHASPAVRRLARELGVDLSQVKGTGKKGRITKEDVQAFVKGAMSAAAA 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 170 ESRPTPAPLATPAVPLPPQAMATppytrpmippvstpgqpNVVGTFTEIPASNIRRVIAKRLTESKSTVPHAYATTDCDL 249
Cdd:PRK11855 291 AAAAAAAAGGGGLGLLPWPKVDF-----------------SKFGEIETKPLSRIKKISAANLHRSWVTIPHVTQFDEADI 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 250 GAVLKARQSL----VRDDIKVSVNDFIIKAAAVTLKQMPDVNVSWDGEGpKQLPF---IDISVAVATDKGLITPIIKDAA 322
Cdd:PRK11855 354 TDLEALRKQLkkeaEKAGVKLTMLPFFIKAVVAALKEFPVFNASLDEDG-DELTYkkyFNIGFAVDTPNGLVVPVIKDVD 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 323 AKGIREIADSVKALSKKARDGKLLPEEYQGGSFSISNLGMFGIDEFTAVINPPQACILAVGRF--RPVlkltrdeEGNAQ 400
Cdd:PRK11855 433 KKSLLEIAREIAELAKKARDGKLKPDDMQGGCFTISSLGGIGGTAFTPIINAPEVAILGVGKSqmKPV-------WDGKE 505
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1435033878 401 LQRHQLITVTMSSDSRVVDDELATRFLESFKANLENPIRLA 441
Cdd:PRK11855 506 FVPRLMLPLSLSYDHRVIDGATAARFTNYLKQLLADPRRML 546
|
|
| PRK05704 |
PRK05704 |
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase; |
2-440 |
6.14e-72 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
Pssm-ID: 235571 [Multi-domain] Cd Length: 407 Bit Score: 232.03 E-value: 6.14e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 2 PSLSPTMEEGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEGSkNIRLGALIGLLVEEGEdwkhv 81
Cdd:PRK05704 8 PTLPESVTEATIATWHKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGD-TVTVGQVLGRIDEGAA----- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 82 eipkdVGPPSPASKPSVPCPSPEPQISTAVEKEHIPGKLqfrlSPAARNILEKHSLDASQGTATGPRGIFTKEDALKLVQ 161
Cdd:PRK05704 82 -----AGAAAAAAAAAAAAAAAPAQAQAAAAAEQSNDAL----SPAARKLAAENGLDASAVKGTGKGGRVTKEDVLAALA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 162 LKETgkitesrPTPAPLATPAVPLPPQAMATPPYTRPMippvstpgqpnvvgtfteipaSNIRRVIAKRLTESKSTVphA 241
Cdd:PRK05704 153 AAAA-------APAAPAAAAPAAAPAPLGARPEERVPM---------------------TRLRKTIAERLLEAQNTT--A 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 242 YATT--DCDLGAVLKAR-----QSLVRDDIKVSVNDFIIKAAAVTLKQMPDVNVSWDGEGPKQLPFIDISVAVATDKGLI 314
Cdd:PRK05704 203 MLTTfnEVDMTPVMDLRkqykdAFEKKHGVKLGFMSFFVKAVVEALKRYPEVNASIDGDDIVYHNYYDIGIAVGTPRGLV 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 315 TPIIKDAAAKGIREIADSVKALSKKARDGKLLPEEYQGGSFSISNLGMFGIDEFTAVINPPQACILAVGRF--RPVLKlt 392
Cdd:PRK05704 283 VPVLRDADQLSFAEIEKKIAELAKKARDGKLSIEELTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHKIkeRPVAV-- 360
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1435033878 393 rdeegNAQLQRHQLITVTMSSDSRVVDDELATRFLESFKANLENPIRL 440
Cdd:PRK05704 361 -----NGQIVIRPMMYLALSYDHRIIDGKEAVGFLVTIKELLEDPERL 403
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
10-440 |
2.25e-55 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 194.07 E-value: 2.25e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 10 EGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEGSKnIRLGALIGLLVEEGEDWKHVEIPKDVGP 89
Cdd:PRK11854 218 EVEVTEVMVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDK-VKTGSLIMRFEVEGAAPAAAPAKQEAAA 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 90 PSPASKPSVPcPSPEPQISTAVEKEHIPGKLQFRLSPAARNILEKHSLDASQGTATGPRGIFTKEDALKLVqlKETGKIT 169
Cdd:PRK11854 297 PAPAAAKAEA-PAAAPAAKAEGKSEFAENDAYVHATPLVRRLAREFGVNLAKVKGTGRKGRILKEDVQAYV--KDAVKRA 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 170 ESRPTPAPLATPAVPLPPqamatppytrpmIPPVStpgqPNVVGTFTEIPASNIRRVIAKRLTESKSTVPHA--YATTD- 246
Cdd:PRK11854 374 EAAPAAAAAGGGGPGLLP------------WPKVD----FSKFGEIEEVELGRIQKISGANLHRNWVMIPHVtqFDKADi 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 247 CDLGAVLKARQSLV---RDDIKVSVNDFIIKAAAVTLKQMPDVNVSWDGEGpKQL---PFIDISVAVATDKGLITPIIKD 320
Cdd:PRK11854 438 TELEAFRKQQNAEAekrKLGVKITPLVFIMKAVAAALEQMPRFNSSLSEDG-QRLtlkKYVNIGIAVDTPNGLVVPVFKD 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 321 AAAKGIREIADSVKALSKKARDGKLLPEEYQGGSFSISNLGMFGIDEFTAVINPPQACILAVGR--FRPVlkltrdeEGN 398
Cdd:PRK11854 517 VNKKGIIELSRELMDISKKARDGKLTAGDMQGGCFTISSIGGLGTTHFTPIVNAPEVAILGVSKsaMEPV-------WNG 589
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1435033878 399 AQLQRHQLITVTMSSDSRVVDDELATRFLESFKANLENPIRL 440
Cdd:PRK11854 590 KEFAPRLMLPLSLSYDHRVIDGADGARFITIINDRLSDIRRL 631
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
9-440 |
1.13e-52 |
|
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: 185.08 E-value: 1.13e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 9 EEGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEGSKnIRLGALIGLLVEEGEDWKHVEIPKDVG 88
Cdd:TIGR01348 128 EKVTVIEVLVKVGDTVSADQSLITLESDKASMEVPAPASGVVKSVKVKVGDS-VPTGDLILTLSVAGSTPATAPAPASAQ 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 89 PP--SPASKPSVPCPSPEPQISTAVEKEHIPGKLQFRL---SPAARNILEKHSLDASQGTATGPRGIFTKEDALKLVQlk 163
Cdd:TIGR01348 207 PAaqSPAATQPEPAAAPAAAKAQAPAPQQAGTQNPAKVdhaAPAVRRLAREFGVDLSAVKGTGIKGRILREDVQRFVK-- 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 164 etgkiTESRPTPAPLATPAVPLPpqamatppytrpMIPPVstpgqPNV----VGTFTEIPASNIRRVIAKRLTESKSTVP 239
Cdd:TIGR01348 285 -----EPSVRAQAAAASAAGGAP------------GALPW-----PNVdfskFGEVEEVDMSRIRKISGANLTRNWTMIP 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 240 HA--YATTD-CDLGAVLKARQSLVR-DDIKVSVNDFIIKAAAVTLKQMPDVNVSWDgEGPKQL---PFIDISVAVATDKG 312
Cdd:TIGR01348 343 HVthFDKADiTEMEAFRKQQNAAVEkEGVKLTVLHILMKAVAAALKKFPKFNASLD-LGGEQLilkKYVNIGVAVDTPNG 421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 313 LITPIIKDAAAKGIREIADSVKALSKKARDGKLLPEEYQGGSFSISNLGMFGIDEFTAVINPPQACILAVGR--FRPVLK 390
Cdd:TIGR01348 422 LLVPVIKDVDRKGITELALELSDLAKKARDGKLTPDEMQGACFTISSLGGIGGTAFTPIVNAPEVAILGVSKsgMEPVWN 501
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1435033878 391 LTrdeegnaQLQRHQLITVTMSSDSRVVDDELATRFLESFKANLENPIRL 440
Cdd:TIGR01348 502 GK-------EFEPRLMLPLSLSYDHRVIDGADAARFTTYICESLADIRRL 544
|
|
| PTZ00144 |
PTZ00144 |
dihydrolipoamide succinyltransferase; Provisional |
2-440 |
1.04e-51 |
|
dihydrolipoamide succinyltransferase; Provisional
Pssm-ID: 240289 [Multi-domain] Cd Length: 418 Bit Score: 179.49 E-value: 1.04e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 2 PSLSPTMEEGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEGSKnirlgaligllVEEGEDWkhV 81
Cdd:PTZ00144 50 PTMGDSISEGTVVEWKKKVGDYVKEDEVICIIETDKVSVDIRAPASGVITKIFAEEGDT-----------VEVGAPL--S 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 82 EIPKDVGPPS-PASKPSVPCPSPEPQISTAVEKEHIPGKlqfrlspaarnilekhsldasqgtatgprgiftkedalklv 160
Cdd:PTZ00144 117 EIDTGGAPPAaAPAAAAAAKAEKTTPEKPKAAAPTPEPP----------------------------------------- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 161 qlketgkiTESRPTPAPLATPAvplppqamATPPYTRPMIPPVSTPGQPNvvgtfTEIPASNIRRVIAKRLTESKSTvpH 240
Cdd:PTZ00144 156 --------AASKPTPPAAAKPP--------EPAPAAKPPPTPVARADPRE-----TRVPMSRMRQRIAERLKASQNT--C 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 241 AYATT--DCDLGAVLKARQSL-----VRDDIKVSVNDFIIKAAAVTLKQMPDVNVSWDGEGPKQLPFIDISVAVATDKGL 313
Cdd:PTZ00144 213 AMLTTfnECDMSALMELRKEYkddfqKKHGVKLGFMSAFVKASTIALKKMPIVNAYIDGDEIVYRNYVDISVAVATPTGL 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 314 ITPIIKDAAAKGIREIADSVKALSKKARDGKLLPEEYQGGSFSISNLGMFGIDEFTAVINPPQACIL---AVGRfRPVLK 390
Cdd:PTZ00144 293 VVPVIRNCENKSFAEIEKELADLAEKARNNKLTLEDMTGGTFTISNGGVFGSLMGTPIINPPQSAILgmhAIKK-RPVVV 371
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1435033878 391 ltrdeegNAQLQRHQLITVTMSSDSRVVDDELATRFLESFKANLENPIRL 440
Cdd:PTZ00144 372 -------GNEIVIRPIMYLALTYDHRLIDGRDAVTFLKKIKDLIEDPARM 414
|
|
| SucB_Actino |
TIGR02927 |
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model ... |
1-435 |
3.20e-47 |
|
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: 170.96 E-value: 3.20e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 1 MPSLSPTMEEGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEgSKNIRLGALIGLLveeGEDWKH 80
Cdd:TIGR02927 131 MPELGESVTEGTVTSWLKAVGDTVEVDEPLLEVSTDKVDTEIPSPVAGTLLEIRAPE-DDTVEVGTVLAII---GDANAA 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 81 VEIPKDVGPPSPASKPSVPCPSPEPQISTAVEKEHIPGKLQFRLSPAA------------------RNILEKHSLDASQG 142
Cdd:TIGR02927 207 PAEPAEEEAPAPSEAGSEPAPDPAARAPHAAPDPPAPAPAPAKTAAPAaaapvssgdsgpyvtplvRKLAKDKGVDLSTV 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 143 TATGPRGIFTKEDALKLVQlketgKITESRPTPAPLATPAVPLPPQAMATPPytrpmippvsTPGQPNVVGTFTEipASN 222
Cdd:TIGR02927 287 KGTGVGGRIRKQDVLAAAK-----AAEEARAAAAAPAAAAAPAAPAAAAKPA----------EPDTAKLRGTTQK--MNR 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 223 IRRVIAKRLTESKSTVPHAYATTDCDLGAVLKARQS-----LVRDDIKVSVNDFIIKAAAVTLKQMPDVNVSWDGEGpKQ 297
Cdd:TIGR02927 350 IRQITADKTIESLQTSAQLTQVHEVDMTRVAALRARakndfLEKNGVNLTFLPFFVQAVTEALKAHPNVNASYNAET-KE 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 298 LPFID---ISVAVATDKGLITPIIKDAAAKGIREIADSVKALSKKARDGKLLPEEYQGGSFSISNLGMFGIDEFTAVINP 374
Cdd:TIGR02927 429 VTYHDvehVGIAVDTPRGLLVPVIHNAGDLSLPGLAKAINDLAARARDNKLKPDELSGGTFTITNIGSGGALFDTPILNP 508
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1435033878 375 PQACILAVGRFRPVLKLTRDEEGNAQLQRHQLITVTMSSDSRVVDDELATRFLESFKANLE 435
Cdd:TIGR02927 509 PQAAILGTGAIVKRPRVIKDEDGGESIAIRSVCYLPLTYDHRLVDGADAGRFLTTIKKRLE 569
|
|
| PLN02528 |
PLN02528 |
2-oxoisovalerate dehydrogenase E2 component |
10-440 |
8.57e-45 |
|
2-oxoisovalerate dehydrogenase E2 component
Pssm-ID: 215289 [Multi-domain] Cd Length: 416 Bit Score: 161.04 E-value: 8.57e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 10 EGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEGSKnIRLG-ALIGLLVEEGEDwkhvEIPKDVG 88
Cdd:PLN02528 12 ECELLRWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGKVAQINFSPGDI-VKVGeTLLKIMVEDSQH----LRSDSLL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 89 PPSPASKPSVPCPSPEpqistavEKEHIPGKLQfrlSPAARNILEKHSLDASQGTATGPRGIFTKEDALKLVQLKEtgki 168
Cdd:PLN02528 87 LPTDSSNIVSLAESDE-------RGSNLSGVLS---TPAVRHLAKQYGIDLNDILGTGKDGRVLKEDVLKYAAQKG---- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 169 tesrptpaplatpAVPLPPQA-MATPPYTRPMIPPVSTP-GQPNVVGTfteIPASNIRRVIAKRLTESKStVPHAYATTD 246
Cdd:PLN02528 153 -------------VVKDSSSAeEATIAEQEEFSTSVSTPtEQSYEDKT---IPLRGFQRAMVKTMTAAAK-VPHFHYVEE 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 247 CDLGAVLKARQSL----VRDDIKVSVNDFIIKAAAVTLKQMPDVNVSWDGEGPK--QLPFIDISVAVATDKGLITPIIKD 320
Cdd:PLN02528 216 INVDALVELKASFqennTDPTVKHTFLPFLIKSLSMALSKYPLLNSCFNEETSEirLKGSHNIGVAMATEHGLVVPNIKN 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 321 AAAKGIREIADSVKALSKKARDGKLLPEEYQGGSFSISNLGMFGIDEFTAVINPPQACILAVGRFRpvlKLTR-DEEGNA 399
Cdd:PLN02528 296 VQSLSLLEITKELSRLQHLAAENKLNPEDITGGTITLSNIGAIGGKFGSPVLNLPEVAIIALGRIQ---KVPRfVDDGNV 372
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1435033878 400 QLQRhqLITVTMSSDSRVVDDELATRFLESFKANLENPIRL 440
Cdd:PLN02528 373 YPAS--IMTVTIGADHRVLDGATVARFCNEWKSYVEKPELL 411
|
|
| PRK14843 |
PRK14843 |
dihydrolipoamide acetyltransferase; Provisional |
121-440 |
2.57e-40 |
|
dihydrolipoamide acetyltransferase; Provisional
Pssm-ID: 184847 [Multi-domain] Cd Length: 347 Bit Score: 147.36 E-value: 2.57e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 121 QFRLSPAARNILEKHSLDASQGTATGPRGIFTKEDALKLVqlketgkitesrptPAPLATPAVPLPPQAMATppytrpmi 200
Cdd:PRK14843 48 VVRISPLAKRIALEHNIAWQEIQGTGHRGKIMKKDVLALL--------------PENIENDSIKSPAQIEKV-------- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 201 ppVSTPGQPNVVGTFTEIPASNIRRVIAKRLTESKSTVPHAYATTDCDLGAVLKARQSLVrDDI------KVSVNDFIIK 274
Cdd:PRK14843 106 --EEVPDNVTPYGEIERIPMTPMRKVIAQRMVESYLTAPTFTLNYEVDMTEMLALRKKVL-EPImeatgkKTTVTDLLSL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 275 AAAVTLKQMPDVNVSWDGEGPKQLP--FIDISVAVATDKGLITPIIKDAAAKGIREIADSVKALSKKARDGKLLPEEYQG 352
Cdd:PRK14843 183 AVVKTLMKHPYINASLTEDGKTIIThnYVNLAMAVGMDNGLMTPVVYNAEKMSLSELVVAFKDVIGRTLDGKLAPSELQN 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 353 GSFSISNLGMFGIDEFTAVINPPQACILAVGRF--RPVLKltrdeegNAQLQRHQLITVTMSSDSRVVDDELATRFLESF 430
Cdd:PRK14843 263 STFTISNLGMFGVQSFGPIINQPNSAILGVSSTieKPVVV-------NGEIVIRPIMSLGLTIDHRVVDGMAGAKFMKDL 335
|
330
....*....|
gi 1435033878 431 KANLENPIRL 440
Cdd:PRK14843 336 KELIETPISM 345
|
|
| PLN02226 |
PLN02226 |
2-oxoglutarate dehydrogenase E2 component |
1-440 |
5.43e-38 |
|
2-oxoglutarate dehydrogenase E2 component
Pssm-ID: 177871 [Multi-domain] Cd Length: 463 Bit Score: 143.74 E-value: 5.43e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 1 MPSLSPTMEEGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEGSkNIRLGALIGLLVEEGEDWKH 80
Cdd:PLN02226 96 VPHMGESITDGTLATFLKKPGERVQADEAIAQIETDKVTIDIASPASGVIQEFLVKEGD-TVEPGTKVAIISKSEDAASQ 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 81 VEiPKDVGPPSPASKPSVPC-PSPEPQIstavekehipgklqfrlspaarnilekhsldasqgtatgprgiftkedalkl 159
Cdd:PLN02226 175 VT-PSQKIPETTDPKPSPPAeDKQKPKV---------------------------------------------------- 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 160 vqlkETGKITESRPTPAPlatpavPLPPQAMATppytRPMIPPVSTPgqpnvvgtfTEIPASNIRRVIAKRLTESKSTVP 239
Cdd:PLN02226 202 ----ESAPVAEKPKAPSS------PPPPKQSAK----EPQLPPKERE---------RRVPMTRLRKRVATRLKDSQNTFA 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 240 HAYATTDCDLGAVLKARQS-----LVRDDIKVSVNDFIIKAAAVTLKQMPDVNVSWDGEGPKQLPFIDISVAVATDKGLI 314
Cdd:PLN02226 259 LLTTFNEVDMTNLMKLRSQykdafYEKHGVKLGLMSGFIKAAVSALQHQPVVNAVIDGDDIIYRDYVDISIAVGTSKGLV 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 315 TPIIKDAAAKGIREIADSVKALSKKARDGKLLPEEYQGGSFSISNLGMFGIDEFTAVINPPQACILAVGRF--RPVLKlt 392
Cdd:PLN02226 339 VPVIRGADKMNFAEIEKTINGLAKKANEGTISIDEMAGGSFTVSNGGVYGSLISTPIINPPQSAILGMHSIvsRPMVV-- 416
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1435033878 393 rdeeGNAQLQRhQLITVTMSSDSRVVDDELATRFLESFKANLENPIRL 440
Cdd:PLN02226 417 ----GGSVVPR-PMMYVALTYDHRLIDGREAVYFLRRVKDVVEDPQRL 459
|
|
| PRK11857 |
PRK11857 |
dihydrolipoamide acetyltransferase; Reviewed |
125-437 |
7.90e-34 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237002 [Multi-domain] Cd Length: 306 Bit Score: 128.76 E-value: 7.90e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 125 SPAARNILEKHSLDASQGTATGPRGIFTKEDALKLVqlketgKITESRPTPAPLATpaVPLPPQAMATPPytrPMIPPVS 204
Cdd:PRK11857 5 TPIARALAKKLGIDISLLKGSGRDGKILAEDVENFI------KSLKSAPTPAEAAS--VSSAQQAAKTAA---PAAAPPK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 205 TPGQPNVVGTfteipasnIRRVIAKRLTESKSTVPHAYATTDCDLGAVLKARQSLVRD-----DIKVSVNDFIIKAAAVT 279
Cdd:PRK11857 74 LEGKREKVAP--------IRKAIARAMTNSWSNVAYVNLVNEIDMTKLWDLRKSVKDPvlkteGVKLTFLPFIAKAILIA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 280 LKQMPDVNVSWDgEGPKQLPF---IDISVAVATDKGLITPIIKDAAAKGIREIADSVKALSKKARDGKLLPEEYQGGSFS 356
Cdd:PRK11857 146 LKEFPIFAAKYD-EATSELVYpdtLNLGIAVDTEAGLMVPVIKNAQKLSIVEIAKEISRLAKAARERKIKPDEMKGGSFT 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 357 ISNLGMFGIDEFTAVINPPQACILAVGRF--RPVLKltrdeegNAQLQRHQLITVTMSSDSRVVDDELATRFLESFKANL 434
Cdd:PRK11857 225 ITNYGSVGSLYGVPVINYPELAIAGVGAIidKAIVK-------NGQIVAGKVMHLTVAADHRWIDGATIGRFASRVKELL 297
|
...
gi 1435033878 435 ENP 437
Cdd:PRK11857 298 EKP 300
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
1-110 |
5.34e-32 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 126.96 E-value: 5.34e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 1 MPSLSPTMEEGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEGSKNIRLGALIGLLVEEGEDWKH 80
Cdd:PRK11892 7 MPALSPTMEEGTLAKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKILVPEGTEGVKVNTPIAVLLEEGESASD 86
|
90 100 110
....*....|....*....|....*....|
gi 1435033878 81 VEIPKDVGPPSPASKPSVPCPSPEPQISTA 110
Cdd:PRK11892 87 AGAAPAAAAEAAAAAPAAAAAAAAKKAAPA 116
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
1-71 |
4.07e-26 |
|
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. 2-oxo acid dehydrogenase multienzyme complexes, like pyruvate dehydrogenase (PDH), 2-oxoglutarate dehydrogenase (OGDH) and branched-chain 2-oxo acid dehydrogenase (BCDH), contain at least three different enzymes, 2-oxo acid dehydrogenase (E1), dihydrolipoyl acyltransferase (E2) and dihydrolipoamide dehydrogenase (E3) and play a key role in redox regulation. E2, the central component of the complex, catalyzes the transfer of the acyl group of CoA from E1 to E3 via reductive acetylation of a lipoyl group covalently attached to a lysine residue.
Pssm-ID: 133458 [Multi-domain] Cd Length: 74 Bit Score: 100.56 E-value: 4.07e-26
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1435033878 1 MPSLSPTMEEGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEGSKnIRLGALIGLL 71
Cdd:cd06849 5 MPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDT-VPVGQVIAVI 74
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
1-72 |
2.82e-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: 92.82 E-value: 2.82e-23
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1435033878 1 MPSLSPTMEEGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEGSKnIRLGALIGLLV 72
Cdd:COG0508 7 MPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDT-VPVGAVIAVIA 77
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
1-75 |
2.64e-17 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 83.07 E-value: 2.64e-17
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1435033878 1 MPSLSPTMEEGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEGSkNIRLGALIGLLVEEG 75
Cdd:PRK14875 7 MPKWGLSMTEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGE-TLPVGALLAVVADAE 80
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
1-60 |
4.15e-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: 66.85 E-value: 4.15e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 1 MPSLSPTMEEGnIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEGSK 60
Cdd:pfam00364 5 SPMIGESVREG-VVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDT 63
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
2-60 |
7.82e-14 |
|
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: 66.31 E-value: 7.82e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1435033878 2 PSLSPTMEEGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEGSK 60
Cdd:cd06663 5 PDLAQHLGDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTK 63
|
|
| kgd |
PRK12270 |
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ... |
125-383 |
6.77e-12 |
|
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;
Pssm-ID: 237030 [Multi-domain] Cd Length: 1228 Bit Score: 67.61 E-value: 6.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 125 SPAARNILEK-HSLDASQGTATGPRGIFTKEDALKLVQLKETGKITESRPTPAPLATPAVPLPPQAMATPPYTRPMIPPV 203
Cdd:PRK12270 26 DPSWREFFADyGPGSTAAPTAAAAAAAAAASAPAAAPAAKAPAAPAPAPPAAAAPAAPPKPAAAAAAAAAPAAPPAAAAA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 204 STPGQPNVVGTFTeiPASNIRRVIAKRLTESKStVPhaYATTDCDLGAVLKARQSLVRDD-------IKVSVNDFIIKAA 276
Cdd:PRK12270 106 AAPAAAAVEDEVT--PLRGAAAAVAKNMDASLE-VP--TATSVRAVPAKLLIDNRIVINNhlkrtrgGKVSFTHLIGYAL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 277 AVTLKQMPDVNVSWDGEGPKqlPFI----DISVAVATD-------KGLITPIIKDAAAKGIREIADSVKALSKKARDGKL 345
Cdd:PRK12270 181 VQALKAFPNMNRHYAEVDGK--PTLvtpaHVNLGLAIDlpkkdgsRQLVVPAIKGAETMDFAQFWAAYEDIVRRARDGKL 258
|
250 260 270
....*....|....*....|....*....|....*...
gi 1435033878 346 LPEEYQGGSFSISNLGMFGIDEFTAVINPPQACILAVG 383
Cdd:PRK12270 259 TADDFQGTTISLTNPGGIGTVHSVPRLMKGQGAIIGVG 296
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
11-59 |
1.04e-08 |
|
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: 51.65 E-value: 1.04e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1435033878 11 GNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEGS 59
Cdd:cd06850 8 GTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGD 56
|
|
| E3_binding |
pfam02817 |
e3 binding domain; This family represents a small domain of the E2 subunit of 2-oxo-acid ... |
123-157 |
1.29e-04 |
|
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: 38.82 E-value: 1.29e-04
10 20 30
....*....|....*....|....*....|....*
gi 1435033878 123 RLSPAARNILEKHSLDASQGTATGPRGIFTKEDAL 157
Cdd:pfam02817 2 LASPAARKLARELGIDLSDVKGTGPGGRITKEDVE 36
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
84-209 |
3.66e-04 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 43.39 E-value: 3.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 84 PKDVGPPSPASKPSVPCPSPEP-QISTAVEKEHIPGKlQFRLSPAARnilekhsldASQGTATGPRGIFTKEDALKLVQl 162
Cdd:PHA03247 2824 PAGPLPPPTSAQPTAPPPPPGPpPPSLPLGGSVAPGG-DVRRRPPSR---------SPAAKPAAPARPPVRRLARPAVS- 2892
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1435033878 163 KETGKITESRPTPAPLATPAVPLPPQAMATPPYTRPMIPPVSTPGQP 209
Cdd:PHA03247 2893 RSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRP 2939
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
11-60 |
1.48e-03 |
|
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the Pathway/BioSystem: Urea cycle
Pssm-ID: 440660 [Multi-domain] Cd Length: 1144 Bit Score: 41.22 E-value: 1.48e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1435033878 11 GNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEGSK 60
Cdd:COG1038 1085 GTVVKVLVKEGDEVKKGDPLLTIEAMKMETTITAPRDGTVKEVLVKEGDQ 1134
|
|
| PRK09282 |
PRK09282 |
pyruvate carboxylase subunit B; Validated |
11-58 |
2.97e-03 |
|
pyruvate carboxylase subunit B; Validated
Pssm-ID: 236449 [Multi-domain] Cd Length: 592 Bit Score: 39.83 E-value: 2.97e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1435033878 11 GNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEG 58
Cdd:PRK09282 531 GTVVKVKVKEGDKVKAGDTVLVLEAMKMENEIQAPVDGTVKEILVKEG 578
|
|
|