|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11856 |
PRK11856 |
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed |
1-418 |
2.44e-177 |
|
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
Pssm-ID: 237001 [Multi-domain] Cd Length: 411 Bit Score: 501.24 E-value: 2.44e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760234714 1 MPIEqMKMPQLGESVTEGTISSWLVKPGDRVNKYDPIAEVMTDKVNAEVPSSFTGVIKDLIAAEGETLPVGEVMCSIQLA 80
Cdd:PRK11856 1 MMFE-FKMPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDVVPVGSVIAVIEEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760234714 81 GEPDSSEEAPKEEKNHSEEKSESLIQTDQSNKA-------------RYSPAVLKLSQEHGINLENVAGSGAGGRITRKDI 147
Cdd:PRK11856 80 GEAEAAAAAEAAPEAPAPEPAPAAAAAAAAAPAaaaapaapaaaaaKASPAVRKLARELGVDLSTVKGSGPGGRITKEDV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760234714 148 LKAVESGTAAKAQVNIENAEPKADTqmyepnlgvkqkssgsdmkiESGDREIPVTGIRKAIAQNMVRSKHEIPHAWTMVE 227
Cdd:PRK11856 160 EAAAAAAAPAAAAAAAAAAAPPAAA--------------------AEGEERVPLSGMRKAIAKRMVESKREIPHFTLTDE 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760234714 228 ADVTNLVQYRDSLKKEfrqkeGYNLTYFAFFVKAVAQALKEFPEMNSMWAGDKIVRKKDINISIAVSTDEALYVPVIKFA 307
Cdd:PRK11856 220 VDVTALLALRKQLKAI-----GVKLTVTDFLIKAVALALKKFPELNASWDDDAIVLKKYVNIGIAVATDGGLIVPVIRDA 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760234714 308 DEKTIKGIAREINELAEKVRSGKLKSEDMQGGTFTVNNTGSFGSIQSMGIINHPQAAILQVESIVKKPVVMHGnMIAIRD 387
Cdd:PRK11856 295 DKKSLFELAREIKDLAEKAREGKLKPEELQGGTFTISNLGMFGGDYFTPIINPPEVAILGVGAIVERPVVVDG-EIVVRK 373
|
410 420 430
....*....|....*....|....*....|.
gi 1760234714 388 RVNLCLSLDHRILDGLVCGRFLARVKDILEH 418
Cdd:PRK11856 374 VMPLSLSFDHRVIDGADAARFLKALKELLEN 404
|
|
| sucB |
TIGR01347 |
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ... |
7-417 |
9.58e-103 |
|
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: 310.90 E-value: 9.58e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760234714 7 KMPQLGESVTEGTISSWLVKPGDRVNKYDPIAEVMTDKVNAEVPSSFTGVIKDLIAAEGETLPVGEVMCSIQLAGEPDS- 85
Cdd:TIGR01347 4 KVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAILEEGNDATAa 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760234714 86 SEEAPKEEKNHSEEKSESLIQTDQSNKARYSPAVLKLSQEHGINLENVAGSGAGGRITRKDILKAVESGTAAKAQVNIEN 165
Cdd:TIGR01347 84 PPAKSGEEKEETPAASAAAAPTAAANRPSLSPAARRLAKEHGIDLSAVPGTGVTGRVTKEDIIKKTEAPASAQPPAAAAA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760234714 166 AepKADTQMYEPNlgvkqkssgsdmkiesgdREIPVTGIRKAIAQNMVRSKHEIPHAWTMVEADVTNLVQYRDSLKKEFR 245
Cdd:TIGR01347 164 A--AAPAAATRPE------------------ERVKMTRLRQRIAERLKEAQNSTAMLTTFNEVDMSAVMELRKRYKEEFE 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760234714 246 QKEGYNLTYFAFFVKAVAQALKEFPEMNSMWAGDKIVRKKDINISIAVSTDEALYVPVIKFADEKTIKGIAREINELAEK 325
Cdd:TIGR01347 224 KKHGVKLGFMSFFVKAVVAALKRFPEVNAEIDGDDIVYKDYYDISVAVSTDRGLVVPVVRNADRMSFADIEKEIADLGKK 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760234714 326 VRSGKLKSEDMQGGTFTVNNTGSFGSIQSMGIINHPQAAILQVESIVKKPVVMHGNmIAIRDRVNLCLSLDHRILDGLVC 405
Cdd:TIGR01347 304 ARDGKLTLEDMTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHGIKERPVAVNGQ-IEIRPMMYLALSYDHRLIDGKEA 382
|
410
....*....|..
gi 1760234714 406 GRFLARVKDILE 417
Cdd:TIGR01347 383 VTFLVTIKELLE 394
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
212-420 |
5.12e-95 |
|
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: 284.05 E-value: 5.12e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760234714 212 MVRSKHEIPHAWTMVEADVTNLVQYRDSLKKEFrQKEGYNLTYFAFFVKAVAQALKEFPEMNSMWAGDK--IVRKKDINI 289
Cdd:pfam00198 1 MTESKQTIPHFTLTDEVDVTELLALREELKEDA-ADEETKLTFLPFLVKAVALALKKFPELNASWDGEEgeIVYKKYVNI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760234714 290 SIAVSTDEALYVPVIKFADEKTIKGIAREINELAEKVRSGKLKSEDMQGGTFTVNNTGSFGSIQSMGIINHPQAAILQVE 369
Cdd:pfam00198 80 GIAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVG 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1760234714 370 SIVKKPVVMHGNmIAIRDRVNLCLSLDHRILDGLVCGRFLARVKDILEHIT 420
Cdd:pfam00198 160 RIRKRPVVVDGE-IVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPE 209
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
1-77 |
6.88e-31 |
|
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: 113.24 E-value: 6.88e-31
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1760234714 1 MPIEqMKMPQLGESVTEGTISSWLVKPGDRVNKYDPIAEVMTDKVNAEVPSSFTGVIKDLIAAEGETLPVGEVMCSI 77
Cdd:COG0508 1 MAIE-IKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
5-77 |
2.46e-28 |
|
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: 106.33 E-value: 2.46e-28
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1760234714 5 QMKMPQLGESVTEGTISSWLVKPGDRVNKYDPIAEVMTDKVNAEVPSSFTGVIKDLIAAEGETLPVGEVMCSI 77
Cdd:cd06849 2 EIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11856 |
PRK11856 |
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed |
1-418 |
2.44e-177 |
|
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
Pssm-ID: 237001 [Multi-domain] Cd Length: 411 Bit Score: 501.24 E-value: 2.44e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760234714 1 MPIEqMKMPQLGESVTEGTISSWLVKPGDRVNKYDPIAEVMTDKVNAEVPSSFTGVIKDLIAAEGETLPVGEVMCSIQLA 80
Cdd:PRK11856 1 MMFE-FKMPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDVVPVGSVIAVIEEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760234714 81 GEPDSSEEAPKEEKNHSEEKSESLIQTDQSNKA-------------RYSPAVLKLSQEHGINLENVAGSGAGGRITRKDI 147
Cdd:PRK11856 80 GEAEAAAAAEAAPEAPAPEPAPAAAAAAAAAPAaaaapaapaaaaaKASPAVRKLARELGVDLSTVKGSGPGGRITKEDV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760234714 148 LKAVESGTAAKAQVNIENAEPKADTqmyepnlgvkqkssgsdmkiESGDREIPVTGIRKAIAQNMVRSKHEIPHAWTMVE 227
Cdd:PRK11856 160 EAAAAAAAPAAAAAAAAAAAPPAAA--------------------AEGEERVPLSGMRKAIAKRMVESKREIPHFTLTDE 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760234714 228 ADVTNLVQYRDSLKKEfrqkeGYNLTYFAFFVKAVAQALKEFPEMNSMWAGDKIVRKKDINISIAVSTDEALYVPVIKFA 307
Cdd:PRK11856 220 VDVTALLALRKQLKAI-----GVKLTVTDFLIKAVALALKKFPELNASWDDDAIVLKKYVNIGIAVATDGGLIVPVIRDA 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760234714 308 DEKTIKGIAREINELAEKVRSGKLKSEDMQGGTFTVNNTGSFGSIQSMGIINHPQAAILQVESIVKKPVVMHGnMIAIRD 387
Cdd:PRK11856 295 DKKSLFELAREIKDLAEKAREGKLKPEELQGGTFTISNLGMFGGDYFTPIINPPEVAILGVGAIVERPVVVDG-EIVVRK 373
|
410 420 430
....*....|....*....|....*....|.
gi 1760234714 388 RVNLCLSLDHRILDGLVCGRFLARVKDILEH 418
Cdd:PRK11856 374 VMPLSLSFDHRVIDGADAARFLKALKELLEN 404
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
3-417 |
7.61e-120 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 359.52 E-value: 7.61e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760234714 3 IEQMKMPQLGEsVTEGTISSWLVKPGDRVNKYDPIAEVMTDKVNAEVPSSFTGVIKDLIAAEGETLPVGEVMCSIQLAGE 82
Cdd:PRK11855 119 VVEVKVPDIGE-ITEVEVIEWLVKVGDTVEEDQSLITVETDKATMEIPSPVAGVVKEIKVKVGDKVSVGSLLVVIEVAAA 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760234714 83 PDSSEEAPKEEK---------------NHSEEKSESLIQTDQSNKARYSPAVLKLSQEHGINLENVAGSGAGGRITRKDI 147
Cdd:PRK11855 198 APAAAAAPAAAApaaaaaaapapapaaAAAPAAAAPAAAAAPGKAPHASPAVRRLARELGVDLSQVKGTGKKGRITKEDV 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760234714 148 LKAVESGTAAKAQVnienAEPKADTQMYEPNLGVKQKSSGSDmkiESGDREIPVTGIRKAIAQNMVRSKHEIPHAWTMVE 227
Cdd:PRK11855 278 QAFVKGAMSAAAAA----AAAAAAAGGGGLGLLPWPKVDFSK---FGEIETKPLSRIKKISAANLHRSWVTIPHVTQFDE 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760234714 228 ADVTNLVQYRDSLKKEFrQKEGYNLTYFAFFVKAVAQALKEFPEMNSM--WAGDKIVRKKDINISIAVSTDEALYVPVIK 305
Cdd:PRK11855 351 ADITDLEALRKQLKKEA-EKAGVKLTMLPFFIKAVVAALKEFPVFNASldEDGDELTYKKYFNIGFAVDTPNGLVVPVIK 429
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760234714 306 FADEKTIKGIAREINELAEKVRSGKLKSEDMQGGTFTVNNTGSFGSIQSMGIINHPQAAILQVESIVKKPvVMHGNMIAI 385
Cdd:PRK11855 430 DVDKKSLLEIAREIAELAKKARDGKLKPDDMQGGCFTISSLGGIGGTAFTPIINAPEVAILGVGKSQMKP-VWDGKEFVP 508
|
410 420 430
....*....|....*....|....*....|..
gi 1760234714 386 RDRVNLCLSLDHRILDGLVCGRFLARVKDILE 417
Cdd:PRK11855 509 RLMLPLSLSYDHRVIDGATAARFTNYLKQLLA 540
|
|
| PRK05704 |
PRK05704 |
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase; |
1-417 |
5.94e-110 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
Pssm-ID: 235571 [Multi-domain] Cd Length: 407 Bit Score: 329.49 E-value: 5.94e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760234714 1 MPIEqMKMPQLGESVTEGTISSWLVKPGDRVNKYDPIAEVMTDKVNAEVPSSFTGVIKDLIAAEGETLPVGEVMCSIQLA 80
Cdd:PRK05704 1 MMVE-IKVPTLPESVTEATIATWHKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGDTVTVGQVLGRIDEG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760234714 81 GEPDSSEEAP--KEEKNHSEEKSESLIQTDQSNKARySPAVLKLSQEHGINLENVAGSGAGGRITRKDILKAVESGTAAK 158
Cdd:PRK05704 80 AAAGAAAAAAaaAAAAAAAPAQAQAAAAAEQSNDAL-SPAARKLAAENGLDASAVKGTGKGGRVTKEDVLAALAAAAAAP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760234714 159 AQVNIENAEPKAdtqmyepnlgvkqksSGSDMKIESgdREiPVTGIRKAIAQNMVRSKHEIPHAWTMVEADVTNLVQYRD 238
Cdd:PRK05704 159 AAPAAAAPAAAP---------------APLGARPEE--RV-PMTRLRKTIAERLLEAQNTTAMLTTFNEVDMTPVMDLRK 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760234714 239 SLKKEFRQKEGYNLTYFAFFVKAVAQALKEFPEMNSMWAGDKIVRKKDINISIAVSTDEALYVPVIKFADEKTIKGIARE 318
Cdd:PRK05704 221 QYKDAFEKKHGVKLGFMSFFVKAVVEALKRYPEVNASIDGDDIVYHNYYDIGIAVGTPRGLVVPVLRDADQLSFAEIEKK 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760234714 319 INELAEKVRSGKLKSEDMQGGTFTVNNTGSFGSIQSMGIINHPQAAILQVESIVKKPVVMHGNmIAIRDRVNLCLSLDHR 398
Cdd:PRK05704 301 IAELAKKARDGKLSIEELTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHKIKERPVAVNGQ-IVIRPMMYLALSYDHR 379
|
410
....*....|....*....
gi 1760234714 399 ILDGLVCGRFLARVKDILE 417
Cdd:PRK05704 380 IIDGKEAVGFLVTIKELLE 398
|
|
| sucB |
TIGR01347 |
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ... |
7-417 |
9.58e-103 |
|
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: 310.90 E-value: 9.58e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760234714 7 KMPQLGESVTEGTISSWLVKPGDRVNKYDPIAEVMTDKVNAEVPSSFTGVIKDLIAAEGETLPVGEVMCSIQLAGEPDS- 85
Cdd:TIGR01347 4 KVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAILEEGNDATAa 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760234714 86 SEEAPKEEKNHSEEKSESLIQTDQSNKARYSPAVLKLSQEHGINLENVAGSGAGGRITRKDILKAVESGTAAKAQVNIEN 165
Cdd:TIGR01347 84 PPAKSGEEKEETPAASAAAAPTAAANRPSLSPAARRLAKEHGIDLSAVPGTGVTGRVTKEDIIKKTEAPASAQPPAAAAA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760234714 166 AepKADTQMYEPNlgvkqkssgsdmkiesgdREIPVTGIRKAIAQNMVRSKHEIPHAWTMVEADVTNLVQYRDSLKKEFR 245
Cdd:TIGR01347 164 A--AAPAAATRPE------------------ERVKMTRLRQRIAERLKEAQNSTAMLTTFNEVDMSAVMELRKRYKEEFE 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760234714 246 QKEGYNLTYFAFFVKAVAQALKEFPEMNSMWAGDKIVRKKDINISIAVSTDEALYVPVIKFADEKTIKGIAREINELAEK 325
Cdd:TIGR01347 224 KKHGVKLGFMSFFVKAVVAALKRFPEVNAEIDGDDIVYKDYYDISVAVSTDRGLVVPVVRNADRMSFADIEKEIADLGKK 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760234714 326 VRSGKLKSEDMQGGTFTVNNTGSFGSIQSMGIINHPQAAILQVESIVKKPVVMHGNmIAIRDRVNLCLSLDHRILDGLVC 405
Cdd:TIGR01347 304 ARDGKLTLEDMTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHGIKERPVAVNGQ-IEIRPMMYLALSYDHRLIDGKEA 382
|
410
....*....|..
gi 1760234714 406 GRFLARVKDILE 417
Cdd:TIGR01347 383 VTFLVTIKELLE 394
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
3-419 |
3.14e-99 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 309.24 E-value: 3.14e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760234714 3 IEQMKMPQLGesVTEGTISSWLVKPGDRVNKYDPIAEVMTDKVNAEVPSSFTGVIKDLIAAEGETLPVGEVMCSIQLAG- 81
Cdd:PRK11854 206 VKDVNVPDIG--GDEVEVTEVMVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVKTGSLIMRFEVEGa 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760234714 82 -----EPDSSEEAPKEEKNHSEEKSESLIQTDQS--------NKARYSPAVLKLSQEHGINLENVAGSGAGGRITRKDIL 148
Cdd:PRK11854 284 apaaaPAKQEAAAPAPAAAKAEAPAAAPAAKAEGksefaendAYVHATPLVRRLAREFGVNLAKVKGTGRKGRILKEDVQ 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760234714 149 KAVEsgtAAKAQVniENAEPKADTQMYEPNLGVKQKSSGSDMK-IEsgdrEIPVTGIRKAIAQNMVRSKHEIPHAWTMVE 227
Cdd:PRK11854 364 AYVK---DAVKRA--EAAPAAAAAGGGGPGLLPWPKVDFSKFGeIE----EVELGRIQKISGANLHRNWVMIPHVTQFDK 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760234714 228 ADVTNLVQYRDSLKKE-FRQKEGYNLTYFAFFVKAVAQALKEFPEMNSMWA--GDKIVRKKDINISIAVSTDEALYVPVI 304
Cdd:PRK11854 435 ADITELEAFRKQQNAEaEKRKLGVKITPLVFIMKAVAAALEQMPRFNSSLSedGQRLTLKKYVNIGIAVDTPNGLVVPVF 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760234714 305 KFADEKTIKGIAREINELAEKVRSGKLKSEDMQGGTFTVNNTGSFGSIQSMGIINHPQAAILQVESIVKKPvVMHGNMIA 384
Cdd:PRK11854 515 KDVNKKGIIELSRELMDISKKARDGKLTAGDMQGGCFTISSIGGLGTTHFTPIVNAPEVAILGVSKSAMEP-VWNGKEFA 593
|
410 420 430
....*....|....*....|....*....|....*
gi 1760234714 385 IRDRVNLCLSLDHRILDGLVCGRFLARVKDILEHI 419
Cdd:PRK11854 594 PRLMLPLSLSYDHRVIDGADGARFITIINDRLSDI 628
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
212-420 |
5.12e-95 |
|
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: 284.05 E-value: 5.12e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760234714 212 MVRSKHEIPHAWTMVEADVTNLVQYRDSLKKEFrQKEGYNLTYFAFFVKAVAQALKEFPEMNSMWAGDK--IVRKKDINI 289
Cdd:pfam00198 1 MTESKQTIPHFTLTDEVDVTELLALREELKEDA-ADEETKLTFLPFLVKAVALALKKFPELNASWDGEEgeIVYKKYVNI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760234714 290 SIAVSTDEALYVPVIKFADEKTIKGIAREINELAEKVRSGKLKSEDMQGGTFTVNNTGSFGSIQSMGIINHPQAAILQVE 369
Cdd:pfam00198 80 GIAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVG 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1760234714 370 SIVKKPVVMHGNmIAIRDRVNLCLSLDHRILDGLVCGRFLARVKDILEHIT 420
Cdd:pfam00198 160 RIRKRPVVVDGE-IVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPE 209
|
|
| SucB_Actino |
TIGR02927 |
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model ... |
5-417 |
3.12e-93 |
|
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: 292.30 E-value: 3.12e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760234714 5 QMKMPQLGESVTEGTISSWLVKPGDRVNKYDPIAEVMTDKVNAEVPSSFTGVIKDLIAAEGETLPVGEVMCSIQLAGE-- 82
Cdd:TIGR02927 128 EVKMPELGESVTEGTVTSWLKAVGDTVEVDEPLLEVSTDKVDTEIPSPVAGTLLEIRAPEDDTVEVGTVLAIIGDANAap 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760234714 83 ------------------------------PDSSEEAPKEEKnhSEEKSESLIQTDQSNKARYSPAVLKLSQEHGINLEN 132
Cdd:TIGR02927 208 aepaeeeapapseagsepapdpaaraphaaPDPPAPAPAPAK--TAAPAAAAPVSSGDSGPYVTPLVRKLAKDKGVDLST 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760234714 133 VAGSGAGGRITRKDILKAVESGTAAKAQV-----NIENAEPKADTQMYEPNlgvKQKSSGSDMKiesgdreipVTGIRKA 207
Cdd:TIGR02927 286 VKGTGVGGRIRKQDVLAAAKAAEEARAAAaapaaAAAPAAPAAAAKPAEPD---TAKLRGTTQK---------MNRIRQI 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760234714 208 IAQNMVRSKHEIPHAWTMVEADVTNLVQYRDSLKKEFRQKEGYNLTYFAFFVKAVAQALKEFPEMNSMWAGD--KIVRKK 285
Cdd:TIGR02927 354 TADKTIESLQTSAQLTQVHEVDMTRVAALRARAKNDFLEKNGVNLTFLPFFVQAVTEALKAHPNVNASYNAEtkEVTYHD 433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760234714 286 DINISIAVSTDEALYVPVIKFADEKTIKGIAREINELAEKVRSGKLKSEDMQGGTFTVNNTGSFGSIQSMGIINHPQAAI 365
Cdd:TIGR02927 434 VEHVGIAVDTPRGLLVPVIHNAGDLSLPGLAKAINDLAARARDNKLKPDELSGGTFTITNIGSGGALFDTPILNPPQAAI 513
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1760234714 366 LQVESIVKKPVVMH----GNMIAIRDRVNLCLSLDHRILDGLVCGRFLARVKDILE 417
Cdd:TIGR02927 514 LGTGAIVKRPRVIKdedgGESIAIRSVCYLPLTYDHRLVDGADAGRFLTTIKKRLE 569
|
|
| PTZ00144 |
PTZ00144 |
dihydrolipoamide succinyltransferase; Provisional |
3-417 |
1.27e-85 |
|
dihydrolipoamide succinyltransferase; Provisional
Pssm-ID: 240289 [Multi-domain] Cd Length: 418 Bit Score: 267.32 E-value: 1.27e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760234714 3 IEQMKMPQLGESVTEGTISSWLVKPGDRVNKYDPIAEVMTDKVNAEVPSSFTGVIKDLIAAEGETLPVGEVMCSIQLAGE 82
Cdd:PTZ00144 44 IKVIKVPTMGDSISEGTVVEWKKKVGDYVKEDEVICIIETDKVSVDIRAPASGVITKIFAEEGDTVEVGAPLSEIDTGGA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760234714 83 PdsSEEAPKEEKNHSEEKSESliqtdqsnkaryspavlklsqehginlenvagsgaggritrkdilKAVESGTAAKAQVN 162
Cdd:PTZ00144 124 P--PAAAPAAAAAAKAEKTTP---------------------------------------------EKPKAAAPTPEPPA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760234714 163 IENAEPKADTQMYEPNLGVKQKSSGSDMKIESgDREIPVTGIRKAIAQNMVRSKHEIPHAWTMVEADVTNLVQYRDSLKK 242
Cdd:PTZ00144 157 ASKPTPPAAAKPPEPAPAAKPPPTPVARADPR-ETRVPMSRMRQRIAERLKASQNTCAMLTTFNECDMSALMELRKEYKD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760234714 243 EFRQKEGYNLTYFAFFVKAVAQALKEFPEMNSMWAGDKIVRKKDINISIAVSTDEALYVPVIKFADEKTIKGIAREINEL 322
Cdd:PTZ00144 236 DFQKKHGVKLGFMSAFVKASTIALKKMPIVNAYIDGDEIVYRNYVDISVAVATPTGLVVPVIRNCENKSFAEIEKELADL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760234714 323 AEKVRSGKLKSEDMQGGTFTVNNTGSFGSIQSMGIINHPQAAILQVESIVKKPVVMhGNMIAIRDRVNLCLSLDHRILDG 402
Cdd:PTZ00144 316 AEKARNNKLTLEDMTGGTFTISNGGVFGSLMGTPIINPPQSAILGMHAIKKRPVVV-GNEIVIRPIMYLALTYDHRLIDG 394
|
410
....*....|....*
gi 1760234714 403 LVCGRFLARVKDILE 417
Cdd:PTZ00144 395 RDAVTFLKKIKDLIE 409
|
|
| PDHac_trf_mito |
TIGR01349 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
6-417 |
1.22e-83 |
|
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: 262.81 E-value: 1.22e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760234714 6 MKMPQLGESVTEGTISSWLVKPGDRVNKYDPIAEVMTDKVNAEVPSSFTGVIKDLIAAEG-ETLPVGEVMCSI------- 77
Cdd:TIGR01349 2 ITMPALSPTMTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEGtKDVPVNKPIAVLveekedv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760234714 78 -----------QLAGEPDSSEEAPKEEKNHSEEKSESLIQ----------TDQSNKARY--SPAVLKLSQEHGINLENVA 134
Cdd:TIGR01349 82 adafknyklesSASPAPKPSEIAPTAPPSAPKPSPAPQKQspepsspaplSDKESGDRIfaSPLAKKLAKEKGIDLSAVA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760234714 135 GSGAGGRITRKDILKAVE-----SGTAAKAQVNIENAEPK-ADTQMYEpnlgvkqkssgsdmkiesgdrEIPVTGIRKAI 208
Cdd:TIGR01349 162 GSGPNGRIVKKDIESFVPqspasANQQAAATTPATYPAAApVSTGSYE---------------------DVPLSNIRKII 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760234714 209 AQNMVRSKHEIPHAWTMVEADVTNLVQYRDSLKKEFRQKegYNLTYFAFFVKAVAQALKEFPEMNSMWAGDKIVRKKDIN 288
Cdd:TIGR01349 221 AKRLLESKQTIPHYYVSIECNVDKLLALRKELNAMASEV--YKLSVNDFIIKASALALREVPEANSSWTDNFIRRYKNVD 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760234714 289 ISIAVSTDEALYVPVIKFADEKTIKGIAREINELAEKVRSGKLKSEDMQGGTFTVNNTGSFGSIQSMGIINHPQAAILQV 368
Cdd:TIGR01349 299 ISVAVATPDGLITPIVRNADAKGLSTISNEIKDLAKRARNNKLKPEEFQGGTFTISNLGMFGIKDFTAIINPPQACILAV 378
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1760234714 369 ESIVKKPVVMHG--NMIAIRDRVNLCLSLDHRILDGLVCGRFLARVKDILE 417
Cdd:TIGR01349 379 GAVEDVAVVDNDeeKGFAVASIMSVTLSCDHRVIDGAVGAEFLKSFKKYLE 429
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
3-419 |
1.61e-71 |
|
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: 234.77 E-value: 1.61e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760234714 3 IEQMKMPQLGeSVTEGTISSWLVKPGDRVNKYDPIAEVMTDKVNAEVPSSFTGVIKDLIAAEGETLPVGEVMCSIQLAGE 82
Cdd:TIGR01348 116 VQEVTVPDIG-DIEKVTVIEVLVKVGDTVSADQSLITLESDKASMEVPAPASGVVKSVKVKVGDSVPTGDLILTLSVAGS 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760234714 83 PDSSEEAPKEEKNHS-----------------EEKSESLIQTDQSNKARY---SPAVLKLSQEHGINLENVAGSGAGGRI 142
Cdd:TIGR01348 195 TPATAPAPASAQPAAqspaatqpepaaapaaaKAQAPAPQQAGTQNPAKVdhaAPAVRRLAREFGVDLSAVKGTGIKGRI 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760234714 143 TRKDILKAVesgtaaKAQVNIENAEPkADTQMYEPNLGVKQKSSGSDMkiesGD-REIPVTGIRKAIAQNMVRSKHEIPH 221
Cdd:TIGR01348 275 LREDVQRFV------KEPSVRAQAAA-ASAAGGAPGALPWPNVDFSKF----GEvEEVDMSRIRKISGANLTRNWTMIPH 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760234714 222 AWTMVEADVTNLVQYRDSLKKEFRqKEGYNLTYFAFFVKAVAQALKEFPEMNSMWA--GDKIVRKKDINISIAVSTDEAL 299
Cdd:TIGR01348 344 VTHFDKADITEMEAFRKQQNAAVE-KEGVKLTVLHILMKAVAAALKKFPKFNASLDlgGEQLILKKYVNIGVAVDTPNGL 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760234714 300 YVPVIKFADEKTIKGIAREINELAEKVRSGKLKSEDMQGGTFTVNNTGSFGSIQSMGIINHPQAAILQVESIVKKPvVMH 379
Cdd:TIGR01348 423 LVPVIKDVDRKGITELALELSDLAKKARDGKLTPDEMQGACFTISSLGGIGGTAFTPIVNAPEVAILGVSKSGMEP-VWN 501
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1760234714 380 GNMIAIRDRVNLCLSLDHRILDGLVCGRFLARVKDILEHI 419
Cdd:TIGR01348 502 GKEFEPRLMLPLSLSYDHRVIDGADAARFTTYICESLADI 541
|
|
| PLN02744 |
PLN02744 |
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex |
2-421 |
1.47e-69 |
|
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
Pssm-ID: 215397 [Multi-domain] Cd Length: 539 Bit Score: 229.35 E-value: 1.47e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760234714 2 PIEQMKMPQLGESVTEGTISSWLVKPGDRVNKYDPIAEVMTDKVNAEVPSSFTGVIKDLIAAEG-ETLPVGEVMC----- 75
Cdd:PLN02744 111 PHQEIGMPSLSPTMTEGNIARWLKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVKGDGaKEIKVGEVIAitvee 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760234714 76 ------------SIQLAGEPDSSEEAPKEEKNHSEEKSESLIQTDQS---------NKARYSPAVLKLSQEHGINLENVA 134
Cdd:PLN02744 191 eedigkfkdykpSSSAAPAAPKAKPSPPPPKEEEVEKPASSPEPKASkpsappssgDRIFASPLARKLAEDNNVPLSSIK 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760234714 135 GSGAGGRITRKDILKAVESGTaakaqvniENAEPKADTQMYEPNLGVKqkssgsdmkiesgdrEIPVTGIRKAIAQNMVR 214
Cdd:PLN02744 271 GTGPDGRIVKADIEDYLASGG--------KGATAPPSTDSKAPALDYT---------------DIPNTQIRKVTASRLLQ 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760234714 215 SKHEIPHAWTMVEADVTNLVQYRDSLKKEFRQKEGYNLTYFAFFVKAVAQALKEFPEMNSMWAGDKIVRKKDINISIAVS 294
Cdd:PLN02744 328 SKQTIPHYYLTVDTRVDKLMALRSQLNSLQEASGGKKISVNDLVIKAAALALRKVPQCNSSWTDDYIRQYHNVNINVAVQ 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760234714 295 TDEALYVPVIKFADEKTIKGIAREINELAEKVRSGKLKSEDMQGGTFTVNNTGS-FGSIQSMGIINHPQAAILQVESIVK 373
Cdd:PLN02744 408 TENGLYVPVVKDADKKGLSTIAEEVKQLAQKARENSLKPEDYEGGTFTVSNLGGpFGIKQFCAIINPPQSAILAVGSAEK 487
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1760234714 374 KPVVMHGN-MIAIRDRVNLCLSLDHRILDGLVCGRFLARVKDILEHITS 421
Cdd:PLN02744 488 RVIPGSGPdQYNFASFMSVTLSCDHRVIDGAIGAEWLKAFKGYIENPES 536
|
|
| PLN02528 |
PLN02528 |
2-oxoisovalerate dehydrogenase E2 component |
10-418 |
5.80e-67 |
|
2-oxoisovalerate dehydrogenase E2 component
Pssm-ID: 215289 [Multi-domain] Cd Length: 416 Bit Score: 219.21 E-value: 5.80e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760234714 10 QLGESVTEGTISSWLVKPGDRVNKYDPIAEVMTDKVNAEVPSSFTGVIKDLIAAEGETLPVGEVMCSIQLAGEPDSSEEA 89
Cdd:PLN02528 5 QTGEGIAECELLRWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGKVAQINFSPGDIVKVGETLLKIMVEDSQHLRSDS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760234714 90 PKEEKNHSEEKS--ESLIQTDQSNKARYSPAVLKLSQEHGINLENVAGSGAGGRITRKDILKAVESGTAAKAQVNIENAE 167
Cdd:PLN02528 85 LLLPTDSSNIVSlaESDERGSNLSGVLSTPAVRHLAKQYGIDLNDILGTGKDGRVLKEDVLKYAAQKGVVKDSSSAEEAT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760234714 168 PKADTQMYEpnlGVKQKSSGSDmkiesGDREIPVTGIRKAIAQNMVRSKhEIPHAWTMVEADVTNLVQYRDSLKKEFRQk 247
Cdd:PLN02528 165 IAEQEEFST---SVSTPTEQSY-----EDKTIPLRGFQRAMVKTMTAAA-KVPHFHYVEEINVDALVELKASFQENNTD- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760234714 248 EGYNLTYFAFFVKAVAQALKEFPEMNSMWAGD--KIVRKKDINISIAVSTDEALYVPVIKFADEKTIKGIAREINELAEK 325
Cdd:PLN02528 235 PTVKHTFLPFLIKSLSMALSKYPLLNSCFNEEtsEIRLKGSHNIGVAMATEHGLVVPNIKNVQSLSLLEITKELSRLQHL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760234714 326 VRSGKLKSEDMQGGTFTVNNTGSFGSIQSMGIINHPQAAILQVESIVKKPVVMHGNMIAIRDRVNLCLSLDHRILDGLVC 405
Cdd:PLN02528 315 AAENKLNPEDITGGTITLSNIGAIGGKFGSPVLNLPEVAIIALGRIQKVPRFVDDGNVYPASIMTVTIGADHRVLDGATV 394
|
410
....*....|...
gi 1760234714 406 GRFLARVKDILEH 418
Cdd:PLN02528 395 ARFCNEWKSYVEK 407
|
|
| PLN02226 |
PLN02226 |
2-oxoglutarate dehydrogenase E2 component |
8-417 |
5.27e-64 |
|
2-oxoglutarate dehydrogenase E2 component
Pssm-ID: 177871 [Multi-domain] Cd Length: 463 Bit Score: 212.69 E-value: 5.27e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760234714 8 MPQLGESVTEGTISSWLVKPGDRVNKYDPIAEVMTDKVNAEVPSSFTGVIKDLIAAEGETLPVGEVMCSIQLAgEPDSSE 87
Cdd:PLN02226 96 VPHMGESITDGTLATFLKKPGERVQADEAIAQIETDKVTIDIASPASGVIQEFLVKEGDTVEPGTKVAIISKS-EDAASQ 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760234714 88 EAPKEEKNHSEEKSESliqtdqsnkarySPAVLKLSQEhginlenvagsgaggritrkdilkaVESGTAAKaqvnienaE 167
Cdd:PLN02226 175 VTPSQKIPETTDPKPS------------PPAEDKQKPK-------------------------VESAPVAE--------K 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760234714 168 PKADTQMYEPnlgvKQKSSGSDMKIESGDREIPVTGIRKAIAQNMVRSKHEIPHAWTMVEADVTNLVQYRDSLKKEFRQK 247
Cdd:PLN02226 210 PKAPSSPPPP----KQSAKEPQLPPKERERRVPMTRLRKRVATRLKDSQNTFALLTTFNEVDMTNLMKLRSQYKDAFYEK 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760234714 248 EGYNLTYFAFFVKAVAQALKEFPEMNSMWAGDKIVRKKDINISIAVSTDEALYVPVIKFADEKTIKGIAREINELAEKVR 327
Cdd:PLN02226 286 HGVKLGLMSGFIKAAVSALQHQPVVNAVIDGDDIIYRDYVDISIAVGTSKGLVVPVIRGADKMNFAEIEKTINGLAKKAN 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760234714 328 SGKLKSEDMQGGTFTVNNTGSFGSIQSMGIINHPQAAILQVESIVKKPVVMHGNMIAiRDRVNLCLSLDHRILDGLVCGR 407
Cdd:PLN02226 366 EGTISIDEMAGGSFTVSNGGVYGSLISTPIINPPQSAILGMHSIVSRPMVVGGSVVP-RPMMYVALTYDHRLIDGREAVY 444
|
410
....*....|
gi 1760234714 408 FLARVKDILE 417
Cdd:PLN02226 445 FLRRVKDVVE 454
|
|
| PRK11857 |
PRK11857 |
dihydrolipoamide acetyltransferase; Reviewed |
112-417 |
1.11e-58 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237002 [Multi-domain] Cd Length: 306 Bit Score: 194.24 E-value: 1.11e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760234714 112 KARYSPAVLKLSQEHGINLENVAGSGAGGRITRKDILKAVESGTAAKAQV------NIENAEPKADTQMYEPNLGvkqks 185
Cdd:PRK11857 1 KILATPIARALAKKLGIDISLLKGSGRDGKILAEDVENFIKSLKSAPTPAeaasvsSAQQAAKTAAPAAAPPKLE----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760234714 186 sgsdmkiesGDREiPVTGIRKAIAQNMVRSKHEIPHAWTMVEADVTNLVQYRDSLKKEFRQKEGYNLTYFAFFVKAVAQA 265
Cdd:PRK11857 76 ---------GKRE-KVAPIRKAIARAMTNSWSNVAYVNLVNEIDMTKLWDLRKSVKDPVLKTEGVKLTFLPFIAKAILIA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760234714 266 LKEFPEMNSMW--AGDKIVRKKDINISIAVSTDEALYVPVIKFADEKTIKGIAREINELAEKVRSGKLKSEDMQGGTFTV 343
Cdd:PRK11857 146 LKEFPIFAAKYdeATSELVYPDTLNLGIAVDTEAGLMVPVIKNAQKLSIVEIAKEISRLAKAARERKIKPDEMKGGSFTI 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1760234714 344 NNTGSFGSIQSMGIINHPQAAILQVESIVKKPVVMHGNMIAIRdRVNLCLSLDHRILDGLVCGRFLARVKDILE 417
Cdd:PRK11857 226 TNYGSVGSLYGVPVINYPELAIAGVGAIIDKAIVKNGQIVAGK-VMHLTVAADHRWIDGATIGRFASRVKELLE 298
|
|
| PRK14843 |
PRK14843 |
dihydrolipoamide acetyltransferase; Provisional |
110-417 |
3.97e-45 |
|
dihydrolipoamide acetyltransferase; Provisional
Pssm-ID: 184847 [Multi-domain] Cd Length: 347 Bit Score: 159.69 E-value: 3.97e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760234714 110 SNKARYSPAVLKLSQEHGINLENVAGSGAGGRITRKDILKAVESgtaakaqvNIENAEPKADTQmyepnlgVKQKSSGSD 189
Cdd:PRK14843 46 TNVVRISPLAKRIALEHNIAWQEIQGTGHRGKIMKKDVLALLPE--------NIENDSIKSPAQ-------IEKVEEVPD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760234714 190 MKIESGDRE-IPVTGIRKAIAQNMVRSKHEIPHAWTMVEADVTNLVQYRDSLKKEFRQKEGYNLTYFAFFVKAVAQALKE 268
Cdd:PRK14843 111 NVTPYGEIErIPMTPMRKVIAQRMVESYLTAPTFTLNYEVDMTEMLALRKKVLEPIMEATGKKTTVTDLLSLAVVKTLMK 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760234714 269 FPEMNSMWA--GDKIVRKKDINISIAVSTDEALYVPVIKFADEKTIKGIAREINELAEKVRSGKLKSEDMQGGTFTVNNT 346
Cdd:PRK14843 191 HPYINASLTedGKTIITHNYVNLAMAVGMDNGLMTPVVYNAEKMSLSELVVAFKDVIGRTLDGKLAPSELQNSTFTISNL 270
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1760234714 347 GSFGsIQSMG-IINHPQAAILQVESIVKKPVVMHGNmIAIRDRVNLCLSLDHRILDGLVCGRFLARVKDILE 417
Cdd:PRK14843 271 GMFG-VQSFGpIINQPNSAILGVSSTIEKPVVVNGE-IVIRPIMSLGLTIDHRVVDGMAGAKFMKDLKELIE 340
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
1-77 |
6.88e-31 |
|
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: 113.24 E-value: 6.88e-31
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1760234714 1 MPIEqMKMPQLGESVTEGTISSWLVKPGDRVNKYDPIAEVMTDKVNAEVPSSFTGVIKDLIAAEGETLPVGEVMCSI 77
Cdd:COG0508 1 MAIE-IKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
5-77 |
2.46e-28 |
|
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: 106.33 E-value: 2.46e-28
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1760234714 5 QMKMPQLGESVTEGTISSWLVKPGDRVNKYDPIAEVMTDKVNAEVPSSFTGVIKDLIAAEGETLPVGEVMCSI 77
Cdd:cd06849 2 EIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
2-89 |
4.92e-23 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 99.63 E-value: 4.92e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760234714 2 PIEQMKMPQLGESVTEGTISSWLVKPGDRVNKYDPIAEVMTDKVNAEVPSSFTGVIKDLIAAEGETLPVGEVMCSIQLAG 81
Cdd:PRK14875 1 SITPITMPKWGLSMTEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGETLPVGALLAVVADAE 80
|
....*...
gi 1760234714 82 EPDSSEEA 89
Cdd:PRK14875 81 VSDAEIDA 88
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
4-77 |
1.11e-18 |
|
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue binds biotin in one group and lipoic acid in the other. Note that the HMM does not currently recognize the Glycine cleavage system H proteins.
Pssm-ID: 395290 [Multi-domain] Cd Length: 73 Bit Score: 79.95 E-value: 1.11e-18
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1760234714 4 EQMKMPQLGESVTEGtISSWLVKPGDRVNKYDPIAEVMTDKVNAEVPSSFTGVIKDLIAAEGETLPVGEVMCSI 77
Cdd:pfam00364 1 TEIKSPMIGESVREG-VVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
|
|
| kgd |
PRK12270 |
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ... |
193-416 |
1.78e-17 |
|
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;
Pssm-ID: 237030 [Multi-domain] Cd Length: 1228 Bit Score: 84.94 E-value: 1.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760234714 193 ESGDREIPVTGIRKAIAQNMVRSKhEIPHAWTM----VEADVTNLVQYRDSLKK------EFRQKEGYnltyfaffvkAV 262
Cdd:PRK12270 112 AVEDEVTPLRGAAAAVAKNMDASL-EVPTATSVravpAKLLIDNRIVINNHLKRtrggkvSFTHLIGY----------AL 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760234714 263 AQALKEFPEMNSMWAGDK----IVRKKDINISIAVST-----DEALYVPVIKFADEKTIKGIAREINELAEKVRSGKLKS 333
Cdd:PRK12270 181 VQALKAFPNMNRHYAEVDgkptLVTPAHVNLGLAIDLpkkdgSRQLVVPAIKGAETMDFAQFWAAYEDIVRRARDGKLTA 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760234714 334 EDMQGGTFTVNNTGSFGSIQSMGIINHPQAAILQVESIvKKPVVMHG------NMIAIRDRVNLCLSLDHRILDGLVCGR 407
Cdd:PRK12270 261 DDFQGTTISLTNPGGIGTVHSVPRLMKGQGAIIGVGAM-EYPAEFQGaseerlAELGISKVMTLTSTYDHRIIQGAESGE 339
|
....*....
gi 1760234714 408 FLARVKDIL 416
Cdd:PRK12270 340 FLRTIHQLL 348
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
1-118 |
1.96e-12 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 68.79 E-value: 1.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760234714 1 MPIEqMKMPQLGESVTEGTISSWLVKPGDRVNKYDPIAEVMTDKVNAEVPSSFTGVIKDLIAAEG-ETLPVGEVMCSIQL 79
Cdd:PRK11892 1 MAIE-ILMPALSPTMEEGTLAKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKILVPEGtEGVKVNTPIAVLLE 79
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1760234714 80 AGE---PDSSEEAPKEEKNHSEEKSESLIQTDQSNKARYSPA 118
Cdd:PRK11892 80 EGEsasDAGAAPAAAAEAAAAAPAAAAAAAAKKAAPAPAAPA 121
|
|
| E3_binding |
pfam02817 |
e3 binding domain; This family represents a small domain of the E2 subunit of 2-oxo-acid ... |
114-148 |
3.76e-11 |
|
e3 binding domain; This family represents a small domain of the E2 subunit of 2-oxo-acid dehydrogenases responsible for the binding of the E3 subunit.
Pssm-ID: 460710 [Multi-domain] Cd Length: 36 Bit Score: 57.31 E-value: 3.76e-11
10 20 30
....*....|....*....|....*....|....*
gi 1760234714 114 RYSPAVLKLSQEHGINLENVAGSGAGGRITRKDIL 148
Cdd:pfam02817 2 LASPAARKLARELGIDLSDVKGTGPGGRITKEDVE 36
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
9-77 |
7.05e-10 |
|
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases, and the H-protein of the glycine cleavage system (GCS). These domains transport CO2, acyl, or methylamine, respectively, between components of the complex/protein via a biotinyl or lipoyl group, which is covalently attached to a highly conserved lysine residue.
Pssm-ID: 133456 [Multi-domain] Cd Length: 73 Bit Score: 55.14 E-value: 7.05e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1760234714 9 PQLGESVTEGTISSWLVKPGDRVNKYDPIAEVMTDKVNAEVPSSFTGVIKDLIAAEGETLPVGEVMCSI 77
Cdd:cd06663 5 PDLAQHLGDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKVEGDTPLVKI 73
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
18-77 |
8.48e-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: 48.95 E-value: 8.48e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1760234714 18 GTISSWLVKPGDRVNKYDPIA--EVMtdKVNAEVPSSFTGVIKDLIAAEGETLPVGEVMCSI 77
Cdd:cd06850 8 GTVVKVLVKEGDKVEAGQPLAvlEAM--KMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| PRK09282 |
PRK09282 |
pyruvate carboxylase subunit B; Validated |
18-78 |
8.29e-06 |
|
pyruvate carboxylase subunit B; Validated
Pssm-ID: 236449 [Multi-domain] Cd Length: 592 Bit Score: 47.91 E-value: 8.29e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1760234714 18 GTISSWLVKPGDRVNKYDPIA--EVMtdKVNAEVPSSFTGVIKDLIAAEGETLPVGEVMCSIQ 78
Cdd:PRK09282 531 GTVVKVKVKEGDKVKAGDTVLvlEAM--KMENEIQAPVDGTVKEILVKEGDRVNPGDVLMEIE 591
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
18-72 |
1.96e-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: 40.45 E-value: 1.96e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1760234714 18 GTISSWLVKPGDRVNKYDPIA--EVMtdKVNAEVPSSFTGVIKDLIAAEGETLPVGE 72
Cdd:COG1038 1085 GTVVKVLVKEGDEVKKGDPLLtiEAM--KMETTITAPRDGTVKEVLVKEGDQVEAGD 1139
|
|
| PRK14040 |
PRK14040 |
oxaloacetate decarboxylase subunit alpha; |
12-77 |
8.97e-03 |
|
oxaloacetate decarboxylase subunit alpha;
Pssm-ID: 237592 [Multi-domain] Cd Length: 593 Bit Score: 38.37 E-value: 8.97e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1760234714 12 GESVT---EGTISSWLVKPGDRVNKYDP--IAEVMtdKVNAEVPSSFTGVIKDLIAAEGETLPVGEVMCSI 77
Cdd:PRK14040 524 GEPVTaplAGNIFKVIVTEGQTVAEGDVllILEAM--KMETEIRAAQAGTVRGIAVKEGDAVAVGDTLLTL 592
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
18-72 |
9.02e-03 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 38.58 E-value: 9.02e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1760234714 18 GTISSWLVKPGDRVNKYDPIA--EVMtdKVNAEVPSSFTGVIKDLIAAEGETLPVGE 72
Cdd:PRK12999 1085 GSVVTVLVKEGDEVKAGDPLAviEAM--KMETTITAPVDGTVKRVLVKAGDQVEAGD 1139
|
|
| |
