|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11856 |
PRK11856 |
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed |
1-418 |
3.03e-176 |
|
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
Pssm-ID: 237001 [Multi-domain] Cd Length: 411 Bit Score: 498.16 E-value: 3.03e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52348820 1 MAVEqMTMPQLGESVTEGTISKWLVSVGDHVNKYDPIAEVMTDKVNAEVPSSFTGTIAELVGKEGETLQVGDVICKVETN 80
Cdd:PRK11856 1 MMFE-FKMPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDVVPVGSVIAVIEEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52348820 81 EEAKPEAEAVSKPDQEEAEPAKPEAKDTS--------------QKKRYSPAVLRLAGEHNIDLEQVEGTGAGGRITRKDI 146
Cdd:PRK11856 80 GEAEAAAAAEAAPEAPAPEPAPAAAAAAAaapaaaaapaapaaAAAKASPAVRKLARELGVDLSTVKGSGPGGRITKEDV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52348820 147 QRIIASGAVPQTDAAPEKQPGANAAGAIEPdqkpaqaapqaappqsaagdvEIPVTGIRNAIATNMVRSKHEIPHAWTMM 226
Cdd:PRK11856 160 EAAAAAAAPAAAAAAAAAAAPPAAAAEGEE---------------------RVPLSGMRKAIAKRMVESKREIPHFTLTD 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52348820 227 EVDVTGLVSYRNKIKNEFKKkegfsLTFFAFFVKAVAQALKEFPQMNSMWAGDKIIQKKDINISIAVATEDALYVPVIKH 306
Cdd:PRK11856 219 EVDVTALLALRKQLKAIGVK-----LTVTDFLIKAVALALKKFPELNASWDDDAIVLKKYVNIGIAVATDGGLIVPVIRD 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52348820 307 ADEKTIKGIAREISELAHKVRSGKLTSGDMSGGTFTVNNTGSFGSVQSMGIINHPQAAILQVESIVKRPVVMEhGMIAVR 386
Cdd:PRK11856 294 ADKKSLFELAREIKDLAEKAREGKLKPEELQGGTFTISNLGMFGGDYFTPIINPPEVAILGVGAIVERPVVVD-GEIVVR 372
|
410 420 430
....*....|....*....|....*....|..
gi 52348820 387 DMVNLCLSLDHRVLDGLICGRFLARVKEILEQ 418
Cdd:PRK11856 373 KVMPLSLSFDHRVIDGADAARFLKALKELLEN 404
|
|
| sucB |
TIGR01347 |
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ... |
9-417 |
1.41e-105 |
|
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: 318.22 E-value: 1.41e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52348820 9 PQLGESVTEGTISKWLVSVGDHVNKYDPIAEVMTDKVNAEVPSSFTGTIAELVGKEGETLQVGDVICKVETNEEAKPEAE 88
Cdd:TIGR01347 6 PELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAILEEGNDATAAPP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52348820 89 AVSKPDQEE--AEPAKPEAKDTSQKKRYSPAVLRLAGEHNIDLEQVEGTGAGGRITRKDIQRIIASGAVPQTDAAPEKQP 166
Cdd:TIGR01347 86 AKSGEEKEEtpAASAAAAPTAAANRPSLSPAARRLAKEHGIDLSAVPGTGVTGRVTKEDIIKKTEAPASAQPPAAAAAAA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52348820 167 GANAAGAIEpdqkpaqaapqaappqsaagdVEIPVTGIRNAIATNMVRSKHEIPHAWTMMEVDVTGLVSYRNKIKNEFKK 246
Cdd:TIGR01347 166 APAAATRPE---------------------ERVKMTRLRQRIAERLKEAQNSTAMLTTFNEVDMSAVMELRKRYKEEFEK 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52348820 247 KEGFSLTFFAFFVKAVAQALKEFPQMNSMWAGDKIIQKKDINISIAVATEDALYVPVIKHADEKTIKGIAREISELAHKV 326
Cdd:TIGR01347 225 KHGVKLGFMSFFVKAVVAALKRFPEVNAEIDGDDIVYKDYYDISVAVSTDRGLVVPVVRNADRMSFADIEKEIADLGKKA 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52348820 327 RSGKLTSGDMSGGTFTVNNTGSFGSVQSMGIINHPQAAILQVESIVKRPVVmEHGMIAVRDMVNLCLSLDHRVLDGLICG 406
Cdd:TIGR01347 305 RDGKLTLEDMTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHGIKERPVA-VNGQIEIRPMMYLALSYDHRLIDGKEAV 383
|
410
....*....|.
gi 52348820 407 RFLARVKEILE 417
Cdd:TIGR01347 384 TFLVTIKELLE 394
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
212-419 |
6.50e-94 |
|
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: 281.35 E-value: 6.50e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52348820 212 MVRSKHEIPHAWTMMEVDVTGLVSYRNKIKNEFKKKEGfSLTFFAFFVKAVAQALKEFPQMNSMWAGDK--IIQKKDINI 289
Cdd:pfam00198 1 MTESKQTIPHFTLTDEVDVTELLALREELKEDAADEET-KLTFLPFLVKAVALALKKFPELNASWDGEEgeIVYKKYVNI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52348820 290 SIAVATEDALYVPVIKHADEKTIKGIAREISELAHKVRSGKLTSGDMSGGTFTVNNTGSFGSVQSMGIINHPQAAILQVE 369
Cdd:pfam00198 80 GIAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVG 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 52348820 370 SIVKRPVVMEhGMIAVRDMVNLCLSLDHRVLDGLICGRFLARVKEILEQI 419
Cdd:pfam00198 160 RIRKRPVVVD-GEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENP 208
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
1-77 |
2.90e-29 |
|
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: 109.00 E-value: 2.90e-29
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 52348820 1 MAVEqMTMPQLGESVTEGTISKWLVSVGDHVNKYDPIAEVMTDKVNAEVPSSFTGTIAELVGKEGETLQVGDVICKV 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 |
3.22e-27 |
|
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: 103.25 E-value: 3.22e-27
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 52348820 5 QMTMPQLGESVTEGTISKWLVSVGDHVNKYDPIAEVMTDKVNAEVPSSFTGTIAELVGKEGETLQVGDVICKV 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 |
3.03e-176 |
|
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
Pssm-ID: 237001 [Multi-domain] Cd Length: 411 Bit Score: 498.16 E-value: 3.03e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52348820 1 MAVEqMTMPQLGESVTEGTISKWLVSVGDHVNKYDPIAEVMTDKVNAEVPSSFTGTIAELVGKEGETLQVGDVICKVETN 80
Cdd:PRK11856 1 MMFE-FKMPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDVVPVGSVIAVIEEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52348820 81 EEAKPEAEAVSKPDQEEAEPAKPEAKDTS--------------QKKRYSPAVLRLAGEHNIDLEQVEGTGAGGRITRKDI 146
Cdd:PRK11856 80 GEAEAAAAAEAAPEAPAPEPAPAAAAAAAaapaaaaapaapaaAAAKASPAVRKLARELGVDLSTVKGSGPGGRITKEDV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52348820 147 QRIIASGAVPQTDAAPEKQPGANAAGAIEPdqkpaqaapqaappqsaagdvEIPVTGIRNAIATNMVRSKHEIPHAWTMM 226
Cdd:PRK11856 160 EAAAAAAAPAAAAAAAAAAAPPAAAAEGEE---------------------RVPLSGMRKAIAKRMVESKREIPHFTLTD 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52348820 227 EVDVTGLVSYRNKIKNEFKKkegfsLTFFAFFVKAVAQALKEFPQMNSMWAGDKIIQKKDINISIAVATEDALYVPVIKH 306
Cdd:PRK11856 219 EVDVTALLALRKQLKAIGVK-----LTVTDFLIKAVALALKKFPELNASWDDDAIVLKKYVNIGIAVATDGGLIVPVIRD 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52348820 307 ADEKTIKGIAREISELAHKVRSGKLTSGDMSGGTFTVNNTGSFGSVQSMGIINHPQAAILQVESIVKRPVVMEhGMIAVR 386
Cdd:PRK11856 294 ADKKSLFELAREIKDLAEKAREGKLKPEELQGGTFTISNLGMFGGDYFTPIINPPEVAILGVGAIVERPVVVD-GEIVVR 372
|
410 420 430
....*....|....*....|....*....|..
gi 52348820 387 DMVNLCLSLDHRVLDGLICGRFLARVKEILEQ 418
Cdd:PRK11856 373 KVMPLSLSFDHRVIDGADAARFLKALKELLEN 404
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
2-419 |
3.22e-123 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 368.38 E-value: 3.22e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52348820 2 AVEQMTMPQLGEsVTEGTISKWLVSVGDHVNKYDPIAEVMTDKVNAEVPSSFTGTIAELVGKEGETLQVGDVICKVETNE 81
Cdd:PRK11855 118 GVVEVKVPDIGE-ITEVEVIEWLVKVGDTVEEDQSLITVETDKATMEIPSPVAGVVKEIKVKVGDKVSVGSLLVVIEVAA 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52348820 82 EAKPEAEAVSKPDQEEAEPAKPEA---------------KDTSQKKRY-SPAVLRLAGEHNIDLEQVEGTGAGGRITRKD 145
Cdd:PRK11855 197 AAPAAAAAPAAAAPAAAAAAAPAPapaaaaapaaaapaaAAAPGKAPHaSPAVRRLARELGVDLSQVKGTGKKGRITKED 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52348820 146 IQRIIASGAVPQTDAAPEKQPGANAAGAIEPdqkpaqaapQAAPPQSAAGDVEI-PVTGIRNAIATNMVRSKHEIPHAWT 224
Cdd:PRK11855 277 VQAFVKGAMSAAAAAAAAAAAAGGGGLGLLP---------WPKVDFSKFGEIETkPLSRIKKISAANLHRSWVTIPHVTQ 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52348820 225 MMEVDVTGLVSYRNKIKNEFKKKeGFSLTFFAFFVKAVAQALKEFPQMNSM--WAGDKIIQKKDINISIAVATEDALYVP 302
Cdd:PRK11855 348 FDEADITDLEALRKQLKKEAEKA-GVKLTMLPFFIKAVVAALKEFPVFNASldEDGDELTYKKYFNIGFAVDTPNGLVVP 426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52348820 303 VIKHADEKTIKGIAREISELAHKVRSGKLTSGDMSGGTFTVNNTGSFGSVQSMGIINHPQAAILQVESIVKRPvVMEHGM 382
Cdd:PRK11855 427 VIKDVDKKSLLEIAREIAELAKKARDGKLKPDDMQGGCFTISSLGGIGGTAFTPIINAPEVAILGVGKSQMKP-VWDGKE 505
|
410 420 430
....*....|....*....|....*....|....*..
gi 52348820 383 IAVRDMVNLCLSLDHRVLDGLICGRFLARVKEILEQI 419
Cdd:PRK11855 506 FVPRLMLPLSLSYDHRVIDGATAARFTNYLKQLLADP 542
|
|
| PRK05704 |
PRK05704 |
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase; |
1-418 |
1.10e-113 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
Pssm-ID: 235571 [Multi-domain] Cd Length: 407 Bit Score: 339.12 E-value: 1.10e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52348820 1 MAVEQMTmPQLGESVTEGTISKWLVSVGDHVNKYDPIAEVMTDKVNAEVPSSFTGTIAELVGKEGETLQVGDVICKVETN 80
Cdd:PRK05704 1 MMVEIKV-PTLPESVTEATIATWHKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGDTVTVGQVLGRIDEG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52348820 81 EEA--KPEAEAVSKPDQEEAEPAKPEAKDTSQKKRYSPAVLRLAGEHNIDLEQVEGTGAGGRITRKDIQRIIASGAVPQT 158
Cdd:PRK05704 80 AAAgaAAAAAAAAAAAAAAPAQAQAAAAAEQSNDALSPAARKLAAENGLDASAVKGTGKGGRVTKEDVLAALAAAAAAPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52348820 159 DAAPEKQPGANAAGAIEPDqkpaqaapqaappqsaagdVEIPVTGIRNAIATNMVRSKHEIPHAWTMMEVDVTGLVSYRN 238
Cdd:PRK05704 160 APAAAAPAAAPAPLGARPE-------------------ERVPMTRLRKTIAERLLEAQNTTAMLTTFNEVDMTPVMDLRK 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52348820 239 KIKNEFKKKEGFSLTFFAFFVKAVAQALKEFPQMNSMWAGDKIIQKKDINISIAVATEDALYVPVIKHADEKTIKGIARE 318
Cdd:PRK05704 221 QYKDAFEKKHGVKLGFMSFFVKAVVEALKRYPEVNASIDGDDIVYHNYYDIGIAVGTPRGLVVPVLRDADQLSFAEIEKK 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52348820 319 ISELAHKVRSGKLTSGDMSGGTFTVNNTGSFGSVQSMGIINHPQAAILQVESIVKRPVVmEHGMIAVRDMVNLCLSLDHR 398
Cdd:PRK05704 301 IAELAKKARDGKLSIEELTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHKIKERPVA-VNGQIVIRPMMYLALSYDHR 379
|
410 420
....*....|....*....|
gi 52348820 399 VLDGLICGRFLARVKEILEQ 418
Cdd:PRK05704 380 IIDGKEAVGFLVTIKELLED 399
|
|
| sucB |
TIGR01347 |
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ... |
9-417 |
1.41e-105 |
|
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: 318.22 E-value: 1.41e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52348820 9 PQLGESVTEGTISKWLVSVGDHVNKYDPIAEVMTDKVNAEVPSSFTGTIAELVGKEGETLQVGDVICKVETNEEAKPEAE 88
Cdd:TIGR01347 6 PELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAILEEGNDATAAPP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52348820 89 AVSKPDQEE--AEPAKPEAKDTSQKKRYSPAVLRLAGEHNIDLEQVEGTGAGGRITRKDIQRIIASGAVPQTDAAPEKQP 166
Cdd:TIGR01347 86 AKSGEEKEEtpAASAAAAPTAAANRPSLSPAARRLAKEHGIDLSAVPGTGVTGRVTKEDIIKKTEAPASAQPPAAAAAAA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52348820 167 GANAAGAIEpdqkpaqaapqaappqsaagdVEIPVTGIRNAIATNMVRSKHEIPHAWTMMEVDVTGLVSYRNKIKNEFKK 246
Cdd:TIGR01347 166 APAAATRPE---------------------ERVKMTRLRQRIAERLKEAQNSTAMLTTFNEVDMSAVMELRKRYKEEFEK 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52348820 247 KEGFSLTFFAFFVKAVAQALKEFPQMNSMWAGDKIIQKKDINISIAVATEDALYVPVIKHADEKTIKGIAREISELAHKV 326
Cdd:TIGR01347 225 KHGVKLGFMSFFVKAVVAALKRFPEVNAEIDGDDIVYKDYYDISVAVSTDRGLVVPVVRNADRMSFADIEKEIADLGKKA 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52348820 327 RSGKLTSGDMSGGTFTVNNTGSFGSVQSMGIINHPQAAILQVESIVKRPVVmEHGMIAVRDMVNLCLSLDHRVLDGLICG 406
Cdd:TIGR01347 305 RDGKLTLEDMTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHGIKERPVA-VNGQIEIRPMMYLALSYDHRLIDGKEAV 383
|
410
....*....|.
gi 52348820 407 RFLARVKEILE 417
Cdd:TIGR01347 384 TFLVTIKELLE 394
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
2-421 |
1.59e-103 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 320.41 E-value: 1.59e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52348820 2 AVEQMTMPQLGesVTEGTISKWLVSVGDHVNKYDPIAEVMTDKVNAEVPSSFTGTIAELVGKEGETLQVGDVICKVET-- 79
Cdd:PRK11854 205 GVKDVNVPDIG--GDEVEVTEVMVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVKTGSLIMRFEVeg 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52348820 80 ---------NEEAKPEAEAVSKPDQEEAEPAKPEAKD---TSQKKRY-SPAVLRLAGEHNIDLEQVEGTGAGGRITRKDI 146
Cdd:PRK11854 283 aapaaapakQEAAAPAPAAAKAEAPAAAPAAKAEGKSefaENDAYVHaTPLVRRLAREFGVNLAKVKGTGRKGRILKEDV 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52348820 147 QRIiASGAVPQTDAAPEKQPGANAAGAIEPDQKPAQAAPqaappqsaaGDVE-IPVTGIRNAIATNMVRSKHEIPHAWTM 225
Cdd:PRK11854 363 QAY-VKDAVKRAEAAPAAAAAGGGGPGLLPWPKVDFSKF---------GEIEeVELGRIQKISGANLHRNWVMIPHVTQF 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52348820 226 MEVDVTGLVSYRnKIKN--EFKKKEGFSLTFFAFFVKAVAQALKEFPQMNSMWA--GDKIIQKKDINISIAVATEDALYV 301
Cdd:PRK11854 433 DKADITELEAFR-KQQNaeAEKRKLGVKITPLVFIMKAVAAALEQMPRFNSSLSedGQRLTLKKYVNIGIAVDTPNGLVV 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52348820 302 PVIKHADEKTIKGIAREISELAHKVRSGKLTSGDMSGGTFTVNNTGSFGSVQSMGIINHPQAAILQVESIVKRPvVMEHG 381
Cdd:PRK11854 512 PVFKDVNKKGIIELSRELMDISKKARDGKLTAGDMQGGCFTISSIGGLGTTHFTPIVNAPEVAILGVSKSAMEP-VWNGK 590
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 52348820 382 MIAVRDMVNLCLSLDHRVLDGLICGRFLARVKEILEQIDD 421
Cdd:PRK11854 591 EFAPRLMLPLSLSYDHRVIDGADGARFITIINDRLSDIRR 630
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
212-419 |
6.50e-94 |
|
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: 281.35 E-value: 6.50e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52348820 212 MVRSKHEIPHAWTMMEVDVTGLVSYRNKIKNEFKKKEGfSLTFFAFFVKAVAQALKEFPQMNSMWAGDK--IIQKKDINI 289
Cdd:pfam00198 1 MTESKQTIPHFTLTDEVDVTELLALREELKEDAADEET-KLTFLPFLVKAVALALKKFPELNASWDGEEgeIVYKKYVNI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52348820 290 SIAVATEDALYVPVIKHADEKTIKGIAREISELAHKVRSGKLTSGDMSGGTFTVNNTGSFGSVQSMGIINHPQAAILQVE 369
Cdd:pfam00198 80 GIAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVG 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 52348820 370 SIVKRPVVMEhGMIAVRDMVNLCLSLDHRVLDGLICGRFLARVKEILEQI 419
Cdd:pfam00198 160 RIRKRPVVVD-GEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENP 208
|
|
| SucB_Actino |
TIGR02927 |
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model ... |
8-420 |
5.25e-92 |
|
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: 288.83 E-value: 5.25e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52348820 8 MPQLGESVTEGTISKWLVSVGDHVNKYDPIAEVMTDKVNAEVPSSFTGTIAELVGKEGETLQVGDVICKV---------- 77
Cdd:TIGR02927 131 MPELGESVTEGTVTSWLKAVGDTVEVDEPLLEVSTDKVDTEIPSPVAGTLLEIRAPEDDTVEVGTVLAIIgdanaapaep 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52348820 78 -----ETNEEAKPE------AEAVSKPDQEEAEPAKPEAK----------DTSQKKRYSPAVLRLAGEHNIDLEQVEGTG 136
Cdd:TIGR02927 211 aeeeaPAPSEAGSEpapdpaARAPHAAPDPPAPAPAPAKTaapaaaapvsSGDSGPYVTPLVRKLAKDKGVDLSTVKGTG 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52348820 137 AGGRITRKDIQriiasgAVPQTDAAPEKQPGANAAGAiEPDQKPAQAAPQAAPPQSAAGDVEiPVTGIRNAIATNMVRSK 216
Cdd:TIGR02927 291 VGGRIRKQDVL------AAAKAAEEARAAAAAPAAAA-APAAPAAAAKPAEPDTAKLRGTTQ-KMNRIRQITADKTIESL 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52348820 217 HEIPHAWTMMEVDVTGLVSYRNKIKNEFKKKEGFSLTFFAFFVKAVAQALKEFPQMNSMWAGD--KIIQKKDINISIAVA 294
Cdd:TIGR02927 363 QTSAQLTQVHEVDMTRVAALRARAKNDFLEKNGVNLTFLPFFVQAVTEALKAHPNVNASYNAEtkEVTYHDVEHVGIAVD 442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52348820 295 TEDALYVPVIKHADEKTIKGIAREISELAHKVRSGKLTSGDMSGGTFTVNNTGSFGSVQSMGIINHPQAAILQVESIVKR 374
Cdd:TIGR02927 443 TPRGLLVPVIHNAGDLSLPGLAKAINDLAARARDNKLKPDELSGGTFTITNIGSGGALFDTPILNPPQAAILGTGAIVKR 522
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 52348820 375 PVVM--EHG--MIAVRDMVNLCLSLDHRVLDGLICGRFLARVKEILEQID 420
Cdd:TIGR02927 523 PRVIkdEDGgeSIAIRSVCYLPLTYDHRLVDGADAGRFLTTIKKRLEEGD 572
|
|
| PTZ00144 |
PTZ00144 |
dihydrolipoamide succinyltransferase; Provisional |
2-417 |
2.55e-84 |
|
dihydrolipoamide succinyltransferase; Provisional
Pssm-ID: 240289 [Multi-domain] Cd Length: 418 Bit Score: 264.24 E-value: 2.55e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52348820 2 AVEQMTMPQLGESVTEGTISKWLVSVGDHVNKYDPIAEVMTDKVNAEVPSSFTGTIAELVGKEGETLQVGDVICKVETNE 81
Cdd:PTZ00144 43 SIKVIKVPTMGDSISEGTVVEWKKKVGDYVKEDEVICIIETDKVSVDIRAPASGVITKIFAEEGDTVEVGAPLSEIDTGG 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52348820 82 eaKPEAEAVSKPDQEEAEPAKPEAKDTSQKKRYSPAvlrlagehnidleqvegtgaggritrkdiqriiASGAVPQTDAA 161
Cdd:PTZ00144 123 --APPAAAPAAAAAAKAEKTTPEKPKAAAPTPEPPA---------------------------------ASKPTPPAAAK 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52348820 162 PEKQPgANAAGAIEPdqkpaqaapqaaPPQSAAGDVEIPVTGIRNAIATNMVRSKHEIPHAWTMMEVDVTGLVSYRNKIK 241
Cdd:PTZ00144 168 PPEPA-PAAKPPPTP------------VARADPRETRVPMSRMRQRIAERLKASQNTCAMLTTFNECDMSALMELRKEYK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52348820 242 NEFKKKEGFSLTFFAFFVKAVAQALKEFPQMNSMWAGDKIIQKKDINISIAVATEDALYVPVIKHADEKTIKGIAREISE 321
Cdd:PTZ00144 235 DDFQKKHGVKLGFMSAFVKASTIALKKMPIVNAYIDGDEIVYRNYVDISVAVATPTGLVVPVIRNCENKSFAEIEKELAD 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52348820 322 LAHKVRSGKLTSGDMSGGTFTVNNTGSFGSVQSMGIINHPQAAILQVESIVKRPVVMEhGMIAVRDMVNLCLSLDHRVLD 401
Cdd:PTZ00144 315 LAEKARNNKLTLEDMTGGTFTISNGGVFGSLMGTPIINPPQSAILGMHAIKKRPVVVG-NEIVIRPIMYLALTYDHRLID 393
|
410
....*....|....*.
gi 52348820 402 GLICGRFLARVKEILE 417
Cdd:PTZ00144 394 GRDAVTFLKKIKDLIE 409
|
|
| PDHac_trf_mito |
TIGR01349 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
6-417 |
8.76e-81 |
|
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: 255.49 E-value: 8.76e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52348820 6 MTMPQLGESVTEGTISKWLVSVGDHVNKYDPIAEVMTDKVNAEVPSSFTGTIAELVGKEG-ETLQVGDVICKVETNEEAK 84
Cdd:TIGR01349 2 ITMPALSPTMTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEGtKDVPVNKPIAVLVEEKEDV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52348820 85 PEAEAVSKPDQEEAEPAKPEAK------------DTSQKKR-------------------YSPAVLRLAGEHNIDLEQVE 133
Cdd:TIGR01349 82 ADAFKNYKLESSASPAPKPSEIaptappsapkpsPAPQKQSpepsspaplsdkesgdrifASPLAKKLAKEKGIDLSAVA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52348820 134 GTGAGGRITRKDIQRIIASGAVPQTDAAPEKQPGANAAGAIEPDQKPaqaapqaappqsaagdVEIPVTGIRNAIATNMV 213
Cdd:TIGR01349 162 GSGPNGRIVKKDIESFVPQSPASANQQAAATTPATYPAAAPVSTGSY----------------EDVPLSNIRKIIAKRLL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52348820 214 RSKHEIPHAWTMMEVDVTGLVSYR---NKIKNEFKKkegfsLTFFAFFVKAVAQALKEFPQMNSMWAGDKIIQKKDINIS 290
Cdd:TIGR01349 226 ESKQTIPHYYVSIECNVDKLLALRkelNAMASEVYK-----LSVNDFIIKASALALREVPEANSSWTDNFIRRYKNVDIS 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52348820 291 IAVATEDALYVPVIKHADEKTIKGIAREISELAHKVRSGKLTSGDMSGGTFTVNNTGSFGSVQSMGIINHPQAAILQVES 370
Cdd:TIGR01349 301 VAVATPDGLITPIVRNADAKGLSTISNEIKDLAKRARNNKLKPEEFQGGTFTISNLGMFGIKDFTAIINPPQACILAVGA 380
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 52348820 371 IVKRPVVM--EHGMIAVRDMVNLCLSLDHRVLDGLICGRFLARVKEILE 417
Cdd:TIGR01349 381 VEDVAVVDndEEKGFAVASIMSVTLSCDHRVIDGAVGAEFLKSFKKYLE 429
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
3-419 |
1.35e-78 |
|
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: 253.26 E-value: 1.35e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52348820 3 VEQMTMPQLGeSVTEGTISKWLVSVGDHVNKYDPIAEVMTDKVNAEVPSSFTGTIAELVGKEGETLQVGDVICKVETNEE 82
Cdd:TIGR01348 116 VQEVTVPDIG-DIEKVTVIEVLVKVGDTVSADQSLITLESDKASMEVPAPASGVVKSVKVKVGDSVPTGDLILTLSVAGS 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52348820 83 AKPEAE-------AVSKPDQEEAEPAKPEAKDTSQKK--------------RYSPAVLRLAGEHNIDLEQVEGTGAGGRI 141
Cdd:TIGR01348 195 TPATAPapasaqpAAQSPAATQPEPAAAPAAAKAQAPapqqagtqnpakvdHAAPAVRRLAREFGVDLSAVKGTGIKGRI 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52348820 142 TRKDIQRIIASgAVPQTDAAPEKQPGANAAGAIEPDQKPAQAapqaappqsaaGDVE-IPVTGIRNAIATNMVRSKHEIP 220
Cdd:TIGR01348 275 LREDVQRFVKE-PSVRAQAAAASAAGGAPGALPWPNVDFSKF-----------GEVEeVDMSRIRKISGANLTRNWTMIP 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52348820 221 HAWTMMEVDVTGLVSYRNKIkNEFKKKEGFSLTFFAFFVKAVAQALKEFPQMNSMWA--GDKIIQKKDINISIAVATEDA 298
Cdd:TIGR01348 343 HVTHFDKADITEMEAFRKQQ-NAAVEKEGVKLTVLHILMKAVAAALKKFPKFNASLDlgGEQLILKKYVNIGVAVDTPNG 421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52348820 299 LYVPVIKHADEKTIKGIAREISELAHKVRSGKLTSGDMSGGTFTVNNTGSFGSVQSMGIINHPQAAILQVESIVKRPvVM 378
Cdd:TIGR01348 422 LLVPVIKDVDRKGITELALELSDLAKKARDGKLTPDEMQGACFTISSLGGIGGTAFTPIVNAPEVAILGVSKSGMEP-VW 500
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 52348820 379 EHGMIAVRDMVNLCLSLDHRVLDGLICGRFLARVKEILEQI 419
Cdd:TIGR01348 501 NGKEFEPRLMLPLSLSYDHRVIDGADAARFTTYICESLADI 541
|
|
| PLN02744 |
PLN02744 |
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex |
4-417 |
7.12e-73 |
|
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
Pssm-ID: 215397 [Multi-domain] Cd Length: 539 Bit Score: 237.83 E-value: 7.12e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52348820 4 EQMTMPQLGESVTEGTISKWLVSVGDHVNKYDPIAEVMTDKVNAEVPSSFTGTIAELVGKEG-ETLQVGDVIC-KVETNE 81
Cdd:PLN02744 113 QEIGMPSLSPTMTEGNIARWLKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVKGDGaKEIKVGEVIAiTVEEEE 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52348820 82 E---------------AKPEAEAVSKPDQEE-----AEPAKPEAKDTSQKKR------YSPAVLRLAGEHNIDLEQVEGT 135
Cdd:PLN02744 193 DigkfkdykpsssaapAAPKAKPSPPPPKEEevekpASSPEPKASKPSAPPSsgdrifASPLARKLAEDNNVPLSSIKGT 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52348820 136 GAGGRITRKDIQRIIASGAvpqTDAAPEKQPGANAAGaiepdqkpaqaapqaappqsaAGDVEIPVTGIRNAIATNMVRS 215
Cdd:PLN02744 273 GPDGRIVKADIEDYLASGG---KGATAPPSTDSKAPA---------------------LDYTDIPNTQIRKVTASRLLQS 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52348820 216 KHEIPHAWTMMEVDVTGLVSYRNKIKNEFKKKEGFSLTFFAFFVKAVAQALKEFPQMNSMWAGDKIIQKKDINISIAVAT 295
Cdd:PLN02744 329 KQTIPHYYLTVDTRVDKLMALRSQLNSLQEASGGKKISVNDLVIKAAALALRKVPQCNSSWTDDYIRQYHNVNINVAVQT 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52348820 296 EDALYVPVIKHADEKTIKGIAREISELAHKVRSGKLTSGDMSGGTFTVNNTGS-FGSVQSMGIINHPQAAILQVESIVKR 374
Cdd:PLN02744 409 ENGLYVPVVKDADKKGLSTIAEEVKQLAQKARENSLKPEDYEGGTFTVSNLGGpFGIKQFCAIINPPQSAILAVGSAEKR 488
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 52348820 375 PVVME-HGMIAVRDMVNLCLSLDHRVLDGLICGRFLARVKEILE 417
Cdd:PLN02744 489 VIPGSgPDQYNFASFMSVTLSCDHRVIDGAIGAEWLKAFKGYIE 532
|
|
| PLN02528 |
PLN02528 |
2-oxoisovalerate dehydrogenase E2 component |
10-418 |
6.88e-65 |
|
2-oxoisovalerate dehydrogenase E2 component
Pssm-ID: 215289 [Multi-domain] Cd Length: 416 Bit Score: 213.81 E-value: 6.88e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52348820 10 QLGESVTEGTISKWLVSVGDHVNKYDPIAEVMTDKVNAEVPSSFTGTIAELVGKEGETLQVGDVICKVETNEEAKPEAEA 89
Cdd:PLN02528 5 QTGEGIAECELLRWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGKVAQINFSPGDIVKVGETLLKIMVEDSQHLRSDS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52348820 90 VSKPDQEEAEPAKPEAKDTSQKKR---YSPAVLRLAGEHNIDLEQVEGTGAGGRITRKDIQRIIASGAVPQTDAApekqp 166
Cdd:PLN02528 85 LLLPTDSSNIVSLAESDERGSNLSgvlSTPAVRHLAKQYGIDLNDILGTGKDGRVLKEDVLKYAAQKGVVKDSSS----- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52348820 167 ganaAGAIEPDQKPAQAAPQAAPPQSAAGDVEIPVTGIRNAIATNMVRSKhEIPHAWTMMEVDVTGLVSYRNKIKNEfKK 246
Cdd:PLN02528 160 ----AEEATIAEQEEFSTSVSTPTEQSYEDKTIPLRGFQRAMVKTMTAAA-KVPHFHYVEEINVDALVELKASFQEN-NT 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52348820 247 KEGFSLTFFAFFVKAVAQALKEFPQMNSMWAGD--KIIQKKDINISIAVATEDALYVPVIKHADEKTIKGIAREISELAH 324
Cdd:PLN02528 234 DPTVKHTFLPFLIKSLSMALSKYPLLNSCFNEEtsEIRLKGSHNIGVAMATEHGLVVPNIKNVQSLSLLEITKELSRLQH 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52348820 325 KVRSGKLTSGDMSGGTFTVNNTGSFGSVQSMGIINHPQAAILQVESIVKRPVVMEHGMIAVRDMVNLCLSLDHRVLDGLI 404
Cdd:PLN02528 314 LAAENKLNPEDITGGTITLSNIGAIGGKFGSPVLNLPEVAIIALGRIQKVPRFVDDGNVYPASIMTVTIGADHRVLDGAT 393
|
410
....*....|....
gi 52348820 405 CGRFLARVKEILEQ 418
Cdd:PLN02528 394 VARFCNEWKSYVEK 407
|
|
| PRK11857 |
PRK11857 |
dihydrolipoamide acetyltransferase; Reviewed |
115-418 |
1.05e-61 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237002 [Multi-domain] Cd Length: 306 Bit Score: 201.95 E-value: 1.05e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52348820 115 SPAVLRLAGEHNIDLEQVEGTGAGGRITRKDIQRIIASGAVPQTDAAPEKQPGANAAGAIEPdqkpaqaapQAAPPQSAA 194
Cdd:PRK11857 5 TPIARALAKKLGIDISLLKGSGRDGKILAEDVENFIKSLKSAPTPAEAASVSSAQQAAKTAA---------PAAAPPKLE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52348820 195 GDVEiPVTGIRNAIATNMVRSKHEIPHAWTMMEVDVTGLVSYRNKIKNEFKKKEGFSLTFFAFFVKAVAQALKEFPQMNS 274
Cdd:PRK11857 76 GKRE-KVAPIRKAIARAMTNSWSNVAYVNLVNEIDMTKLWDLRKSVKDPVLKTEGVKLTFLPFIAKAILIALKEFPIFAA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52348820 275 MW--AGDKIIQKKDINISIAVATEDALYVPVIKHADEKTIKGIAREISELAHKVRSGKLTSGDMSGGTFTVNNTGSFGSV 352
Cdd:PRK11857 155 KYdeATSELVYPDTLNLGIAVDTEAGLMVPVIKNAQKLSIVEIAKEISRLAKAARERKIKPDEMKGGSFTITNYGSVGSL 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 52348820 353 QSMGIINHPQAAILQVESIVKRPVVMEHGMIAVRDMvNLCLSLDHRVLDGLICGRFLARVKEILEQ 418
Cdd:PRK11857 235 YGVPVINYPELAIAGVGAIIDKAIVKNGQIVAGKVM-HLTVAADHRWIDGATIGRFASRVKELLEK 299
|
|
| PLN02226 |
PLN02226 |
2-oxoglutarate dehydrogenase E2 component |
3-417 |
1.89e-61 |
|
2-oxoglutarate dehydrogenase E2 component
Pssm-ID: 177871 [Multi-domain] Cd Length: 463 Bit Score: 206.14 E-value: 1.89e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52348820 3 VEQMTMPQLGESVTEGTISKWLVSVGDHVNKYDPIAEVMTDKVNAEVPSSFTGTIAELVGKEGETLQVGDVICKVETNEE 82
Cdd:PLN02226 91 TVEAVVPHMGESITDGTLATFLKKPGERVQADEAIAQIETDKVTIDIASPASGVIQEFLVKEGDTVEPGTKVAIISKSED 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52348820 83 AKPEAEAVSKPDQEEAEPAKPEAKDTSQKKryspavlrlagehnidleqvegtgaggritrkdiqriIASGAVPQTDAAP 162
Cdd:PLN02226 171 AASQVTPSQKIPETTDPKPSPPAEDKQKPK-------------------------------------VESAPVAEKPKAP 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52348820 163 EKQPGANAAgAIEPDQKPAQAapqaappqsaagDVEIPVTGIRNAIATNMVRSKHEIPHAWTMMEVDVTGLVSYRNKIKN 242
Cdd:PLN02226 214 SSPPPPKQS-AKEPQLPPKER------------ERRVPMTRLRKRVATRLKDSQNTFALLTTFNEVDMTNLMKLRSQYKD 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52348820 243 EFKKKEGFSLTFFAFFVKAVAQALKEFPQMNSMWAGDKIIQKKDINISIAVATEDALYVPVIKHADEKTIKGIAREISEL 322
Cdd:PLN02226 281 AFYEKHGVKLGLMSGFIKAAVSALQHQPVVNAVIDGDDIIYRDYVDISIAVGTSKGLVVPVIRGADKMNFAEIEKTINGL 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52348820 323 AHKVRSGKLTSGDMSGGTFTVNNTGSFGSVQSMGIINHPQAAILQVESIVKRPVVMeHGMIAVRDMVNLCLSLDHRVLDG 402
Cdd:PLN02226 361 AKKANEGTISIDEMAGGSFTVSNGGVYGSLISTPIINPPQSAILGMHSIVSRPMVV-GGSVVPRPMMYVALTYDHRLIDG 439
|
410
....*....|....*
gi 52348820 403 LICGRFLARVKEILE 417
Cdd:PLN02226 440 REAVYFLRRVKDVVE 454
|
|
| PRK14843 |
PRK14843 |
dihydrolipoamide acetyltransferase; Provisional |
106-417 |
2.74e-46 |
|
dihydrolipoamide acetyltransferase; Provisional
Pssm-ID: 184847 [Multi-domain] Cd Length: 347 Bit Score: 162.77 E-value: 2.74e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52348820 106 KDTSQKkRYSPAVLRLAGEHNIDLEQVEGTGAGGRITRKDIQRIIASGAVPQTDAAPEKQPGANAAgaiePDQKPAQaap 185
Cdd:PRK14843 44 KDTNVV-RISPLAKRIALEHNIAWQEIQGTGHRGKIMKKDVLALLPENIENDSIKSPAQIEKVEEV----PDNVTPY--- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52348820 186 qaappqsaaGDVE-IPVTGIRNAIATNMVRSKHEIPHAWTMMEVDVTGLVSYRNKIKNEFKKKEGFSLTFFAFFVKAVAQ 264
Cdd:PRK14843 116 ---------GEIErIPMTPMRKVIAQRMVESYLTAPTFTLNYEVDMTEMLALRKKVLEPIMEATGKKTTVTDLLSLAVVK 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52348820 265 ALKEFPQMNSMWA--GDKIIQKKDINISIAVATEDALYVPVIKHADEKTIKGIAREISELAHKVRSGKLTSGDMSGGTFT 342
Cdd:PRK14843 187 TLMKHPYINASLTedGKTIITHNYVNLAMAVGMDNGLMTPVVYNAEKMSLSELVVAFKDVIGRTLDGKLAPSELQNSTFT 266
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 52348820 343 VNNTGSFGsVQSMG-IINHPQAAILQVESIVKRPVVMeHGMIAVRDMVNLCLSLDHRVLDGLICGRFLARVKEILE 417
Cdd:PRK14843 267 ISNLGMFG-VQSFGpIINQPNSAILGVSSTIEKPVVV-NGEIVIRPIMSLGLTIDHRVVDGMAGAKFMKDLKELIE 340
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
1-77 |
2.90e-29 |
|
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: 109.00 E-value: 2.90e-29
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 52348820 1 MAVEqMTMPQLGESVTEGTISKWLVSVGDHVNKYDPIAEVMTDKVNAEVPSSFTGTIAELVGKEGETLQVGDVICKV 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 |
3.22e-27 |
|
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: 103.25 E-value: 3.22e-27
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 52348820 5 QMTMPQLGESVTEGTISKWLVSVGDHVNKYDPIAEVMTDKVNAEVPSSFTGTIAELVGKEGETLQVGDVICKV 77
Cdd:cd06849 2 EIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
|
|
| kgd |
PRK12270 |
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ... |
151-416 |
4.67e-22 |
|
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;
Pssm-ID: 237030 [Multi-domain] Cd Length: 1228 Bit Score: 99.19 E-value: 4.67e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52348820 151 ASGAVPQTDAAPEKQPGANAAGAiEPDQKPAQAAPQAAPPQSAAGDVEIPVTGIRNAIATNMVRSKhEIPHAWTMMEVDV 230
Cdd:PRK12270 71 APAPPAAAAPAAPPKPAAAAAAA-AAPAAPPAAAAAAAPAAAAVEDEVTPLRGAAAAVAKNMDASL-EVPTATSVRAVPA 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52348820 231 TGLVSYRNKIKNEFKKKEGFSLTFFAFFVKAVAQALKEFPQMNSMWAGDK----IIQKKDINISIA--VATED---ALYV 301
Cdd:PRK12270 149 KLLIDNRIVINNHLKRTRGGKVSFTHLIGYALVQALKAFPNMNRHYAEVDgkptLVTPAHVNLGLAidLPKKDgsrQLVV 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52348820 302 PVIKHADEKTIKGIAREISELAHKVRSGKLTSGDMSGGTFTVNNTGSFGSVQSMGIINHPQAAILQVESivkrpvvMEH- 380
Cdd:PRK12270 229 PAIKGAETMDFAQFWAAYEDIVRRARDGKLTADDFQGTTISLTNPGGIGTVHSVPRLMKGQGAIIGVGA-------MEYp 301
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 52348820 381 -----------GMIAVRDMVNLCLSLDHRVLDGLICGRFLARVKEIL 416
Cdd:PRK12270 302 aefqgaseerlAELGISKVMTLTSTYDHRIIQGAESGEFLRTIHQLL 348
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
7-153 |
1.47e-21 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 95.40 E-value: 1.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52348820 7 TMPQLGESVTEGTISKWLVSVGDHVNKYDPIAEVMTDKVNAEVPSSFTGTIAELVGKEGETLQVGDVICKVETNEEAKPE 86
Cdd:PRK14875 6 TMPKWGLSMTEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGETLPVGALLAVVADAEVSDAE 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 52348820 87 AEAVSKPDQEEAEPAkpeakdtsqkkryspavlrlagehNIDLEQVEGTGAGGRITRKDIqRIIASG 153
Cdd:PRK14875 86 IDAFIAPFARRFAPE------------------------GIDEEDAGPAPRKARIGGRTV-RYLRLG 127
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
4-77 |
5.11e-20 |
|
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: 83.42 E-value: 5.11e-20
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 52348820 4 EQMTMPQLGESVTEGtISKWLVSVGDHVNKYDPIAEVMTDKVNAEVPSSFTGTIAELVGKEGETLQVGDVICKV 77
Cdd:pfam00364 1 TEIKSPMIGESVREG-VVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
1-105 |
7.77e-18 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 85.82 E-value: 7.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52348820 1 MAVEqMTMPQLGesVTEGTISKWLVSVGDHVNKYDPIAEVMTDKVNAEVPSSFTGTIAELVGKEGETLQVGDVICKVETN 80
Cdd:PRK11854 1 MAIE-IKVPDIG--ADEVEVTEILVKVGDKVEAEQSLITVEGDKASMEVPSPQAGVVKEIKVKVGDKVETGALIMIFESA 77
|
90 100
....*....|....*....|....*
gi 52348820 81 EEAKPEAEAVSKPDQEEAEPAKPEA 105
Cdd:PRK11854 78 DGAADAAPAQAEEKKEAAPAAAPAA 102
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
1-135 |
5.48e-13 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 70.33 E-value: 5.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52348820 1 MAVEqMTMPQLGESVTEGTISKWLVSVGDHVNKYDPIAEVMTDKVNAEVPSSFTGTIAELVGKEG-ETLQVGDVICKV-- 77
Cdd:PRK11892 1 MAIE-ILMPALSPTMEEGTLAKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKILVPEGtEGVKVNTPIAVLle 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 52348820 78 ETNEEAKPEAEAVSKPDQEEAEPAKPEAKDTSQKKRYSPAVLRLAGEHNIDLEQVEGT 135
Cdd:PRK11892 80 EGESASDAGAAPAAAAEAAAAAPAAAAAAAAKKAAPAPAAPAAPAAEVAADPDIPAGT 137
|
|
| E3_binding |
pfam02817 |
e3 binding domain; This family represents a small domain of the E2 subunit of 2-oxo-acid ... |
113-147 |
4.95e-12 |
|
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: 60.01 E-value: 4.95e-12
10 20 30
....*....|....*....|....*....|....*
gi 52348820 113 RYSPAVLRLAGEHNIDLEQVEGTGAGGRITRKDIQ 147
Cdd:pfam02817 2 LASPAARKLARELGIDLSDVKGTGPGGRITKEDVE 36
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
9-77 |
3.67e-09 |
|
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: 52.83 E-value: 3.67e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 52348820 9 PQLGESVTEGTISKWLVSVGDHVNKYDPIAEVMTDKVNAEVPSSFTGTIAELVGKEGETLQVGDVICKV 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 |
1.77e-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: 50.88 E-value: 1.77e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 52348820 18 GTISKWLVSVGDHVNKYDPIA--EVMtdKVNAEVPSSFTGTIAELVGKEGETLQVGDVICKV 77
Cdd:cd06850 8 GTVVKVLVKEGDKVEAGQPLAvlEAM--KMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| PRK09282 |
PRK09282 |
pyruvate carboxylase subunit B; Validated |
18-78 |
2.82e-05 |
|
pyruvate carboxylase subunit B; Validated
Pssm-ID: 236449 [Multi-domain] Cd Length: 592 Bit Score: 46.37 E-value: 2.82e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 52348820 18 GTISKWLVSVGDHVNKYDPIA--EVMtdKVNAEVPSSFTGTIAELVGKEGETLQVGDVICKVE 78
Cdd:PRK09282 531 GTVVKVKVKEGDKVKAGDTVLvlEAM--KMENEIQAPVDGTVKEILVKEGDRVNPGDVLMEIE 591
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
7-77 |
7.89e-05 |
|
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: 45.07 E-value: 7.89e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 52348820 7 TMPqlgesvteGTISKWLVSVGDHVNKYDPIA--EVMtdKVNAEVPSSFTGTIAELVGKEGETLQVGDVICKV 77
Cdd:COG1038 1082 PMP--------GTVVKVLVKEGDEVKKGDPLLtiEAM--KMETTITAPRDGTVKEVLVKEGDQVEAGDLLIEL 1144
|
|
| PRK14040 |
PRK14040 |
oxaloacetate decarboxylase subunit alpha; |
2-74 |
9.96e-05 |
|
oxaloacetate decarboxylase subunit alpha;
Pssm-ID: 237592 [Multi-domain] Cd Length: 593 Bit Score: 44.54 E-value: 9.96e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 52348820 2 AVEQMTMPQLGESVT---EGTISKWLVSVGDHVNKYDP--IAEVMtdKVNAEVPSSFTGTIAELVGKEGETLQVGDVI 74
Cdd:PRK14040 514 AAAAAPAAAAGEPVTaplAGNIFKVIVTEGQTVAEGDVllILEAM--KMETEIRAAQAGTVRGIAVKEGDAVAVGDTL 589
|
|
| |
