|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02744 |
PLN02744 |
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex |
1-539 |
0e+00 |
|
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
Pssm-ID: 215397 [Multi-domain] Cd Length: 539 Bit Score: 1013.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400212 1 MASRIINHSKKLKHVSALLRRDHAVAVRCFSNSTHPSLVGREDIFKARLNYSSVERISKCGTGNVTMLSGISTTSTKLSS 80
Cdd:PLN02744 2 YASRIINHSKKLRNVSNLLRREHAALVRYFSNSTRSSLGKGDDIAKRRGYPPLERRSQPKVSSLGLFGSNISRTARKNGS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400212 81 PMAGPKLFKEFISSQMRSVRGFSSSSDLPPHQEIGMPSLSPTMTEGNIARWLKKEGDKVAPGEVLCEVETDKATVEMECM 160
Cdd:PLN02744 82 PMTGSGLFKSLSSSQMQSARGFSSSSDLPPHQEIGMPSLSPTMTEGNIARWLKKEGDKVSPGEVLCEVETDKATVEMECM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400212 161 EEGFLAKIVKEEGAKEIQVGEVIAITVEDEDDIQKFKDYTPSSDTGPAAPEAKPAPSLPKEEKVEKPASAPEAKISKPSS 240
Cdd:PLN02744 162 EEGYLAKIVKGDGAKEIKVGEVIAITVEEEEDIGKFKDYKPSSSAAPAAPKAKPSPPPPKEEEVEKPASSPEPKASKPSA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400212 241 AP-SEDRIFASPLARKLAEDNNVPLSSIKGTGPEGRIVKADVEDFLASGSKETTAKPSKqvDSKVPALDYVDIPHTQIRK 319
Cdd:PLN02744 242 PPsSGDRIFASPLARKLAEDNNVPLSSIKGTGPDGRIVKADIEDYLASGGKGATAPPST--DSKAPALDYTDIPNTQIRK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400212 320 VTASRLAFSKQTIPHYYLTVDTCVDKMMGLRSQLNSFQEASGGKRISVNDLVIKAAALALRKVPQCNSSWTDEYIRQFKN 399
Cdd:PLN02744 320 VTASRLLQSKQTIPHYYLTVDTRVDKLMALRSQLNSLQEASGGKKISVNDLVIKAAALALRKVPQCNSSWTDDYIRQYHN 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400212 400 VNINVAVQTENGLYVPVVKDADKKGLSTIGEEVRFLAQKAKENSLKPEDYEGGTFTVSNLGGPFGIKQFCAVINPPQAAI 479
Cdd:PLN02744 400 VNINVAVQTENGLYVPVVKDADKKGLSTIAEEVKQLAQKARENSLKPEDYEGGTFTVSNLGGPFGIKQFCAIINPPQSAI 479
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400212 480 LAIGSAEKRVVPGTGPDQYNVASYMSVTLSCDHRVIDGAIGAEWLKAFKGYIETPESMLL 539
Cdd:PLN02744 480 LAVGSAEKRVIPGSGPDQYNFASFMSVTLSCDHRVIDGAIGAEWLKAFKGYIENPESMLL 539
|
|
| PDHac_trf_mito |
TIGR01349 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
113-539 |
0e+00 |
|
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: 523.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400212 113 EIGMPSLSPTMTEGNIARWLKKEGDKVAPGEVLCEVETDKATVEMECMEEGFLAKIVKEEGAKEIQVGEVIAITVEDEDD 192
Cdd:TIGR01349 1 KITMPALSPTMTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEGTKDVPVNKPIAVLVEEKED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400212 193 IQK-FKDYTPSSDTGPAAPEAKPAPSLPKEEKVEKPASAPEAKiSKPSSAP-----SEDRIFASPLARKLAEDNNVPLSS 266
Cdd:TIGR01349 81 VADaFKNYKLESSASPAPKPSEIAPTAPPSAPKPSPAPQKQSP-EPSSPAPlsdkeSGDRIFASPLAKKLAKEKGIDLSA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400212 267 IKGTGPEGRIVKADVEDFL------ASGSKETTAKPSKQVDSKVPALDYVDIPHTQIRKVTASRLAFSKQTIPHYYLTVD 340
Cdd:TIGR01349 160 VAGSGPNGRIVKKDIESFVpqspasANQQAAATTPATYPAAAPVSTGSYEDVPLSNIRKIIAKRLLESKQTIPHYYVSIE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400212 341 TCVDKMMGLRSQLNSfqEASGGKRISVNDLVIKAAALALRKVPQCNSSWTDEYIRQFKNVNINVAVQTENGLYVPVVKDA 420
Cdd:TIGR01349 240 CNVDKLLALRKELNA--MASEVYKLSVNDFIIKASALALREVPEANSSWTDNFIRRYKNVDISVAVATPDGLITPIVRNA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400212 421 DKKGLSTIGEEVRFLAQKAKENSLKPEDYEGGTFTVSNLgGPFGIKQFCAVINPPQAAILAIGSAEKRVVPGTGPDQ-YN 499
Cdd:TIGR01349 318 DAKGLSTISNEIKDLAKRARNNKLKPEEFQGGTFTISNL-GMFGIKDFTAIINPPQACILAVGAVEDVAVVDNDEEKgFA 396
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 18400212 500 VASYMSVTLSCDHRVIDGAIGAEWLKAFKGYIETPESMLL 539
Cdd:TIGR01349 397 VASIMSVTLSCDHRVIDGAVGAEFLKSFKKYLENPIEMLL 436
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
328-538 |
4.59e-91 |
|
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: 277.89 E-value: 4.59e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400212 328 SKQTIPHYYLTVDTCVDKMMGLRSQLNSfQEASGGKRISVNDLVIKAAALALRKVPQCNSSWTDE--YIRQFKNVNINVA 405
Cdd:pfam00198 4 SKQTIPHFTLTDEVDVTELLALREELKE-DAADEETKLTFLPFLVKAVALALKKFPELNASWDGEegEIVYKKYVNIGIA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400212 406 VQTENGLYVPVVKDADKKGLSTIGEEVRFLAQKAKENSLKPEDYEGGTFTVSNLGGpFGIKQFCAVINPPQAAILAIGSA 485
Cdd:pfam00198 83 VATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGM-FGVTFFTPIINPPQVAILGVGRI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 18400212 486 EKRVVPGTGpdQYNVASYMSVTLSCDHRVIDGAIGAEWLKAFKGYIETPESML 538
Cdd:pfam00198 162 RKRPVVVDG--EIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELLL 212
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
112-185 |
6.48e-30 |
|
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: 111.73 E-value: 6.48e-30
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18400212 112 QEIGMPSLSPTMTEGNIARWLKKEGDKVAPGEVLCEVETDKATVEMECMEEGFLAKIVKEEGAKeIQVGEVIAI 185
Cdd:cd06849 1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDT-VPVGQVIAV 73
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
112-185 |
7.72e-27 |
|
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: 103.22 E-value: 7.72e-27
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18400212 112 QEIGMPSLSPTMTEGNIARWLKKEGDKVAPGEVLCEVETDKATVEMECMEEGFLAKIVKEEGAKeIQVGEVIAI 185
Cdd:COG0508 3 IEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDT-VPVGAVIAV 75
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02744 |
PLN02744 |
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex |
1-539 |
0e+00 |
|
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
Pssm-ID: 215397 [Multi-domain] Cd Length: 539 Bit Score: 1013.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400212 1 MASRIINHSKKLKHVSALLRRDHAVAVRCFSNSTHPSLVGREDIFKARLNYSSVERISKCGTGNVTMLSGISTTSTKLSS 80
Cdd:PLN02744 2 YASRIINHSKKLRNVSNLLRREHAALVRYFSNSTRSSLGKGDDIAKRRGYPPLERRSQPKVSSLGLFGSNISRTARKNGS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400212 81 PMAGPKLFKEFISSQMRSVRGFSSSSDLPPHQEIGMPSLSPTMTEGNIARWLKKEGDKVAPGEVLCEVETDKATVEMECM 160
Cdd:PLN02744 82 PMTGSGLFKSLSSSQMQSARGFSSSSDLPPHQEIGMPSLSPTMTEGNIARWLKKEGDKVSPGEVLCEVETDKATVEMECM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400212 161 EEGFLAKIVKEEGAKEIQVGEVIAITVEDEDDIQKFKDYTPSSDTGPAAPEAKPAPSLPKEEKVEKPASAPEAKISKPSS 240
Cdd:PLN02744 162 EEGYLAKIVKGDGAKEIKVGEVIAITVEEEEDIGKFKDYKPSSSAAPAAPKAKPSPPPPKEEEVEKPASSPEPKASKPSA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400212 241 AP-SEDRIFASPLARKLAEDNNVPLSSIKGTGPEGRIVKADVEDFLASGSKETTAKPSKqvDSKVPALDYVDIPHTQIRK 319
Cdd:PLN02744 242 PPsSGDRIFASPLARKLAEDNNVPLSSIKGTGPDGRIVKADIEDYLASGGKGATAPPST--DSKAPALDYTDIPNTQIRK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400212 320 VTASRLAFSKQTIPHYYLTVDTCVDKMMGLRSQLNSFQEASGGKRISVNDLVIKAAALALRKVPQCNSSWTDEYIRQFKN 399
Cdd:PLN02744 320 VTASRLLQSKQTIPHYYLTVDTRVDKLMALRSQLNSLQEASGGKKISVNDLVIKAAALALRKVPQCNSSWTDDYIRQYHN 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400212 400 VNINVAVQTENGLYVPVVKDADKKGLSTIGEEVRFLAQKAKENSLKPEDYEGGTFTVSNLGGPFGIKQFCAVINPPQAAI 479
Cdd:PLN02744 400 VNINVAVQTENGLYVPVVKDADKKGLSTIAEEVKQLAQKARENSLKPEDYEGGTFTVSNLGGPFGIKQFCAIINPPQSAI 479
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400212 480 LAIGSAEKRVVPGTGPDQYNVASYMSVTLSCDHRVIDGAIGAEWLKAFKGYIETPESMLL 539
Cdd:PLN02744 480 LAVGSAEKRVIPGSGPDQYNFASFMSVTLSCDHRVIDGAIGAEWLKAFKGYIENPESMLL 539
|
|
| PDHac_trf_mito |
TIGR01349 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
113-539 |
0e+00 |
|
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: 523.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400212 113 EIGMPSLSPTMTEGNIARWLKKEGDKVAPGEVLCEVETDKATVEMECMEEGFLAKIVKEEGAKEIQVGEVIAITVEDEDD 192
Cdd:TIGR01349 1 KITMPALSPTMTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEGTKDVPVNKPIAVLVEEKED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400212 193 IQK-FKDYTPSSDTGPAAPEAKPAPSLPKEEKVEKPASAPEAKiSKPSSAP-----SEDRIFASPLARKLAEDNNVPLSS 266
Cdd:TIGR01349 81 VADaFKNYKLESSASPAPKPSEIAPTAPPSAPKPSPAPQKQSP-EPSSPAPlsdkeSGDRIFASPLAKKLAKEKGIDLSA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400212 267 IKGTGPEGRIVKADVEDFL------ASGSKETTAKPSKQVDSKVPALDYVDIPHTQIRKVTASRLAFSKQTIPHYYLTVD 340
Cdd:TIGR01349 160 VAGSGPNGRIVKKDIESFVpqspasANQQAAATTPATYPAAAPVSTGSYEDVPLSNIRKIIAKRLLESKQTIPHYYVSIE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400212 341 TCVDKMMGLRSQLNSfqEASGGKRISVNDLVIKAAALALRKVPQCNSSWTDEYIRQFKNVNINVAVQTENGLYVPVVKDA 420
Cdd:TIGR01349 240 CNVDKLLALRKELNA--MASEVYKLSVNDFIIKASALALREVPEANSSWTDNFIRRYKNVDISVAVATPDGLITPIVRNA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400212 421 DKKGLSTIGEEVRFLAQKAKENSLKPEDYEGGTFTVSNLgGPFGIKQFCAVINPPQAAILAIGSAEKRVVPGTGPDQ-YN 499
Cdd:TIGR01349 318 DAKGLSTISNEIKDLAKRARNNKLKPEEFQGGTFTISNL-GMFGIKDFTAIINPPQACILAVGAVEDVAVVDNDEEKgFA 396
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 18400212 500 VASYMSVTLSCDHRVIDGAIGAEWLKAFKGYIETPESMLL 539
Cdd:TIGR01349 397 VASIMSVTLSCDHRVIDGAVGAEFLKSFKKYLENPIEMLL 436
|
|
| PRK11856 |
PRK11856 |
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed |
113-539 |
5.26e-163 |
|
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
Pssm-ID: 237001 [Multi-domain] Cd Length: 411 Bit Score: 469.27 E-value: 5.26e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400212 113 EIGMPSLSPTMTEGNIARWLKKEGDKVAPGEVLCEVETDKATVEMECMEEGFLAKIVKEEGAKeIQVGEVIAiTVEDEDD 192
Cdd:PRK11856 4 EFKMPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDV-VPVGSVIA-VIEEEGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400212 193 iqkfkdytpssDTGPAAPEAKPAPSLPKEEKVEKPASAPEAKISKPSSAPSEDRIFASPLARKLAEDNNVPLSSIKGTGP 272
Cdd:PRK11856 82 -----------AEAAAAAEAAPEAPAPEPAPAAAAAAAAAPAAAAAPAAPAAAAAKASPAVRKLARELGVDLSTVKGSGP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400212 273 EGRIVKADVEDFLASGSKETTAKPSKQVDSKVPALDYVD-IPHTQIRKVTASRLAFSKQTIPHYYLTVDTCVDKMMGLRS 351
Cdd:PRK11856 151 GGRITKEDVEAAAAAAAPAAAAAAAAAAAPPAAAAEGEErVPLSGMRKAIAKRMVESKREIPHFTLTDEVDVTALLALRK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400212 352 QLNSFQEasggkRISVNDLVIKAAALALRKVPQCNSSWTDEYIRQFKNVNINVAVQTENGLYVPVVKDADKKGLSTIGEE 431
Cdd:PRK11856 231 QLKAIGV-----KLTVTDFLIKAVALALKKFPELNASWDDDAIVLKKYVNIGIAVATDGGLIVPVIRDADKKSLFELARE 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400212 432 VRFLAQKAKENSLKPEDYEGGTFTVSNLGGpFGIKQFCAVINPPQAAILAIGSAEKRVVPGTGpdQYNVASYMSVTLSCD 511
Cdd:PRK11856 306 IKDLAEKAREGKLKPEELQGGTFTISNLGM-FGGDYFTPIINPPEVAILGVGAIVERPVVVDG--EIVVRKVMPLSLSFD 382
|
410 420
....*....|....*....|....*...
gi 18400212 512 HRVIDGAIGAEWLKAFKGYIETPESMLL 539
Cdd:PRK11856 383 HRVIDGADAARFLKALKELLENPALLLL 410
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
328-538 |
4.59e-91 |
|
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: 277.89 E-value: 4.59e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400212 328 SKQTIPHYYLTVDTCVDKMMGLRSQLNSfQEASGGKRISVNDLVIKAAALALRKVPQCNSSWTDE--YIRQFKNVNINVA 405
Cdd:pfam00198 4 SKQTIPHFTLTDEVDVTELLALREELKE-DAADEETKLTFLPFLVKAVALALKKFPELNASWDGEegEIVYKKYVNIGIA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400212 406 VQTENGLYVPVVKDADKKGLSTIGEEVRFLAQKAKENSLKPEDYEGGTFTVSNLGGpFGIKQFCAVINPPQAAILAIGSA 485
Cdd:pfam00198 83 VATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGM-FGVTFFTPIINPPQVAILGVGRI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 18400212 486 EKRVVPGTGpdQYNVASYMSVTLSCDHRVIDGAIGAEWLKAFKGYIETPESML 538
Cdd:pfam00198 162 RKRPVVVDG--EIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELLL 212
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
124-539 |
9.01e-90 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 285.95 E-value: 9.01e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400212 124 TEGNIARWLKKEGDKVAPGEVLCEVETDKATVEMECMEEGFLAKIVKEEGAKeIQVGEVIAItVEDEddiqkfkdytpss 203
Cdd:PRK11855 131 TEVEVIEWLVKVGDTVEEDQSLITVETDKATMEIPSPVAGVVKEIKVKVGDK-VSVGSLLVV-IEVA------------- 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400212 204 dTGPAAPEAKPAPSLPKEEKVEKPASAPEAKISKPSSAPSE-----DRIFASPLARKLAEDNNVPLSSIKGTGPEGRIVK 278
Cdd:PRK11855 196 -AAAPAAAAAPAAAAPAAAAAAAPAPAPAAAAAPAAAAPAAaaapgKAPHASPAVRRLARELGVDLSQVKGTGKKGRITK 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400212 279 ADVEDFL---------------ASGSKETTAKPSKQVD-SKVPALDYVdiPHTQIRKVTASRLAFSKQTIPHYYLTVDTC 342
Cdd:PRK11855 275 EDVQAFVkgamsaaaaaaaaaaAAGGGGLGLLPWPKVDfSKFGEIETK--PLSRIKKISAANLHRSWVTIPHVTQFDEAD 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400212 343 VDKMMGLRSQLNSFQEASGGKrISVNDLVIKAAALALRKVPQCNSSW---TDEYIRqFKNVNINVAVQTENGLYVPVVKD 419
Cdd:PRK11855 353 ITDLEALRKQLKKEAEKAGVK-LTMLPFFIKAVVAALKEFPVFNASLdedGDELTY-KKYFNIGFAVDTPNGLVVPVIKD 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400212 420 ADKKGLSTIGEEVRFLAQKAKENSLKPEDYEGGTFTVSNLGGpFGIKQFCAVINPPQAAILAIGSAEKRvvPGTGPDQYN 499
Cdd:PRK11855 431 VDKKSLLEIAREIAELAKKARDGKLKPDDMQGGCFTISSLGG-IGGTAFTPIINAPEVAILGVGKSQMK--PVWDGKEFV 507
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 18400212 500 VASYMSVTLSCDHRVIDGAIGAEWLKAFKGYIETPESMLL 539
Cdd:PRK11855 508 PRLMLPLSLSYDHRVIDGATAARFTNYLKQLLADPRRMLL 547
|
|
| PRK05704 |
PRK05704 |
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase; |
113-539 |
1.40e-77 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
Pssm-ID: 235571 [Multi-domain] Cd Length: 407 Bit Score: 249.75 E-value: 1.40e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400212 113 EIGMPSLSPTMTEGNIARWLKKEGDKVAPGEVLCEVETDKATVEMECMEEGFLAKIVKEEGAKeIQVGEVIAITVEDEdd 192
Cdd:PRK05704 4 EIKVPTLPESVTEATIATWHKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGDT-VTVGQVLGRIDEGA-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400212 193 iqkfkdytpssdtgpaAPEAKPAPSLPKEEKVEKPASAPEAKISKPSSAPsedrifASPLARKLAEDNNVPLSSIKGTGP 272
Cdd:PRK05704 81 ----------------AAGAAAAAAAAAAAAAAAPAQAQAAAAAEQSNDA------LSPAARKLAAENGLDASAVKGTGK 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400212 273 EGRIVKADVEDFLASGSKETTAKPSKQVDSKVPALDY---VDIPHTQIRKVTASRLAFSKQTIPhyYLTVDTCVD--KMM 347
Cdd:PRK05704 139 GGRVTKEDVLAALAAAAAAPAAPAAAAPAAAPAPLGArpeERVPMTRLRKTIAERLLEAQNTTA--MLTTFNEVDmtPVM 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400212 348 GLRSQLNSFQEASGGKRISVNDLVIKAAALALRKVPQCNSS--WTDEYIRQFknVNINVAVQTENGLYVPVVKDADKKGL 425
Cdd:PRK05704 217 DLRKQYKDAFEKKHGVKLGFMSFFVKAVVEALKRYPEVNASidGDDIVYHNY--YDIGIAVGTPRGLVVPVLRDADQLSF 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400212 426 STIGEEVRFLAQKAKENSLKPEDYEGGTFTVSNlGGPFGIKQFCAVINPPQAAILAIGSAEKR--VVPGtgpdQYNVASY 503
Cdd:PRK05704 295 AEIEKKIAELAKKARDGKLSIEELTGGTFTITN-GGVFGSLMSTPIINPPQSAILGMHKIKERpvAVNG----QIVIRPM 369
|
410 420 430
....*....|....*....|....*....|....*.
gi 18400212 504 MSVTLSCDHRVIDGAIGAEWLKAFKGYIETPESMLL 539
Cdd:PRK05704 370 MYLALSYDHRIIDGKEAVGFLVTIKELLEDPERLLL 405
|
|
| sucB |
TIGR01347 |
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ... |
113-539 |
7.62e-73 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This model describes the TCA cycle 2-oxoglutarate system E2 component, dihydrolipoamide succinyltransferase. It is closely related to the pyruvate dehydrogenase E2 component, dihydrolipoamide acetyltransferase. The seed for this model includes mitochondrial and Gram-negative bacterial forms. Mycobacterial candidates are highly derived, differ in having and extra copy of the lipoyl-binding domain at the N-terminus. They score below the trusted cutoff, but above the noise cutoff and above all examples of dihydrolipoamide acetyltransferase. [Energy metabolism, TCA cycle]
Pssm-ID: 273565 [Multi-domain] Cd Length: 403 Bit Score: 237.32 E-value: 7.62e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400212 113 EIGMPSLSPTMTEGNIARWLKKEGDKVAPGEVLCEVETDKATVEMECMEEGFLAKIVKEEGAKeIQVGEVIAItvededd 192
Cdd:TIGR01347 2 EIKVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDT-VESGQVLAI------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400212 193 IQKFKDYTPSSDTGpaapeakpapslPKEEKVEKPASAPEAKISKPSSAPSedrifASPLARKLAEDNNVPLSSIKGTGP 272
Cdd:TIGR01347 74 LEEGNDATAAPPAK------------SGEEKEETPAASAAAAPTAAANRPS-----LSPAARRLAKEHGIDLSAVPGTGV 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400212 273 EGRIVKADVEDFLASgsKETTAKPSKQVDSKVPALDY---VDIPHTQIRKVTASRLAFSKQTIPhyYLTVDTCVD--KMM 347
Cdd:TIGR01347 137 TGRVTKEDIIKKTEA--PASAQPPAAAAAAAAPAAATrpeERVKMTRLRQRIAERLKEAQNSTA--MLTTFNEVDmsAVM 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400212 348 GLRSQLNSFQEASGGKRISVNDLVIKAAALALRKVPQCNSSWTDEYIRQFKNVNINVAVQTENGLYVPVVKDADKKGLST 427
Cdd:TIGR01347 213 ELRKRYKEEFEKKHGVKLGFMSFFVKAVVAALKRFPEVNAEIDGDDIVYKDYYDISVAVSTDRGLVVPVVRNADRMSFAD 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400212 428 IGEEVRFLAQKAKENSLKPEDYEGGTFTVSNlGGPFGIKQFCAVINPPQAAILAIGSAEKRvvPGTGPDQYNVASYMSVT 507
Cdd:TIGR01347 293 IEKEIADLGKKARDGKLTLEDMTGGTFTITN-GGVFGSLMSTPIINPPQSAILGMHGIKER--PVAVNGQIEIRPMMYLA 369
|
410 420 430
....*....|....*....|....*....|..
gi 18400212 508 LSCDHRVIDGAIGAEWLKAFKGYIETPESMLL 539
Cdd:TIGR01347 370 LSYDHRLIDGKEAVTFLVTIKELLEDPRRLLL 401
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
112-539 |
3.06e-68 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 231.43 E-value: 3.06e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400212 112 QEIGMPSLSptMTEGNIARWLKKEGDKVAPGEVLCEVETDKATVEMECMEEGFLAKIVKEEGAKeIQVGEVIAiTVEDEd 191
Cdd:PRK11854 207 KDVNVPDIG--GDEVEVTEVMVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDK-VKTGSLIM-RFEVE- 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400212 192 diqkfkdytpSSDTGPAAPEAKPAPSLPKEEKVEKPASAPEAKISKPSSAPSEDR-IFASPLARKLAEDNNVPLSSIKGT 270
Cdd:PRK11854 282 ----------GAAPAAAPAKQEAAAPAPAAAKAEAPAAAPAAKAEGKSEFAENDAyVHATPLVRRLAREFGVNLAKVKGT 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400212 271 GPEGRIVKADV----EDFLASGSKETTAKPSKQVDSKVPALDYVD---------IPHTQIRKVTASRLAFSKQTIPHYYL 337
Cdd:PRK11854 352 GRKGRILKEDVqayvKDAVKRAEAAPAAAAAGGGGPGLLPWPKVDfskfgeieeVELGRIQKISGANLHRNWVMIPHVTQ 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400212 338 TVDTCVDKMMGLRSQLN--SFQEASGGKrISVNDLVIKAAALALRKVPQCNSSW---TDEYIRQfKNVNINVAVQTENGL 412
Cdd:PRK11854 432 FDKADITELEAFRKQQNaeAEKRKLGVK-ITPLVFIMKAVAAALEQMPRFNSSLsedGQRLTLK-KYVNIGIAVDTPNGL 509
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400212 413 YVPVVKDADKKGLSTIGEEVRFLAQKAKENSLKPEDYEGGTFTVSNLGGpFGIKQFCAVINPPQAAILAIGSAEKRvvPG 492
Cdd:PRK11854 510 VVPVFKDVNKKGIIELSRELMDISKKARDGKLTAGDMQGGCFTISSIGG-LGTTHFTPIVNAPEVAILGVSKSAME--PV 586
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 18400212 493 TGPDQYNVASYMSVTLSCDHRVIDGAIGAEWLKAFKGYIETPESMLL 539
Cdd:PRK11854 587 WNGKEFAPRLMLPLSLSYDHRVIDGADGARFITIINDRLSDIRRLVL 633
|
|
| PLN02528 |
PLN02528 |
2-oxoisovalerate dehydrogenase E2 component |
130-539 |
8.14e-63 |
|
2-oxoisovalerate dehydrogenase E2 component
Pssm-ID: 215289 [Multi-domain] Cd Length: 416 Bit Score: 211.50 E-value: 8.14e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400212 130 RWLKKEGDKVAPGEVLCEVETDKATVEMECMEEGFLAKIVKEEGAKeIQVGE-VIAITVEDEDDIQKFKDYTPSSDTGPA 208
Cdd:PLN02528 17 RWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGKVAQINFSPGDI-VKVGEtLLKIMVEDSQHLRSDSLLLPTDSSNIV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400212 209 ApeakpapslpkeekvekpASAPEAKISKPSSapsedrIFASPLARKLAEDNNVPLSSIKGTGPEGRIVKADVEDFLA-- 286
Cdd:PLN02528 96 S------------------LAESDERGSNLSG------VLSTPAVRHLAKQYGIDLNDILGTGKDGRVLKEDVLKYAAqk 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400212 287 ------SGSKETTAKPSKQVDSKVPALD---YVD--IPHTQIRKVTASRLAFSKQtIPHYYLTVDTCVDKMMGLRSQLNS 355
Cdd:PLN02528 152 gvvkdsSSAEEATIAEQEEFSTSVSTPTeqsYEDktIPLRGFQRAMVKTMTAAAK-VPHFHYVEEINVDALVELKASFQE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400212 356 FQEASGGKrISVNDLVIKAAALALRKVPQCNSSWTDEY--IRQFKNVNINVAVQTENGLYVPVVKDADKKGLSTIGEEVR 433
Cdd:PLN02528 231 NNTDPTVK-HTFLPFLIKSLSMALSKYPLLNSCFNEETseIRLKGSHNIGVAMATEHGLVVPNIKNVQSLSLLEITKELS 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400212 434 FLAQKAKENSLKPEDYEGGTFTVSNLG---GPFGikqfCAVINPPQAAILAIGSAEK--RVVpgtgpDQYNV--ASYMSV 506
Cdd:PLN02528 310 RLQHLAAENKLNPEDITGGTITLSNIGaigGKFG----SPVLNLPEVAIIALGRIQKvpRFV-----DDGNVypASIMTV 380
|
410 420 430
....*....|....*....|....*....|...
gi 18400212 507 TLSCDHRVIDGAIGAEWLKAFKGYIETPESMLL 539
Cdd:PLN02528 381 TIGADHRVLDGATVARFCNEWKSYVEKPELLML 413
|
|
| PTZ00144 |
PTZ00144 |
dihydrolipoamide succinyltransferase; Provisional |
66-539 |
1.11e-60 |
|
dihydrolipoamide succinyltransferase; Provisional
Pssm-ID: 240289 [Multi-domain] Cd Length: 418 Bit Score: 206.07 E-value: 1.11e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400212 66 TMLSGISTTSTKLSSpmagpkLFKEFISSQMRSVRGFSSSSDLpphQEIGMPSLSPTMTEGNIARWLKKEGDKVAPGEVL 145
Cdd:PTZ00144 8 RLNKPLLSSVKGMFR------RFSLRKLQPACSAHFSKSYFSI---KVIKVPTMGDSISEGTVVEWKKKVGDYVKEDEVI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400212 146 CEVETDKATVEMECMEEGFLAKIVKEEGAKeIQVGE---VIAITVEDEDDIQKfkdyTPSSDTGPAAPEAKPAPSLPKEE 222
Cdd:PTZ00144 79 CIIETDKVSVDIRAPASGVITKIFAEEGDT-VEVGAplsEIDTGGAPPAAAPA----AAAAAKAEKTTPEKPKAAAPTPE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400212 223 KVEKPASAPEAKISKPSSAPSEDRIfASPLARKLAEDNNVPLSSIkgtgpegrivkadvedflasgskettakpskqvds 302
Cdd:PTZ00144 154 PPAASKPTPPAAAKPPEPAPAAKPP-PTPVARADPRETRVPMSRM----------------------------------- 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400212 303 kvpaldyvdiphtqiRKVTASRLAFSKQTiphYYL--TVDTC-VDKMMGLRSQLN-SFQEASGGKrISVNDLVIKAAALA 378
Cdd:PTZ00144 198 ---------------RQRIAERLKASQNT---CAMltTFNECdMSALMELRKEYKdDFQKKHGVK-LGFMSAFVKASTIA 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400212 379 LRKVPQCNSSWTDEYIRQFKNVNINVAVQTENGLYVPVVKDADKKGLSTIGEEVRFLAQKAKENSLKPEDYEGGTFTVSN 458
Cdd:PTZ00144 259 LKKMPIVNAYIDGDEIVYRNYVDISVAVATPTGLVVPVIRNCENKSFAEIEKELADLAEKARNNKLTLEDMTGGTFTISN 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400212 459 lGGPFGIKQFCAVINPPQAAILAIGSAEKR-VVPGtgpDQYNVASYMSVTLSCDHRVIDGAIGAEWLKAFKGYIETPESM 537
Cdd:PTZ00144 339 -GGVFGSLMGTPIINPPQSAILGMHAIKKRpVVVG---NEIVIRPIMYLALTYDHRLIDGRDAVTFLKKIKDLIEDPARM 414
|
..
gi 18400212 538 LL 539
Cdd:PTZ00144 415 LL 416
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
112-539 |
7.27e-60 |
|
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: 207.03 E-value: 7.27e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400212 112 QEIGMPSLSpTMTEGNIARWLKKEGDKVAPGEVLCEVETDKATVEMECMEEGflakIVKEegaKEIQVGEviaiTVEDED 191
Cdd:TIGR01348 117 QEVTVPDIG-DIEKVTVIEVLVKVGDTVSADQSLITLESDKASMEVPAPASG----VVKS---VKVKVGD----SVPTGD 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400212 192 DIQKFKDYTPSSDTGPAAPEAKPAPSLPKEEKVEKPAS--APEAKISKPSSAPSEDR---IFASPLARKLAEDNNVPLSS 266
Cdd:TIGR01348 185 LILTLSVAGSTPATAPAPASAQPAAQSPAATQPEPAAApaAAKAQAPAPQQAGTQNPakvDHAAPAVRRLAREFGVDLSA 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400212 267 IKGTGPEGRIVKADVEDFLASGSKETTAK------------PSKQVD-SKVPALDYVDIphTQIRKVTASRLAFSKQTIP 333
Cdd:TIGR01348 265 VKGTGIKGRILREDVQRFVKEPSVRAQAAaasaaggapgalPWPNVDfSKFGEVEEVDM--SRIRKISGANLTRNWTMIP 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400212 334 HYYLTVDTCVDKMMGLRSQLNSFQEASGGKrISVNDLVIKAAALALRKVPQCNSSW--TDEYIRQFKNVNINVAVQTENG 411
Cdd:TIGR01348 343 HVTHFDKADITEMEAFRKQQNAAVEKEGVK-LTVLHILMKAVAAALKKFPKFNASLdlGGEQLILKKYVNIGVAVDTPNG 421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400212 412 LYVPVVKDADKKGLSTIGEEVRFLAQKAKENSLKPEDYEGGTFTVSNLGGpFGIKQFCAVINPPQAAILaiGSAEKRVVP 491
Cdd:TIGR01348 422 LLVPVIKDVDRKGITELALELSDLAKKARDGKLTPDEMQGACFTISSLGG-IGGTAFTPIVNAPEVAIL--GVSKSGMEP 498
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 18400212 492 GTGPDQYNVASYMSVTLSCDHRVIDGAIGAEWLKAFKGYIETPESMLL 539
Cdd:TIGR01348 499 VWNGKEFEPRLMLPLSLSYDHRVIDGADAARFTTYICESLADIRRLLL 546
|
|
| SucB_Actino |
TIGR02927 |
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model ... |
113-533 |
2.03e-58 |
|
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: 204.09 E-value: 2.03e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400212 113 EIGMPSLSPTMTEGNIARWLKKEGDKVAPGEVLCEVETDKATVEMECMEEGFLAKIVKEEGaKEIQVGEVIAItVEDEDD 192
Cdd:TIGR02927 128 EVKMPELGESVTEGTVTSWLKAVGDTVEVDEPLLEVSTDKVDTEIPSPVAGTLLEIRAPED-DTVEVGTVLAI-IGDANA 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400212 193 IQKFK---DYTPSSDTGPAAPEAKPAPSLPKEEKVEKPASAPEAKISKPSSAP---SEDRIFASPLARKLAEDNNVPLSS 266
Cdd:TIGR02927 206 APAEPaeeEAPAPSEAGSEPAPDPAARAPHAAPDPPAPAPAPAKTAAPAAAAPvssGDSGPYVTPLVRKLAKDKGVDLST 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400212 267 IKGTGPEGRIVKADVEDfLASGSKETTAKPSKQVDSKVPALDY-------VDIPH--------TQIRKVTASRLAFSKQT 331
Cdd:TIGR02927 286 VKGTGVGGRIRKQDVLA-AAKAAEEARAAAAAPAAAAAPAAPAaaakpaePDTAKlrgttqkmNRIRQITADKTIESLQT 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400212 332 IPHYYLTVDTCVDKMMGLR-SQLNSFQEASGGKrISVNDLVIKAAALALRKVPQCNSSWTDEY--IRQFKNVNINVAVQT 408
Cdd:TIGR02927 365 SAQLTQVHEVDMTRVAALRaRAKNDFLEKNGVN-LTFLPFFVQAVTEALKAHPNVNASYNAETkeVTYHDVEHVGIAVDT 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400212 409 ENGLYVPVVKDADKKGLSTIGEEVRFLAQKAKENSLKPEDYEGGTFTVSNLGGPfGIKQFCAVINPPQAAILAIGSAEKR 488
Cdd:TIGR02927 444 PRGLLVPVIHNAGDLSLPGLAKAINDLAARARDNKLKPDELSGGTFTITNIGSG-GALFDTPILNPPQAAILGTGAIVKR 522
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 18400212 489 ---VVPGTGPDQYNVASYMSVTLSCDHRVIDGAIGAEWLKAFKGYIET 533
Cdd:TIGR02927 523 prvIKDEDGGESIAIRSVCYLPLTYDHRLVDGADAGRFLTTIKKRLEE 570
|
|
| PRK14843 |
PRK14843 |
dihydrolipoamide acetyltransferase; Provisional |
227-539 |
8.54e-56 |
|
dihydrolipoamide acetyltransferase; Provisional
Pssm-ID: 184847 [Multi-domain] Cd Length: 347 Bit Score: 190.89 E-value: 8.54e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400212 227 PASAPEAKISKP--SSAPSEDRIFASPLARKLAEDNNVPLSSIKGTGPEGRIVKADVEDFLASGSKETTAKPSKQV---- 300
Cdd:PRK14843 27 SGSGANGRVHKEdvETYKDTNVVRISPLAKRIALEHNIAWQEIQGTGHRGKIMKKDVLALLPENIENDSIKSPAQIekve 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400212 301 ---DSKVPALDYVDIPHTQIRKVTASRLAFSKQTIPHYYLTVDTCVDKMMGLRSQLNSFQEASGGKRISVNDLVIKAAAL 377
Cdd:PRK14843 107 evpDNVTPYGEIERIPMTPMRKVIAQRMVESYLTAPTFTLNYEVDMTEMLALRKKVLEPIMEATGKKTTVTDLLSLAVVK 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400212 378 ALRKVPQCNSSWTDE--YIRQFKNVNINVAVQTENGLYVPVVKDADKKGLSTIGEEVRFLAQKAKENSLKPEDYEGGTFT 455
Cdd:PRK14843 187 TLMKHPYINASLTEDgkTIITHNYVNLAMAVGMDNGLMTPVVYNAEKMSLSELVVAFKDVIGRTLDGKLAPSELQNSTFT 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400212 456 VSNLgGPFGIKQFCAVINPPQAAILAIGSA-EKRVVPGtgpDQYNVASYMSVTLSCDHRVIDGAIGAEWLKAFKGYIETP 534
Cdd:PRK14843 267 ISNL-GMFGVQSFGPIINQPNSAILGVSSTiEKPVVVN---GEIVIRPIMSLGLTIDHRVVDGMAGAKFMKDLKELIETP 342
|
....*
gi 18400212 535 ESMLL 539
Cdd:PRK14843 343 ISMLI 347
|
|
| PLN02226 |
PLN02226 |
2-oxoglutarate dehydrogenase E2 component |
24-539 |
1.73e-43 |
|
2-oxoglutarate dehydrogenase E2 component
Pssm-ID: 177871 [Multi-domain] Cd Length: 463 Bit Score: 160.69 E-value: 1.73e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400212 24 AVAVRCFSNSTHPSLVGREdIFKARLNYSSVERISKCGTGNVTMLSGISTTSTKLSSP-MAGPKLFKEFISSQM-RSVRG 101
Cdd:PLN02226 5 AVIRRASTRGSSPSLFGKS-LQSSRVAASSPSLLSGSETGALLHRGNHAHSFHNLALPgNSGISRSASLVSSTLqRWVRP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400212 102 FSSSSDlpPHQEIGMPSLSPTMTEGNIARWLKKEGDKVAPGEVLCEVETDKATVEMECMEEGFLAKIVKEEGaKEIQVGE 181
Cdd:PLN02226 84 FSSESG--DTVEAVVPHMGESITDGTLATFLKKPGERVQADEAIAQIETDKVTIDIASPASGVIQEFLVKEG-DTVEPGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400212 182 VIAITVEDEDDIQKFKdytpssdtgpaapeakpapslPKEEKVEKPASAPeakiSKPSSAPSEDRIFASPLARKlaednn 261
Cdd:PLN02226 161 KVAIISKSEDAASQVT---------------------PSQKIPETTDPKP----SPPAEDKQKPKVESAPVAEK------ 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400212 262 vplssikgtgpegrivkadvedflasgSKETTAKPSKQVDSKVPALDYVD----IPHTQIRKVTASRLAFSKQTIPhyYL 337
Cdd:PLN02226 210 ---------------------------PKAPSSPPPPKQSAKEPQLPPKErerrVPMTRLRKRVATRLKDSQNTFA--LL 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400212 338 TVDTCVD--KMMGLRSQL-NSFQEASGGKrISVNDLVIKAAALALRKVPQCNSSWTDEYIRQFKNVNINVAVQTENGLYV 414
Cdd:PLN02226 261 TTFNEVDmtNLMKLRSQYkDAFYEKHGVK-LGLMSGFIKAAVSALQHQPVVNAVIDGDDIIYRDYVDISIAVGTSKGLVV 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400212 415 PVVKDADKKGLSTIGEEVRFLAQKAKENSLKPEDYEGGTFTVSNlGGPFGIKQFCAVINPPQAAILAIGSAEKR--VVPG 492
Cdd:PLN02226 340 PVIRGADKMNFAEIEKTINGLAKKANEGTISIDEMAGGSFTVSN-GGVYGSLISTPIINPPQSAILGMHSIVSRpmVVGG 418
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 18400212 493 TGPDQynvaSYMSVTLSCDHRVIDGAIGAEWLKAFKGYIETPESMLL 539
Cdd:PLN02226 419 SVVPR----PMMYVALTYDHRLIDGREAVYFLRRVKDVVEDPQRLLL 461
|
|
| PRK11857 |
PRK11857 |
dihydrolipoamide acetyltransferase; Reviewed |
246-535 |
3.52e-37 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237002 [Multi-domain] Cd Length: 306 Bit Score: 139.54 E-value: 3.52e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400212 246 RIFASPLARKLAEDNNVPLSSIKGTGPEGRIVKADVEDFL------------ASGSKETTAKPSKQVDSKVPALDYVDIP 313
Cdd:PRK11857 1 KILATPIARALAKKLGIDISLLKGSGRDGKILAEDVENFIkslksaptpaeaASVSSAQQAAKTAAPAAAPPKLEGKREK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400212 314 HTQIRKVTASRLAFSKQTIPHYYLTVDTCVDKMMGLRSQLNSFQEASGGKRISVNDLVIKAAALALRKVPQCNSSWtDEY 393
Cdd:PRK11857 81 VAPIRKAIARAMTNSWSNVAYVNLVNEIDMTKLWDLRKSVKDPVLKTEGVKLTFLPFIAKAILIALKEFPIFAAKY-DEA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400212 394 IRQF---KNVNINVAVQTENGLYVPVVKDADKKGLSTIGEEVRFLAQKAKENSLKPEDYEGGTFTVSN---LGGPFGIkq 467
Cdd:PRK11857 160 TSELvypDTLNLGIAVDTEAGLMVPVIKNAQKLSIVEIAKEISRLAKAARERKIKPDEMKGGSFTITNygsVGSLYGV-- 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18400212 468 fcAVINPPQAAILAIGSAEKRVVPGTGpdQYNVASYMSVTLSCDHRVIDGAIGAEWLKAFKGYIETPE 535
Cdd:PRK11857 238 --PVINYPELAIAGVGAIIDKAIVKNG--QIVAGKVMHLTVAADHRWIDGATIGRFASRVKELLEKPE 301
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
113-242 |
5.16e-31 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 125.41 E-value: 5.16e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400212 113 EIGMPSLSPTMTEGNIARWLKKEGDKVAPGEVLCEVETDKATVEMECMEEGFLAKIVKEEGAKEIQVGEVIAITVEDEDD 192
Cdd:PRK11892 4 EILMPALSPTMEEGTLAKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKILVPEGTEGVKVNTPIAVLLEEGES 83
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 18400212 193 IQKFKDYTPSSDTgpAAPEAKPAPSLPKEEKVEKPASAPEAKISKPSSAP 242
Cdd:PRK11892 84 ASDAGAAPAAAAE--AAAAAPAAAAAAAAKKAAPAPAAPAAPAAEVAADP 131
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
112-185 |
6.48e-30 |
|
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: 111.73 E-value: 6.48e-30
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18400212 112 QEIGMPSLSPTMTEGNIARWLKKEGDKVAPGEVLCEVETDKATVEMECMEEGFLAKIVKEEGAKeIQVGEVIAI 185
Cdd:cd06849 1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDT-VPVGQVIAV 73
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
112-185 |
7.72e-27 |
|
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: 103.22 E-value: 7.72e-27
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18400212 112 QEIGMPSLSPTMTEGNIARWLKKEGDKVAPGEVLCEVETDKATVEMECMEEGFLAKIVKEEGAKeIQVGEVIAI 185
Cdd:COG0508 3 IEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDT-VPVGAVIAV 75
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
112-196 |
1.43e-18 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 87.31 E-value: 1.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400212 112 QEIGMPSLSPTMTEGNIARWLKKEGDKVAPGEVLCEVETDKATVEMECMEEGFLAKIVKEEGaKEIQVGEVIAITVEDE- 190
Cdd:PRK14875 3 TPITMPKWGLSMTEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEG-ETLPVGALLAVVADAEv 81
|
....*...
gi 18400212 191 --DDIQKF 196
Cdd:PRK14875 82 sdAEIDAF 89
|
|
| E3_binding |
pfam02817 |
e3 binding domain; This family represents a small domain of the E2 subunit of 2-oxo-acid ... |
247-282 |
7.46e-16 |
|
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: 71.18 E-value: 7.46e-16
10 20 30
....*....|....*....|....*....|....*.
gi 18400212 247 IFASPLARKLAEDNNVPLSSIKGTGPEGRIVKADVE 282
Cdd:pfam02817 1 VLASPAARKLARELGIDLSDVKGTGPGGRITKEDVE 36
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
113-185 |
1.18e-15 |
|
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: 71.86 E-value: 1.18e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18400212 113 EIGMPSLSPTMTEGnIARWLKKEGDKVAPGEVLCEVETDKATVEMECMEEGFLAKIVKEEGAKeIQVGEVIAI 185
Cdd:pfam00364 2 EIKSPMIGESVREG-VVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDT-VEVGDPLAK 72
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
113-175 |
1.97e-14 |
|
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases, and the H-protein of the glycine cleavage system (GCS). These domains transport CO2, acyl, or methylamine, respectively, between components of the complex/protein via a biotinyl or lipoyl group, which is covalently attached to a highly conserved lysine residue.
Pssm-ID: 133456 [Multi-domain] Cd Length: 73 Bit Score: 68.24 E-value: 1.97e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18400212 113 EIGMPSLSPTMTEGNIARWLKKEGDKVAPGEVLCEVETDKATVEMECMEEGFLAKIVKEEGAK 175
Cdd:cd06663 1 TILIPDLAQHLGDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTK 63
|
|
| kgd |
PRK12270 |
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ... |
350-525 |
1.67e-10 |
|
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;
Pssm-ID: 237030 [Multi-domain] Cd Length: 1228 Bit Score: 64.14 E-value: 1.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400212 350 RSQLNSFQEASGGKRISVNDLVIKAAALALRKVPQCNSSWTDE----YIRQFKNVNINVA--VQTENG---LYVPVVKDA 420
Cdd:PRK12270 155 RIVINNHLKRTRGGKVSFTHLIGYALVQALKAFPNMNRHYAEVdgkpTLVTPAHVNLGLAidLPKKDGsrqLVVPAIKGA 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400212 421 DKKGLStigeevRFLA------QKAKENSLKPEDYEGGTFTVSNLGGpFGIKQFCAVINPPQAAILAIGS----AEKRvv 490
Cdd:PRK12270 235 ETMDFA------QFWAayedivRRARDGKLTADDFQGTTISLTNPGG-IGTVHSVPRLMKGQGAIIGVGAmeypAEFQ-- 305
|
170 180 190
....*....|....*....|....*....|....*...
gi 18400212 491 pGTGPDQYN---VASYMSVTLSCDHRVIDGAIGAEWLK 525
Cdd:PRK12270 306 -GASEERLAelgISKVMTLTSTYDHRIIQGAESGEFLR 342
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
126-185 |
5.52e-05 |
|
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: 41.25 E-value: 5.52e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18400212 126 GNIARWLKKEGDKVAPGEVLCEVETDKatveMEcME-----EGFLAKIVKEEGAKeIQVGEVIAI 185
Cdd:cd06850 8 GTVVKVLVKEGDKVEAGQPLAVLEAMK----ME-NEvtapvAGVVKEILVKEGDQ-VEAGQLLVV 66
|
|
| PRK09282 |
PRK09282 |
pyruvate carboxylase subunit B; Validated |
126-185 |
3.99e-03 |
|
pyruvate carboxylase subunit B; Validated
Pssm-ID: 236449 [Multi-domain] Cd Length: 592 Bit Score: 39.83 E-value: 3.99e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400212 126 GNIARWLKKEGDKVAPGEVLCEVETDKATVEMECMEEGFLAKIVKEEGAKeIQVGEVIAI 185
Cdd:PRK09282 531 GTVVKVKVKEGDKVKAGDTVLVLEAMKMENEIQAPVDGTVKEILVKEGDR-VNPGDVLME 589
|
|
| |
