|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02744 |
PLN02744 |
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex |
2-539 |
0e+00 |
|
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
Pssm-ID: 215397 [Multi-domain] Cd Length: 539 Bit Score: 1030.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79319911 2 AYASRIINHSKKLKDVSTLLRRENAATIRYYSNTNRAPLNREDTFNSRLGYPPLERISICSTSTL--PVSIIFSTTRSNL 79
Cdd:PLN02744 1 AYASRIINHSKKLRNVSNLLRREHAALVRYFSNSTRSSLGKGDDIAKRRGYPPLERRSQPKVSSLglFGSNISRTARKNG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79319911 80 SSAMGRPIFGKEFSCLMQSARGFSSGSDLPPHQEIGMPSLSPTMTEGNIARWLKKEGDKVAPGEVLCEVETDKATVEMEC 159
Cdd:PLN02744 81 SPMTGSGLFKSLSSSQMQSARGFSSSSDLPPHQEIGMPSLSPTMTEGNIARWLKKEGDKVSPGEVLCEVETDKATVEMEC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79319911 160 MEEGYLAKIVKAEGSKEIQVGEVIAITVEDEEDIGKFKDYTPSSTADAAPTKAEPTPAPPKEEKVKQPSSPPEPKASKPS 239
Cdd:PLN02744 161 MEEGYLAKIVKGDGAKEIKVGEVIAITVEEEEDIGKFKDYKPSSSAAPAAPKAKPSPPPPKEEEVEKPASSPEPKASKPS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79319911 240 TPP-TGDRVFASPLARKLAEDNNVPLSDIEGTGPEGRIVKADIDEYLASSGKGATAKPSksTDSKAPALDYVDIPHSQIR 318
Cdd:PLN02744 241 APPsSGDRIFASPLARKLAEDNNVPLSSIKGTGPDGRIVKADIEDYLASGGKGATAPPS--TDSKAPALDYTDIPNTQIR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79319911 319 KVTASRLAFSKQTIPHYYLTVDTCVDKLMALRSQLNSFKEASGGKRISVNDLVVKAAALALRKVPQCNSSWTDDYIRQFK 398
Cdd:PLN02744 319 KVTASRLLQSKQTIPHYYLTVDTRVDKLMALRSQLNSLQEASGGKKISVNDLVIKAAALALRKVPQCNSSWTDDYIRQYH 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79319911 399 NVNINVAVQTENGLYVPVVKDADRKGLSTIGEEVRLLAQKAKENSLKPEDYEGGTFTVSNLGGPFGIKQFCAVVNPPQAA 478
Cdd:PLN02744 399 NVNINVAVQTENGLYVPVVKDADKKGLSTIAEEVKQLAQKARENSLKPEDYEGGTFTVSNLGGPFGIKQFCAIINPPQSA 478
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 79319911 479 ILAVGSAEKRVVPGNGPDQFNFASYMPVTLSCDHRVVDGAIGAEWLKAFKGYIENPKSMLL 539
Cdd:PLN02744 479 ILAVGSAEKRVIPGSGPDQYNFASFMSVTLSCDHRVIDGAIGAEWLKAFKGYIENPESMLL 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: 552.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79319911 113 EIGMPSLSPTMTEGNIARWLKKEGDKVAPGEVLCEVETDKATVEMECMEEGYLAKIVKAEGSKEIQVGEVIAITVEDEED 192
Cdd:TIGR01349 1 KITMPALSPTMTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEGTKDVPVNKPIAVLVEEKED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79319911 193 IGK-FKDYTPSSTADAAPTKAEPTPAPPKEEKVKQPSSPPEPKASKPSTPPT----GDRVFASPLARKLAEDNNVPLSDI 267
Cdd:TIGR01349 81 VADaFKNYKLESSASPAPKPSEIAPTAPPSAPKPSPAPQKQSPEPSSPAPLSdkesGDRIFASPLAKKLAKEKGIDLSAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79319911 268 EGTGPEGRIVKADIDEYLASSGKGATAKPSKSTDSKAPAL------DYVDIPHSQIRKVTASRLAFSKQTIPHYYLTVDT 341
Cdd:TIGR01349 161 AGSGPNGRIVKKDIESFVPQSPASANQQAAATTPATYPAAapvstgSYEDVPLSNIRKIIAKRLLESKQTIPHYYVSIEC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79319911 342 CVDKLMALRSQLNsfKEASGGKRISVNDLVVKAAALALRKVPQCNSSWTDDYIRQFKNVNINVAVQTENGLYVPVVKDAD 421
Cdd:TIGR01349 241 NVDKLLALRKELN--AMASEVYKLSVNDFIIKASALALREVPEANSSWTDNFIRRYKNVDISVAVATPDGLITPIVRNAD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79319911 422 RKGLSTIGEEVRLLAQKAKENSLKPEDYEGGTFTVSNLgGPFGIKQFCAVVNPPQAAILAVGSAEKRVVPGNGPDQ-FNF 500
Cdd:TIGR01349 319 AKGLSTISNEIKDLAKRARNNKLKPEEFQGGTFTISNL-GMFGIKDFTAIINPPQACILAVGAVEDVAVVDNDEEKgFAV 397
|
410 420 430
....*....|....*....|....*....|....*....
gi 79319911 501 ASYMPVTLSCDHRVVDGAIGAEWLKAFKGYIENPKSMLL 539
Cdd:TIGR01349 398 ASIMSVTLSCDHRVIDGAVGAEFLKSFKKYLENPIEMLL 436
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
328-538 |
1.51e-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: 286.75 E-value: 1.51e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79319911 328 SKQTIPHYYLTVDTCVDKLMALRSQLNSfKEASGGKRISVNDLVVKAAALALRKVPQCNSSWTDD--YIRQFKNVNINVA 405
Cdd:pfam00198 4 SKQTIPHFTLTDEVDVTELLALREELKE-DAADEETKLTFLPFLVKAVALALKKFPELNASWDGEegEIVYKKYVNIGIA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79319911 406 VQTENGLYVPVVKDADRKGLSTIGEEVRLLAQKAKENSLKPEDYEGGTFTVSNLGGpFGIKQFCAVVNPPQAAILAVGSA 485
Cdd:pfam00198 83 VATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGM-FGVTFFTPIINPPQVAILGVGRI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 79319911 486 EKRVVPGNGpdQFNFASYMPVTLSCDHRVVDGAIGAEWLKAFKGYIENPKSML 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 |
8.72e-31 |
|
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: 114.42 E-value: 8.72e-31
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 79319911 112 QEIGMPSLSPTMTEGNIARWLKKEGDKVAPGEVLCEVETDKATVEMECMEEGYLAKIVKAEGSKeIQVGEVIAI 185
Cdd:cd06849 1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDT-VPVGQVIAV 73
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
112-185 |
7.93e-28 |
|
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: 106.30 E-value: 7.93e-28
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 79319911 112 QEIGMPSLSPTMTEGNIARWLKKEGDKVAPGEVLCEVETDKATVEMECMEEGYLAKIVKAEGSKeIQVGEVIAI 185
Cdd:COG0508 3 IEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDT-VPVGAVIAV 75
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02744 |
PLN02744 |
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex |
2-539 |
0e+00 |
|
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
Pssm-ID: 215397 [Multi-domain] Cd Length: 539 Bit Score: 1030.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79319911 2 AYASRIINHSKKLKDVSTLLRRENAATIRYYSNTNRAPLNREDTFNSRLGYPPLERISICSTSTL--PVSIIFSTTRSNL 79
Cdd:PLN02744 1 AYASRIINHSKKLRNVSNLLRREHAALVRYFSNSTRSSLGKGDDIAKRRGYPPLERRSQPKVSSLglFGSNISRTARKNG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79319911 80 SSAMGRPIFGKEFSCLMQSARGFSSGSDLPPHQEIGMPSLSPTMTEGNIARWLKKEGDKVAPGEVLCEVETDKATVEMEC 159
Cdd:PLN02744 81 SPMTGSGLFKSLSSSQMQSARGFSSSSDLPPHQEIGMPSLSPTMTEGNIARWLKKEGDKVSPGEVLCEVETDKATVEMEC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79319911 160 MEEGYLAKIVKAEGSKEIQVGEVIAITVEDEEDIGKFKDYTPSSTADAAPTKAEPTPAPPKEEKVKQPSSPPEPKASKPS 239
Cdd:PLN02744 161 MEEGYLAKIVKGDGAKEIKVGEVIAITVEEEEDIGKFKDYKPSSSAAPAAPKAKPSPPPPKEEEVEKPASSPEPKASKPS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79319911 240 TPP-TGDRVFASPLARKLAEDNNVPLSDIEGTGPEGRIVKADIDEYLASSGKGATAKPSksTDSKAPALDYVDIPHSQIR 318
Cdd:PLN02744 241 APPsSGDRIFASPLARKLAEDNNVPLSSIKGTGPDGRIVKADIEDYLASGGKGATAPPS--TDSKAPALDYTDIPNTQIR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79319911 319 KVTASRLAFSKQTIPHYYLTVDTCVDKLMALRSQLNSFKEASGGKRISVNDLVVKAAALALRKVPQCNSSWTDDYIRQFK 398
Cdd:PLN02744 319 KVTASRLLQSKQTIPHYYLTVDTRVDKLMALRSQLNSLQEASGGKKISVNDLVIKAAALALRKVPQCNSSWTDDYIRQYH 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79319911 399 NVNINVAVQTENGLYVPVVKDADRKGLSTIGEEVRLLAQKAKENSLKPEDYEGGTFTVSNLGGPFGIKQFCAVVNPPQAA 478
Cdd:PLN02744 399 NVNINVAVQTENGLYVPVVKDADKKGLSTIAEEVKQLAQKARENSLKPEDYEGGTFTVSNLGGPFGIKQFCAIINPPQSA 478
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 79319911 479 ILAVGSAEKRVVPGNGPDQFNFASYMPVTLSCDHRVVDGAIGAEWLKAFKGYIENPKSMLL 539
Cdd:PLN02744 479 ILAVGSAEKRVIPGSGPDQYNFASFMSVTLSCDHRVIDGAIGAEWLKAFKGYIENPESMLL 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: 552.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79319911 113 EIGMPSLSPTMTEGNIARWLKKEGDKVAPGEVLCEVETDKATVEMECMEEGYLAKIVKAEGSKEIQVGEVIAITVEDEED 192
Cdd:TIGR01349 1 KITMPALSPTMTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEGTKDVPVNKPIAVLVEEKED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79319911 193 IGK-FKDYTPSSTADAAPTKAEPTPAPPKEEKVKQPSSPPEPKASKPSTPPT----GDRVFASPLARKLAEDNNVPLSDI 267
Cdd:TIGR01349 81 VADaFKNYKLESSASPAPKPSEIAPTAPPSAPKPSPAPQKQSPEPSSPAPLSdkesGDRIFASPLAKKLAKEKGIDLSAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79319911 268 EGTGPEGRIVKADIDEYLASSGKGATAKPSKSTDSKAPAL------DYVDIPHSQIRKVTASRLAFSKQTIPHYYLTVDT 341
Cdd:TIGR01349 161 AGSGPNGRIVKKDIESFVPQSPASANQQAAATTPATYPAAapvstgSYEDVPLSNIRKIIAKRLLESKQTIPHYYVSIEC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79319911 342 CVDKLMALRSQLNsfKEASGGKRISVNDLVVKAAALALRKVPQCNSSWTDDYIRQFKNVNINVAVQTENGLYVPVVKDAD 421
Cdd:TIGR01349 241 NVDKLLALRKELN--AMASEVYKLSVNDFIIKASALALREVPEANSSWTDNFIRRYKNVDISVAVATPDGLITPIVRNAD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79319911 422 RKGLSTIGEEVRLLAQKAKENSLKPEDYEGGTFTVSNLgGPFGIKQFCAVVNPPQAAILAVGSAEKRVVPGNGPDQ-FNF 500
Cdd:TIGR01349 319 AKGLSTISNEIKDLAKRARNNKLKPEEFQGGTFTISNL-GMFGIKDFTAIINPPQACILAVGAVEDVAVVDNDEEKgFAV 397
|
410 420 430
....*....|....*....|....*....|....*....
gi 79319911 501 ASYMPVTLSCDHRVVDGAIGAEWLKAFKGYIENPKSMLL 539
Cdd:TIGR01349 398 ASIMSVTLSCDHRVIDGAVGAEFLKSFKKYLENPIEMLL 436
|
|
| PRK11856 |
PRK11856 |
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed |
113-539 |
2.27e-169 |
|
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
Pssm-ID: 237001 [Multi-domain] Cd Length: 411 Bit Score: 485.45 E-value: 2.27e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79319911 113 EIGMPSLSPTMTEGNIARWLKKEGDKVAPGEVLCEVETDKATVEMECMEEGYLAKIVKAEGSKeIQVGEVIAITVEDEEd 192
Cdd:PRK11856 4 EFKMPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDV-VPVGSVIAVIEEEGE- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79319911 193 igkfkdytpssTADAAPTKAEPTPAPPKEEKVKQPSSPPEPKASKPSTPPTGDRVFASPLARKLAEDNNVPLSDIEGTGP 272
Cdd:PRK11856 82 -----------AEAAAAAEAAPEAPAPEPAPAAAAAAAAAPAAAAAPAAPAAAAAKASPAVRKLARELGVDLSTVKGSGP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79319911 273 EGRIVKADIDEYLASSGKGATAKPSKSTDSKAPALDYVD-IPHSQIRKVTASRLAFSKQTIPHYYLTVDTCVDKLMALRS 351
Cdd:PRK11856 151 GGRITKEDVEAAAAAAAPAAAAAAAAAAAPPAAAAEGEErVPLSGMRKAIAKRMVESKREIPHFTLTDEVDVTALLALRK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79319911 352 QLNSFKEasggkRISVNDLVVKAAALALRKVPQCNSSWTDDYIRQFKNVNINVAVQTENGLYVPVVKDADRKGLSTIGEE 431
Cdd:PRK11856 231 QLKAIGV-----KLTVTDFLIKAVALALKKFPELNASWDDDAIVLKKYVNIGIAVATDGGLIVPVIRDADKKSLFELARE 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79319911 432 VRLLAQKAKENSLKPEDYEGGTFTVSNLGGpFGIKQFCAVVNPPQAAILAVGSAEKRVVPGNGpdQFNFASYMPVTLSCD 511
Cdd:PRK11856 306 IKDLAEKAREGKLKPEELQGGTFTISNLGM-FGGDYFTPIINPPEVAILGVGAIVERPVVVDG--EIVVRKVMPLSLSFD 382
|
410 420
....*....|....*....|....*...
gi 79319911 512 HRVVDGAIGAEWLKAFKGYIENPKSMLL 539
Cdd:PRK11856 383 HRVIDGADAARFLKALKELLENPALLLL 410
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
124-539 |
9.41e-97 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 304.05 E-value: 9.41e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79319911 124 TEGNIARWLKKEGDKVAPGEVLCEVETDKATVEMECMEEGYLAKIVKAEGSKeIQVGEVIAItVEDEedigkfkdytpss 203
Cdd:PRK11855 131 TEVEVIEWLVKVGDTVEEDQSLITVETDKATMEIPSPVAGVVKEIKVKVGDK-VSVGSLLVV-IEVA------------- 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79319911 204 tADAAPTKAEPTPAPPKEEKVKQPSSPPEPKASKPSTPP-----TGDRVFASPLARKLAEDNNVPLSDIEGTGPEGRIVK 278
Cdd:PRK11855 196 -AAAPAAAAAPAAAAPAAAAAAAPAPAPAAAAAPAAAAPaaaaaPGKAPHASPAVRRLARELGVDLSQVKGTGKKGRITK 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79319911 279 ADIDEYL---ASSGKGATAKPSKSTDSKAPALDYVDI-----------PHSQIRKVTASRLAFSKQTIPHYYLTVDTCVD 344
Cdd:PRK11855 275 EDVQAFVkgaMSAAAAAAAAAAAAGGGGLGLLPWPKVdfskfgeietkPLSRIKKISAANLHRSWVTIPHVTQFDEADIT 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79319911 345 KLMALRSQLNSFKEASGGKrISVNDLVVKAAALALRKVPQCNSSWTDD--YIRQFKNVNINVAVQTENGLYVPVVKDADR 422
Cdd:PRK11855 355 DLEALRKQLKKEAEKAGVK-LTMLPFFIKAVVAALKEFPVFNASLDEDgdELTYKKYFNIGFAVDTPNGLVVPVIKDVDK 433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79319911 423 KGLSTIGEEVRLLAQKAKENSLKPEDYEGGTFTVSNLGGpFGIKQFCAVVNPPQAAILAVGSAEKRvvPGNGPDQFNFAS 502
Cdd:PRK11855 434 KSLLEIAREIAELAKKARDGKLKPDDMQGGCFTISSLGG-IGGTAFTPIINAPEVAILGVGKSQMK--PVWDGKEFVPRL 510
|
410 420 430
....*....|....*....|....*....|....*..
gi 79319911 503 YMPVTLSCDHRVVDGAIGAEWLKAFKGYIENPKSMLL 539
Cdd:PRK11855 511 MLPLSLSYDHRVIDGATAARFTNYLKQLLADPRRMLL 547
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
328-538 |
1.51e-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: 286.75 E-value: 1.51e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79319911 328 SKQTIPHYYLTVDTCVDKLMALRSQLNSfKEASGGKRISVNDLVVKAAALALRKVPQCNSSWTDD--YIRQFKNVNINVA 405
Cdd:pfam00198 4 SKQTIPHFTLTDEVDVTELLALREELKE-DAADEETKLTFLPFLVKAVALALKKFPELNASWDGEegEIVYKKYVNIGIA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79319911 406 VQTENGLYVPVVKDADRKGLSTIGEEVRLLAQKAKENSLKPEDYEGGTFTVSNLGGpFGIKQFCAVVNPPQAAILAVGSA 485
Cdd:pfam00198 83 VATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGM-FGVTFFTPIINPPQVAILGVGRI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 79319911 486 EKRVVPGNGpdQFNFASYMPVTLSCDHRVVDGAIGAEWLKAFKGYIENPKSML 538
Cdd:pfam00198 162 RKRPVVVDG--EIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELLL 212
|
|
| PRK05704 |
PRK05704 |
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase; |
113-539 |
2.09e-81 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
Pssm-ID: 235571 [Multi-domain] Cd Length: 407 Bit Score: 259.77 E-value: 2.09e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79319911 113 EIGMPSLSPTMTEGNIARWLKKEGDKVAPGEVLCEVETDKATVEMECMEEGYLAKIVKAEGSKeIQVGEVIAITVEdeed 192
Cdd:PRK05704 4 EIKVPTLPESVTEATIATWHKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGDT-VTVGQVLGRIDE---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79319911 193 igkfkdytpsstaDAAPTKAEPTPAPPKEEKVKQPSSPPEPKASKPSTPptgdrvfASPLARKLAEDNNVPLSDIEGTGP 272
Cdd:PRK05704 79 -------------GAAAGAAAAAAAAAAAAAAAPAQAQAAAAAEQSNDA-------LSPAARKLAAENGLDASAVKGTGK 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79319911 273 EGRIVKADIDEYLASSGKGATAKPSKSTDSKAPALDY---VDIPHSQIRKVTASRLAFSKQTIPhyYLTVDTCVD--KLM 347
Cdd:PRK05704 139 GGRVTKEDVLAALAAAAAAPAAPAAAAPAAAPAPLGArpeERVPMTRLRKTIAERLLEAQNTTA--MLTTFNEVDmtPVM 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79319911 348 ALRSQLNSFKEASGGKRISVNDLVVKAAALALRKVPQCNSSWTDDYI--RQFknVNINVAVQTENGLYVPVVKDADRKGL 425
Cdd:PRK05704 217 DLRKQYKDAFEKKHGVKLGFMSFFVKAVVEALKRYPEVNASIDGDDIvyHNY--YDIGIAVGTPRGLVVPVLRDADQLSF 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79319911 426 STIGEEVRLLAQKAKENSLKPEDYEGGTFTVSNlGGPFGIKQFCAVVNPPQAAILAVGSAEKRVVPGNGpdQFNFASYMP 505
Cdd:PRK05704 295 AEIEKKIAELAKKARDGKLSIEELTGGTFTITN-GGVFGSLMSTPIINPPQSAILGMHKIKERPVAVNG--QIVIRPMMY 371
|
410 420 430
....*....|....*....|....*....|....
gi 79319911 506 VTLSCDHRVVDGAIGAEWLKAFKGYIENPKSMLL 539
Cdd:PRK05704 372 LALSYDHRIIDGKEAVGFLVTIKELLEDPERLLL 405
|
|
| sucB |
TIGR01347 |
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ... |
113-539 |
4.78e-80 |
|
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: 256.20 E-value: 4.78e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79319911 113 EIGMPSLSPTMTEGNIARWLKKEGDKVAPGEVLCEVETDKATVEMECMEEGYLAKIVKAEGSKeIQVGEVIAItvedeed 192
Cdd:TIGR01347 2 EIKVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDT-VESGQVLAI------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79319911 193 IGKFKDYTPSSTADAAPTKAEPTPAPPKEEKVKQPSSPPepkaskpstpptgdrvfASPLARKLAEDNNVPLSDIEGTGP 272
Cdd:TIGR01347 74 LEEGNDATAAPPAKSGEEKEETPAASAAAAPTAAANRPS-----------------LSPAARRLAKEHGIDLSAVPGTGV 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79319911 273 EGRIVKADIDEYLASSGKGATAKPSKSTDSKAPALDYVD-IPHSQIRKVTASRLAFSKQTIPhyYLTVDTCVD--KLMAL 349
Cdd:TIGR01347 137 TGRVTKEDIIKKTEAPASAQPPAAAAAAAAPAAATRPEErVKMTRLRQRIAERLKEAQNSTA--MLTTFNEVDmsAVMEL 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79319911 350 RSQLNSFKEASGGKRISVNDLVVKAAALALRKVPQCNSSWTDDYIRQFKNVNINVAVQTENGLYVPVVKDADRKGLSTIG 429
Cdd:TIGR01347 215 RKRYKEEFEKKHGVKLGFMSFFVKAVVAALKRFPEVNAEIDGDDIVYKDYYDISVAVSTDRGLVVPVVRNADRMSFADIE 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79319911 430 EEVRLLAQKAKENSLKPEDYEGGTFTVSNlGGPFGIKQFCAVVNPPQAAILAVGSAEKRVVPGNGpdQFNFASYMPVTLS 509
Cdd:TIGR01347 295 KEIADLGKKARDGKLTLEDMTGGTFTITN-GGVFGSLMSTPIINPPQSAILGMHGIKERPVAVNG--QIEIRPMMYLALS 371
|
410 420 430
....*....|....*....|....*....|
gi 79319911 510 CDHRVVDGAIGAEWLKAFKGYIENPKSMLL 539
Cdd:TIGR01347 372 YDHRLIDGKEAVTFLVTIKELLEDPRRLLL 401
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
112-539 |
1.07e-79 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 261.86 E-value: 1.07e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79319911 112 QEIGMPSLSptMTEGNIARWLKKEGDKVAPGEVLCEVETDKATVEMECMEEGYLAKIVKAEGSKeIQVGEVIAiTVEDEE 191
Cdd:PRK11854 207 KDVNVPDIG--GDEVEVTEVMVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDK-VKTGSLIM-RFEVEG 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79319911 192 digkfkdyTPSSTADAAPTKAEPTPAPPKEEKVKqpSSPPEPKASKPSTPPTGDRVFASPLARKLAEDNNVPLSDIEGTG 271
Cdd:PRK11854 283 --------AAPAAAPAKQEAAAPAPAAAKAEAPA--AAPAAKAEGKSEFAENDAYVHATPLVRRLAREFGVNLAKVKGTG 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79319911 272 PEGRIVKADIDEYLASSGKGATAKPSKSTDSKA-------PALDYV------DIPHSQIRKVTASRLAFSKQTIPHYYLT 338
Cdd:PRK11854 353 RKGRILKEDVQAYVKDAVKRAEAAPAAAAAGGGgpgllpwPKVDFSkfgeieEVELGRIQKISGANLHRNWVMIPHVTQF 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79319911 339 VDTCVDKLMALRSQLN--SFKEASGGKrISVNDLVVKAAALALRKVPQCNSSWTDD---YIRQfKNVNINVAVQTENGLY 413
Cdd:PRK11854 433 DKADITELEAFRKQQNaeAEKRKLGVK-ITPLVFIMKAVAAALEQMPRFNSSLSEDgqrLTLK-KYVNIGIAVDTPNGLV 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79319911 414 VPVVKDADRKGLSTIGEEVRLLAQKAKENSLKPEDYEGGTFTVSNLGGpFGIKQFCAVVNPPQAAILAVGSAEKRvvPGN 493
Cdd:PRK11854 511 VPVFKDVNKKGIIELSRELMDISKKARDGKLTAGDMQGGCFTISSIGG-LGTTHFTPIVNAPEVAILGVSKSAME--PVW 587
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 79319911 494 GPDQFNFASYMPVTLSCDHRVVDGAIGAEWLKAFKGYIENPKSMLL 539
Cdd:PRK11854 588 NGKEFAPRLMLPLSLSYDHRVIDGADGARFITIINDRLSDIRRLVL 633
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
112-539 |
1.79e-66 |
|
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: 224.75 E-value: 1.79e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79319911 112 QEIGMPSLSpTMTEGNIARWLKKEGDKVAPGEVLCEVETDKATVEMECMEEGyLAKIVKAEGSKEIQVGEVIaITVEDEE 191
Cdd:TIGR01348 117 QEVTVPDIG-DIEKVTVIEVLVKVGDTVSADQSLITLESDKASMEVPAPASG-VVKSVKVKVGDSVPTGDLI-LTLSVAG 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79319911 192 DigkfkdyTPSstADAAPTKAEPTPAPPKEEKVKQPSSPPEPKASKPSTPPTGDR-----VFASPLARKLAEDNNVPLSD 266
Cdd:TIGR01348 194 S-------TPA--TAPAPASAQPAAQSPAATQPEPAAAPAAAKAQAPAPQQAGTQnpakvDHAAPAVRRLAREFGVDLSA 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79319911 267 IEGTGPEGRIVKADIDEYLASSGKGATAKPSKSTDSKA-----PALDYV------DIPHSQIRKVTASRLAFSKQTIPHY 335
Cdd:TIGR01348 265 VKGTGIKGRILREDVQRFVKEPSVRAQAAAASAAGGAPgalpwPNVDFSkfgeveEVDMSRIRKISGANLTRNWTMIPHV 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79319911 336 YLTVDTCVDKLMALRSQLNSFKEASGGKrISVNDLVVKAAALALRKVPQCNSSWTDD---YIRQfKNVNINVAVQTENGL 412
Cdd:TIGR01348 345 THFDKADITEMEAFRKQQNAAVEKEGVK-LTVLHILMKAVAAALKKFPKFNASLDLGgeqLILK-KYVNIGVAVDTPNGL 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79319911 413 YVPVVKDADRKGLSTIGEEVRLLAQKAKENSLKPEDYEGGTFTVSNLGGpFGIKQFCAVVNPPQAAILAVGSAEKRVVpG 492
Cdd:TIGR01348 423 LVPVIKDVDRKGITELALELSDLAKKARDGKLTPDEMQGACFTISSLGG-IGGTAFTPIVNAPEVAILGVSKSGMEPV-W 500
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 79319911 493 NGpDQFNFASYMPVTLSCDHRVVDGAIGAEWLKAFKGYIENPKSMLL 539
Cdd:TIGR01348 501 NG-KEFEPRLMLPLSLSYDHRVIDGADAARFTTYICESLADIRRLLL 546
|
|
| PTZ00144 |
PTZ00144 |
dihydrolipoamide succinyltransferase; Provisional |
114-539 |
1.46e-65 |
|
dihydrolipoamide succinyltransferase; Provisional
Pssm-ID: 240289 [Multi-domain] Cd Length: 418 Bit Score: 218.78 E-value: 1.46e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79319911 114 IGMPSLSPTMTEGNIARWLKKEGDKVAPGEVLCEVETDKATVEMECMEEGYLAKIVKAEGSKeIQVG-EVIAITVEDEED 192
Cdd:PTZ00144 47 IKVPTMGDSISEGTVVEWKKKVGDYVKEDEVICIIETDKVSVDIRAPASGVITKIFAEEGDT-VEVGaPLSEIDTGGAPP 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79319911 193 IGKFKdyTPSSTADAAPTKAEPTPAPPKEEKVKQPSSPPEPKASKPSTPPTGDRVfASPLARKLAEDNNVPLSdiegtgp 272
Cdd:PTZ00144 126 AAAPA--AAAAAKAEKTTPEKPKAAAPTPEPPAASKPTPPAAAKPPEPAPAAKPP-PTPVARADPRETRVPMS------- 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79319911 273 egrivkadideylassgkgatakpskstdskapaldyvdiphsQIRKVTASRLAFSKQTiphYYL--TVDTC-VDKLMAL 349
Cdd:PTZ00144 196 -------------------------------------------RMRQRIAERLKASQNT---CAMltTFNECdMSALMEL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79319911 350 RSQLNSFKEASGGKRISVNDLVVKAAALALRKVPQCNSSWTDDYIRQFKNVNINVAVQTENGLYVPVVKDADRKGLSTIG 429
Cdd:PTZ00144 230 RKEYKDDFQKKHGVKLGFMSAFVKASTIALKKMPIVNAYIDGDEIVYRNYVDISVAVATPTGLVVPVIRNCENKSFAEIE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79319911 430 EEVRLLAQKAKENSLKPEDYEGGTFTVSNlGGPFGIKQFCAVVNPPQAAILAVGSAEKRVVPGNgpDQFNFASYMPVTLS 509
Cdd:PTZ00144 310 KELADLAEKARNNKLTLEDMTGGTFTISN-GGVFGSLMGTPIINPPQSAILGMHAIKKRPVVVG--NEIVIRPIMYLALT 386
|
410 420 430
....*....|....*....|....*....|
gi 79319911 510 CDHRVVDGAIGAEWLKAFKGYIENPKSMLL 539
Cdd:PTZ00144 387 YDHRLIDGRDAVTFLKKIKDLIEDPARMLL 416
|
|
| PLN02528 |
PLN02528 |
2-oxoisovalerate dehydrogenase E2 component |
130-539 |
2.89e-64 |
|
2-oxoisovalerate dehydrogenase E2 component
Pssm-ID: 215289 [Multi-domain] Cd Length: 416 Bit Score: 215.35 E-value: 2.89e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79319911 130 RWLKKEGDKVAPGEVLCEVETDKATVEMECMEEGYLAKIVKAEGSKeIQVGE-VIAITVEDEEDIGKFKDYTPSSTADAA 208
Cdd:PLN02528 17 RWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGKVAQINFSPGDI-VKVGEtLLKIMVEDSQHLRSDSLLLPTDSSNIV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79319911 209 PTKAEptpappkEEKVKQPSSppepkaskpstpptgdrVFASPLARKLAEDNNVPLSDIEGTGPEGRIVKADIDEYLA-- 286
Cdd:PLN02528 96 SLAES-------DERGSNLSG-----------------VLSTPAVRHLAKQYGIDLNDILGTGKDGRVLKEDVLKYAAqk 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79319911 287 ------SSGKGATAKPSKSTDSKAPALD---YVD--IPHSQIRKVTASRLAFSKQtIPHYYLTVDTCVDKLMALRSQLNS 355
Cdd:PLN02528 152 gvvkdsSSAEEATIAEQEEFSTSVSTPTeqsYEDktIPLRGFQRAMVKTMTAAAK-VPHFHYVEEINVDALVELKASFQE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79319911 356 FKEASGGKrISVNDLVVKAAALALRKVPQCNSSWTDDY--IRQFKNVNINVAVQTENGLYVPVVKDADRKGLSTIGEEVR 433
Cdd:PLN02528 231 NNTDPTVK-HTFLPFLIKSLSMALSKYPLLNSCFNEETseIRLKGSHNIGVAMATEHGLVVPNIKNVQSLSLLEITKELS 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79319911 434 LLAQKAKENSLKPEDYEGGTFTVSNLG---GPFGikqfCAVVNPPQAAILAVGSAEKrvVPGNGPDQFNF-ASYMPVTLS 509
Cdd:PLN02528 310 RLQHLAAENKLNPEDITGGTITLSNIGaigGKFG----SPVLNLPEVAIIALGRIQK--VPRFVDDGNVYpASIMTVTIG 383
|
410 420 430
....*....|....*....|....*....|
gi 79319911 510 CDHRVVDGAIGAEWLKAFKGYIENPKSMLL 539
Cdd:PLN02528 384 ADHRVLDGATVARFCNEWKSYVEKPELLML 413
|
|
| SucB_Actino |
TIGR02927 |
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model ... |
113-532 |
1.32e-61 |
|
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: 212.57 E-value: 1.32e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79319911 113 EIGMPSLSPTMTEGNIARWLKKEGDKVAPGEVLCEVETDKATVEMECMEEGYLAKIvKAEGSKEIQVGEVIAITVEDEED 192
Cdd:TIGR02927 128 EVKMPELGESVTEGTVTSWLKAVGDTVEVDEPLLEVSTDKVDTEIPSPVAGTLLEI-RAPEDDTVEVGTVLAIIGDANAA 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79319911 193 IGKFKDYTPSSTADAAPT-KAEPTPAPPKEEKVKQPSSPPEPKASKPSTPP---TGDRV-FASPLARKLAEDNNVPLSDI 267
Cdd:TIGR02927 207 PAEPAEEEAPAPSEAGSEpAPDPAARAPHAAPDPPAPAPAPAKTAAPAAAApvsSGDSGpYVTPLVRKLAKDKGVDLSTV 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79319911 268 EGTGPEGRIVKADIDEYL--ASSGKGATAKPSKSTDSKAPALDY----VDIPH--------SQIRKVTASRLAFSKQTIP 333
Cdd:TIGR02927 287 KGTGVGGRIRKQDVLAAAkaAEEARAAAAAPAAAAAPAAPAAAAkpaePDTAKlrgttqkmNRIRQITADKTIESLQTSA 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79319911 334 HYYLTVDTCVDKLMALRSQLNSFKEASGGKRISVNDLVVKAAALALRKVPQCNSSWTDDY--IRQFKNVNINVAVQTENG 411
Cdd:TIGR02927 367 QLTQVHEVDMTRVAALRARAKNDFLEKNGVNLTFLPFFVQAVTEALKAHPNVNASYNAETkeVTYHDVEHVGIAVDTPRG 446
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79319911 412 LYVPVVKDADRKGLSTIGEEVRLLAQKAKENSLKPEDYEGGTFTVSNLGGPfGIKQFCAVVNPPQAAILAVGSAEKR--- 488
Cdd:TIGR02927 447 LLVPVIHNAGDLSLPGLAKAINDLAARARDNKLKPDELSGGTFTITNIGSG-GALFDTPILNPPQAAILGTGAIVKRprv 525
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 79319911 489 VVPGNGPDQFNFASYMPVTLSCDHRVVDGAIGAEWLKAFKGYIE 532
Cdd:TIGR02927 526 IKDEDGGESIAIRSVCYLPLTYDHRLVDGADAGRFLTTIKKRLE 569
|
|
| PRK14843 |
PRK14843 |
dihydrolipoamide acetyltransferase; Provisional |
250-539 |
1.68e-53 |
|
dihydrolipoamide acetyltransferase; Provisional
Pssm-ID: 184847 [Multi-domain] Cd Length: 347 Bit Score: 184.72 E-value: 1.68e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79319911 250 SPLARKLAEDNNVPLSDIEGTGPEGRIVKADIDEYLASSGKGATAKPSKSTDSKAPALDYVD-------IPHSQIRKVTA 322
Cdd:PRK14843 52 SPLAKRIALEHNIAWQEIQGTGHRGKIMKKDVLALLPENIENDSIKSPAQIEKVEEVPDNVTpygeierIPMTPMRKVIA 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79319911 323 SRLAFSKQTIPHYYLTVDTCVDKLMALRSQLNSFKEASGGKRISVNDLVVKAAALALRKVPQCNSSWTDD--YIRQFKNV 400
Cdd:PRK14843 132 QRMVESYLTAPTFTLNYEVDMTEMLALRKKVLEPIMEATGKKTTVTDLLSLAVVKTLMKHPYINASLTEDgkTIITHNYV 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79319911 401 NINVAVQTENGLYVPVVKDADRKGLSTIGEEVRLLAQKAKENSLKPEDYEGGTFTVSNLgGPFGIKQFCAVVNPPQAAIL 480
Cdd:PRK14843 212 NLAMAVGMDNGLMTPVVYNAEKMSLSELVVAFKDVIGRTLDGKLAPSELQNSTFTISNL-GMFGVQSFGPIINQPNSAIL 290
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 79319911 481 AVGSAEKRVVPGNGpdQFNFASYMPVTLSCDHRVVDGAIGAEWLKAFKGYIENPKSMLL 539
Cdd:PRK14843 291 GVSSTIEKPVVVNG--EIVIRPIMSLGLTIDHRVVDGMAGAKFMKDLKELIETPISMLI 347
|
|
| PLN02226 |
PLN02226 |
2-oxoglutarate dehydrogenase E2 component |
93-539 |
4.64e-43 |
|
2-oxoglutarate dehydrogenase E2 component
Pssm-ID: 177871 [Multi-domain] Cd Length: 463 Bit Score: 159.54 E-value: 4.64e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79319911 93 SCLMQSARGFSSgsDLPPHQEIGMPSLSPTMTEGNIARWLKKEGDKVAPGEVLCEVETDKATVEMECMEEGYLAKIVKAE 172
Cdd:PLN02226 75 STLQRWVRPFSS--ESGDTVEAVVPHMGESITDGTLATFLKKPGERVQADEAIAQIETDKVTIDIASPASGVIQEFLVKE 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79319911 173 GSKeIQVGEVIAITVEDEEDIGKFkdyTPSstaDAAPTKAEPTPAPPKEEKVKqPSSPPEPKASKPSTPPTgdrvfaSPL 252
Cdd:PLN02226 153 GDT-VEPGTKVAIISKSEDAASQV---TPS---QKIPETTDPKPSPPAEDKQK-PKVESAPVAEKPKAPSS------PPP 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79319911 253 ARKLAEDNNVPLSDIEGTgpegrivkadideylassgkgatakpskstdskapaldyvdIPHSQIRKVTASRLAFSKQTI 332
Cdd:PLN02226 219 PKQSAKEPQLPPKERERR-----------------------------------------VPMTRLRKRVATRLKDSQNTF 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79319911 333 PhyYLTVDTCVD--KLMALRSQL-NSFKEASGGKrISVNDLVVKAAALALRKVPQCNSSWTDDYIRQFKNVNINVAVQTE 409
Cdd:PLN02226 258 A--LLTTFNEVDmtNLMKLRSQYkDAFYEKHGVK-LGLMSGFIKAAVSALQHQPVVNAVIDGDDIIYRDYVDISIAVGTS 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79319911 410 NGLYVPVVKDADRKGLSTIGEEVRLLAQKAKENSLKPEDYEGGTFTVSNlGGPFGIKQFCAVVNPPQAAILAVGSAEKR- 488
Cdd:PLN02226 335 KGLVVPVIRGADKMNFAEIEKTINGLAKKANEGTISIDEMAGGSFTVSN-GGVYGSLISTPIINPPQSAILGMHSIVSRp 413
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 79319911 489 -VVPGNGPDQfnfaSYMPVTLSCDHRVVDGAIGAEWLKAFKGYIENPKSMLL 539
Cdd:PLN02226 414 mVVGGSVVPR----PMMYVALTYDHRLIDGREAVYFLRRVKDVVEDPQRLLL 461
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
113-245 |
2.82e-37 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 143.52 E-value: 2.82e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79319911 113 EIGMPSLSPTMTEGNIARWLKKEGDKVAPGEVLCEVETDKATVEMECMEEGYLAKIVKAEGSKEIQVGEVIAITVEDEED 192
Cdd:PRK11892 4 EILMPALSPTMEEGTLAKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKILVPEGTEGVKVNTPIAVLLEEGES 83
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 79319911 193 IgkfkDYTPSSTADAAPTKAEPTPAPPKEEKVKQPSSPPEPKASKPSTPPTGD 245
Cdd:PRK11892 84 A----SDAGAAPAAAAEAAAAAPAAAAAAAAKKAAPAPAAPAAPAAEVAADPD 132
|
|
| PRK11857 |
PRK11857 |
dihydrolipoamide acetyltransferase; Reviewed |
246-534 |
1.92e-34 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237002 [Multi-domain] Cd Length: 306 Bit Score: 131.84 E-value: 1.92e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79319911 246 RVFASPLARKLAEDNNVPLSDIEGTGPEGRIVKADIDEYLASSGKGAT------------AKPSKSTDSKAPALDYVDIP 313
Cdd:PRK11857 1 KILATPIARALAKKLGIDISLLKGSGRDGKILAEDVENFIKSLKSAPTpaeaasvssaqqAAKTAAPAAAPPKLEGKREK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79319911 314 HSQIRKVTASRLAFSKQTIPHYYLTVDTCVDKLMALRSQLNSFKEASGGKRISVNDLVVKAAALALRKVPQCNSSWTD-- 391
Cdd:PRK11857 81 VAPIRKAIARAMTNSWSNVAYVNLVNEIDMTKLWDLRKSVKDPVLKTEGVKLTFLPFIAKAILIALKEFPIFAAKYDEat 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79319911 392 ---DYIrqfKNVNINVAVQTENGLYVPVVKDADRKGLSTIGEEVRLLAQKAKENSLKPEDYEGGTFTVSN---LGGPFGI 465
Cdd:PRK11857 161 selVYP---DTLNLGIAVDTEAGLMVPVIKNAQKLSIVEIAKEISRLAKAARERKIKPDEMKGGSFTITNygsVGSLYGV 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 79319911 466 kqfcAVVNPPQAAILAVGSAEKRVVPGNGpdQFNFASYMPVTLSCDHRVVDGAIGAEWLKAFKGYIENP 534
Cdd:PRK11857 238 ----PVINYPELAIAGVGAIIDKAIVKNG--QIVAGKVMHLTVAADHRWIDGATIGRFASRVKELLEKP 300
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
112-185 |
8.72e-31 |
|
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: 114.42 E-value: 8.72e-31
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 79319911 112 QEIGMPSLSPTMTEGNIARWLKKEGDKVAPGEVLCEVETDKATVEMECMEEGYLAKIVKAEGSKeIQVGEVIAI 185
Cdd:cd06849 1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDT-VPVGQVIAV 73
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
112-185 |
7.93e-28 |
|
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: 106.30 E-value: 7.93e-28
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 79319911 112 QEIGMPSLSPTMTEGNIARWLKKEGDKVAPGEVLCEVETDKATVEMECMEEGYLAKIVKAEGSKeIQVGEVIAI 185
Cdd:COG0508 3 IEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDT-VPVGAVIAV 75
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
112-283 |
1.04e-19 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 90.77 E-value: 1.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79319911 112 QEIGMPSLSPTMTEGNIARWLKKEGDKVAPGEVLCEVETDKATVEMECMEEGYLAKIVKAEGSkEIQVGEVIAItVEDEE 191
Cdd:PRK14875 3 TPITMPKWGLSMTEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGE-TLPVGALLAV-VADAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79319911 192 digkfkdyTPSSTADAaptkaeptpappkeekvkqpssppepkaskpstpptgdrvFASPLARKLAEDNnvplSDIEGTG 271
Cdd:PRK14875 81 --------VSDAEIDA----------------------------------------FIAPFARRFAPEG----IDEEDAG 108
|
170
....*....|..
gi 79319911 272 PEGRivKADIDE 283
Cdd:PRK14875 109 PAPR--KARIGG 118
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
113-185 |
2.18e-16 |
|
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: 73.79 E-value: 2.18e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 79319911 113 EIGMPSLSPTMTEGnIARWLKKEGDKVAPGEVLCEVETDKATVEMECMEEGYLAKIVKAEGSKeIQVGEVIAI 185
Cdd:pfam00364 2 EIKSPMIGESVREG-VVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDT-VEVGDPLAK 72
|
|
| E3_binding |
pfam02817 |
e3 binding domain; This family represents a small domain of the E2 subunit of 2-oxo-acid ... |
247-282 |
7.98e-15 |
|
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: 68.10 E-value: 7.98e-15
10 20 30
....*....|....*....|....*....|....*.
gi 79319911 247 VFASPLARKLAEDNNVPLSDIEGTGPEGRIVKADID 282
Cdd:pfam02817 1 VLASPAARKLARELGIDLSDVKGTGPGGRITKEDVE 36
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
113-175 |
9.03e-15 |
|
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: 69.01 E-value: 9.03e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 79319911 113 EIGMPSLSPTMTEGNIARWLKKEGDKVAPGEVLCEVETDKATVEMECMEEGYLAKIVKAEGSK 175
Cdd:cd06663 1 TILIPDLAQHLGDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTK 63
|
|
| kgd |
PRK12270 |
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ... |
196-525 |
1.97e-14 |
|
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;
Pssm-ID: 237030 [Multi-domain] Cd Length: 1228 Bit Score: 76.47 E-value: 1.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79319911 196 FKDYTP-----SSTADAAPTKAEPTPAPPKEEKVKQPSSPPEPKASKPSTPPTGDRVFASPLARKLAEDNNVPLSDIEGT 270
Cdd:PRK12270 33 FADYGPgstaaPTAAAAAAAAAASAPAAAPAAKAPAAPAPAPPAAAAPAAPPKPAAAAAAAAAPAAPPAAAAAAAPAAAA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79319911 271 GPEGRIVKadideylassgKGATAKPSKSTDSKapaldyVDIPhsqirkvTASrlafSKQTIPHyyltvdtcvdKLMAL- 349
Cdd:PRK12270 113 VEDEVTPL-----------RGAAAAVAKNMDAS------LEVP-------TAT----SVRAVPA----------KLLIDn 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79319911 350 RSQLNSF-KEASGGKrISVNDLVVKAAALALRKVPQCNSSWTDD----YIRQFKNVNINVA--VQTENG---LYVPVVKD 419
Cdd:PRK12270 155 RIVINNHlKRTRGGK-VSFTHLIGYALVQALKAFPNMNRHYAEVdgkpTLVTPAHVNLGLAidLPKKDGsrqLVVPAIKG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79319911 420 ADRKG----LSTIGEEVRllaqKAKENSLKPEDYEGGTFTVSNLGGpFGIKQFCAVVNPPQAAILAVGS----AEKRvvp 491
Cdd:PRK12270 234 AETMDfaqfWAAYEDIVR----RARDGKLTADDFQGTTISLTNPGG-IGTVHSVPRLMKGQGAIIGVGAmeypAEFQ--- 305
|
330 340 350
....*....|....*....|....*....|....*..
gi 79319911 492 GNGPDQFNFASYMPV-TLSC--DHRVVDGAIGAEWLK 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 |
3.28e-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: 42.02 E-value: 3.28e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 79319911 126 GNIARWLKKEGDKVAPGEVLCEVETDKatveMEcME-----EGYLAKIVKAEGSKeIQVGEVIAI 185
Cdd:cd06850 8 GTVVKVLVKEGDKVEAGQPLAVLEAMK----ME-NEvtapvAGVVKEILVKEGDQ-VEAGQLLVV 66
|
|
| PLN02983 |
PLN02983 |
biotin carboxyl carrier protein of acetyl-CoA carboxylase |
201-253 |
4.65e-04 |
|
biotin carboxyl carrier protein of acetyl-CoA carboxylase
Pssm-ID: 215533 [Multi-domain] Cd Length: 274 Bit Score: 42.13 E-value: 4.65e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 79319911 201 PSSTADAAPTKAEPTPAPPKEEKVKQPSSPPEPKASKPSTPPtgdrvFASPLA 253
Cdd:PLN02983 158 PHAMPPASPPAAQPAPSAPASSPPPTPASPPPAKAPKSSHPP-----LKSPMA 205
|
|
| |
