|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
4-538 |
0e+00 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 546.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498181543 4 YQFNLPDIGEgIAEGTVGEWHVKEGDEVKEDGDLVQIENDKSVEELPSPVAGKITKILVPEGETAEVGQPLVELEVADGK 83
Cdd:PRK11855 3 IEFKVPDIGE-VVEVEVIEWLVKEGDTVEEDQPLVTVETDKATMEIPSPAAGVVKEIKVKVGDTVSVGGLLAVIEAAGAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498181543 84 GNVSGEAAPEKPA-----QEEKASATAPAGNGNSGTDTYQFNLPDIGEgIAEGTVGEWHVKEGDEVKEDGDLVQIENDKS 158
Cdd:PRK11855 82 AAAAAPAAAAAPAaaaaaAPAPAAAAPAAAAAAAGGGVVEVKVPDIGE-ITEVEVIEWLVKVGDTVEEDQSLITVETDKA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498181543 159 VEELPSPVAGKITKILVPEGETAEVGQPLVELEVAAGKGNVEGGTTKEAPVAESKETPAANTAAAAPTG-----EKQDHS 233
Cdd:PRK11855 161 TMEIPSPVAGVVKEIKVKVGDKVSVGSLLVVIEVAAAAPAAAAAPAAAAPAAAAAAAPAPAPAAAAAPAaaapaAAAAPG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498181543 234 LPVLAMPGVRAYARDKGADLTQISGSGNHGQILKTDIDSFLAGGGAKAAEAEKTTEQPAEKQKA--PAALVSTSTDWPEH 311
Cdd:PRK11855 241 KAPHASPAVRRLARELGVDLSQVKGTGKKGRITKEDVQAFVKGAMSAAAAAAAAAAAAGGGGLGllPWPKVDFSKFGEIE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498181543 312 TEKMSGIRYATAKAMTRSNDNVPHVHIFDEVVVDKMWDHRKKYKELAASKGVHLTFLAYVTKALAVVLKEFPIFNSQVDM 391
Cdd:PRK11855 321 TKPLSRIKKISAANLHRSWVTIPHVTQFDEADITDLEALRKQLKKEAEKAGVKLTMLPFFIKAVVAALKEFPVFNASLDE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498181543 392 DNKQSVFKDYINIGIATDTDRGLFVPNVKHADQQSLFDIARSISANTEKAKDGKLSSGDMSHTGISITNIGSVGGGFFTP 471
Cdd:PRK11855 401 DGDELTYKKYFNIGFAVDTPNGLVVPVIKDVDKKSLLEIAREIAELAKKARDGKLKPDDMQGGCFTISSLGGIGGTAFTP 480
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 498181543 472 IINFPEVAILGIGKISPEPVVVDGEVKSARVLKLTMAFDHRVIDGATAQRAVNRLKELLGDPELLLM 538
Cdd:PRK11855 481 IINAPEVAILGVGKSQMKPVWDGKEFVPRLMLPLSLSYDHRVIDGATAARFTNYLKQLLADPRRMLL 547
|
|
| PRK11856 |
PRK11856 |
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed |
116-539 |
1.76e-151 |
|
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
Pssm-ID: 237001 [Multi-domain] Cd Length: 411 Bit Score: 440.00 E-value: 1.76e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498181543 116 TYQFNLPDIGEGIAEGTVGEWHVKEGDEVKEDGDLVQIENDKSVEELPSPVAGKITKILVPEGETAEVGQPLVELEVAAG 195
Cdd:PRK11856 2 MFEFKMPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDVVPVGSVIAVIEEEGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498181543 196 KGNVEGGTTKEAPVAESKETPAANTAAAAPTGEKQDHSLP---VLAMPGVRAYARDKGADLTQISGSGNHGQILKTDIDS 272
Cdd:PRK11856 82 AEAAAAAEAAPEAPAPEPAPAAAAAAAAAPAAAAAPAAPAaaaAKASPAVRKLARELGVDLSTVKGSGPGGRITKEDVEA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498181543 273 FLAGggakaaeaektTEQPAEKQKAPAALVSTSTDWPEHTEKMSGIRYATAKAMTRSNDNVPHVHIFDEVVVDKMWDHRK 352
Cdd:PRK11856 162 AAAA-----------AAPAAAAAAAAAAAPPAAAAEGEERVPLSGMRKAIAKRMVESKREIPHFTLTDEVDVTALLALRK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498181543 353 KYKElaasKGVHLTFLAYVTKALAVVLKEFPIFNSQVDMDNkqSVFKDYINIGIATDTDRGLFVPNVKHADQQSLFDIAR 432
Cdd:PRK11856 231 QLKA----IGVKLTVTDFLIKAVALALKKFPELNASWDDDA--IVLKKYVNIGIAVATDGGLIVPVIRDADKKSLFELAR 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498181543 433 SISANTEKAKDGKLSSGDMSHTGISITNIGSVGGGFFTPIINFPEVAILGIGKISPEPVVVDGEVKSARVLKLTMAFDHR 512
Cdd:PRK11856 305 EIKDLAEKAREGKLKPEELQGGTFTISNLGMFGGDYFTPIINPPEVAILGVGAIVERPVVVDGEIVVRKVMPLSLSFDHR 384
|
410 420
....*....|....*....|....*..
gi 498181543 513 VIDGATAQRAVNRLKELLGDPELLLME 539
Cdd:PRK11856 385 VIDGADAARFLKALKELLENPALLLLE 411
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
8-538 |
4.10e-106 |
|
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: 328.37 E-value: 4.10e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498181543 8 LPDIGEGiAEGTVGEWHVKEGDEVKEDGDLVQIENDKSVEELPSPVAGKITKILVPEGETAEVGQPLVELEVADG----- 82
Cdd:TIGR01348 5 VPDIGDN-EEGEVIEVLVKPGDKVEAGQSLITLESDKASMEVPSSAAGIIKEIKVKVGDTLPVGGVIATLEVGAGaqaqa 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498181543 83 --KGNVSGEAAPEKPAQEEKASATAPAGNGNSGTDTyqfNLPDIGeGIAEGTVGEWHVKEGDEVKEDGDLVQIENDKSVE 160
Cdd:TIGR01348 84 eaKKEAAPAPTAGAPAPAAQAQAAPAAGQSSGVQEV---TVPDIG-DIEKVTVIEVLVKVGDTVSADQSLITLESDKASM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498181543 161 ELPSPVAGKITKILVPEGETAEVGQPLVELEVAAGKGNVEGgTTKEAPVAESKETPAANTAAAAPTGEKQDHSLPVL--- 237
Cdd:TIGR01348 160 EVPAPASGVVKSVKVKVGDSVPTGDLILTLSVAGSTPATAP-APASAQPAAQSPAATQPEPAAAPAAAKAQAPAPQQagt 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498181543 238 --------AMPGVRAYARDKGADLTQISGSGNHGQILKTDIDSFLAGGGAKAAEAEKTTEQPAeKQKAPAALVSTSTDWP 309
Cdd:TIGR01348 239 qnpakvdhAAPAVRRLAREFGVDLSAVKGTGIKGRILREDVQRFVKEPSVRAQAAAASAAGGA-PGALPWPNVDFSKFGE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498181543 310 EHTEKMSGIRYATAKAMTRSNDNVPHVHIFDEVVVDKMWDHRKKYKELAASKGVHLTFLAYVTKALAVVLKEFPIFNSQV 389
Cdd:TIGR01348 318 VEEVDMSRIRKISGANLTRNWTMIPHVTHFDKADITEMEAFRKQQNAAVEKEGVKLTVLHILMKAVAAALKKFPKFNASL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498181543 390 DMDNKQSVFKDYINIGIATDTDRGLFVPNVKHADQQSLFDIARSISANTEKAKDGKLSSGDMSHTGISITNIGSVGGGFF 469
Cdd:TIGR01348 398 DLGGEQLILKKYVNIGVAVDTPNGLLVPVIKDVDRKGITELALELSDLAKKARDGKLTPDEMQGACFTISSLGGIGGTAF 477
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 498181543 470 TPIINFPEVAILGIGKISPEPVVVDGEVKSARVLKLTMAFDHRVIDGATAQRAVNRLKELLGDPELLLM 538
Cdd:TIGR01348 478 TPIVNAPEVAILGVSKSGMEPVWNGKEFEPRLMLPLSLSYDHRVIDGADAARFTTYICESLADIRRLLL 546
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
7-538 |
4.97e-106 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 330.81 E-value: 4.97e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498181543 7 NLPDIGEGiaEGTVGEWHVKEGDEVKEDGDLVQIENDKSVEELPSPVAGKITKILVPEGETAEVGQPLVELEVAdgkgnv 86
Cdd:PRK11854 109 HVPDIGSD--EVEVTEILVKVGDTVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVSTGSLIMVFEVA------ 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498181543 87 sGEAAPEKPAQEEKASATAPAGNGNSGTDTyqfNLPDIGEGiaEGTVGEWHVKEGDEVKEDGDLVQIENDKSVEELPSPV 166
Cdd:PRK11854 181 -GEAPAAAPAAAEAAAPAAAPAAAAGVKDV---NVPDIGGD--EVEVTEVMVKVGDKVEAEQSLITVEGDKASMEVPAPF 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498181543 167 AGKITKILVPEGETAEVGQPLVELEVA----AGKGNVEGGTTKEAPVAESKETPAANTAAAAPTGEKQDHSLPVLAMPGV 242
Cdd:PRK11854 255 AGTVKEIKVNVGDKVKTGSLIMRFEVEgaapAAAPAKQEAAAPAPAAAKAEAPAAAPAAKAEGKSEFAENDAYVHATPLV 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498181543 243 RAYARDKGADLTQISGSGNHGQILKTDIDSFLAGGGakaaeaektteQPAEKQKAPAALVSTSTD---WPE--------- 310
Cdd:PRK11854 335 RRLAREFGVNLAKVKGTGRKGRILKEDVQAYVKDAV-----------KRAEAAPAAAAAGGGGPGllpWPKvdfskfgei 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498181543 311 HTEKMSGIRYATAKAMTRSNDNVPHVHIFDEVVVDKMWDHRKKYKELAASK--GVHLTFLAYVTKALAVVLKEFPIFNSQ 388
Cdd:PRK11854 404 EEVELGRIQKISGANLHRNWVMIPHVTQFDKADITELEAFRKQQNAEAEKRklGVKITPLVFIMKAVAAALEQMPRFNSS 483
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498181543 389 VDMDNKQSVFKDYINIGIATDTDRGLFVPNVKHADQQSLFDIARSISANTEKAKDGKLSSGDMSHTGISITNIGSVGGGF 468
Cdd:PRK11854 484 LSEDGQRLTLKKYVNIGIAVDTPNGLVVPVFKDVNKKGIIELSRELMDISKKARDGKLTAGDMQGGCFTISSIGGLGTTH 563
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498181543 469 FTPIINFPEVAILGIGKISPEPVVVDGEVKSARVLKLTMAFDHRVIDGATAQRAVNRLKELLGDPELLLM 538
Cdd:PRK11854 564 FTPIVNAPEVAILGVSKSAMEPVWNGKEFAPRLMLPLSLSYDHRVIDGADGARFITIINDRLSDIRRLVL 633
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
326-537 |
1.82e-93 |
|
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to three copies of a lipoyl binding domain followed by the catalytic domain.
Pssm-ID: 425518 [Multi-domain] Cd Length: 212 Bit Score: 284.05 E-value: 1.82e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498181543 326 MTRSNDNVPHVHIFDEVVVDKMWDHRKKYKELAASKGVHLTFLAYVTKALAVVLKEFPIFNSQVDMDNKQSVFKDYINIG 405
Cdd:pfam00198 1 MTESKQTIPHFTLTDEVDVTELLALREELKEDAADEETKLTFLPFLVKAVALALKKFPELNASWDGEEGEIVYKKYVNIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498181543 406 IATDTDRGLFVPNVKHADQQSLFDIARSISANTEKAKDGKLSSGDMSHTGISITNIGSVGGGFFTPIINFPEVAILGIGK 485
Cdd:pfam00198 81 IAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVGR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 498181543 486 ISPEPVVVDGEVKSARVLKLTMAFDHRVIDGATAQRAVNRLKELLGDPELLL 537
Cdd:pfam00198 161 IRKRPVVVDGEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELLL 212
|
|
| PRK05704 |
PRK05704 |
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase; |
122-540 |
1.93e-87 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
Pssm-ID: 235571 [Multi-domain] Cd Length: 407 Bit Score: 275.56 E-value: 1.93e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498181543 122 PDIGEGIAEGTVGEWHVKEGDEVKEDGDLVQIENDKSVEELPSPVAGKITKILVPEGETAEVGQPLVELEVAAGKGNVEG 201
Cdd:PRK05704 8 PTLPESVTEATIATWHKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGDTVTVGQVLGRIDEGAAAGAAAA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498181543 202 GTTKEAPVAESKETPAANTAAAAPtgekqdhslPVLAMPGVRAYARDKGADLTQISGSGNHGQILKTDIDSFLAGGGaka 281
Cdd:PRK05704 88 AAAAAAAAAAAPAQAQAAAAAEQS---------NDALSPAARKLAAENGLDASAVKGTGKGGRVTKEDVLAALAAAA--- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498181543 282 aeaektTEQPAEKQKAPAALVSTSTDWPEHTEKMSGIRYATAKAMTRSNDNVPHVHIFDEVVVDKMWDHRKKYKELAASK 361
Cdd:PRK05704 156 ------AAPAAPAAAAPAAAPAPLGARPEERVPMTRLRKTIAERLLEAQNTTAMLTTFNEVDMTPVMDLRKQYKDAFEKK 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498181543 362 -GVHLTFLAYVTKALAVVLKEFPIFNSQVDMDNkqSVFKDYINIGIATDTDRGLFVPNVKHADQQSLFDIARSISANTEK 440
Cdd:PRK05704 230 hGVKLGFMSFFVKAVVEALKRYPEVNASIDGDD--IVYHNYYDIGIAVGTPRGLVVPVLRDADQLSFAEIEKKIAELAKK 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498181543 441 AKDGKLSSGDMSHTGISITNIGSVGGGFFTPIINFPEVAILGIGKISPEPVVVDGEVKSARVLKLTMAFDHRVIDGATAQ 520
Cdd:PRK05704 308 ARDGKLSIEELTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHKIKERPVAVNGQIVIRPMMYLALSYDHRIIDGKEAV 387
|
410 420
....*....|....*....|
gi 498181543 521 RAVNRLKELLGDPELLLMEG 540
Cdd:PRK05704 388 GFLVTIKELLEDPERLLLDL 407
|
|
| sucB |
TIGR01347 |
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ... |
120-539 |
3.24e-86 |
|
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: 272.38 E-value: 3.24e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498181543 120 NLPDIGEGIAEGTVGEWHVKEGDEVKEDGDLVQIENDKSVEELPSPVAGKITKILVPEGETAEVGQPLVELEvaagKGNV 199
Cdd:TIGR01347 4 KVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAILE----EGND 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498181543 200 EGGTTKEAPVAESKETPAANTAAAAPTGEKQDHslpvlAMPGVRAYARDKGADLTQISGSGNHGQILKTDIDSFLAGGGA 279
Cdd:TIGR01347 80 ATAAPPAKSGEEKEETPAASAAAAPTAAANRPS-----LSPAARRLAKEHGIDLSAVPGTGVTGRVTKEDIIKKTEAPAS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498181543 280 kaaeaektTEQPAEKQKAPAALVSTStdwPEHTEKMSGIRYATAKAMTRSNDNVPHVHIFDEVVVDKMWDHRKKYKELAA 359
Cdd:TIGR01347 155 --------AQPPAAAAAAAAPAAATR---PEERVKMTRLRQRIAERLKEAQNSTAMLTTFNEVDMSAVMELRKRYKEEFE 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498181543 360 SK-GVHLTFLAYVTKALAVVLKEFPIFNSQVDMDnkQSVFKDYINIGIATDTDRGLFVPNVKHADQQSLFDIARSISANT 438
Cdd:TIGR01347 224 KKhGVKLGFMSFFVKAVVAALKRFPEVNAEIDGD--DIVYKDYYDISVAVSTDRGLVVPVVRNADRMSFADIEKEIADLG 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498181543 439 EKAKDGKLSSGDMSHTGISITNIGSVGGGFFTPIINFPEVAILGIGKISPEPVVVDGEVKSARVLKLTMAFDHRVIDGAT 518
Cdd:TIGR01347 302 KKARDGKLTLEDMTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHGIKERPVAVNGQIEIRPMMYLALSYDHRLIDGKE 381
|
410 420
....*....|....*....|.
gi 498181543 519 AQRAVNRLKELLGDPELLLME 539
Cdd:TIGR01347 382 AVTFLVTIKELLEDPRRLLLD 402
|
|
| PLN02528 |
PLN02528 |
2-oxoisovalerate dehydrogenase E2 component |
119-538 |
3.92e-83 |
|
2-oxoisovalerate dehydrogenase E2 component
Pssm-ID: 215289 [Multi-domain] Cd Length: 416 Bit Score: 264.66 E-value: 3.92e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498181543 119 FNLPDIGEGIAEGTVGEWHVKEGDEVKEDGDLVQIENDKSVEELPSPVAGKITKILVPEGETAEVGQPLVELEVAAGKGN 198
Cdd:PLN02528 1 VPLAQTGEGIAECELLRWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGKVAQINFSPGDIVKVGETLLKIMVEDSQHL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498181543 199 VEGGTTKEAPVAESKETPaantaaaaptGEKQDHSLP--VLAMPGVRAYARDKGADLTQISGSGNHGQILKTDIDSFLAG 276
Cdd:PLN02528 81 RSDSLLLPTDSSNIVSLA----------ESDERGSNLsgVLSTPAVRHLAKQYGIDLNDILGTGKDGRVLKEDVLKYAAQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498181543 277 GGAKAAEAEKTTEQPAEkQKAPAALVSTSTDW--PEHTEKMSGIRYATAKAMTRSNdNVPHVHIFDEVVVDKMWDHRKKY 354
Cdd:PLN02528 151 KGVVKDSSSAEEATIAE-QEEFSTSVSTPTEQsyEDKTIPLRGFQRAMVKTMTAAA-KVPHFHYVEEINVDALVELKASF 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498181543 355 KELAASKGVHLTFLAYVTKALAVVLKEFPIFNSQVDMDNKQSVFKDYINIGIATDTDRGLFVPNVKHADQQSLFDIARSI 434
Cdd:PLN02528 229 QENNTDPTVKHTFLPFLIKSLSMALSKYPLLNSCFNEETSEIRLKGSHNIGVAMATEHGLVVPNIKNVQSLSLLEITKEL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498181543 435 SANTEKAKDGKLSSGDMSHTGISITNIGSVGGGFFTPIINFPEVAILGIGKISPEPVVVD-GEVKSARVLKLTMAFDHRV 513
Cdd:PLN02528 309 SRLQHLAAENKLNPEDITGGTITLSNIGAIGGKFGSPVLNLPEVAIIALGRIQKVPRFVDdGNVYPASIMTVTIGADHRV 388
|
410 420
....*....|....*....|....*
gi 498181543 514 IDGATAQRAVNRLKELLGDPELLLM 538
Cdd:PLN02528 389 LDGATVARFCNEWKSYVEKPELLML 413
|
|
| PRK11857 |
PRK11857 |
dihydrolipoamide acetyltransferase; Reviewed |
236-536 |
1.63e-77 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237002 [Multi-domain] Cd Length: 306 Bit Score: 246.24 E-value: 1.63e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498181543 236 VLAMPGVRAYARDKGADLTQISGSGNHGQILKTDIDSFLAGGGAKAAEAEKTTEQPAEKQKAPAALVSTSTDWPEHTEKM 315
Cdd:PRK11857 2 ILATPIARALAKKLGIDISLLKGSGRDGKILAEDVENFIKSLKSAPTPAEAASVSSAQQAAKTAAPAAAPPKLEGKREKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498181543 316 SGIRYATAKAMTRSNDNVPHVHIFDEVVVDKMWDHRKKYKE-LAASKGVHLTFLAYVTKALAVVLKEFPIFNSQVDMDNK 394
Cdd:PRK11857 82 APIRKAIARAMTNSWSNVAYVNLVNEIDMTKLWDLRKSVKDpVLKTEGVKLTFLPFIAKAILIALKEFPIFAAKYDEATS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498181543 395 QSVFKDYINIGIATDTDRGLFVPNVKHADQQSLFDIARSISANTEKAKDGKLSSGDMSHTGISITNIGSVGGGFFTPIIN 474
Cdd:PRK11857 162 ELVYPDTLNLGIAVDTEAGLMVPVIKNAQKLSIVEIAKEISRLAKAARERKIKPDEMKGGSFTITNYGSVGSLYGVPVIN 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 498181543 475 FPEVAILGIGKISPEPVVVDGEVKSARVLKLTMAFDHRVIDGATAQRAVNRLKELLGDPELL 536
Cdd:PRK11857 242 YPELAIAGVGAIIDKAIVKNGQIVAGKVMHLTVAADHRWIDGATIGRFASRVKELLEKPEIL 303
|
|
| PTZ00144 |
PTZ00144 |
dihydrolipoamide succinyltransferase; Provisional |
120-539 |
2.19e-62 |
|
dihydrolipoamide succinyltransferase; Provisional
Pssm-ID: 240289 [Multi-domain] Cd Length: 418 Bit Score: 210.31 E-value: 2.19e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498181543 120 NLPDIGEGIAEGTVGEWHVKEGDEVKEDGDLVQIENDKSVEELPSPVAGKITKILVPEGETAEVGQPLVELEvAAGKGNV 199
Cdd:PTZ00144 48 KVPTMGDSISEGTVVEWKKKVGDYVKEDEVICIIETDKVSVDIRAPASGVITKIFAEEGDTVEVGAPLSEID-TGGAPPA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498181543 200 EGGTTKEAPVAESKETPAANTAAAAPTGEKQDHSLPVlampgvrayardkgadltqisgsgnhgqilktdidsflaggga 279
Cdd:PTZ00144 127 AAPAAAAAAKAEKTTPEKPKAAAPTPEPPAASKPTPP------------------------------------------- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498181543 280 kaaEAEKTTEQPAEKQKAPAALvsTSTDWPEHTEKMSGIRYATAKAMTRSNDNVPHVHIFDEVVVDKMWDHRKKYKELAA 359
Cdd:PTZ00144 164 ---AAAKPPEPAPAAKPPPTPV--ARADPRETRVPMSRMRQRIAERLKASQNTCAMLTTFNECDMSALMELRKEYKDDFQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498181543 360 SK-GVHLTFLAYVTKALAVVLKEFPIFNSQVDmdNKQSVFKDYINIGIATDTDRGLFVPNVKHADQQSLFDIARSISANT 438
Cdd:PTZ00144 239 KKhGVKLGFMSAFVKASTIALKKMPIVNAYID--GDEIVYRNYVDISVAVATPTGLVVPVIRNCENKSFAEIEKELADLA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498181543 439 EKAKDGKLSSGDMSHTGISITNIGSVGGGFFTPIINFPEVAILGIGKISPEPVVVDGEVKSARVLKLTMAFDHRVIDGAT 518
Cdd:PTZ00144 317 EKARNNKLTLEDMTGGTFTISNGGVFGSLMGTPIINPPQSAILGMHAIKKRPVVVGNEIVIRPIMYLALTYDHRLIDGRD 396
|
410 420
....*....|....*....|.
gi 498181543 519 AQRAVNRLKELLGDPELLLME 539
Cdd:PTZ00144 397 AVTFLKKIKDLIEDPARMLLD 417
|
|
| PDHac_trf_mito |
TIGR01349 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
120-538 |
2.39e-56 |
|
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: 195.01 E-value: 2.39e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498181543 120 NLPDIGEGIAEGTVGEWHVKEGDEVKEDGDLVQIENDKSVEELPSPVAGKITKILVPEG-ETAEVGQPLV-------ELE 191
Cdd:TIGR01349 3 TMPALSPTMTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEGtKDVPVNKPIAvlveekeDVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498181543 192 VAAGKGNVEGG------TTKEAPVAE-----SKETPAANTAAAAPTGEKQDHSLP--VLAMPGVRAYARDKGADLTQISG 258
Cdd:TIGR01349 83 DAFKNYKLESSaspapkPSEIAPTAPpsapkPSPAPQKQSPEPSSPAPLSDKESGdrIFASPLAKKLAKEKGIDLSAVAG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498181543 259 SGNHGQILKTDIDSFLAGGGAKAAEAEKTTEQPAekqKAPAALVSTS--TDWPehtekMSGIRYATAKAMTRSNDNVPHV 336
Cdd:TIGR01349 163 SGPNGRIVKKDIESFVPQSPASANQQAAATTPAT---YPAAAPVSTGsyEDVP-----LSNIRKIIAKRLLESKQTIPHY 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498181543 337 HIFDEVVVDKMWDHRKKYKELAASKgVHLTFLAYVTKALAVVLKEFPIFNSQVdMDNKQSVFKDyINIGIATDTDRGLFV 416
Cdd:TIGR01349 235 YVSIECNVDKLLALRKELNAMASEV-YKLSVNDFIIKASALALREVPEANSSW-TDNFIRRYKN-VDISVAVATPDGLIT 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498181543 417 PNVKHADQQSLFDIARSISANTEKAKDGKLSSGDMSHTGISITNIGSVGGGFFTPIINFPEVAILGIGKISPEPVVVDGE 496
Cdd:TIGR01349 312 PIVRNADAKGLSTISNEIKDLAKRARNNKLKPEEFQGGTFTISNLGMFGIKDFTAIINPPQACILAVGAVEDVAVVDNDE 391
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 498181543 497 VKS---ARVLKLTMAFDHRVIDGATAQRAVNRLKELLGDPELLLM 538
Cdd:TIGR01349 392 EKGfavASIMSVTLSCDHRVIDGAVGAEFLKSFKKYLENPIEMLL 436
|
|
| PLN02744 |
PLN02744 |
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex |
121-538 |
1.90e-44 |
|
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
Pssm-ID: 215397 [Multi-domain] Cd Length: 539 Bit Score: 165.03 E-value: 1.90e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498181543 121 LPDIGEGIAEGTVGEWHVKEGDEVKEDGDLVQIENDKSVEELPSPVAGKITKILVPEG-ETAEVGQPL---VELEVAAGK 196
Cdd:PLN02744 117 MPSLSPTMTEGNIARWLKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVKGDGaKEIKVGEVIaitVEEEEDIGK 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498181543 197 ---------GNVEGGTTKEAPVAESKETPAANTAAAAPTGEKQDHSLP----VLAMPGVRAYARDKGADLTQISGSGNHG 263
Cdd:PLN02744 197 fkdykpsssAAPAAPKAKPSPPPPKEEEVEKPASSPEPKASKPSAPPSsgdrIFASPLARKLAEDNNVPLSSIKGTGPDG 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498181543 264 QILKTDIDSFLAGGGakaaeaektTEQPAEKQKAPAALVSTSTDWPeHTEkmsgIRYATAKAMTRSNDNVPHVHIFDEVV 343
Cdd:PLN02744 277 RIVKADIEDYLASGG---------KGATAPPSTDSKAPALDYTDIP-NTQ----IRKVTASRLLQSKQTIPHYYLTVDTR 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498181543 344 VDKMWDHRKKYKELA-ASKGVHLTFLAYVTKALAVVLKEFPIFNSQVdMDNKQSVFKDyINIGIATDTDRGLFVPNVKHA 422
Cdd:PLN02744 343 VDKLMALRSQLNSLQeASGGKKISVNDLVIKAAALALRKVPQCNSSW-TDDYIRQYHN-VNINVAVQTENGLYVPVVKDA 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498181543 423 DQQSLFDIARSISANTEKAKDGKLSSGDMSHTGISITNIgsvGGGF----FTPIINFPEVAILGIGkiSPEPVVV----D 494
Cdd:PLN02744 421 DKKGLSTIAEEVKQLAQKARENSLKPEDYEGGTFTVSNL---GGPFgikqFCAIINPPQSAILAVG--SAEKRVIpgsgP 495
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 498181543 495 GEVKSARVLKLTMAFDHRVIDGATAQRAVNRLKELLGDPELLLM 538
Cdd:PLN02744 496 DQYNFASFMSVTLSCDHRVIDGAIGAEWLKAFKGYIENPESMLL 539
|
|
| PLN02226 |
PLN02226 |
2-oxoglutarate dehydrogenase E2 component |
115-539 |
4.71e-43 |
|
2-oxoglutarate dehydrogenase E2 component
Pssm-ID: 177871 [Multi-domain] Cd Length: 463 Bit Score: 159.54 E-value: 4.71e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498181543 115 DTYQFNLPDIGEGIAEGTVGEWHVKEGDEVKEDGDLVQIENDKSVEELPSPVAGKITKILVPEGETAEVGQPLVEL---- 190
Cdd:PLN02226 90 DTVEAVVPHMGESITDGTLATFLKKPGERVQADEAIAQIETDKVTIDIASPASGVIQEFLVKEGDTVEPGTKVAIIskse 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498181543 191 ----EVAAGKGNVEGGTTKEAPVAESKEtpaantaaaaptgEKQDHSLPVLAMPgvrayardkgadltqisgsgnhgqil 266
Cdd:PLN02226 170 daasQVTPSQKIPETTDPKPSPPAEDKQ-------------KPKVESAPVAEKP-------------------------- 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498181543 267 ktdidsflagggakaaeaEKTTEQPAEKQKAPAALVStstdwPEHTEK---MSGIRYATAKAMTRSNDNVPHVHIFDEVV 343
Cdd:PLN02226 211 ------------------KAPSSPPPPKQSAKEPQLP-----PKERERrvpMTRLRKRVATRLKDSQNTFALLTTFNEVD 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498181543 344 VDKMWDHRKKYKELAASK-GVHLTFLAYVTKALAVVLKEFPIFNSQVDMDNkqSVFKDYINIGIATDTDRGLFVPNVKHA 422
Cdd:PLN02226 268 MTNLMKLRSQYKDAFYEKhGVKLGLMSGFIKAAVSALQHQPVVNAVIDGDD--IIYRDYVDISIAVGTSKGLVVPVIRGA 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498181543 423 DQQSLFDIARSISANTEKAKDGKLSSGDMSHTGISITNIGSVGGGFFTPIINFPEVAILGIGKISPEPVVVDGEVKSARV 502
Cdd:PLN02226 346 DKMNFAEIEKTINGLAKKANEGTISIDEMAGGSFTVSNGGVYGSLISTPIINPPQSAILGMHSIVSRPMVVGGSVVPRPM 425
|
410 420 430
....*....|....*....|....*....|....*..
gi 498181543 503 LKLTMAFDHRVIDGATAQRAVNRLKELLGDPELLLME 539
Cdd:PLN02226 426 MYVALTYDHRLIDGREAVYFLRRVKDVVEDPQRLLLD 462
|
|
| PRK14843 |
PRK14843 |
dihydrolipoamide acetyltransferase; Provisional |
240-538 |
1.42e-36 |
|
dihydrolipoamide acetyltransferase; Provisional
Pssm-ID: 184847 [Multi-domain] Cd Length: 347 Bit Score: 138.88 E-value: 1.42e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498181543 240 PGVRAYARDKGADLTQISGSGNHGQILKTDIDSFLAGGGAKAaeaekTTEQPAEKQKAPAALVSTSTDWPEHTEKMSGIR 319
Cdd:PRK14843 53 PLAKRIALEHNIAWQEIQGTGHRGKIMKKDVLALLPENIEND-----SIKSPAQIEKVEEVPDNVTPYGEIERIPMTPMR 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498181543 320 YATAKAMTRSNDNVPHVHIFDEVVVDKMWDHRKKYKE-LAASKGVHLTFLAYVTKALAVVLKEFPIFNSQVDMDNKQSVF 398
Cdd:PRK14843 128 KVIAQRMVESYLTAPTFTLNYEVDMTEMLALRKKVLEpIMEATGKKTTVTDLLSLAVVKTLMKHPYINASLTEDGKTIIT 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498181543 399 KDYINIGIATDTDRGLFVPNVKHADQQSLFDIARSISANTEKAKDGKLSSGDMSHTGISITNIGSVGGGFFTPIINFPEV 478
Cdd:PRK14843 208 HNYVNLAMAVGMDNGLMTPVVYNAEKMSLSELVVAFKDVIGRTLDGKLAPSELQNSTFTISNLGMFGVQSFGPIINQPNS 287
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 498181543 479 AILGIGKISPEPVVVDGEVKSARVLKLTMAFDHRVIDGATAQRAVNRLKELLGDPELLLM 538
Cdd:PRK14843 288 AILGVSSTIEKPVVVNGEIVIRPIMSLGLTIDHRVVDGMAGAKFMKDLKELIETPISMLI 347
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
4-77 |
5.70e-26 |
|
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. 2-oxo acid dehydrogenase multienzyme complexes, like pyruvate dehydrogenase (PDH), 2-oxoglutarate dehydrogenase (OGDH) and branched-chain 2-oxo acid dehydrogenase (BCDH), contain at least three different enzymes, 2-oxo acid dehydrogenase (E1), dihydrolipoyl acyltransferase (E2) and dihydrolipoamide dehydrogenase (E3) and play a key role in redox regulation. E2, the central component of the complex, catalyzes the transfer of the acyl group of CoA from E1 to E3 via reductive acetylation of a lipoyl group covalently attached to a lysine residue.
Pssm-ID: 133458 [Multi-domain] Cd Length: 74 Bit Score: 100.94 E-value: 5.70e-26
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 498181543 4 YQFNLPDIGEGIAEGTVGEWHVKEGDEVKEDGDLVQIENDKSVEELPSPVAGKITKILVPEGETAEVGQPLVEL 77
Cdd:cd06849 1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
117-190 |
5.70e-26 |
|
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. 2-oxo acid dehydrogenase multienzyme complexes, like pyruvate dehydrogenase (PDH), 2-oxoglutarate dehydrogenase (OGDH) and branched-chain 2-oxo acid dehydrogenase (BCDH), contain at least three different enzymes, 2-oxo acid dehydrogenase (E1), dihydrolipoyl acyltransferase (E2) and dihydrolipoamide dehydrogenase (E3) and play a key role in redox regulation. E2, the central component of the complex, catalyzes the transfer of the acyl group of CoA from E1 to E3 via reductive acetylation of a lipoyl group covalently attached to a lysine residue.
Pssm-ID: 133458 [Multi-domain] Cd Length: 74 Bit Score: 100.94 E-value: 5.70e-26
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 498181543 117 YQFNLPDIGEGIAEGTVGEWHVKEGDEVKEDGDLVQIENDKSVEELPSPVAGKITKILVPEGETAEVGQPLVEL 190
Cdd:cd06849 1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
116-190 |
8.19e-26 |
|
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: 100.53 E-value: 8.19e-26
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 498181543 116 TYQFNLPDIGEGIAEGTVGEWHVKEGDEVKEDGDLVQIENDKSVEELPSPVAGKITKILVPEGETAEVGQPLVEL 190
Cdd:COG0508 2 AIEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
4-77 |
8.44e-26 |
|
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: 100.53 E-value: 8.44e-26
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 498181543 4 YQFNLPDIGEGIAEGTVGEWHVKEGDEVKEDGDLVQIENDKSVEELPSPVAGKITKILVPEGETAEVGQPLVEL 77
Cdd:COG0508 3 IEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
5-77 |
6.20e-18 |
|
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue binds biotin in one group and lipoic acid in the other. Note that the HMM does not currently recognize the Glycine cleavage system H proteins.
Pssm-ID: 395290 [Multi-domain] Cd Length: 73 Bit Score: 78.02 E-value: 6.20e-18
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 498181543 5 QFNLPDIGEGIAEGTVgEWHVKEGDEVKEDGDLVQIENDKSVEELPSPVAGKITKILVPEGETAEVGQPLVEL 77
Cdd:pfam00364 2 EIKSPMIGESVREGVV-EWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
118-190 |
6.20e-18 |
|
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue binds biotin in one group and lipoic acid in the other. Note that the HMM does not currently recognize the Glycine cleavage system H proteins.
Pssm-ID: 395290 [Multi-domain] Cd Length: 73 Bit Score: 78.02 E-value: 6.20e-18
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 498181543 118 QFNLPDIGEGIAEGTVgEWHVKEGDEVKEDGDLVQIENDKSVEELPSPVAGKITKILVPEGETAEVGQPLVEL 190
Cdd:pfam00364 2 EIKSPMIGESVREGVV-EWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
|
|
| kgd |
PRK12270 |
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ... |
288-530 |
3.23e-15 |
|
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;
Pssm-ID: 237030 [Multi-domain] Cd Length: 1228 Bit Score: 79.16 E-value: 3.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498181543 288 TEQPAEKQKAPAALVSTSTDWPEHTEKMSGIRYATAKAMTRSNDnVPHVHIFDEVVVDKMWDHRKKYKE-LAASKGVHLT 366
Cdd:PRK12270 93 AAAPAAPPAAAAAAAPAAAAVEDEVTPLRGAAAAVAKNMDASLE-VPTATSVRAVPAKLLIDNRIVINNhLKRTRGGKVS 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498181543 367 F---LAYvtkALAVVLKEFPIFNSQVDM-DNKQSVFKD-YINIGIATDT-----DRGLFVPNVKHADQQSLF-------D 429
Cdd:PRK12270 172 FthlIGY---ALVQALKAFPNMNRHYAEvDGKPTLVTPaHVNLGLAIDLpkkdgSRQLVVPAIKGAETMDFAqfwaayeD 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498181543 430 IARsisanteKAKDGKLSSGDMSHTGISITN---IGSV--------GGGfftpiinfpevAILGIGKI---------SPE 489
Cdd:PRK12270 249 IVR-------RARDGKLTADDFQGTTISLTNpggIGTVhsvprlmkGQG-----------AIIGVGAMeypaefqgaSEE 310
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 498181543 490 PVVVDGEVKsarVLKLTMAFDHRVIDGATAQRAVNRLKELL 530
Cdd:PRK12270 311 RLAELGISK---VMTLTSTYDHRIIQGAESGEFLRTIHQLL 348
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
8-77 |
7.59e-13 |
|
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: 63.61 E-value: 7.59e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498181543 8 LPDIGEGIAEGTVGEWHVKEGDEVKEDGDLVQIENDKSVEELPSPVAGKITKILVPEGETAEVGQPLVEL 77
Cdd:cd06663 4 IPDLAQHLGDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKVEGDTPLVKI 73
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
121-190 |
7.59e-13 |
|
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: 63.61 E-value: 7.59e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498181543 121 LPDIGEGIAEGTVGEWHVKEGDEVKEDGDLVQIENDKSVEELPSPVAGKITKILVPEGETAEVGQPLVEL 190
Cdd:cd06663 4 IPDLAQHLGDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKVEGDTPLVKI 73
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
116-220 |
1.12e-12 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 70.42 E-value: 1.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498181543 116 TYQFNLPDIGEGiaEGTVGEWHVKEGDEVKEDGDLVQIENDKSVEELPSPVAGKITKILVPEGETAEVGQPLVELEVAAG 195
Cdd:PRK11854 2 AIEIKVPDIGAD--EVEVTEILVKVGDKVEAEQSLITVEGDKASMEVPSPQAGVVKEIKVKVGDKVETGALIMIFESADG 79
|
90 100
....*....|....*....|....*
gi 498181543 196 KgnveggttkeapvAESKETPAANT 220
Cdd:PRK11854 80 A-------------ADAAPAQAEEK 91
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
8-74 |
1.12e-11 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 66.51 E-value: 1.12e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 498181543 8 LPDIGEGIAEGTVGEWHVKEGDEVKEDGDLVQIENDKSVEELPSPVAGKITKILVPEGETAEVGQPL 74
Cdd:PRK14875 7 MPKWGLSMTEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGETLPVGALL 73
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
121-187 |
1.12e-11 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 66.51 E-value: 1.12e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 498181543 121 LPDIGEGIAEGTVGEWHVKEGDEVKEDGDLVQIENDKSVEELPSPVAGKITKILVPEGETAEVGQPL 187
Cdd:PRK14875 7 MPKWGLSMTEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGETLPVGALL 73
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
18-77 |
9.09e-11 |
|
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: 57.43 E-value: 9.09e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 498181543 18 GTVGEWHVKEGDEVKEDGDLVQIENDKSVEELPSPVAGKITKILVPEGETAEVGQPLVEL 77
Cdd:cd06850 8 GTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
131-190 |
9.09e-11 |
|
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: 57.43 E-value: 9.09e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 498181543 131 GTVGEWHVKEGDEVKEDGDLVQIENDKSVEELPSPVAGKITKILVPEGETAEVGQPLVEL 190
Cdd:cd06850 8 GTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
17-107 |
2.36e-10 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 62.63 E-value: 2.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498181543 17 EGTVGEWHVKEGDEVKEdGD-LVQIENDKSVEELPSPVAGKITKILVPEG-ETAEVGQPLVELeVADGKGNVSGEAAPEK 94
Cdd:PRK11892 16 EGTLAKWLKKEGDKVKS-GDvIAEIETDKATMEVEAVDEGTLGKILVPEGtEGVKVNTPIAVL-LEEGESASDAGAAPAA 93
|
90
....*....|...
gi 498181543 95 PAQEEKASATAPA 107
Cdd:PRK11892 94 AAEAAAAAPAAAA 106
|
|
| PRK09282 |
PRK09282 |
pyruvate carboxylase subunit B; Validated |
30-191 |
7.35e-09 |
|
pyruvate carboxylase subunit B; Validated
Pssm-ID: 236449 [Multi-domain] Cd Length: 592 Bit Score: 58.32 E-value: 7.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498181543 30 EVKEDGDLVQIENDKSVEELPSPVAGKITKILVpEGETAEVGQPLVELEVADG---KGNVSGEAAPEKPAQEEKASATAP 106
Cdd:PRK09282 440 EEREAGELKPEPEPKEAAAAGAEGIPTEFKVEV-DGEKYEVKIEGVKAEGKRPfylRVDGMPEEVVVEPLKEIVVGGRPR 518
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498181543 107 AGNGNSGTDTYQfnlpdigegiaeGTVGEWHVKEGDEVKEdGD-LVQIENDKSVEELPSPVAGKITKILVPEGETAEVGQ 185
Cdd:PRK09282 519 ASAPGAVTSPMP------------GTVVKVKVKEGDKVKA-GDtVLVLEAMKMENEIQAPVDGTVKEILVKEGDRVNPGD 585
|
....*.
gi 498181543 186 PLVELE 191
Cdd:PRK09282 586 VLMEIE 591
|
|
| AccB |
COG0511 |
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ... |
74-191 |
1.46e-08 |
|
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440277 [Multi-domain] Cd Length: 136 Bit Score: 53.36 E-value: 1.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498181543 74 LVELEVADGKGNVS---GEAAPEKPAQEEKASATAPAGNGNSGTDtyqfnlPDIGEGIA-----EGTVGEWH-------V 138
Cdd:COG0511 10 LTELEVEEGEYKVRikrGGAAAAAPVAAPAAAAPAAAAPAAAAAA------AAASGGGAvkspmVGTFYRAPspgakpfV 83
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 498181543 139 KEGDEVKEdGD-LVQIENDKSVEELPSPVAGKITKILVPEGETAEVGQPLVELE 191
Cdd:COG0511 84 KVGDKVKA-GDtLCIIEAMKMMNEIEAPVSGTVVEILVENGQPVEYGQPLFVIE 136
|
|
| AccB |
COG0511 |
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ... |
25-78 |
1.65e-08 |
|
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440277 [Multi-domain] Cd Length: 136 Bit Score: 53.36 E-value: 1.65e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 498181543 25 VKEGDEVKEdGD-LVQIENDKSVEELPSPVAGKITKILVPEGETAEVGQPLVELE 78
Cdd:COG0511 83 VKVGDKVKA-GDtLCIIEAMKMMNEIEAPVSGTVVEILVENGQPVEYGQPLFVIE 136
|
|
| E3_binding |
pfam02817 |
e3 binding domain; This family represents a small domain of the E2 subunit of 2-oxo-acid ... |
236-271 |
1.76e-08 |
|
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: 49.99 E-value: 1.76e-08
10 20 30
....*....|....*....|....*....|....*.
gi 498181543 236 VLAMPGVRAYARDKGADLTQISGSGNHGQILKTDID 271
Cdd:pfam02817 1 VLASPAARKLARELGIDLSDVKGTGPGGRITKEDVE 36
|
|
| PRK05641 |
PRK05641 |
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
25-77 |
2.20e-08 |
|
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235540 [Multi-domain] Cd Length: 153 Bit Score: 53.33 E-value: 2.20e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 498181543 25 VKEGDEVKEDGDLVQIENDKSVEELPSPVAGKITKILVPEGETAEVGQPLVEL 77
Cdd:PRK05641 100 VREGQQVKVGQGLLILEAMKMENEIPAPKDGVVKKILVKEGDTVDTGQPLIEL 152
|
|
| PRK05641 |
PRK05641 |
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
138-190 |
2.20e-08 |
|
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235540 [Multi-domain] Cd Length: 153 Bit Score: 53.33 E-value: 2.20e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 498181543 138 VKEGDEVKEDGDLVQIENDKSVEELPSPVAGKITKILVPEGETAEVGQPLVEL 190
Cdd:PRK05641 100 VREGQQVKVGQGLLILEAMKMENEIPAPKDGVVKKILVKEGDTVDTGQPLIEL 152
|
|
| PRK09282 |
PRK09282 |
pyruvate carboxylase subunit B; Validated |
18-78 |
4.28e-08 |
|
pyruvate carboxylase subunit B; Validated
Pssm-ID: 236449 [Multi-domain] Cd Length: 592 Bit Score: 56.00 E-value: 4.28e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 498181543 18 GTVGEWHVKEGDEVKEdGD-LVQIENDKSVEELPSPVAGKITKILVPEGETAEVGQPLVELE 78
Cdd:PRK09282 531 GTVVKVKVKEGDKVKA-GDtVLVLEAMKMENEIQAPVDGTVKEILVKEGDRVNPGDVLMEIE 591
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
130-242 |
1.32e-07 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 54.15 E-value: 1.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498181543 130 EGTVGEWHVKEGDEVKEdGD-LVQIENDKSVEELPSPVAGKITKILVPEG-ETAEVGQPLVELevaAGKGNvEGGTTKEA 207
Cdd:PRK11892 16 EGTLAKWLKKEGDKVKS-GDvIAEIETDKATMEVEAVDEGTLGKILVPEGtEGVKVNTPIAVL---LEEGE-SASDAGAA 90
|
90 100 110
....*....|....*....|....*....|....*
gi 498181543 208 PVAESKETPAANTAAAAPTGEKQDHSLPVLAMPGV 242
Cdd:PRK11892 91 PAAAAEAAAAAPAAAAAAAAKKAAPAPAAPAAPAA 125
|
|
| PRK14040 |
PRK14040 |
oxaloacetate decarboxylase subunit alpha; |
63-190 |
1.19e-06 |
|
oxaloacetate decarboxylase subunit alpha;
Pssm-ID: 237592 [Multi-domain] Cd Length: 593 Bit Score: 51.08 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498181543 63 PEGETAEV-GQPLVeLEVADGkGNVSGEAAPEKPAQEEKASATAPAGNGnsgtdtyqfnlpdiGEGIA---EGTVGEWHV 138
Cdd:PRK14040 477 SETYTVEVeGKAYV-VKVSEG-GDISQITPAAPAAAPAAAAAAAPAAAA--------------GEPVTaplAGNIFKVIV 540
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 498181543 139 KEGDEVKEdGDLVQI-ENDKSVEELPSPVAGKITKILVPEGETAEVGQPLVEL 190
Cdd:PRK14040 541 TEGQTVAE-GDVLLIlEAMKMETEIRAAQAGTVRGIAVKEGDAVAVGDTLLTL 592
|
|
| PRK08225 |
PRK08225 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
18-78 |
1.14e-05 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 181304 [Multi-domain] Cd Length: 70 Bit Score: 43.24 E-value: 1.14e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 498181543 18 GTVGEWHVKEGDEVKEDGDLVQIENDKSVEELPSPVAGKITKILVPEGETAEVGQPLVELE 78
Cdd:PRK08225 10 GNVWKIVVKVGDTVEEGQDVVILESMKMEIPIVAEEAGTVKKINVQEGDFVNEGDVLLEIE 70
|
|
| PRK08225 |
PRK08225 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
131-191 |
1.14e-05 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 181304 [Multi-domain] Cd Length: 70 Bit Score: 43.24 E-value: 1.14e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 498181543 131 GTVGEWHVKEGDEVKEDGDLVQIENDKSVEELPSPVAGKITKILVPEGETAEVGQPLVELE 191
Cdd:PRK08225 10 GNVWKIVVKVGDTVEEGQDVVILESMKMEIPIVAEEAGTVKKINVQEGDFVNEGDVLLEIE 70
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
18-78 |
3.44e-05 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 46.67 E-value: 3.44e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 498181543 18 GTVGEWHVKEGDEVKEdGD-LVQIENDKSVEELPSPVAGKITKILVPEGETAEVGQPLVELE 78
Cdd:PRK12999 1085 GSVVTVLVKEGDEVKA-GDpLAVIEAMKMETTITAPVDGTVKRVLVKAGDQVEAGDLLVELE 1145
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
131-191 |
3.44e-05 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 46.67 E-value: 3.44e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 498181543 131 GTVGEWHVKEGDEVKEdGD-LVQIENDKSVEELPSPVAGKITKILVPEGETAEVGQPLVELE 191
Cdd:PRK12999 1085 GSVVTVLVKEGDEVKA-GDpLAVIEAMKMETTITAPVDGTVKRVLVKAGDQVEAGDLLVELE 1145
|
|
| AcrA |
COG0845 |
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ... |
39-190 |
3.56e-05 |
|
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope biogenesis, Defense mechanisms];
Pssm-ID: 440606 [Multi-domain] Cd Length: 324 Bit Score: 46.09 E-value: 3.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498181543 39 QIENDKSVEeLPSPVAGKITKILVPEGETAEVGQPLVELEVADGKGNVSGeaapekpAQEEKASATAPAGNGNSGTDTYQ 118
Cdd:COG0845 17 TVEARREVE-VRARVSGRVEEVLVDEGDRVKKGQVLARLDPPDLQAALAQ-------AQAQLAAAQAQLELAKAELERYK 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 498181543 119 fNLPDIGeGIAEGTV----GEWHVKEGDEVKEDGDLVQIENDKSVEELPSPVAGKITKILVPEGETAEVGQPLVEL 190
Cdd:COG0845 89 -ALLKKG-AVSQQELdqakAALDQAQAALAAAQAALEQARANLAYTTIRAPFDGVVGERNVEPGQLVSAGTPLFTI 162
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
18-77 |
4.95e-05 |
|
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the Pathway/BioSystem: Urea cycle
Pssm-ID: 440660 [Multi-domain] Cd Length: 1144 Bit Score: 46.23 E-value: 4.95e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 498181543 18 GTVGEWHVKEGDEVKEDGDLVQIENDKSVEELPSPVAGKITKILVPEGETAEVGQPLVEL 77
Cdd:COG1038 1085 GTVVKVLVKEGDEVKKGDPLLTIEAMKMETTITAPRDGTVKEVLVKEGDQVEAGDLLIEL 1144
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
131-190 |
4.95e-05 |
|
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the Pathway/BioSystem: Urea cycle
Pssm-ID: 440660 [Multi-domain] Cd Length: 1144 Bit Score: 46.23 E-value: 4.95e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 498181543 131 GTVGEWHVKEGDEVKEDGDLVQIENDKSVEELPSPVAGKITKILVPEGETAEVGQPLVEL 190
Cdd:COG1038 1085 GTVVKVLVKEGDEVKKGDPLLTIEAMKMETTITAPRDGTVKEVLVKEGDQVEAGDLLIEL 1144
|
|
| PRK06549 |
PRK06549 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
90-188 |
5.72e-05 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235826 [Multi-domain] Cd Length: 130 Bit Score: 42.88 E-value: 5.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498181543 90 AAPEKPAQEEKASATAPAGNGnsGTDTYQFNLPdigegiaeGTVGEWHVKEGDEVKEDGDLVQIENDKSVEELPSPVAGK 169
Cdd:PRK06549 39 PVPTEASPQVEAQAPQPAAAA--GADAMPSPMP--------GTILKVLVAVGDQVTENQPLLILEAMKMENEIVASSAGT 108
|
90
....*....|....*....
gi 498181543 170 ITKILVPEGETAEVGQPLV 188
Cdd:PRK06549 109 VTAIHVTPGQVVNPGDGLI 127
|
|
| PRK14040 |
PRK14040 |
oxaloacetate decarboxylase subunit alpha; |
18-77 |
7.00e-05 |
|
oxaloacetate decarboxylase subunit alpha;
Pssm-ID: 237592 [Multi-domain] Cd Length: 593 Bit Score: 45.69 E-value: 7.00e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 498181543 18 GTVGEWHVKEGDEVKEdGDLVQI-ENDKSVEELPSPVAGKITKILVPEGETAEVGQPLVEL 77
Cdd:PRK14040 533 GNIFKVIVTEGQTVAE-GDVLLIlEAMKMETEIRAAQAGTVRGIAVKEGDAVAVGDTLLTL 592
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
48-79 |
5.05e-04 |
|
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: 38.55 E-value: 5.05e-04
10 20 30
....*....|....*....|....*....|..
gi 498181543 48 ELPSPVAGKITKILVPEGETAEVGQPLVELEV 79
Cdd:cd06850 1 EVTAPMPGTVVKVLVKEGDKVEAGQPLAVLEA 32
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
161-192 |
5.05e-04 |
|
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: 38.55 E-value: 5.05e-04
10 20 30
....*....|....*....|....*....|..
gi 498181543 161 ELPSPVAGKITKILVPEGETAEVGQPLVELEV 192
Cdd:cd06850 1 EVTAPMPGTVVKVLVKEGDKVEAGQPLAVLEA 32
|
|
| PRK07051 |
PRK07051 |
biotin carboxyl carrier domain-containing protein; |
25-78 |
1.10e-03 |
|
biotin carboxyl carrier domain-containing protein;
Pssm-ID: 180811 [Multi-domain] Cd Length: 80 Bit Score: 38.07 E-value: 1.10e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 498181543 25 VKEGDEVKEDGDLVQIENDKSVEELPSPVAGKITKILVPEGETAEVGQPLVELE 78
Cdd:PRK07051 26 VEVGDAVAAGDVVGLIEVMKQFTEVEAEAAGRVVEFLVEDGEPVEAGQVLARIE 79
|
|
| PRK07051 |
PRK07051 |
biotin carboxyl carrier domain-containing protein; |
138-191 |
1.10e-03 |
|
biotin carboxyl carrier domain-containing protein;
Pssm-ID: 180811 [Multi-domain] Cd Length: 80 Bit Score: 38.07 E-value: 1.10e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 498181543 138 VKEGDEVKEDGDLVQIENDKSVEELPSPVAGKITKILVPEGETAEVGQPLVELE 191
Cdd:PRK07051 26 VEVGDAVAAGDVVGLIEVMKQFTEVEAEAAGRVVEFLVEDGEPVEAGQVLARIE 79
|
|
| GCS_H |
cd06848 |
Glycine cleavage H-protein. Glycine cleavage H-proteins are part of the glycine cleavage ... |
26-60 |
1.27e-03 |
|
Glycine cleavage H-protein. Glycine cleavage H-proteins are part of the glycine cleavage system (GCS) found in bacteria, archea and the mitochondria of eukaryotes. GCS is a multienzyme complex consisting of 4 different components (P-, H-, T- and L-proteins) which catalyzes the oxidative cleavage of glycine. The H-protein shuttles the methylamine group of glycine from the P-protein (glycine dehydrogenase) to the T-protein (aminomethyltransferase) via a lipoyl group, attached to a completely conserved lysine residue.
Pssm-ID: 133457 [Multi-domain] Cd Length: 96 Bit Score: 38.28 E-value: 1.27e-03
10 20 30
....*....|....*....|....*....|....*
gi 498181543 26 KEGDEVKEDGDLVQIENDKSVEELPSPVAGKITKI 60
Cdd:cd06848 38 EVGTEVKKGDPFGSVESVKAASDLYSPVSGEVVEV 72
|
|
| GCS_H |
cd06848 |
Glycine cleavage H-protein. Glycine cleavage H-proteins are part of the glycine cleavage ... |
139-173 |
1.27e-03 |
|
Glycine cleavage H-protein. Glycine cleavage H-proteins are part of the glycine cleavage system (GCS) found in bacteria, archea and the mitochondria of eukaryotes. GCS is a multienzyme complex consisting of 4 different components (P-, H-, T- and L-proteins) which catalyzes the oxidative cleavage of glycine. The H-protein shuttles the methylamine group of glycine from the P-protein (glycine dehydrogenase) to the T-protein (aminomethyltransferase) via a lipoyl group, attached to a completely conserved lysine residue.
Pssm-ID: 133457 [Multi-domain] Cd Length: 96 Bit Score: 38.28 E-value: 1.27e-03
10 20 30
....*....|....*....|....*....|....*
gi 498181543 139 KEGDEVKEDGDLVQIENDKSVEELPSPVAGKITKI 173
Cdd:cd06848 38 EVGTEVKKGDPFGSVESVKAASDLYSPVSGEVVEV 72
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
28-230 |
3.25e-03 |
|
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 40.36 E-value: 3.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498181543 28 GDEVKEDGDLVQIENDKSVEELPSPVAGkitkilvpEGETAEVGQPLVELEvADGKGNVSGEAAPEKPAQ---EEKASAT 104
Cdd:TIGR00927 628 GDLSKGDVAEAEHTGERTGEEGERPTEA--------EGENGEESGGEAEQE-GETETKGENESEGEIPAErkgEQEGEGE 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498181543 105 APAGNGNSGTDTYQFNLPDIGEGIAEGTV--GEWHVKEGDEVKEDGDLVQIENDKSVEELPSPVAGKITKILVPEGETAE 182
Cdd:TIGR00927 699 IEAKEADHKGETEAEEVEHEGETEAEGTEdeGEIETGEEGEEVEDEGEGEAEGKHEVETEGDRKETEHEGETEAEGKEDE 778
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 498181543 183 vgqplVELEVAAGK-GNVEGGTTKEAPVAESKETPAANTAAAAPTGEKQ 230
Cdd:TIGR00927 779 -----DEGEIQAGEdGEMKGDEGAEGKVEHEGETEAGEKDEHEGQSETQ 822
|
|
| PRK14042 |
PRK14042 |
pyruvate carboxylase subunit B; Provisional |
18-80 |
4.11e-03 |
|
pyruvate carboxylase subunit B; Provisional
Pssm-ID: 172536 [Multi-domain] Cd Length: 596 Bit Score: 40.09 E-value: 4.11e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 498181543 18 GTVGEWHVKEGDEVKEDGDLVQIENDKSVEELPSPVAGKITKILVPEGETAEVGQPLVELEVA 80
Cdd:PRK14042 534 GSIIAIHVSAGDEVKAGQAVLVIEAMKMETEIKAPANGVVAEILCQKGDKVTPGQVLIRVEVS 596
|
|
| PRK14042 |
PRK14042 |
pyruvate carboxylase subunit B; Provisional |
131-193 |
4.11e-03 |
|
pyruvate carboxylase subunit B; Provisional
Pssm-ID: 172536 [Multi-domain] Cd Length: 596 Bit Score: 40.09 E-value: 4.11e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 498181543 131 GTVGEWHVKEGDEVKEDGDLVQIENDKSVEELPSPVAGKITKILVPEGETAEVGQPLVELEVA 193
Cdd:PRK14042 534 GSIIAIHVSAGDEVKAGQAVLVIEAMKMETEIKAPANGVVAEILCQKGDKVTPGQVLIRVEVS 596
|
|
| |
