|
Name |
Accession |
Description |
Interval |
E-value |
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
1-631 |
0e+00 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 1024.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737230220 1 MAIEINVPDIGADEVEITEILVKVGDKVEAEQSLITVEGDKASMEVPSPQAGIVKEIKVSVGDKTETGKLIMIFDSADGA 80
Cdd:PRK11854 1 MAIEIKVPDIGADEVEVTEILVKVGDKVEAEQSLITVEGDKASMEVPSPQAGVVKEIKVKVGDKVETGALIMIFESADGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737230220 81 AAAAPAQEEKKEAAPAAAPAAAAAAKEVNVPDIGGDEVEVTEILVKVGDTVAAEQSLITVEGDKASMEVPAPFAGTVKEI 160
Cdd:PRK11854 81 ADAAPAQAEEKKEAAPAAAPAAAAAKDVHVPDIGSDEVEVTEILVKVGDTVEAEQSLITVEGDKASMEVPAPFAGTVKEI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737230220 161 KINTGDKVSTGSLIMVFEVAGAAPAAAPAQAAAPAPAAAPAAAGGAKDVNVPDIGGDEVEVTEVMVKVGDKVAAEQSLIT 240
Cdd:PRK11854 161 KVNVGDKVSTGSLIMVFEVAGEAPAAAPAAAEAAAPAAAPAAAAGVKDVNVPDIGGDEVEVTEVMVKVGDKVEAEQSLIT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737230220 241 VEGDKASMEVPAPFAGTVKEIKISTGDKVSTGSLIMVFEVEGAAPAAAPAAAAAPAPAAAPAQAAKPAAAPAAKAE-KSE 319
Cdd:PRK11854 241 VEGDKASMEVPAPFAGTVKEIKVNVGDKVKTGSLIMRFEVEGAAPAAAPAKQEAAAPAPAAAKAEAPAAAPAAKAEgKSE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737230220 320 FAENDAYVHATPLIRRLAREFGVNLAKVKGTGRKGRILREDVQAYVKDAVKRAEAAPAAAAG-GGIPGMLPWPKVDFSKF 398
Cdd:PRK11854 321 FAENDAYVHATPLVRRLAREFGVNLAKVKGTGRKGRILKEDVQAYVKDAVKRAEAAPAAAAAgGGGPGLLPWPKVDFSKF 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737230220 399 GEIEEVELGRIQKISGANLSRNWVMIPHVTHFDKTDITDLEAFRKQQNAEAEKRKLDVKFTPVVFIMKAVAAALEQMPRF 478
Cdd:PRK11854 401 GEIEEVELGRIQKISGANLHRNWVMIPHVTQFDKADITELEAFRKQQNAEAEKRKLGVKITPLVFIMKAVAAALEQMPRF 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737230220 479 NSSLSEDGQKLTLKKYINIGVAVDTPNGLVVPVFKDVNKKSITELSRELTTISKKARDGKLTAGEMQGGCFTISSIGGLG 558
Cdd:PRK11854 481 NSSLSEDGQRLTLKKYVNIGIAVDTPNGLVVPVFKDVNKKGIIELSRELMDISKKARDGKLTAGDMQGGCFTISSIGGLG 560
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1737230220 559 TTHFAPIVNAPEVAILGVSKSAMEPVWNGKEFVPRLMMPISLSFDHRVIDGADGARFITIINNTLSDIRRLVM 631
Cdd:PRK11854 561 TTHFTPIVNAPEVAILGVSKSAMEPVWNGKEFAPRLMLPLSLSYDHRVIDGADGARFITIINDRLSDIRRLVL 633
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
108-631 |
0e+00 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 730.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737230220 108 VNVPDIGG-DEVEVTEILVKVGDTVAAEQSLITVEGDKASMEVPAPFAGTVKEIKINTGDKVSTGSLIMVFEVA------ 180
Cdd:PRK11855 5 FKVPDIGEvVEVEVIEWLVKEGDTVEEDQPLVTVETDKATMEIPSPAAGVVKEIKVKVGDTVSVGGLLAVIEAAgaaaaa 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737230220 181 ---------GAAPAAAPAQAAAPAPAAAPAAAGGAKDVNVPDIGG-DEVEVTEVMVKVGDKVAAEQSLITVEGDKASMEV 250
Cdd:PRK11855 85 aapaaaaapAAAAAAAPAPAAAAPAAAAAAAGGGVVEVKVPDIGEiTEVEVIEWLVKVGDTVEEDQSLITVETDKATMEI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737230220 251 PAPFAGTVKEIKISTGDKVSTGSLIMVFEVEGAAPAAAPAAAAAPAPAAAPAQ--AAKPAAAPAAKAEKSEFAENDAYVH 328
Cdd:PRK11855 165 PSPVAGVVKEIKVKVGDKVSVGSLLVVIEVAAAAPAAAAAPAAAAPAAAAAAApaPAPAAAAAPAAAAPAAAAAPGKAPH 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737230220 329 ATPLIRRLAREFGVNLAKVKGTGRKGRILREDVQAYVKDAVKRAEAAPAAAAGGG--IPGMLPWPKVDFSKFGEIEEVEL 406
Cdd:PRK11855 245 ASPAVRRLARELGVDLSQVKGTGKKGRITKEDVQAFVKGAMSAAAAAAAAAAAAGggGLGLLPWPKVDFSKFGEIETKPL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737230220 407 GRIQKISGANLSRNWVMIPHVTHFDKTDITDLEAFRKQQNAEAEKrkLDVKFTPVVFIMKAVAAALEQMPRFNSSLSEDG 486
Cdd:PRK11855 325 SRIKKISAANLHRSWVTIPHVTQFDEADITDLEALRKQLKKEAEK--AGVKLTMLPFFIKAVVAALKEFPVFNASLDEDG 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737230220 487 QKLTLKKYINIGVAVDTPNGLVVPVFKDVNKKSITELSRELTTISKKARDGKLTAGEMQGGCFTISSIGGLGTTHFAPIV 566
Cdd:PRK11855 403 DELTYKKYFNIGFAVDTPNGLVVPVIKDVDKKSLLEIAREIAELAKKARDGKLKPDDMQGGCFTISSLGGIGGTAFTPII 482
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1737230220 567 NAPEVAILGVSKSAMEPVWNGKEFVPRLMMPISLSFDHRVIDGADGARFITIINNTLSDIRRLVM 631
Cdd:PRK11855 483 NAPEVAILGVGKSQMKPVWDGKEFVPRLMLPLSLSYDHRVIDGATAARFTNYLKQLLADPRRMLL 547
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
110-631 |
0e+00 |
|
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: 708.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737230220 110 VPDIG-GDEVEVTEILVKVGDTVAAEQSLITVEGDKASMEVPAPFAGTVKEIKINTGDKVSTGSLIMVFEVAGAAPAAAP 188
Cdd:TIGR01348 5 VPDIGdNEEGEVIEVLVKPGDKVEAGQSLITLESDKASMEVPSSAAGIIKEIKVKVGDTLPVGGVIATLEVGAGAQAQAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737230220 189 AQAAAPAPAAA--------------PAAAGGAKDVNVPDIGGDE-VEVTEVMVKVGDKVAAEQSLITVEGDKASMEVPAP 253
Cdd:TIGR01348 85 AKKEAAPAPTAgapapaaqaqaapaAGQSSGVQEVTVPDIGDIEkVTVIEVLVKVGDTVSADQSLITLESDKASMEVPAP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737230220 254 FAGTVKEIKISTGDKVSTGSLIMVFEVEGAAPAAAPAAAAAPAPAAAPAQAAKP------AAAPAAKAEKSEFAENDAYV 327
Cdd:TIGR01348 165 ASGVVKSVKVKVGDSVPTGDLILTLSVAGSTPATAPAPASAQPAAQSPAATQPEpaaapaAAKAQAPAPQQAGTQNPAKV 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737230220 328 -HATPLIRRLAREFGVNLAKVKGTGRKGRILREDVQAYVKDAVKRAEAAPAAAAGGGIPgMLPWPKVDFSKFGEIEEVEL 406
Cdd:TIGR01348 245 dHAAPAVRRLAREFGVDLSAVKGTGIKGRILREDVQRFVKEPSVRAQAAAASAAGGAPG-ALPWPNVDFSKFGEVEEVDM 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737230220 407 GRIQKISGANLSRNWVMIPHVTHFDKTDITDLEAFRKQQNAEAEKrkLDVKFTPVVFIMKAVAAALEQMPRFNSSLSEDG 486
Cdd:TIGR01348 324 SRIRKISGANLTRNWTMIPHVTHFDKADITEMEAFRKQQNAAVEK--EGVKLTVLHILMKAVAAALKKFPKFNASLDLGG 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737230220 487 QKLTLKKYINIGVAVDTPNGLVVPVFKDVNKKSITELSRELTTISKKARDGKLTAGEMQGGCFTISSIGGLGTTHFAPIV 566
Cdd:TIGR01348 402 EQLILKKYVNIGVAVDTPNGLLVPVIKDVDRKGITELALELSDLAKKARDGKLTPDEMQGACFTISSLGGIGGTAFTPIV 481
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1737230220 567 NAPEVAILGVSKSAMEPVWNGKEFVPRLMMPISLSFDHRVIDGADGARFITIINNTLSDIRRLVM 631
Cdd:TIGR01348 482 NAPEVAILGVSKSGMEPVWNGKEFEPRLMLPLSLSYDHRVIDGADAARFTTYICESLADIRRLLL 546
|
|
| PRK11856 |
PRK11856 |
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed |
207-631 |
1.95e-139 |
|
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
Pssm-ID: 237001 [Multi-domain] Cd Length: 411 Bit Score: 412.26 E-value: 1.95e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737230220 207 KDVNVPDIG--GDEVEVTEVMVKVGDKVAAEQSLITVEGDKASMEVPAPFAGTVKEIKISTGDKVSTGSLIMVFEVEGAA 284
Cdd:PRK11856 3 FEFKMPDLGegMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDVVPVGSVIAVIEEEGEA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737230220 285 PAAAPAAAAAPAPAAAPAQAAKPAAAPAAKAEKSEFAENDAYVHATPLIRRLAREFGVNLAKVKGTGRKGRILREDVQAY 364
Cdd:PRK11856 83 EAAAAAEAAPEAPAPEPAPAAAAAAAAAPAAAAAPAAPAAAAAKASPAVRKLARELGVDLSTVKGSGPGGRITKEDVEAA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737230220 365 VKDAVKRAEAAPAaaagggipgmlPWPKVDFSKFGEIEEVELGRIQKISGANLSRNWVMIPHVTHFDKTDITDLEAFRKQ 444
Cdd:PRK11856 163 AAAAAPAAAAAAA-----------AAAAPPAAAAEGEERVPLSGMRKAIAKRMVESKREIPHFTLTDEVDVTALLALRKQ 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737230220 445 QNAEAekrkldVKFTPVVFIMKAVAAALEQMPRFNSSLseDGQKLTLKKYINIGVAVDTPNGLVVPVFKDVNKKSITELS 524
Cdd:PRK11856 232 LKAIG------VKLTVTDFLIKAVALALKKFPELNASW--DDDAIVLKKYVNIGIAVATDGGLIVPVIRDADKKSLFELA 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737230220 525 RELTTISKKARDGKLTAGEMQGGCFTISSIGGLGTTHFAPIVNAPEVAILGVSKSAMEPVWNGKEFVPRLMMPISLSFDH 604
Cdd:PRK11856 304 REIKDLAEKAREGKLKPEELQGGTFTISNLGMFGGDYFTPIINPPEVAILGVGAIVERPVVVDGEIVVRKVMPLSLSFDH 383
|
410 420
....*....|....*....|....*..
gi 1737230220 605 RVIDGADGARFITIINNTLSDIRRLVM 631
Cdd:PRK11856 384 RVIDGADAARFLKALKELLENPALLLL 410
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
417-629 |
1.36e-90 |
|
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: 279.43 E-value: 1.36e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737230220 417 LSRNWVMIPHVTHFDKTDITDLEAFRKQQNAEAEKRKldVKFTPVVFIMKAVAAALEQMPRFNSSLSEDGQKLTLKKYIN 496
Cdd:pfam00198 1 MTESKQTIPHFTLTDEVDVTELLALREELKEDAADEE--TKLTFLPFLVKAVALALKKFPELNASWDGEEGEIVYKKYVN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737230220 497 IGVAVDTPNGLVVPVFKDVNKKSITELSRELTTISKKARDGKLTAGEMQGGCFTISSIGGLGTTHFAPIVNAPEVAILGV 576
Cdd:pfam00198 79 IGIAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGV 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1737230220 577 SKSAMEPVWNGKEFVPRLMMPISLSFDHRVIDGADGARFITIINNTLSDIRRL 629
Cdd:pfam00198 159 GRIRKRPVVVDGEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELL 211
|
|
| PRK05704 |
PRK05704 |
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase; |
208-631 |
1.34e-68 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
Pssm-ID: 235571 [Multi-domain] Cd Length: 407 Bit Score: 228.57 E-value: 1.34e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737230220 208 DVNVPDIGgdevE-VTEVMV-----KVGDKVAAEQSLITVEGDKASMEVPAPFAGTVKEIKISTGDKVSTGSLIMVFEVE 281
Cdd:PRK05704 4 EIKVPTLP----EsVTEATIatwhkKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGDTVTVGQVLGRIDEG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737230220 282 GAAPAAAPAAAAAPAPAAAPAQAAKPAaapaakaeksefAENDAYVHATPLIRRLAREFGVNLAKVKGTGRKGRILREDV 361
Cdd:PRK05704 80 AAAGAAAAAAAAAAAAAAAPAQAQAAA------------AAEQSNDALSPAARKLAAENGLDASAVKGTGKGGRVTKEDV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737230220 362 QAYVKDAVKRAEAAPAAAAGGGipgmlpwPKVDFSKfgEIEEVELGRIQKisgaNLSRNWVMIPH----VTHFDKTDITD 437
Cdd:PRK05704 148 LAALAAAAAAPAAPAAAAPAAA-------PAPLGAR--PEERVPMTRLRK----TIAERLLEAQNttamLTTFNEVDMTP 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737230220 438 LEAFRKQQNAEAEKRKlDVKFTPVVFIMKAVAAALEQMPRFNSSLseDGQKLTLKKYINIGVAVDTPNGLVVPVFKDVNK 517
Cdd:PRK05704 215 VMDLRKQYKDAFEKKH-GVKLGFMSFFVKAVVEALKRYPEVNASI--DGDDIVYHNYYDIGIAVGTPRGLVVPVLRDADQ 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737230220 518 KSITELSRELTTISKKARDGKLTAGEMQGGCFTISSIGGLGTTHFAPIVNAPEVAILGVSKSAMEPVWNGKEFVPRLMMP 597
Cdd:PRK05704 292 LSFAEIEKKIAELAKKARDGKLSIEELTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHKIKERPVAVNGQIVIRPMMY 371
|
410 420 430
....*....|....*....|....*....|....
gi 1737230220 598 ISLSFDHRVIDGADGARFITIINNTLSDIRRLVM 631
Cdd:PRK05704 372 LALSYDHRIIDGKEAVGFLVTIKELLEDPERLLL 405
|
|
| sucB |
TIGR01347 |
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ... |
208-631 |
8.35e-68 |
|
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: 226.54 E-value: 8.35e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737230220 208 DVNVPDIGGD--EVEVTEVMVKVGDKVAAEQSLITVEGDKASMEVPAPFAGTVKEIKISTGDKVSTGSLIMVFEVEGAAP 285
Cdd:TIGR01347 2 EIKVPELAESitEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAILEEGNDAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737230220 286 AAAPAAAAAPAPAAAPAQaakpaaapaakaEKSEFAENDAYVHATPLIRRLAREFGVNLAKVKGTGRKGRILREDVqayV 365
Cdd:TIGR01347 82 AAPPAKSGEEKEETPAAS------------AAAAPTAAANRPSLSPAARRLAKEHGIDLSAVPGTGVTGRVTKEDI---I 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737230220 366 KDAVKRAEAAPAAAAGGGIPGmLPWPKVDfskfgeiEEVELGRIQKISGANL---SRNWVMIphvTHFDKTDITDLEAFR 442
Cdd:TIGR01347 147 KKTEAPASAQPPAAAAAAAAP-AAATRPE-------ERVKMTRLRQRIAERLkeaQNSTAML---TTFNEVDMSAVMELR 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737230220 443 KQQNAEAEKrKLDVKFTPVVFIMKAVAAALEQMPRFNSSLseDGQKLTLKKYINIGVAVDTPNGLVVPVFKDVNKKSITE 522
Cdd:TIGR01347 216 KRYKEEFEK-KHGVKLGFMSFFVKAVVAALKRFPEVNAEI--DGDDIVYKDYYDISVAVSTDRGLVVPVVRNADRMSFAD 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737230220 523 LSRELTTISKKARDGKLTAGEMQGGCFTISSIGGLGTTHFAPIVNAPEVAILGVSKSAMEPVWNGKEFVPRLMMPISLSF 602
Cdd:TIGR01347 293 IEKEIADLGKKARDGKLTLEDMTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHGIKERPVAVNGQIEIRPMMYLALSY 372
|
410 420
....*....|....*....|....*....
gi 1737230220 603 DHRVIDGADGARFITIINNTLSDIRRLVM 631
Cdd:TIGR01347 373 DHRLIDGKEAVTFLVTIKELLEDPRRLLL 401
|
|
| SucB_Actino |
TIGR02927 |
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model ... |
108-623 |
6.20e-65 |
|
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: 223.74 E-value: 6.20e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737230220 108 VNVPDIGGDEVE--VTEILVKVGDTVAAEQSLITVEGDKASMEVPAPFAGTVKEIKINTGDKVSTGSLIMVF-------- 177
Cdd:TIGR02927 5 VKMPALGESVTEgtVTSWLKAVGDTVEADEPLLEVSTDKVDTEIPSPAAGVLLEIRAPEDDTVEVGGVLAIIgepgeags 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737230220 178 -------------EVAGAAPAAAPAQAAAPAPAAAPAAAGGAKDVNVPDIGGDEVE--VTEVMVKVGDKVAAEQSLITVE 242
Cdd:TIGR02927 85 epapaapepeaapEPEAPAPAPTPAAEAPAPAAPQAGGSGEATEVKMPELGESVTEgtVTSWLKAVGDTVEVDEPLLEVS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737230220 243 GDKASMEVPAPFAGTVKEIKISTGDKVSTGSLIMVF-----------EVEGAAPAAAPAAAAAPAPAAAPAQAAKPAAAP 311
Cdd:TIGR02927 165 TDKVDTEIPSPVAGTLLEIRAPEDDTVEVGTVLAIIgdanaapaepaEEEAPAPSEAGSEPAPDPAARAPHAAPDPPAPA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737230220 312 AAKAEKSEFAE------NDAYVHATPLIRRLAREFGVNLAKVKGTGRKGRILREDVQAYVK---DAVKRAEAAPAAAAGG 382
Cdd:TIGR02927 245 PAPAKTAAPAAaapvssGDSGPYVTPLVRKLAKDKGVDLSTVKGTGVGGRIRKQDVLAAAKaaeEARAAAAAPAAAAAPA 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737230220 383 GIPGMLPWPKVDFSKF-GEIEEVElgRIQKISGANLSRNWVMIPHVTHFDKTDITDLEAFRKQQNAE-AEKRKLDVKFTP 460
Cdd:TIGR02927 325 APAAAAKPAEPDTAKLrGTTQKMN--RIRQITADKTIESLQTSAQLTQVHEVDMTRVAALRARAKNDfLEKNGVNLTFLP 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737230220 461 vvFIMKAVAAALEQMPRFNSSLSEDGQKLTLKKYINIGVAVDTPNGLVVPVFKDVNKKSITELSRELTTISKKARDGKLT 540
Cdd:TIGR02927 403 --FFVQAVTEALKAHPNVNASYNAETKEVTYHDVEHVGIAVDTPRGLLVPVIHNAGDLSLPGLAKAINDLAARARDNKLK 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737230220 541 AGEMQGGCFTISSIGGLGTTHFAPIVNAPEVAILGVSKSAMEPV-----WNGKEFVPRLMMPISLSFDHRVIDGADGARF 615
Cdd:TIGR02927 481 PDELSGGTFTITNIGSGGALFDTPILNPPQAAILGTGAIVKRPRvikdeDGGESIAIRSVCYLPLTYDHRLVDGADAGRF 560
|
....*...
gi 1737230220 616 ITIINNTL 623
Cdd:TIGR02927 561 LTTIKKRL 568
|
|
| PDHac_trf_mito |
TIGR01349 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
226-617 |
1.73e-60 |
|
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: 208.11 E-value: 1.73e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737230220 226 VKVGDKVAAEQSLITVEGDKASMEVPAPFAGTVKEIKISTGDK-VSTGSLIMVFEVEGAAPAAAPAAAAAPAPAAAPAQA 304
Cdd:TIGR01349 21 KKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEGTKdVPVNKPIAVLVEEKEDVADAFKNYKLESSASPAPKP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737230220 305 AKPAAAPAAKAEKSEFA-----------------ENDAYVHATPLIRRLAREFGVNLAKVKGTGRKGRILREDVQAYVKD 367
Cdd:TIGR01349 101 SEIAPTAPPSAPKPSPApqkqspepsspaplsdkESGDRIFASPLAKKLAKEKGIDLSAVAGSGPNGRIVKKDIESFVPQ 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737230220 368 AVKRAEAAPAAAAGGGIPGMLPWPKvdfskfGEIEEVELGRIQKISGANLSRNWVMIPHVTHFDKTDITDLEAFRKQQNA 447
Cdd:TIGR01349 181 SPASANQQAAATTPATYPAAAPVST------GSYEDVPLSNIRKIIAKRLLESKQTIPHYYVSIECNVDKLLALRKELNA 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737230220 448 EAEKR-KLDVKftpvVFIMKAVAAALEQMPRFNSSLSEDgqklTLKKY--INIGVAVDTPNGLVVPVFKDVNKKSITELS 524
Cdd:TIGR01349 255 MASEVyKLSVN----DFIIKASALALREVPEANSSWTDN----FIRRYknVDISVAVATPDGLITPIVRNADAKGLSTIS 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737230220 525 RELTTISKKARDGKLTAGEMQGGCFTISSIGGLGTTHFAPIVNAPEVAILGVSKSAMEPVWNGKE---FVPRLMMPISLS 601
Cdd:TIGR01349 327 NEIKDLAKRARNNKLKPEEFQGGTFTISNLGMFGIKDFTAIINPPQACILAVGAVEDVAVVDNDEekgFAVASIMSVTLS 406
|
410
....*....|....*.
gi 1737230220 602 FDHRVIDGADGARFIT 617
Cdd:TIGR01349 407 CDHRVIDGAVGAEFLK 422
|
|
| PLN02528 |
PLN02528 |
2-oxoisovalerate dehydrogenase E2 component |
218-615 |
1.59e-58 |
|
2-oxoisovalerate dehydrogenase E2 component
Pssm-ID: 215289 [Multi-domain] Cd Length: 416 Bit Score: 202.26 E-value: 1.59e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737230220 218 EVEVTEVMVKVGDKVAAEQSLITVEGDKASMEVPAPFAGTVKEIKISTGDKVSTGSLIMVFEVEGAAPAAAPAAAAAPAP 297
Cdd:PLN02528 12 ECELLRWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGKVAQINFSPGDIVKVGETLLKIMVEDSQHLRSDSLLLPTDS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737230220 298 AAAPAQAakpaaapaakaEKSEFAENDAYVHATPLIRRLAREFGVNLAKVKGTGRKGRILREDVQAYV--KDAVKRAEAA 375
Cdd:PLN02528 92 SNIVSLA-----------ESDERGSNLSGVLSTPAVRHLAKQYGIDLNDILGTGKDGRVLKEDVLKYAaqKGVVKDSSSA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737230220 376 PAAAAGGGIPGMLPWPKVDFSKFGEieevelgriQKISGANLSRNWV--M-----IPHVTHFDKTDITDLEAFRKQQNae 448
Cdd:PLN02528 161 EEATIAEQEEFSTSVSTPTEQSYED---------KTIPLRGFQRAMVktMtaaakVPHFHYVEEINVDALVELKASFQ-- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737230220 449 AEKRKLDVKFTPVVFIMKAVAAALEQMPRFNSSLSEDGQKLTLKKYINIGVAVDTPNGLVVPVFKDVNKKSITELSRELT 528
Cdd:PLN02528 230 ENNTDPTVKHTFLPFLIKSLSMALSKYPLLNSCFNEETSEIRLKGSHNIGVAMATEHGLVVPNIKNVQSLSLLEITKELS 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737230220 529 TISKKARDGKLTAGEMQGGCFTISSIGGLGTTHFAPIVNAPEVAILGVSKSAMEPVWNGKEFV-PRLMMPISLSFDHRVI 607
Cdd:PLN02528 310 RLQHLAAENKLNPEDITGGTITLSNIGAIGGKFGSPVLNLPEVAIIALGRIQKVPRFVDDGNVyPASIMTVTIGADHRVL 389
|
....*...
gi 1737230220 608 DGADGARF 615
Cdd:PLN02528 390 DGATVARF 397
|
|
| PRK11857 |
PRK11857 |
dihydrolipoamide acetyltransferase; Reviewed |
329-617 |
3.12e-50 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237002 [Multi-domain] Cd Length: 306 Bit Score: 176.52 E-value: 3.12e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737230220 329 ATPLIRRLAREFGVNLAKVKGTGRKGRILREDVQAYVKDAVKRAEAAPAAAAGGGIPGMLPWPKVDFSKFGEIEEVELGR 408
Cdd:PRK11857 4 ATPIARALAKKLGIDISLLKGSGRDGKILAEDVENFIKSLKSAPTPAEAASVSSAQQAAKTAAPAAAPPKLEGKREKVAP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737230220 409 IQKISGANLSRNWVMIPHVTHFDKTDITDLEAFRKQQnAEAEKRKLDVKFTPVVFIMKAVAAALEQMPRFNSSLSEDGQK 488
Cdd:PRK11857 84 IRKAIARAMTNSWSNVAYVNLVNEIDMTKLWDLRKSV-KDPVLKTEGVKLTFLPFIAKAILIALKEFPIFAAKYDEATSE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737230220 489 LTLKKYINIGVAVDTPNGLVVPVFKDVNKKSITELSRELTTISKKARDGKLTAGEMQGGCFTISSIGGLGTTHFAPIVNA 568
Cdd:PRK11857 163 LVYPDTLNLGIAVDTEAGLMVPVIKNAQKLSIVEIAKEISRLAKAARERKIKPDEMKGGSFTITNYGSVGSLYGVPVINY 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1737230220 569 PEVAILGVSKSAMEPVWNGKEFVPRLMMPISLSFDHRVIDGADGARFIT 617
Cdd:PRK11857 243 PELAIAGVGAIIDKAIVKNGQIVAGKVMHLTVAADHRWIDGATIGRFAS 291
|
|
| PTZ00144 |
PTZ00144 |
dihydrolipoamide succinyltransferase; Provisional |
207-631 |
1.86e-48 |
|
dihydrolipoamide succinyltransferase; Provisional
Pssm-ID: 240289 [Multi-domain] Cd Length: 418 Bit Score: 174.87 E-value: 1.86e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737230220 207 KDVNVPDIGGD--EVEVTEVMVKVGDKVAAEQSLITVEGDKASMEVPAPFAGTVKEIKISTGDKVSTGSLIMVFEVEGAA 284
Cdd:PTZ00144 45 KVIKVPTMGDSisEGTVVEWKKKVGDYVKEDEVICIIETDKVSVDIRAPASGVITKIFAEEGDTVEVGAPLSEIDTGGAP 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737230220 285 PAAAPAAAAAPAPAAAPAQAakpaaapaakaEKSEFAENDAYVHATPLIRRLAR-EFGVNLAKVKGTGRKGRILREdvqa 363
Cdd:PTZ00144 125 PAAAPAAAAAAKAEKTTPEK-----------PKAAAPTPEPPAASKPTPPAAAKpPEPAPAAKPPPTPVARADPRE---- 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737230220 364 yvkdavKRaeaapaaaagggipgmlpwpkvdfskfgeieeVELGRIQKISGANL--SRN-WVMIphvTHFDKTDITDLEA 440
Cdd:PTZ00144 190 ------TR--------------------------------VPMSRMRQRIAERLkaSQNtCAML---TTFNECDMSALME 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737230220 441 FRKQQNAEAEKrKLDVKFTPVVFIMKAVAAALEQMPRFNSSLseDGQKLTLKKYINIGVAVDTPNGLVVPVFKDVNKKSI 520
Cdd:PTZ00144 229 LRKEYKDDFQK-KHGVKLGFMSAFVKASTIALKKMPIVNAYI--DGDEIVYRNYVDISVAVATPTGLVVPVIRNCENKSF 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737230220 521 TELSRELTTISKKARDGKLTAGEMQGGCFTISSIGGLGTTHFAPIVNAPEVAILGVSKSAMEPVWNGKEFVPRLMMPISL 600
Cdd:PTZ00144 306 AEIEKELADLAEKARNNKLTLEDMTGGTFTISNGGVFGSLMGTPIINPPQSAILGMHAIKKRPVVVGNEIVIRPIMYLAL 385
|
410 420 430
....*....|....*....|....*....|.
gi 1737230220 601 SFDHRVIDGADGARFITIINNTLSDIRRLVM 631
Cdd:PTZ00144 386 TYDHRLIDGRDAVTFLKKIKDLIEDPARMLL 416
|
|
| PRK14843 |
PRK14843 |
dihydrolipoamide acetyltransferase; Provisional |
316-625 |
1.26e-47 |
|
dihydrolipoamide acetyltransferase; Provisional
Pssm-ID: 184847 [Multi-domain] Cd Length: 347 Bit Score: 170.86 E-value: 1.26e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737230220 316 EKSEFAENDAYVHATPLIRRLAREFGVNLAKVKGTGRKGRILREDVQAYVKDAVKRAEAAPAAAAGGGIPgmLPWPKVdf 395
Cdd:PRK14843 38 EDVETYKDTNVVRISPLAKRIALEHNIAWQEIQGTGHRGKIMKKDVLALLPENIENDSIKSPAQIEKVEE--VPDNVT-- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737230220 396 sKFGEIEEVELGRIQKISGANLSRNWVMIPHVTHFDKTDITDLEAFRKQQnAEAEKRKLDVKFTPVVFIMKAVAAALEQM 475
Cdd:PRK14843 114 -PYGEIERIPMTPMRKVIAQRMVESYLTAPTFTLNYEVDMTEMLALRKKV-LEPIMEATGKKTTVTDLLSLAVVKTLMKH 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737230220 476 PRFNSSLSEDGQKLTLKKYINIGVAVDTPNGLVVPVFKDVNKKSITELSRELTTISKKARDGKLTAGEMQGGCFTISSIG 555
Cdd:PRK14843 192 PYINASLTEDGKTIITHNYVNLAMAVGMDNGLMTPVVYNAEKMSLSELVVAFKDVIGRTLDGKLAPSELQNSTFTISNLG 271
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737230220 556 GLGTTHFAPIVNAPEVAILGVSKSAMEPVWNGKEFVPRLMMPISLSFDHRVIDGADGARFITIINNTLSD 625
Cdd:PRK14843 272 MFGVQSFGPIINQPNSAILGVSSTIEKPVVVNGEIVIRPIMSLGLTIDHRVVDGMAGAKFMKDLKELIET 341
|
|
| PLN02744 |
PLN02744 |
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex |
227-616 |
1.43e-44 |
|
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
Pssm-ID: 215397 [Multi-domain] Cd Length: 539 Bit Score: 166.95 E-value: 1.43e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737230220 227 KVGDKVAAEQSLITVEGDKASMEVPAPFAGTVKEIKISTGDK-VSTGSLIMV-FEVEGAAPAAAPAAAAAPAPAAAPAQA 304
Cdd:PLN02744 135 KEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVKGDGAKeIKVGEVIAItVEEEEDIGKFKDYKPSSSAAPAAPKAK 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737230220 305 AKPAAAPAAKAEK------------SEFAENDAYVHATPLIRRLAREFGVNLAKVKGTGRKGRILREDVQAYVKDAVKRA 372
Cdd:PLN02744 215 PSPPPPKEEEVEKpasspepkaskpSAPPSSGDRIFASPLARKLAEDNNVPLSSIKGTGPDGRIVKADIEDYLASGGKGA 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737230220 373 EAAPAAAAgggipgmlPWPKVDFSkfgeieEVELGRIQKISGANLSRNWVMIPHVTHFDKTDITDLEAFRKQQNA--EAE 450
Cdd:PLN02744 295 TAPPSTDS--------KAPALDYT------DIPNTQIRKVTASRLLQSKQTIPHYYLTVDTRVDKLMALRSQLNSlqEAS 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737230220 451 KRKldvKFTPVVFIMKAVAAALEQMPRFNSSLSEDgqklTLKKY--INIGVAVDTPNGLVVPVFKDVNKKSITELSRELT 528
Cdd:PLN02744 361 GGK---KISVNDLVIKAAALALRKVPQCNSSWTDD----YIRQYhnVNINVAVQTENGLYVPVVKDADKKGLSTIAEEVK 433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737230220 529 TISKKARDGKLTAGEMQGGCFTISSIGG-LGTTHFAPIVNAPEVAILGVSkSAMEPVWNGK---EFVPRLMMPISLSFDH 604
Cdd:PLN02744 434 QLAQKARENSLKPEDYEGGTFTVSNLGGpFGIKQFCAIINPPQSAILAVG-SAEKRVIPGSgpdQYNFASFMSVTLSCDH 512
|
410
....*....|..
gi 1737230220 605 RVIDGADGARFI 616
Cdd:PLN02744 513 RVIDGAIGAEWL 524
|
|
| PLN02226 |
PLN02226 |
2-oxoglutarate dehydrogenase E2 component |
227-631 |
2.54e-36 |
|
2-oxoglutarate dehydrogenase E2 component
Pssm-ID: 177871 [Multi-domain] Cd Length: 463 Bit Score: 141.82 E-value: 2.54e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737230220 227 KVGDKVAAEQSLITVEGDKASMEVPAPFAGTVKEIKISTGDKVSTGSLIMVFEvEGAAPAAAPAAAAAPAPAAAPAQAAK 306
Cdd:PLN02226 114 KPGERVQADEAIAQIETDKVTIDIASPASGVIQEFLVKEGDTVEPGTKVAIIS-KSEDAASQVTPSQKIPETTDPKPSPP 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737230220 307 PAAAPAAKAEKSEFAENDAYVHATPLIRRLAREfgvnlakvkgtgrkgrilredVQAYVKDAVKRaeaapaaaagggipg 386
Cdd:PLN02226 193 AEDKQKPKVESAPVAEKPKAPSSPPPPKQSAKE---------------------PQLPPKERERR--------------- 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737230220 387 mlpwpkvdfskfgeieeVELGRIQKISGANLSRNWVMIPHVTHFDKTDITDLEAFRKQQNaEAEKRKLDVKFTPVVFIMK 466
Cdd:PLN02226 237 -----------------VPMTRLRKRVATRLKDSQNTFALLTTFNEVDMTNLMKLRSQYK-DAFYEKHGVKLGLMSGFIK 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737230220 467 AVAAALEQMPRFNSSLseDGQKLTLKKYINIGVAVDTPNGLVVPVFKDVNKKSITELSRELTTISKKARDGKLTAGEMQG 546
Cdd:PLN02226 299 AAVSALQHQPVVNAVI--DGDDIIYRDYVDISIAVGTSKGLVVPVIRGADKMNFAEIEKTINGLAKKANEGTISIDEMAG 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737230220 547 GCFTISSIGGLGTTHFAPIVNAPEVAILGVSKSAMEPVWNGKEFVPRLMMPISLSFDHRVIDGADGARFITIINNTLSDI 626
Cdd:PLN02226 377 GSFTVSNGGVYGSLISTPIINPPQSAILGMHSIVSRPMVVGGSVVPRPMMYVALTYDHRLIDGREAVYFLRRVKDVVEDP 456
|
....*
gi 1737230220 627 RRLVM 631
Cdd:PLN02226 457 QRLLL 461
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
1-74 |
8.94e-23 |
|
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: 92.05 E-value: 8.94e-23
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1737230220 1 MAIEINVPDIG--ADEVEITEILVKVGDKVEAEQSLITVEGDKASMEVPSPQAGIVKEIKVSVGDKTETGKLIMIF 74
Cdd:COG0508 1 MAIEIKMPDLGesMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
2-81 |
8.98e-23 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 102.59 E-value: 8.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737230220 2 AIEINVPDIG-ADEVEITEILVKVGDKVEAEQSLITVEGDKASMEVPSPQAGIVKEIKVSVGDKTETGKLIMIFD----- 75
Cdd:PRK11855 119 VVEVKVPDIGeITEVEVIEWLVKVGDTVEEDQSLITVETDKATMEIPSPVAGVVKEIKVKVGDKVSVGSLLVVIEvaaaa 198
|
90 100 110
....*....|....*....|....*....|.
gi 1737230220 76 -------------------------SADGAA 81
Cdd:PRK11855 199 paaaaapaaaapaaaaaaapapapaAAAAPA 229
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
108-177 |
2.36e-21 |
|
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: 88.20 E-value: 2.36e-21
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1737230220 108 VNVPDIG--GDEVEVTEILVKVGDTVAAEQSLITVEGDKASMEVPAPFAGTVKEIKINTGDKVSTGSLIMVF 177
Cdd:COG0508 5 IKMPDLGesMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
207-278 |
3.35e-21 |
|
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: 87.81 E-value: 3.35e-21
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1737230220 207 KDVNVPDIG--GDEVEVTEVMVKVGDKVAAEQSLITVEGDKASMEVPAPFAGTVKEIKISTGDKVSTGSLIMVF 278
Cdd:COG0508 3 IEIKMPDLGesMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
3-74 |
1.03e-19 |
|
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: 83.61 E-value: 1.03e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1737230220 3 IEINVPDIGAD--EVEITEILVKVGDKVEAEQSLITVEGDKASMEVPSPQAGIVKEIKVSVGDKTETGKLIMIF 74
Cdd:cd06849 1 TEIKMPDLGESmtEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
207-278 |
1.86e-19 |
|
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: 82.65 E-value: 1.86e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1737230220 207 KDVNVPDIGGDEVE-VTEVMVKVGDKVAAEQSLITVEGDKASMEVPAPFAGTVKEIKISTGDKVSTGSLIMVF 278
Cdd:pfam00364 1 TEIKSPMIGESVREgVVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
4-74 |
2.24e-19 |
|
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: 82.65 E-value: 2.24e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1737230220 4 EINVPDIGADEVE-ITEILVKVGDKVEAEQSLITVEGDKASMEVPSPQAGIVKEIKVSVGDKTETGKLIMIF 74
Cdd:pfam00364 2 EIKSPMIGESVREgVVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
108-177 |
4.87e-19 |
|
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: 81.68 E-value: 4.87e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1737230220 108 VNVPDIGGD--EVEVTEILVKVGDTVAAEQSLITVEGDKASMEVPAPFAGTVKEIKINTGDKVSTGSLIMVF 177
Cdd:cd06849 3 IKMPDLGESmtEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
207-278 |
6.21e-19 |
|
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: 81.30 E-value: 6.21e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1737230220 207 KDVNVPDIGGD--EVEVTEVMVKVGDKVAAEQSLITVEGDKASMEVPAPFAGTVKEIKISTGDKVSTGSLIMVF 278
Cdd:cd06849 1 TEIKMPDLGESmtEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
108-177 |
8.68e-19 |
|
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: 80.72 E-value: 8.68e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1737230220 108 VNVPDIGGDEVE-VTEILVKVGDTVAAEQSLITVEGDKASMEVPAPFAGTVKEIKINTGDKVSTGSLIMVF 177
Cdd:pfam00364 3 IKSPMIGESVREgVVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
|
|
| kgd |
PRK12270 |
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ... |
467-623 |
1.99e-15 |
|
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;
Pssm-ID: 237030 [Multi-domain] Cd Length: 1228 Bit Score: 80.32 E-value: 1.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737230220 467 AVAAALEQMPRFNSSLSEDGQKLTLKK--YINIGVAVDT--PNG---LVVPVFKDVNKKSITELSRELTTISKKARDGKL 539
Cdd:PRK12270 179 ALVQALKAFPNMNRHYAEVDGKPTLVTpaHVNLGLAIDLpkKDGsrqLVVPAIKGAETMDFAQFWAAYEDIVRRARDGKL 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737230220 540 TAGEMQGGCFTISSIGGLGTTHFAPIVNAPEVAILGVskSAME-PV-WNG--KEFVPRL----MMPISLSFDHRVIDGAD 611
Cdd:PRK12270 259 TADDFQGTTISLTNPGGIGTVHSVPRLMKGQGAIIGV--GAMEyPAeFQGasEERLAELgiskVMTLTSTYDHRIIQGAE 336
|
170
....*....|..
gi 1737230220 612 GARFITIINNTL 623
Cdd:PRK12270 337 SGEFLRTIHQLL 348
|
|
| E3_binding |
pfam02817 |
e3 binding domain; This family represents a small domain of the E2 subunit of 2-oxo-acid ... |
327-362 |
3.18e-14 |
|
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: 66.56 E-value: 3.18e-14
10 20 30
....*....|....*....|....*....|....*.
gi 1737230220 327 VHATPLIRRLAREFGVNLAKVKGTGRKGRILREDVQ 362
Cdd:pfam02817 1 VLASPAARKLARELGIDLSDVKGTGPGGRITKEDVE 36
|
|
| PRK05704 |
PRK05704 |
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase; |
1-75 |
1.88e-11 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
Pssm-ID: 235571 [Multi-domain] Cd Length: 407 Bit Score: 66.40 E-value: 1.88e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1737230220 1 MAIEINVPDIGAD--EVEITEILVKVGDKVEAEQSLITVEGDKASMEVPSPQAGIVKEIKVSVGDKTETGKLIMIFD 75
Cdd:PRK05704 1 MMVEIKVPTLPESvtEATIATWHKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGDTVTVGQVLGRID 77
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
221-278 |
6.62e-11 |
|
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: 65.49 E-value: 6.62e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737230220 221 VTEVMVKVGDKVAAEQSLITVEGDKasME--VPAPFAGTVKEIKISTGDKVSTGSLIMVF 278
Cdd:COG1038 1087 VVKVLVKEGDEVKKGDPLLTIEAMK--MEttITAPRDGTVKEVLVKEGDQVEAGDLLIEL 1144
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
120-177 |
1.18e-10 |
|
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: 1.18e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1737230220 120 VTEILVKVGDTVAAEQSLITVEGDKASMEVPAPFAGTVKEIKINTGDKVSTGSLIMVF 177
Cdd:cd06850 10 VVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
221-279 |
1.84e-10 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 64.39 E-value: 1.84e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1737230220 221 VTEVMVKVGDKVAAEQSLITVEGDKasME--VPAPFAGTVKEIKISTGDKVSTGSLIMVFE 279
Cdd:PRK12999 1087 VVTVLVKEGDEVKAGDPLAVIEAMK--MEttITAPVDGTVKRVLVKAGDQVEAGDLLVELE 1145
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
120-177 |
1.87e-10 |
|
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: 64.33 E-value: 1.87e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737230220 120 VTEILVKVGDTVAAEQSLITVEGDKasME--VPAPFAGTVKEIKINTGDKVSTGSLIMVF 177
Cdd:COG1038 1087 VVKVLVKEGDEVKKGDPLLTIEAMK--MEttITAPRDGTVKEVLVKEGDQVEAGDLLIEL 1144
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
221-278 |
1.88e-10 |
|
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: 57.04 E-value: 1.88e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1737230220 221 VTEVMVKVGDKVAAEQSLITVEGDKASMEVPAPFAGTVKEIKISTGDKVSTGSLIMVF 278
Cdd:cd06850 10 VVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
120-178 |
4.68e-10 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 62.85 E-value: 4.68e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1737230220 120 VTEILVKVGDTVAAEQSLITVEGDKasME--VPAPFAGTVKEIKINTGDKVSTGSLIMVFE 178
Cdd:PRK12999 1087 VVTVLVKEGDEVKAGDPLAVIEAMK--MEttITAPVDGTVKRVLVKAGDQVEAGDLLVELE 1145
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
17-74 |
6.91e-10 |
|
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: 55.11 E-value: 6.91e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1737230220 17 ITEILVKVGDKVEAEQSLITVEGDKASMEVPSPQAGIVKEIKVSVGDKTETGKLIMIF 74
Cdd:cd06850 10 VVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| PRK09282 |
PRK09282 |
pyruvate carboxylase subunit B; Validated |
221-279 |
1.56e-09 |
|
pyruvate carboxylase subunit B; Validated
Pssm-ID: 236449 [Multi-domain] Cd Length: 592 Bit Score: 60.63 E-value: 1.56e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1737230220 221 VTEVMVKVGDKVAAEQSLITVEGDKASMEVPAPFAGTVKEIKISTGDKVSTGSLIMVFE 279
Cdd:PRK09282 533 VVKVKVKEGDKVKAGDTVLVLEAMKMENEIQAPVDGTVKEILVKEGDRVNPGDVLMEIE 591
|
|
| PRK09282 |
PRK09282 |
pyruvate carboxylase subunit B; Validated |
120-178 |
2.05e-09 |
|
pyruvate carboxylase subunit B; Validated
Pssm-ID: 236449 [Multi-domain] Cd Length: 592 Bit Score: 60.24 E-value: 2.05e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1737230220 120 VTEILVKVGDTVAAEQSLITVEGDKASMEVPAPFAGTVKEIKINTGDKVSTGSLIMVFE 178
Cdd:PRK09282 533 VVKVKVKEGDKVKAGDTVLVLEAMKMENEIQAPVDGTVKEILVKEGDRVNPGDVLMEIE 591
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
221-356 |
5.07e-09 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 58.42 E-value: 5.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737230220 221 VTEVMVKVGDKVAAEQSLITVEGDKASMEVPAPFAGTVKEIKISTGDKVSTGSLIMVFEVEgaapaaapaaaaapapaaa 300
Cdd:PRK14875 19 VAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGETLPVGALLAVVADA------------------- 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1737230220 301 paqaakpaaapaakaEKSEfAENDAYVhaTPLIRRLAREfGVNLAKVKGTGRKGRI 356
Cdd:PRK14875 80 ---------------EVSD-AEIDAFI--APFARRFAPE-GIDEEDAGPAPRKARI 116
|
|
| sucB |
TIGR01347 |
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ... |
3-73 |
5.19e-09 |
|
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: 58.59 E-value: 5.19e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1737230220 3 IEINVPDIGAD--EVEITEILVKVGDKVEAEQSLITVEGDKASMEVPSPQAGIVKEIKVSVGDKTETGKLIMI 73
Cdd:TIGR01347 1 IEIKVPELAESitEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAI 73
|
|
| PRK09282 |
PRK09282 |
pyruvate carboxylase subunit B; Validated |
17-73 |
8.41e-09 |
|
pyruvate carboxylase subunit B; Validated
Pssm-ID: 236449 [Multi-domain] Cd Length: 592 Bit Score: 58.32 E-value: 8.41e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1737230220 17 ITEILVKVGDKVEAEQSLITVEGDKASMEVPSPQAGIVKEIKVSVGDKTETGKLIMI 73
Cdd:PRK09282 533 VVKVKVKEGDKVKAGDTVLVLEAMKMENEIQAPVDGTVKEILVKEGDRVNPGDVLME 589
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
17-74 |
9.43e-09 |
|
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: 58.55 E-value: 9.43e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737230220 17 ITEILVKVGDKVEAEQSLITVEGDKasME--VPSPQAGIVKEIKVSVGDKTETGKLIMIF 74
Cdd:COG1038 1087 VVKVLVKEGDEVKKGDPLLTIEAMK--MEttITAPRDGTVKEVLVKEGDQVEAGDLLIEL 1144
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
120-176 |
1.52e-07 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 53.79 E-value: 1.52e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1737230220 120 VTEILVKVGDTVAAEQSLITVEGDKASMEVPAPFAGTVKEIKINTGDKVSTGSLIMV 176
Cdd:PRK14875 19 VAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGETLPVGALLAV 75
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
17-74 |
2.94e-07 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 53.99 E-value: 2.94e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737230220 17 ITEILVKVGDKVEAEQSLITVEGDKasME--VPSPQAGIVKEIKVSVGDKTETGKLIMIF 74
Cdd:PRK12999 1087 VVTVLVKEGDEVKAGDPLAVIEAMK--MEttITAPVDGTVKRVLVKAGDQVEAGDLLVEL 1144
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
1-71 |
2.98e-07 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 53.02 E-value: 2.98e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1737230220 1 MAIEINVPDIGAD--EVEITEILVKVGDKVEAEQSLITVEGDKASMEVPSPQAGIVKEIKVSVGDKTETGKLI 71
Cdd:PRK14875 1 SITPITMPKWGLSmtEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGETLPVGALL 73
|
|
| PRK05641 |
PRK05641 |
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
16-69 |
5.24e-07 |
|
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235540 [Multi-domain] Cd Length: 153 Bit Score: 49.48 E-value: 5.24e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1737230220 16 EITEILVKVGDKVEAEQSLITVEGDKASMEVPSPQAGIVKEIKVSVGDKTETGK 69
Cdd:PRK05641 94 KILRILVREGQQVKVGQGLLILEAMKMENEIPAPKDGVVKKILVKEGDTVDTGQ 147
|
|
| AccB |
COG0511 |
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ... |
122-178 |
1.47e-06 |
|
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: 47.97 E-value: 1.47e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1737230220 122 EILVKVGDTVAAEQSLITVEGDKASMEVPAPFAGTVKEIKINTGDKVSTGSLIMVFE 178
Cdd:COG0511 80 KPFVKVGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVVEILVENGQPVEYGQPLFVIE 136
|
|
| PTZ00144 |
PTZ00144 |
dihydrolipoamide succinyltransferase; Provisional |
5-75 |
1.50e-06 |
|
dihydrolipoamide succinyltransferase; Provisional
Pssm-ID: 240289 [Multi-domain] Cd Length: 418 Bit Score: 50.84 E-value: 1.50e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1737230220 5 INVPDIGAD--EVEITEILVKVGDKVEAEQSLITVEGDKASMEVPSPQAGIVKEIKVSVGDKTETGKLIMIFD 75
Cdd:PTZ00144 47 IKVPTMGDSisEGTVVEWKKKVGDYVKEDEVICIIETDKVSVDIRAPASGVITKIFAEEGDTVEVGAPLSEID 119
|
|
| AccB |
COG0511 |
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ... |
223-279 |
1.65e-06 |
|
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: 47.58 E-value: 1.65e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1737230220 223 EVMVKVGDKVAAEQSLITVEGDKASMEVPAPFAGTVKEIKISTGDKVSTGSLIMVFE 279
Cdd:COG0511 80 KPFVKVGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVVEILVENGQPVEYGQPLFVIE 136
|
|
| PRK05641 |
PRK05641 |
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
119-171 |
2.35e-06 |
|
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235540 [Multi-domain] Cd Length: 153 Bit Score: 47.93 E-value: 2.35e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1737230220 119 EVTEILVKVGDTVAAEQSLITVEGDKASMEVPAPFAGTVKEIKINTGDKVSTG 171
Cdd:PRK05641 94 KILRILVREGQQVKVGQGLLILEAMKMENEIPAPKDGVVKKILVKEGDTVDTG 146
|
|
| PRK05641 |
PRK05641 |
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
220-272 |
4.01e-06 |
|
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235540 [Multi-domain] Cd Length: 153 Bit Score: 47.16 E-value: 4.01e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1737230220 220 EVTEVMVKVGDKVAAEQSLITVEGDKASMEVPAPFAGTVKEIKISTGDKVSTG 272
Cdd:PRK05641 94 KILRILVREGQQVKVGQGLLILEAMKMENEIPAPKDGVVKKILVKEGDTVDTG 146
|
|
| AccB |
COG0511 |
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ... |
19-75 |
6.45e-06 |
|
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: 46.04 E-value: 6.45e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1737230220 19 EILVKVGDKVEAEQSLITVEGDKASMEVPSPQAGIVKEIKVSVGDKTETGKLIMIFD 75
Cdd:COG0511 80 KPFVKVGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVVEILVENGQPVEYGQPLFVIE 136
|
|
| PRK14040 |
PRK14040 |
oxaloacetate decarboxylase subunit alpha; |
224-276 |
1.05e-05 |
|
oxaloacetate decarboxylase subunit alpha;
Pssm-ID: 237592 [Multi-domain] Cd Length: 593 Bit Score: 48.39 E-value: 1.05e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1737230220 224 VMVKVGDKVAAEQSLITVEGDKASMEVPAPFAGTVKEIKISTGDKVSTGSLIM 276
Cdd:PRK14040 538 VIVTEGQTVAEGDVLLILEAMKMETEIRAAQAGTVRGIAVKEGDAVAVGDTLL 590
|
|
| PLN02226 |
PLN02226 |
2-oxoglutarate dehydrogenase E2 component |
3-73 |
1.13e-05 |
|
2-oxoglutarate dehydrogenase E2 component
Pssm-ID: 177871 [Multi-domain] Cd Length: 463 Bit Score: 48.21 E-value: 1.13e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1737230220 3 IEINVPDIGADEVE--ITEILVKVGDKVEAEQSLITVEGDKASMEVPSPQAGIVKEIKVSVGDKTETGKLIMI 73
Cdd:PLN02226 92 VEAVVPHMGESITDgtLATFLKKPGERVQADEAIAQIETDKVTIDIASPASGVIQEFLVKEGDTVEPGTKVAI 164
|
|
| PRK08225 |
PRK08225 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
120-178 |
1.71e-05 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 181304 [Multi-domain] Cd Length: 70 Bit Score: 42.85 E-value: 1.71e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1737230220 120 VTEILVKVGDTVAAEQSLITVEGDKasMEVP--APFAGTVKEIKINTGDKVSTGSLIMVFE 178
Cdd:PRK08225 12 VWKIVVKVGDTVEEGQDVVILESMK--MEIPivAEEAGTVKKINVQEGDFVNEGDVLLEIE 70
|
|
| GcvH |
COG0509 |
Glycine cleavage system protein H (lipoate-binding) [Amino acid transport and metabolism]; ... |
115-160 |
1.93e-05 |
|
Glycine cleavage system protein H (lipoate-binding) [Amino acid transport and metabolism]; Glycine cleavage system protein H (lipoate-binding) is part of the Pathway/BioSystem: Glycine cleavage
Pssm-ID: 440275 Cd Length: 128 Bit Score: 44.34 E-value: 1.93e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1737230220 115 GDEVEVTeiLVKVGDTVAAEQSLITVEGDKASMEVPAPFAGTVKEI 160
Cdd:COG0509 37 GDIVFVE--LPEVGTEVEAGEPFGVVESVKAVSDLYAPVSGEVVEV 80
|
|
| PRK14040 |
PRK14040 |
oxaloacetate decarboxylase subunit alpha; |
123-175 |
1.93e-05 |
|
oxaloacetate decarboxylase subunit alpha;
Pssm-ID: 237592 [Multi-domain] Cd Length: 593 Bit Score: 47.62 E-value: 1.93e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1737230220 123 ILVKVGDTVAAEQSLITVEGDKASMEVPAPFAGTVKEIKINTGDKVSTGSLIM 175
Cdd:PRK14040 538 VIVTEGQTVAEGDVLLILEAMKMETEIRAAQAGTVRGIAVKEGDAVAVGDTLL 590
|
|
| GCS_H |
cd06848 |
Glycine cleavage H-protein. Glycine cleavage H-proteins are part of the glycine cleavage ... |
115-164 |
1.98e-05 |
|
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: 43.68 E-value: 1.98e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1737230220 115 GDEVEVTeiLVKVGDTVAAEQSLITVEGDKASMEVPAPFAGTVkeIKINT 164
Cdd:cd06848 29 GDIVFVE--LPEVGTEVKKGDPFGSVESVKAASDLYSPVSGEV--VEVNE 74
|
|
| PRK06549 |
PRK06549 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
120-171 |
2.73e-05 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235826 [Multi-domain] Cd Length: 130 Bit Score: 44.03 E-value: 2.73e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1737230220 120 VTEILVKVGDTVAAEQSLITVEGDKASMEVPAPFAGTVKEIKINTGDKVSTG 171
Cdd:PRK06549 72 ILKVLVAVGDQVTENQPLLILEAMKMENEIVASSAGTVTAIHVTPGQVVNPG 123
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
14-74 |
3.10e-05 |
|
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: 42.43 E-value: 3.10e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1737230220 14 EVEITEILVKVGDKVEAEQSLITVEGDKASMEVPSPQAGIVKEIKVSVGDKTETGKLIMIF 74
Cdd:cd06663 13 DGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKVEGDTPLVKI 73
|
|
| PRK14042 |
PRK14042 |
pyruvate carboxylase subunit B; Provisional |
221-280 |
3.45e-05 |
|
pyruvate carboxylase subunit B; Provisional
Pssm-ID: 172536 [Multi-domain] Cd Length: 596 Bit Score: 47.02 E-value: 3.45e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737230220 221 VTEVMVKVGDKVAAEQSLITVEGDKASMEVPAPFAGTVKEIKISTGDKVSTGSLIMVFEV 280
Cdd:PRK14042 536 IIAIHVSAGDEVKAGQAVLVIEAMKMETEIKAPANGVVAEILCQKGDKVTPGQVLIRVEV 595
|
|
| PRK14042 |
PRK14042 |
pyruvate carboxylase subunit B; Provisional |
120-179 |
5.16e-05 |
|
pyruvate carboxylase subunit B; Provisional
Pssm-ID: 172536 [Multi-domain] Cd Length: 596 Bit Score: 46.25 E-value: 5.16e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737230220 120 VTEILVKVGDTVAAEQSLITVEGDKASMEVPAPFAGTVKEIKINTGDKVSTGSLIMVFEV 179
Cdd:PRK14042 536 IIAIHVSAGDEVKAGQAVLVIEAMKMETEIKAPANGVVAEILCQKGDKVTPGQVLIRVEV 595
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
117-168 |
5.64e-05 |
|
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: 41.66 E-value: 5.64e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1737230220 117 EVEVTEILVKVGDTVAAEQSLITVEGDKASMEVPAPFAGTVKEIKINTGDKV 168
Cdd:cd06663 13 DGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKV 64
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
208-269 |
6.46e-05 |
|
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: 41.27 E-value: 6.46e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1737230220 208 DVNVPDIGGDEVEVT--EVMVKVGDKVAAEQSLITVEGDKASMEVPAPFAGTVKEIKISTGDKV 269
Cdd:cd06663 1 TILIPDLAQHLGDGTvvKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKV 64
|
|
| PRK08225 |
PRK08225 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
221-279 |
6.77e-05 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 181304 [Multi-domain] Cd Length: 70 Bit Score: 41.31 E-value: 6.77e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1737230220 221 VTEVMVKVGDKVAAEQSLITVEGDKasMEVP--APFAGTVKEIKISTGDKVSTGSLIMVFE 279
Cdd:PRK08225 12 VWKIVVKVGDTVEEGQDVVILESMK--MEIPivAEEAGTVKKINVQEGDFVNEGDVLLEIE 70
|
|
| GCS_H |
cd06848 |
Glycine cleavage H-protein. Glycine cleavage H-proteins are part of the glycine cleavage ... |
227-261 |
7.32e-05 |
|
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: 42.14 E-value: 7.32e-05
10 20 30
....*....|....*....|....*....|....*
gi 1737230220 227 KVGDKVAAEQSLITVEGDKASMEVPAPFAGTVKEI 261
Cdd:cd06848 38 EVGTEVKKGDPFGSVESVKAASDLYSPVSGEVVEV 72
|
|
| PRK08225 |
PRK08225 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
20-73 |
7.84e-05 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 181304 [Multi-domain] Cd Length: 70 Bit Score: 41.31 E-value: 7.84e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1737230220 20 ILVKVGDKVEAEQSLITVEGDKasMEVP--SPQAGIVKEIKVSVGDKTETGKLIMI 73
Cdd:PRK08225 15 IVVKVGDTVEEGQDVVILESMK--MEIPivAEEAGTVKKINVQEGDFVNEGDVLLE 68
|
|
| GcvH |
COG0509 |
Glycine cleavage system protein H (lipoate-binding) [Amino acid transport and metabolism]; ... |
216-261 |
1.41e-04 |
|
Glycine cleavage system protein H (lipoate-binding) [Amino acid transport and metabolism]; Glycine cleavage system protein H (lipoate-binding) is part of the Pathway/BioSystem: Glycine cleavage
Pssm-ID: 440275 Cd Length: 128 Bit Score: 42.03 E-value: 1.41e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1737230220 216 GDEVEVTevMVKVGDKVAAEQSLITVEGDKASMEVPAPFAGTVKEI 261
Cdd:COG0509 37 GDIVFVE--LPEVGTEVEAGEPFGVVESVKAVSDLYAPVSGEVVEV 80
|
|
| PRK14042 |
PRK14042 |
pyruvate carboxylase subunit B; Provisional |
17-72 |
2.60e-04 |
|
pyruvate carboxylase subunit B; Provisional
Pssm-ID: 172536 [Multi-domain] Cd Length: 596 Bit Score: 43.94 E-value: 2.60e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1737230220 17 ITEILVKVGDKVEAEQSLITVEGDKASMEVPSPQAGIVKEIKVSVGDKTETGKLIM 72
Cdd:PRK14042 536 IIAIHVSAGDEVKAGQAVLVIEAMKMETEIKAPANGVVAEILCQKGDKVTPGQVLI 591
|
|
| PLN02528 |
PLN02528 |
2-oxoisovalerate dehydrogenase E2 component |
11-72 |
2.95e-04 |
|
2-oxoisovalerate dehydrogenase E2 component
Pssm-ID: 215289 [Multi-domain] Cd Length: 416 Bit Score: 43.55 E-value: 2.95e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1737230220 11 GADEVEITEILVKVGDKVEAEQSLITVEGDKASMEVPSPQAGIVKEIKVSVGDKTETGKLIM 72
Cdd:PLN02528 9 GIAECELLRWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGKVAQINFSPGDIVKVGETLL 70
|
|
| PRK14040 |
PRK14040 |
oxaloacetate decarboxylase subunit alpha; |
17-72 |
3.43e-04 |
|
oxaloacetate decarboxylase subunit alpha;
Pssm-ID: 237592 [Multi-domain] Cd Length: 593 Bit Score: 43.77 E-value: 3.43e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1737230220 17 ITEILVKVGDKVEAEQSLITVEGDKASMEVPSPQAGIVKEIKVSVGDKTETGKLIM 72
Cdd:PRK14040 535 IFKVIVTEGQTVAEGDVLLILEAMKMETEIRAAQAGTVRGIAVKEGDAVAVGDTLL 590
|
|
| PRK06549 |
PRK06549 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
17-73 |
4.99e-04 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235826 [Multi-domain] Cd Length: 130 Bit Score: 40.57 E-value: 4.99e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1737230220 17 ITEILVKVGDKVEAEQSLITVEGDKASMEVPSPQAGIVKEIKVSVGDKTETGK-LIMI 73
Cdd:PRK06549 72 ILKVLVAVGDQVTENQPLLILEAMKMENEIVASSAGTVTAIHVTPGQVVNPGDgLITI 129
|
|
| GCS_H |
cd06848 |
Glycine cleavage H-protein. Glycine cleavage H-proteins are part of the glycine cleavage ... |
9-63 |
8.97e-04 |
|
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: 38.67 E-value: 8.97e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1737230220 9 DIGADEV-EITEI-LVKVGDKVEAEQSLITVEGDKASMEVPSPQAGIVKEIKVSVGD 63
Cdd:cd06848 22 DYAQDLLgDIVFVeLPEVGTEVKKGDPFGSVESVKAASDLYSPVSGEVVEVNEALLD 78
|
|
| GcvH |
COG0509 |
Glycine cleavage system protein H (lipoate-binding) [Amino acid transport and metabolism]; ... |
21-67 |
1.37e-03 |
|
Glycine cleavage system protein H (lipoate-binding) [Amino acid transport and metabolism]; Glycine cleavage system protein H (lipoate-binding) is part of the Pathway/BioSystem: Glycine cleavage
Pssm-ID: 440275 Cd Length: 128 Bit Score: 38.95 E-value: 1.37e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1737230220 21 LVKVGDKVEAEQSLITVEGDKASMEVPSPQAGIVKEIKVSVGDKTET 67
Cdd:COG0509 44 LPEVGTEVEAGEPFGVVESVKAVSDLYAPVSGEVVEVNEALEDDPEL 90
|
|
| PRK05889 |
PRK05889 |
biotin/lipoyl-binding carrier protein; |
221-277 |
2.30e-03 |
|
biotin/lipoyl-binding carrier protein;
Pssm-ID: 180306 [Multi-domain] Cd Length: 71 Bit Score: 37.10 E-value: 2.30e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1737230220 221 VTEVMVKVGDKVAAEQSLITVEGDKASMEVPAPFAGTVKEIKISTGDKVSTGSLIMV 277
Cdd:PRK05889 13 VLEVVVNEGDQIGKGDTLVLLESMKMEIPVLAEVAGTVSKVSVSVGDVIQAGDLIAV 69
|
|
| PRK07051 |
PRK07051 |
biotin carboxyl carrier domain-containing protein; |
125-178 |
2.32e-03 |
|
biotin carboxyl carrier domain-containing protein;
Pssm-ID: 180811 [Multi-domain] Cd Length: 80 Bit Score: 37.30 E-value: 2.32e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1737230220 125 VKVGDTVAAEQSLITVEGDKASMEVPAPFAGTVKEIKINTGDKVSTGSLIMVFE 178
Cdd:PRK07051 26 VEVGDAVAAGDVVGLIEVMKQFTEVEAEAAGRVVEFLVEDGEPVEAGQVLARIE 79
|
|
| GCV_H |
pfam01597 |
Glycine cleavage H-protein; This is a family of glycine cleavage H-proteins, part of the ... |
227-261 |
7.34e-03 |
|
Glycine cleavage H-protein; This is a family of glycine cleavage H-proteins, part of the glycine cleavage multienzyme complex (GCV) found in bacteria and the mitochondria of eukaryotes. GCV catalyzes the catabolism of glycine in eukaryotes. A lipoyl group is attached to a completely conserved lysine residue. The H protein shuttles the methylamine group of glycine from the P protein to the T protein.
Pssm-ID: 396258 Cd Length: 122 Bit Score: 36.93 E-value: 7.34e-03
10 20 30
....*....|....*....|....*....|....*
gi 1737230220 227 KVGDKVAAEQSLITVEGDKASMEVPAPFAGTVKEI 261
Cdd:pfam01597 40 EVGTKVKKGESLAAIESVKAASPIYAPVSGEVVEV 74
|
|
| PRK07051 |
PRK07051 |
biotin carboxyl carrier domain-containing protein; |
226-279 |
7.91e-03 |
|
biotin carboxyl carrier domain-containing protein;
Pssm-ID: 180811 [Multi-domain] Cd Length: 80 Bit Score: 35.76 E-value: 7.91e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1737230220 226 VKVGDKVAAEQSLITVEGDKASMEVPAPFAGTVKEIKISTGDKVSTGSLIMVFE 279
Cdd:PRK07051 26 VEVGDAVAAGDVVGLIEVMKQFTEVEAEAAGRVVEFLVEDGEPVEAGQVLARIE 79
|
|
| |
