|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02528 |
PLN02528 |
2-oxoisovalerate dehydrogenase E2 component |
90-504 |
0e+00 |
|
2-oxoisovalerate dehydrogenase E2 component
Pssm-ID: 215289 [Multi-domain] Cd Length: 416 Bit Score: 800.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255551811 90 VPLAQTGEGIAECELLQWFVQEGDEVEEFQPLCEVQSDKATIEITSRYKGKVAQILYVPGDIVKVGETLLKMAVEES--- 166
Cdd:PLN02528 1 VPLAQTGEGIAECELLRWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGKVAQINFSPGDIVKVGETLLKIMVEDSqhl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255551811 167 --LASIPRVDGLKDTKALDLEQEKSQIGGVLCTPAVRHLAKQYGIDLNDVSGTGKDGKILKEDILNYGIQKGVIEDSPGA 244
Cdd:PLN02528 81 rsDSLLLPTDSSNIVSLAESDERGSNLSGVLSTPAVRHLAKQYGIDLNDILGTGKDGRVLKEDVLKYAAQKGVVKDSSSA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255551811 245 SNADSGNQLkkgkEKSTCTSAEVGQLYDDKTVPLRGFQRTMVKTMSIAAKVPHFHYVEEINCNALVELKASFQSNNTDPG 324
Cdd:PLN02528 161 EEATIAEQE----EFSTSVSTPTEQSYEDKTIPLRGFQRAMVKTMTAAAKVPHFHYVEEINVDALVELKASFQENNTDPT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255551811 325 IKHTFLPLLIKSLSMALSKYPWMNSCFNEEAIEVLLKGSHNIGIAMATPHGLVVPNIKNVQSLSILEITKELARLQQLAL 404
Cdd:PLN02528 237 VKHTFLPFLIKSLSMALSKYPLLNSCFNEETSEIRLKGSHNIGVAMATEHGLVVPNIKNVQSLSLLEITKELSRLQHLAA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255551811 405 DNKLNPEDITGGTISLSNIGAIGGKFGAPIINLPEVAIIAIGRIQKVPQFADDGNVYPASIMTVNIGADHRVLDGATVAR 484
Cdd:PLN02528 317 ENKLNPEDITGGTITLSNIGAIGGKFGSPVLNLPEVAIIALGRIQKVPRFVDDGNVYPASIMTVTIGADHRVLDGATVAR 396
|
410 420
....*....|....*....|
gi 255551811 485 FCNEWKQLIEKPELLMLVLR 504
Cdd:PLN02528 397 FCNEWKSYVEKPELLMLHMR 416
|
|
| PRK11856 |
PRK11856 |
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed |
96-501 |
1.05e-129 |
|
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
Pssm-ID: 237001 [Multi-domain] Cd Length: 411 Bit Score: 382.99 E-value: 1.05e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255551811 96 GEGIAECELLQWFVQEGDEVEEFQPLCEVQSDKATIEITSRYKGKVAQILYVPGDIVKVGETLLKMAVEESLASIPRVDG 175
Cdd:PRK11856 11 GEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDVVPVGSVIAVIEEEGEAEAAAAAEA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255551811 176 LKDTKALDLEQEKSQ----------------IGGVLCTPAVRHLAKQYGIDLNDVSGTGKDGKILKEDILNYgIQKGVIE 239
Cdd:PRK11856 91 APEAPAPEPAPAAAAaaaaapaaaaapaapaAAAAKASPAVRKLARELGVDLSTVKGSGPGGRITKEDVEAA-AAAAAPA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255551811 240 DSPGASNADSGNQLKKGKEKstctsaevgqlyddkTVPLRGFQRTMVKTMSIA-AKVPHFHYVEEINCNALVELKASFQS 318
Cdd:PRK11856 170 AAAAAAAAAAPPAAAAEGEE---------------RVPLSGMRKAIAKRMVESkREIPHFTLTDEVDVTALLALRKQLKA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255551811 319 NntdpGIKHTFLPLLIKSLSMALSKYPWMNSCFNEEAIevLLKGSHNIGIAMATPHGLVVPNIKNVQSLSILEITKELAR 398
Cdd:PRK11856 235 I----GVKLTVTDFLIKAVALALKKFPELNASWDDDAI--VLKKYVNIGIAVATDGGLIVPVIRDADKKSLFELAREIKD 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255551811 399 LQQLALDNKLNPEDITGGTISLSNIGAIGGKFGAPIINLPEVAIIAIGRIQKVPqFADDGNVYPASIMTVNIGADHRVLD 478
Cdd:PRK11856 309 LAEKAREGKLKPEELQGGTFTISNLGMFGGDYFTPIINPPEVAILGVGAIVERP-VVVDGEIVVRKVMPLSLSFDHRVID 387
|
410 420
....*....|....*....|...
gi 255551811 479 GATVARFCNEWKQLIEKPELLML 501
Cdd:PRK11856 388 GADAARFLKALKELLENPALLLL 410
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
77-501 |
3.94e-128 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 383.79 E-value: 3.94e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255551811 77 ALADVPIGGGVVDVPLAQTGEgIAECELLQWFVQEGDEVEEFQPLCEVQSDKATIEITSRYKGKVAQILYVPGDIVKVGE 156
Cdd:PRK11855 109 AAAAAAAGGGVVEVKVPDIGE-ITEVEVIEWLVKVGDTVEEDQSLITVETDKATMEIPSPVAGVVKEIKVKVGDKVSVGS 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255551811 157 TLLKMAVEESLASIPRVDGLKDTKALDLEQ------------------EKSQIGGVLCTPAVRHLAKQYGIDLNDVSGTG 218
Cdd:PRK11855 188 LLVVIEVAAAAPAAAAAPAAAAPAAAAAAApapapaaaaapaaaapaaAAAPGKAPHASPAVRRLARELGVDLSQVKGTG 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255551811 219 KDGKILKEDILNYgiQKGVI---EDSPGASNADSGNQLKKgKEKSTCTSAEVGQLyddKTVPLRGFQRTMVKTMSIA-AK 294
Cdd:PRK11855 268 KKGRITKEDVQAF--VKGAMsaaAAAAAAAAAAGGGGLGL-LPWPKVDFSKFGEI---ETKPLSRIKKISAANLHRSwVT 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255551811 295 VPHFHYVEEINCNALVELKASFQSNNTDPGIKHTFLPLLIKSLSMALSKYPWMNSCFNEEAIEVLLKGSHNIGIAMATPH 374
Cdd:PRK11855 342 IPHVTQFDEADITDLEALRKQLKKEAEKAGVKLTMLPFFIKAVVAALKEFPVFNASLDEDGDELTYKKYFNIGFAVDTPN 421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255551811 375 GLVVPNIKNVQSLSILEITKELARLQQLALDNKLNPEDITGGTISLSNIGAIGGKFGAPIINLPEVAIIAIGRIQKVPqF 454
Cdd:PRK11855 422 GLVVPVIKDVDKKSLLEIAREIAELAKKARDGKLKPDDMQGGCFTISSLGGIGGTAFTPIINAPEVAILGVGKSQMKP-V 500
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 255551811 455 ADDGNVYPASIMTVNIGADHRVLDGATVARFCNEWKQLIEKPELLML 501
Cdd:PRK11855 501 WDGKEFVPRLMLPLSLSYDHRVIDGATAARFTNYLKQLLADPRRMLL 547
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
294-500 |
3.11e-96 |
|
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: 289.83 E-value: 3.11e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255551811 294 KVPHFHYVEEINCNALVELKASFQSNNTDPGIKHTFLPLLIKSLSMALSKYPWMNSCFNEEAIEVLLKGSHNIGIAMATP 373
Cdd:pfam00198 7 TIPHFTLTDEVDVTELLALREELKEDAADEETKLTFLPFLVKAVALALKKFPELNASWDGEEGEIVYKKYVNIGIAVATP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255551811 374 HGLVVPNIKNVQSLSILEITKELARLQQLALDNKLNPEDITGGTISLSNIGAIGGKFGAPIINLPEVAIIAIGRIQKVPQ 453
Cdd:pfam00198 87 RGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVGRIRKRPV 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 255551811 454 FAdDGNVYPASIMTVNIGADHRVLDGATVARFCNEWKQLIEKPELLM 500
Cdd:pfam00198 167 VV-DGEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELLL 212
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
77-485 |
3.27e-72 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 241.06 E-value: 3.27e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255551811 77 ALADVPIG-GGVVDVPLAQTGEGiaECELLQWFVQEGDEVEEFQPLCEVQSDKATIEITSRYKGKVAQILYVPGDIVKVG 155
Cdd:PRK11854 195 APAAAPAAaAGVKDVNVPDIGGD--EVEVTEVMVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVKTG 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255551811 156 ETLLKMAVEESL-ASIPRVDGLKDTKALDLEQEKSQIGG----------------VLCTPAVRHLAKQYGIDLNDVSGTG 218
Cdd:PRK11854 273 SLIMRFEVEGAApAAAPAKQEAAAPAPAAAKAEAPAAAPaakaegksefaendayVHATPLVRRLAREFGVNLAKVKGTG 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255551811 219 KDGKILKEDILNYgiQKGVIEdspgasnadsgnQLKKGKEKSTCTSAEVGQLYDDK----------TVPLRGFQ----RT 284
Cdd:PRK11854 353 RKGRILKEDVQAY--VKDAVK------------RAEAAPAAAAAGGGGPGLLPWPKvdfskfgeieEVELGRIQkisgAN 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255551811 285 MVKTMSIAAKVPHFHYVEeincnaLVELKASFQSNN-----TDPGIKHTFLPLLIKSLSMALSKYPWMNSCFNEEAIEVL 359
Cdd:PRK11854 419 LHRNWVMIPHVTQFDKAD------ITELEAFRKQQNaeaekRKLGVKITPLVFIMKAVAAALEQMPRFNSSLSEDGQRLT 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255551811 360 LKGSHNIGIAMATPHGLVVPNIKNVQSLSILEITKELARLQQLALDNKLNPEDITGGTISLSNIGAIGGKFGAPIINLPE 439
Cdd:PRK11854 493 LKKYVNIGIAVDTPNGLVVPVFKDVNKKGIIELSRELMDISKKARDGKLTAGDMQGGCFTISSIGGLGTTHFTPIVNAPE 572
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 255551811 440 VAIIAIGRIQKVPqfADDGNVY-PASIMTVNIGADHRVLDGATVARF 485
Cdd:PRK11854 573 VAILGVSKSAMEP--VWNGKEFaPRLMLPLSLSYDHRVIDGADGARF 617
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
85-501 |
3.00e-68 |
|
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: 228.61 E-value: 3.00e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255551811 85 GGVVDVPLAQTGeGIAECELLQWFVQEGDEVEEFQPLCEVQSDKATIEITSRYKGKVAQILYVPGDIVKVGETLLKMAVE 164
Cdd:TIGR01348 114 SGVQEVTVPDIG-DIEKVTVIEVLVKVGDTVSADQSLITLESDKASMEVPAPASGVVKSVKVKVGDSVPTGDLILTLSVA 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255551811 165 ESLA---------------------SIPRVDGLKDTKALDLEQEKSQIGGVL--CTPAVRHLAKQYGIDLNDVSGTGKDG 221
Cdd:TIGR01348 193 GSTPatapapasaqpaaqspaatqpEPAAAPAAAKAQAPAPQQAGTQNPAKVdhAAPAVRRLAREFGVDLSAVKGTGIKG 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255551811 222 KILKEDILNY-GIQKGVIEDSPGASNADSGNQLKKGKekstCTSAEVGQLyddKTVPLRGFQRTMVKTMSIA-AKVPHFH 299
Cdd:TIGR01348 273 RILREDVQRFvKEPSVRAQAAAASAAGGAPGALPWPN----VDFSKFGEV---EEVDMSRIRKISGANLTRNwTMIPHVT 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255551811 300 YVEEINCNALVELKASFQSNNTDPGIKHTFLPLLIKSLSMALSKYPWMNSCFNEEAIEVLLKGSHNIGIAMATPHGLVVP 379
Cdd:TIGR01348 346 HFDKADITEMEAFRKQQNAAVEKEGVKLTVLHILMKAVAAALKKFPKFNASLDLGGEQLILKKYVNIGVAVDTPNGLLVP 425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255551811 380 NIKNVQSLSILEITKELARLQQLALDNKLNPEDITGGTISLSNIGAIGGKFGAPIINLPEVAIIAIGRIQKVPQFadDGN 459
Cdd:TIGR01348 426 VIKDVDRKGITELALELSDLAKKARDGKLTPDEMQGACFTISSLGGIGGTAFTPIVNAPEVAILGVSKSGMEPVW--NGK 503
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 255551811 460 VY-PASIMTVNIGADHRVLDGATVARFCNEWKQLIEKPELLML 501
Cdd:TIGR01348 504 EFePRLMLPLSLSYDHRVIDGADAARFTTYICESLADIRRLLL 546
|
|
| PRK11857 |
PRK11857 |
dihydrolipoamide acetyltransferase; Reviewed |
194-499 |
6.32e-68 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237002 [Multi-domain] Cd Length: 306 Bit Score: 220.44 E-value: 6.32e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255551811 194 VLCTPAVRHLAKQYGIDLNDVSGTGKDGKILKEDILNYgIQKGVIEDSPGASNADSGNQLKKGKEKSTCTSAEVGQlYDD 273
Cdd:PRK11857 2 ILATPIARALAKKLGIDISLLKGSGRDGKILAEDVENF-IKSLKSAPTPAEAASVSSAQQAAKTAAPAAAPPKLEG-KRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255551811 274 KTVPLR-GFQRTMVKTMSIAAKVphfHYVEEINCNALVELKASFQSN-NTDPGIKHTFLPLLIKSLSMALSKYPWMNSCF 351
Cdd:PRK11857 80 KVAPIRkAIARAMTNSWSNVAYV---NLVNEIDMTKLWDLRKSVKDPvLKTEGVKLTFLPFIAKAILIALKEFPIFAAKY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255551811 352 NEEAIEVLLKGSHNIGIAMATPHGLVVPNIKNVQSLSILEITKELARLQQLALDNKLNPEDITGGTISLSNIGAIGGKFG 431
Cdd:PRK11857 157 DEATSELVYPDTLNLGIAVDTEAGLMVPVIKNAQKLSIVEIAKEISRLAKAARERKIKPDEMKGGSFTITNYGSVGSLYG 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 255551811 432 APIINLPEVAIIAIGRIQKVPqFADDGNVYPASIMTVNIGADHRVLDGATVARFCNEWKQLIEKPELL 499
Cdd:PRK11857 237 VPVINYPELAIAGVGAIIDKA-IVKNGQIVAGKVMHLTVAADHRWIDGATIGRFASRVKELLEKPEIL 303
|
|
| PDHac_trf_mito |
TIGR01349 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
104-501 |
2.21e-62 |
|
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: 210.04 E-value: 2.21e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255551811 104 LLQWFVQEGDEVEEFQPLCEVQSDKATIEITSRYKGKVAQILYVPG-DIVKVGeTLLKMAVEE----------------- 165
Cdd:TIGR01349 16 LAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEGtKDVPVN-KPIAVLVEEkedvadafknyklessa 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255551811 166 --------------SLASIPRVDGLKDTKALDLEQEKSQIGG---VLCTPAVRHLAKQYGIDLNDVSGTGKDGKILKEDI 228
Cdd:TIGR01349 95 spapkpseiaptapPSAPKPSPAPQKQSPEPSSPAPLSDKESgdrIFASPLAKKLAKEKGIDLSAVAGSGPNGRIVKKDI 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255551811 229 LNYgiqkgvIEDSPGASNADSGNQLKKGKEKSTCTSAEVgqlYDDktVPLRGFQRTMVKTMsIAAK--VPHFHYVEEINC 306
Cdd:TIGR01349 175 ESF------VPQSPASANQQAAATTPATYPAAAPVSTGS---YED--VPLSNIRKIIAKRL-LESKqtIPHYYVSIECNV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255551811 307 NALVELKASFQSNNTDPgIKHTFLPLLIKSLSMALSKYPWMNSCFNEEAIevllKGSHN--IGIAMATPHGLVVPNIKNV 384
Cdd:TIGR01349 243 DKLLALRKELNAMASEV-YKLSVNDFIIKASALALREVPEANSSWTDNFI----RRYKNvdISVAVATPDGLITPIVRNA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255551811 385 QSLSILEITKELARLQQLALDNKLNPEDITGGTISLSNIGAIGGKFGAPIINLPEVAIIAIGRIQKVPqFADDGNVYP-- 462
Cdd:TIGR01349 318 DAKGLSTISNEIKDLAKRARNNKLKPEEFQGGTFTISNLGMFGIKDFTAIINPPQACILAVGAVEDVA-VVDNDEEKGfa 396
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 255551811 463 -ASIMTVNIGADHRVLDGATVARFCNEWKQLIEKPELLML 501
Cdd:TIGR01349 397 vASIMSVTLSCDHRVIDGAVGAEFLKSFKKYLENPIEMLL 436
|
|
| sucB |
TIGR01347 |
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ... |
88-501 |
1.16e-60 |
|
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: 204.58 E-value: 1.16e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255551811 88 VDVPLAQTGEGIAECELLQWFVQEGDEVEEFQPLCEVQSDKATIEITSRYKGKVAQILYVPGDIVKVGETLLKMAvEESL 167
Cdd:TIGR01347 1 IEIKVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAILE-EGND 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255551811 168 ASIPRVDGLKDTKA-LDLEQEKSQIGGV----LCTPAVRHLAKQYGIDLNDVSGTGKDGKILKEDILNYGIQKGVIEDSP 242
Cdd:TIGR01347 80 ATAAPPAKSGEEKEeTPAASAAAAPTAAanrpSLSPAARRLAKEHGIDLSAVPGTGVTGRVTKEDIIKKTEAPASAQPPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255551811 243 GASNADSGNQLKKGKEKSTCTSAEvgqlyddKTVPLRgfqrtMVKTMSIAAKVPHFHyveEINCNALVELKASFQSN-NT 321
Cdd:TIGR01347 160 AAAAAAAPAAATRPEERVKMTRLR-------QRIAER-----LKEAQNSTAMLTTFN---EVDMSAVMELRKRYKEEfEK 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255551811 322 DPGIKHTFLPLLIKSLSMALSKYPWMNSCFNEEaiEVLLKGSHNIGIAMATPHGLVVPNIKNVQSLSILEITKELARLQQ 401
Cdd:TIGR01347 225 KHGVKLGFMSFFVKAVVAALKRFPEVNAEIDGD--DIVYKDYYDISVAVSTDRGLVVPVVRNADRMSFADIEKEIADLGK 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255551811 402 LALDNKLNPEDITGGTISLSNIGAIGGKFGAPIINLPEVAIIAIGRIQKVPqFADDGNVYPASIMTVNIGADHRVLDGAT 481
Cdd:TIGR01347 303 KARDGKLTLEDMTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHGIKERP-VAVNGQIEIRPMMYLALSYDHRLIDGKE 381
|
410 420
....*....|....*....|
gi 255551811 482 VARFCNEWKQLIEKPELLML 501
Cdd:TIGR01347 382 AVTFLVTIKELLEDPRRLLL 401
|
|
| PRK05704 |
PRK05704 |
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase; |
88-501 |
3.02e-55 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
Pssm-ID: 235571 [Multi-domain] Cd Length: 407 Bit Score: 190.05 E-value: 3.02e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255551811 88 VDVPlaQTGEGIAECELLQWFVQEGDEVEEFQPLCEVQSDKATIEITSRYKGKVAQILYVPGDIVKVGETLLKMAVEESL 167
Cdd:PRK05704 5 IKVP--TLPESVTEATIATWHKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGDTVTVGQVLGRIDEGAAA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255551811 168 ASIPRVDGLKDTKALDLEQE----KSQIGGVLCTPAVRHLAKQYGIDLNDVSGTGKDGKILKEDILNYGIQKGVIEDSPG 243
Cdd:PRK05704 83 GAAAAAAAAAAAAAAAPAQAqaaaAAEQSNDALSPAARKLAAENGLDASAVKGTGKGGRVTKEDVLAALAAAAAAPAAPA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255551811 244 ASNAdsgnqlkkgkekstctsAEVGQLYDDKTVplrgfQRtmVKtMS-----IAAKVphfhyVE------------EINC 306
Cdd:PRK05704 163 AAAP-----------------AAAPAPLGARPE-----ER--VP-MTrlrktIAERL-----LEaqnttamlttfnEVDM 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255551811 307 NALVEL----KASFQSNNtdpGIKHTFLPLLIKSLSMALSKYPWMNScfneeAI---EVLLKGSHNIGIAMATPHGLVVP 379
Cdd:PRK05704 213 TPVMDLrkqyKDAFEKKH---GVKLGFMSFFVKAVVEALKRYPEVNA-----SIdgdDIVYHNYYDIGIAVGTPRGLVVP 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255551811 380 NIKNVQSLSILEITKELARLQQLALDNKLNPEDITGGTISLSNigaiGGKFGA----PIINLPEVAIIAIGRIQKVPqFA 455
Cdd:PRK05704 285 VLRDADQLSFAEIEKKIAELAKKARDGKLSIEELTGGTFTITN----GGVFGSlmstPIINPPQSAILGMHKIKERP-VA 359
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 255551811 456 DDGNVYPASIMTVNIGADHRVLDGATVARFCNEWKQLIEKPELLML 501
Cdd:PRK05704 360 VNGQIVIRPMMYLALSYDHRIIDGKEAVGFLVTIKELLEDPERLLL 405
|
|
| PLN02744 |
PLN02744 |
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex |
101-501 |
1.23e-48 |
|
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
Pssm-ID: 215397 [Multi-domain] Cd Length: 539 Bit Score: 175.81 E-value: 1.23e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255551811 101 ECELLQWFVQEGDEVEEFQPLCEVQSDKATIEITSRYKGKVAQILYVPG--DIvKVGETL-LKMAVEESLASI------- 170
Cdd:PLN02744 126 EGNIARWLKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVKGDGakEI-KVGEVIaITVEEEEDIGKFkdykpss 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255551811 171 ---------------PRVDGLKDT------KALDLEQEKSQIGGVLCTPAVRHLAKQYGIDLNDVSGTGKDGKILKEDIL 229
Cdd:PLN02744 205 saapaapkakpspppPKEEEVEKPasspepKASKPSAPPSSGDRIFASPLARKLAEDNNVPLSSIKGTGPDGRIVKADIE 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255551811 230 NYGIQKGviedspgasnadsgnqlKKGKEKSTCTSAEVGQLYDDktVPLRGFQR-TMVKTMSIAAKVPHFHYVEEINCNA 308
Cdd:PLN02744 285 DYLASGG-----------------KGATAPPSTDSKAPALDYTD--IPNTQIRKvTASRLLQSKQTIPHYYLTVDTRVDK 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255551811 309 LVELKASFQS-NNTDPGIKHTFLPLLIKSLSMALSKYPWMNSCFNEEAIevllKGSHNIGIAMA--TPHGLVVPNIKNVQ 385
Cdd:PLN02744 346 LMALRSQLNSlQEASGGKKISVNDLVIKAAALALRKVPQCNSSWTDDYI----RQYHNVNINVAvqTENGLYVPVVKDAD 421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255551811 386 SLSILEITKELARLQQLALDNKLNPEDITGGTISLSNigaIGGKFG----APIINLPEVAIIAIGRIQK--VPQFADDGN 459
Cdd:PLN02744 422 KKGLSTIAEEVKQLAQKARENSLKPEDYEGGTFTVSN---LGGPFGikqfCAIINPPQSAILAVGSAEKrvIPGSGPDQY 498
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 255551811 460 VYpASIMTVNIGADHRVLDGATVARFCNEWKQLIEKPELLML 501
Cdd:PLN02744 499 NF-ASFMSVTLSCDHRVIDGAIGAEWLKAFKGYIENPESMLL 539
|
|
| PTZ00144 |
PTZ00144 |
dihydrolipoamide succinyltransferase; Provisional |
87-503 |
7.50e-48 |
|
dihydrolipoamide succinyltransferase; Provisional
Pssm-ID: 240289 [Multi-domain] Cd Length: 418 Bit Score: 170.63 E-value: 7.50e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255551811 87 VVDVPlaQTGEGIAECELLQWFVQEGDEVEEFQPLCEVQSDKATIEITSRYKGKVAQILYVPGDIVKVGETLLKM--AVE 164
Cdd:PTZ00144 46 VIKVP--TMGDSISEGTVVEWKKKVGDYVKEDEVICIIETDKVSVDIRAPASGVITKIFAEEGDTVEVGAPLSEIdtGGA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255551811 165 ESLASIPRVDGLKDTKAldlEQEKSqiggvlctpavrhlakqygidlndvsgtgKDGKILKEdilnygiqkGVIEDSPGA 244
Cdd:PTZ00144 124 PPAAAPAAAAAAKAEKT---TPEKP-----------------------------KAAAPTPE---------PPAASKPTP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255551811 245 SNADSgnQLKKGKEKSTCTSAEVGQLYDDKTVP-----------LRGFQRTMvktmsiaAKVPHFHyveEINCNALVEL- 312
Cdd:PTZ00144 163 PAAAK--PPEPAPAAKPPPTPVARADPRETRVPmsrmrqriaerLKASQNTC-------AMLTTFN---ECDMSALMELr 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255551811 313 ---KASFQSNNtdpGIKHTFLPLLIKSLSMALSKYPWMNSCFNEEAIEvllkgSHN---IGIAMATPHGLVVPNIKNVQS 386
Cdd:PTZ00144 231 keyKDDFQKKH---GVKLGFMSAFVKASTIALKKMPIVNAYIDGDEIV-----YRNyvdISVAVATPTGLVVPVIRNCEN 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255551811 387 LSILEITKELARLQQLALDNKLNPEDITGGTISLSNIGAIGGKFGAPIINLPEVAIIAIGRIQKVPQFADDgNVYPASIM 466
Cdd:PTZ00144 303 KSFAEIEKELADLAEKARNNKLTLEDMTGGTFTISNGGVFGSLMGTPIINPPQSAILGMHAIKKRPVVVGN-EIVIRPIM 381
|
410 420 430
....*....|....*....|....*....|....*..
gi 255551811 467 TVNIGADHRVLDGATVARFCNEWKQLIEKPELLMLVL 503
Cdd:PTZ00144 382 YLALTYDHRLIDGRDAVTFLKKIKDLIEDPARMLLDL 418
|
|
| PRK14843 |
PRK14843 |
dihydrolipoamide acetyltransferase; Provisional |
197-502 |
2.87e-33 |
|
dihydrolipoamide acetyltransferase; Provisional
Pssm-ID: 184847 [Multi-domain] Cd Length: 347 Bit Score: 129.25 E-value: 2.87e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255551811 197 TPAVRHLAKQYGIDLNDVSGTGKDGKILKEDILNYGIQKgVIEDSPGASNADSGNQ-----------------------L 253
Cdd:PRK14843 9 TPAARKLADDLGINLYDVSGSGANGRVHKEDVETYKDTN-VVRISPLAKRIALEHNiawqeiqgtghrgkimkkdvlalL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255551811 254 KKGKEKSTCTSA---EVGQLYDDKTVPLRGFQRTMVKTMS--IAAKV-------PHFHYVEEINCNALVEL-KASFQSNN 320
Cdd:PRK14843 88 PENIENDSIKSPaqiEKVEEVPDNVTPYGEIERIPMTPMRkvIAQRMvesyltaPTFTLNYEVDMTEMLALrKKVLEPIM 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255551811 321 TDPGIKHTFLPLLIKSLSMALSKYPWMNSCFNEEAIEVLLKGSHNIGIAMATPHGLVVPNIKNVQSLSILEITKELARLQ 400
Cdd:PRK14843 168 EATGKKTTVTDLLSLAVVKTLMKHPYINASLTEDGKTIITHNYVNLAMAVGMDNGLMTPVVYNAEKMSLSELVVAFKDVI 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255551811 401 QLALDNKLNPEDITGGTISLSNIGAIGGKFGAPIINLPEVAIIAIGRIQKVPQFAdDGNVYPASIMTVNIGADHRVLDGA 480
Cdd:PRK14843 248 GRTLDGKLAPSELQNSTFTISNLGMFGVQSFGPIINQPNSAILGVSSTIEKPVVV-NGEIVIRPIMSLGLTIDHRVVDGM 326
|
330 340
....*....|....*....|..
gi 255551811 481 TVARFCNEWKQLIEKPeLLMLV 502
Cdd:PRK14843 327 AGAKFMKDLKELIETP-ISMLI 347
|
|
| PLN02226 |
PLN02226 |
2-oxoglutarate dehydrogenase E2 component |
85-501 |
1.22e-25 |
|
2-oxoglutarate dehydrogenase E2 component
Pssm-ID: 177871 [Multi-domain] Cd Length: 463 Bit Score: 109.46 E-value: 1.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255551811 85 GGVVDVPLAQTGEGIAECELLQWFVQEGDEVEEFQPLCEVQSDKATIEITSRYKGKVAQILYVPGDIVKVGETLLKMAVE 164
Cdd:PLN02226 89 GDTVEAVVPHMGESITDGTLATFLKKPGERVQADEAIAQIETDKVTIDIASPASGVIQEFLVKEGDTVEPGTKVAIISKS 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255551811 165 ESLASiprvDGLKDTKALDLEQEKSQiggvlcTPAvrhlakqygidlndvsgtgkdgkilkEDIlnygiQKGVIEDSPGA 244
Cdd:PLN02226 169 EDAAS----QVTPSQKIPETTDPKPS------PPA--------------------------EDK-----QKPKVESAPVA 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255551811 245 SNADSGNQLKKGKEkstctSAEVGQL---YDDKTVPL-RGFQRTMVKTMSIAAKVPHFHYVEEINCNALVELKASFQSNN 320
Cdd:PLN02226 208 EKPKAPSSPPPPKQ-----SAKEPQLppkERERRVPMtRLRKRVATRLKDSQNTFALLTTFNEVDMTNLMKLRSQYKDAF 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255551811 321 TDP-GIKHTFLPLLIKSLSMALSKYPWMNSCFNEEaiEVLLKGSHNIGIAMATPHGLVVPNIKNVQSLSILEITKELARL 399
Cdd:PLN02226 283 YEKhGVKLGLMSGFIKAAVSALQHQPVVNAVIDGD--DIIYRDYVDISIAVGTSKGLVVPVIRGADKMNFAEIEKTINGL 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255551811 400 QQLALDNKLNPEDITGGTISLSNIGAIGGKFGAPIINLPEVAIIAIGRIQKVPQFAdDGNVYPASIMTVNIGADHRVLDG 479
Cdd:PLN02226 361 AKKANEGTISIDEMAGGSFTVSNGGVYGSLISTPIINPPQSAILGMHSIVSRPMVV-GGSVVPRPMMYVALTYDHRLIDG 439
|
410 420
....*....|....*....|..
gi 255551811 480 ATVARFCNEWKQLIEKPELLML 501
Cdd:PLN02226 440 REAVYFLRRVKDVVEDPQRLLL 461
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
88-161 |
1.06e-24 |
|
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: 97.09 E-value: 1.06e-24
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 255551811 88 VDVPLAQTGEGIAECELLQWFVQEGDEVEEFQPLCEVQSDKATIEITSRYKGKVAQILYVPGDIVKVGETLLKM 161
Cdd:cd06849 1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
88-162 |
1.14e-22 |
|
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: 91.67 E-value: 1.14e-22
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 255551811 88 VDVPLAQTGEGIAECELLQWFVQEGDEVEEFQPLCEVQSDKATIEITSRYKGKVAQILYVPGDIVKVGETLLKMA 162
Cdd:COG0508 3 IEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVIA 77
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
88-161 |
1.75e-15 |
|
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue binds biotin in one group and lipoic acid in the other. Note that the HMM does not currently recognize the Glycine cleavage system H proteins.
Pssm-ID: 395290 [Multi-domain] Cd Length: 73 Bit Score: 71.09 E-value: 1.75e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 255551811 88 VDVPLAQTGEGIAECELlQWFVQEGDEVEEFQPLCEVQSDKATIEITSRYKGKVAQILYVPGDIVKVGETLLKM 161
Cdd:pfam00364 1 TEIKSPMIGESVREGVV-EWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
|
|
| kgd |
PRK12270 |
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ... |
254-485 |
5.55e-15 |
|
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;
Pssm-ID: 237030 [Multi-domain] Cd Length: 1228 Bit Score: 78.01 E-value: 5.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255551811 254 KKGKEKSTCTSAEVGQLYDDKTVPLRGFQRTMVKTMSIAAKVPHFHYVEEINCNALVELKAsfQSNN---TDPGIKHTFL 330
Cdd:PRK12270 96 PAAPPAAAAAAAPAAAAVEDEVTPLRGAAAAVAKNMDASLEVPTATSVRAVPAKLLIDNRI--VINNhlkRTRGGKVSFT 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255551811 331 PLLIKSLSMALSKYPWMNSCFNEEAIE-VLLKGSH-NIGIA--MATPHG---LVVPNIKNVQSLSILEITKELARLQQLA 403
Cdd:PRK12270 174 HLIGYALVQALKAFPNMNRHYAEVDGKpTLVTPAHvNLGLAidLPKKDGsrqLVVPAIKGAETMDFAQFWAAYEDIVRRA 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255551811 404 LDNKLNPEDITGGTISLSNIGAIGGKFGAPIINLPEVAIIAIGRIQkvpqfaddgnvYPAS----------------IMT 467
Cdd:PRK12270 254 RDGKLTADDFQGTTISLTNPGGIGTVHSVPRLMKGQGAIIGVGAME-----------YPAEfqgaseerlaelgiskVMT 322
|
250
....*....|....*...
gi 255551811 468 VNIGADHRVLDGATVARF 485
Cdd:PRK12270 323 LTSTYDHRIIQGAESGEF 340
|
|
| E3_binding |
pfam02817 |
e3 binding domain; This family represents a small domain of the E2 subunit of 2-oxo-acid ... |
194-229 |
1.43e-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: 67.33 E-value: 1.43e-14
10 20 30
....*....|....*....|....*....|....*.
gi 255551811 194 VLCTPAVRHLAKQYGIDLNDVSGTGKDGKILKEDIL 229
Cdd:pfam02817 1 VLASPAARKLARELGIDLSDVKGTGPGGRITKEDVE 36
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
98-169 |
1.03e-09 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 60.79 E-value: 1.03e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 255551811 98 GIAECELLQWFVQEGDEVEEFQPLCEVQSDKATIEITSRYKGKVAQILYVPGDIVKVGETLLKMAVEESLAS 169
Cdd:PRK11854 11 GADEVEVTEILVKVGDKVEAEQSLITVEGDKASMEVPSPQAGVVKEIKVKVGDKVETGALIMIFESADGAAD 82
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
104-161 |
2.09e-09 |
|
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: 53.57 E-value: 2.09e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 255551811 104 LLQWFVQEGDEVEEFQPLCEVQSDKATIEITSRYKGKVAQILYVPGDIVKVGETLLKM 161
Cdd:cd06850 10 VVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| AccB |
COG0511 |
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ... |
108-160 |
2.22e-07 |
|
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: 49.89 E-value: 2.22e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 255551811 108 FVQEGDEVEEFQPLCEVQSDKATIEITSRYKGKVAQILYVPGDIVKVGETLLK 160
Cdd:COG0511 82 FVKVGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVVEILVENGQPVEYGQPLFV 134
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
96-228 |
7.94e-07 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 51.10 E-value: 7.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255551811 96 GEGIAECELLQWFVQEGDEVEEFQPLCEVQSDKATIEITSRYKGKVAQILYVPGDIVKVGETLLKMAVEEslASIPRVDg 175
Cdd:PRK14875 11 GLSMTEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGETLPVGALLAVVADAE--VSDAEID- 87
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 255551811 176 lkdtkaldleqeksqiggVLCTPAVRHLAkQYGIDLNDVSGTGKDGKILKEDI 228
Cdd:PRK14875 88 ------------------AFIAPFARRFA-PEGIDEEDAGPAPRKARIGGRTV 121
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
89-160 |
1.60e-06 |
|
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: 45.90 E-value: 1.60e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 255551811 89 DVPLAQTGEGIAECELLQWFVQEGDEVEEFQPLCEVQSDKATIEITSRYKGKVAQILYVPGDIVKVGETLLK 160
Cdd:cd06663 1 TILIPDLAQHLGDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKVEGDTPLVK 72
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| PRK09282 |
PRK09282 |
pyruvate carboxylase subunit B; Validated |
108-161 |
2.43e-04 |
|
pyruvate carboxylase subunit B; Validated
Pssm-ID: 236449 [Multi-domain] Cd Length: 592 Bit Score: 43.68 E-value: 2.43e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 255551811 108 FVQEGDEVEEFQPLCEVQSDKATIEITSRYKGKVAQILYVPGDIVKVGETLLKM 161
Cdd:PRK09282 537 KVKEGDKVKAGDTVLVLEAMKMENEIQAPVDGTVKEILVKEGDRVNPGDVLMEI 590
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| PRK08225 |
PRK08225 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
109-161 |
3.26e-04 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 181304 [Multi-domain] Cd Length: 70 Bit Score: 39.00 E-value: 3.26e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 255551811 109 VQEGDEVEEFQPLCEVQSDKATIEITSRYKGKVAQILYVPGDIVKVGETLLKM 161
Cdd:PRK08225 17 VKVGDTVEEGQDVVILESMKMEIPIVAEEAGTVKKINVQEGDFVNEGDVLLEI 69
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| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
108-161 |
1.68e-03 |
|
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: 41.22 E-value: 1.68e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 255551811 108 FVQEGDEVEEFQPLcevqsdkATIE-------ITSRYKGKVAQILYVPGDIVKVGETLLKM 161
Cdd:COG1038 1091 LVKEGDEVKKGDPL-------LTIEamkmettITAPRDGTVKEVLVKEGDQVEAGDLLIEL 1144
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|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
101-171 |
2.32e-03 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 40.29 E-value: 2.32e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 255551811 101 ECELLQWFVQEGDEVEEFQPLCEVQSDKATIEITSRYKGKVAQILYVPG-DIVKVGETLLKMAVE-ESLASIP 171
Cdd:PRK11892 16 EGTLAKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKILVPEGtEGVKVNTPIAVLLEEgESASDAG 88
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| PRK14040 |
PRK14040 |
oxaloacetate decarboxylase subunit alpha; |
77-162 |
2.78e-03 |
|
oxaloacetate decarboxylase subunit alpha;
Pssm-ID: 237592 [Multi-domain] Cd Length: 593 Bit Score: 40.30 E-value: 2.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255551811 77 ALADVPIGGGVVDVPLAQTgegiaeceLLQWFVQEGDEVEEFQPLCEVQSDKATIEITSRYKGKVAQILYVPGDIVKVGE 156
Cdd:PRK14040 516 AAAPAAAAGEPVTAPLAGN--------IFKVIVTEGQTVAEGDVLLILEAMKMETEIRAAQAGTVRGIAVKEGDAVAVGD 587
|
....*.
gi 255551811 157 TLLKMA 162
Cdd:PRK14040 588 TLLTLA 593
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