|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11856 |
PRK11856 |
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed |
1-380 |
2.01e-139 |
|
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
Pssm-ID: 237001 [Multi-domain] Cd Length: 411 Bit Score: 403.02 E-value: 2.01e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087841467 1 MKTFNLPDLGEGLAESEIVKWHISVGDMVKLDQVVLTVETAKATVDVPAPYGGRIVSRHGEEGDVINIGALLLEIDETGA 80
Cdd:PRK11856 2 MFEFKMPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDVVPVGSVIAVIEEEGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087841467 81 EQTVS--EKKQTADAATVVGNVSQHAHSVNVDDFWIGGEHNPSPdnliTALPSARLLAKKLGVDLELVKGSGPDGLIVDA 158
Cdd:PRK11856 82 AEAAAaaEAAPEAPAPEPAPAAAAAAAAAPAAAAAPAAPAAAAA----KASPAVRKLARELGVDLSTVKGSGPGGRITKE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087841467 159 DIYDEAGKQRP--------------------GTEVLKGARRTMVSTMAESHHNVAAVTITEEAVLEGWKQ---------- 208
Cdd:PRK11856 158 DVEAAAAAAAPaaaaaaaaaaappaaaaegeERVPLSGMRKAIAKRMVESKREIPHFTLTDEVDVTALLAlrkqlkaigv 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087841467 209 GEDISIRLVQAIVHACQEEPAMNAWFDAETMTRcvHSTVNIGIAVDSRHGLYVPVLRHADEYEPQEVRRWLDQTVQGIRE 288
Cdd:PRK11856 238 KLTVTDFLIKAVALALKKFPELNASWDDDAIVL--KKYVNIGIAVATDGGLIVPVIRDADKKSLFELAREIKDLAEKARE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087841467 289 RKIGREQLQHATITLSNFGAIAGIYATPVVTPPQVAIVGAGRIIEKVVIRDGQAVAVKAMPLSITFDHRACTGGEAARFT 368
Cdd:PRK11856 316 GKLKPEELQGGTFTISNLGMFGGDYFTPIINPPEVAILGVGAIVERPVVVDGEIVVRKVMPLSLSFDHRVIDGADAARFL 395
|
410
....*....|..
gi 2087841467 369 KVLAEHLRKPSV 380
Cdd:PRK11856 396 KALKELLENPAL 407
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
4-378 |
2.26e-72 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 235.10 E-value: 2.26e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087841467 4 FNLPDLGEgLAESEIVKWHISVGDMVKLDQVVLTVETAKATVDVPAPYGGRIVSRHGEEGDVINIGALLLEIDETGAEQT 83
Cdd:PRK11855 122 VKVPDIGE-ITEVEVIEWLVKVGDTVEEDQSLITVETDKATMEIPSPVAGVVKEIKVKVGDKVSVGSLLVVIEVAAAAPA 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087841467 84 VSEKKQTADAATVVGNVSQHAHSVNVDDFWIGGEHNPSPDNLITALPSARLLAKKLGVDLELVKGSGPDGLIVDADI--Y 161
Cdd:PRK11855 201 AAAAPAAAAPAAAAAAAPAPAPAAAAAPAAAAPAAAAAPGKAPHASPAVRRLARELGVDLSQVKGTGKKGRITKEDVqaF 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087841467 162 DEAGKQRP-------------------------------GTEVLKGARRTMVSTMAESHHNVAAVTITEEAV---LEGW- 206
Cdd:PRK11855 281 VKGAMSAAaaaaaaaaaagggglgllpwpkvdfskfgeiETKPLSRIKKISAANLHRSWVTIPHVTQFDEADitdLEALr 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087841467 207 ----KQGEDISIRL------VQAIVHACQEEPAMNAWFDAETMTRCVHSTVNIGIAVDSRHGLYVPVLRHADeyepqevr 276
Cdd:PRK11855 361 kqlkKEAEKAGVKLtmlpffIKAVVAALKEFPVFNASLDEDGDELTYKKYFNIGFAVDTPNGLVVPVIKDVD-------- 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087841467 277 rwlDQTVQGI-----------RERKIGREQLQHATITLSNFGAIAGIYATPVVTPPQVAIVGAGRIIEKVVIRDGQAVAV 345
Cdd:PRK11855 433 ---KKSLLEIareiaelakkaRDGKLKPDDMQGGCFTISSLGGIGGTAFTPIINAPEVAILGVGKSQMKPVWDGKEFVPR 509
|
410 420 430
....*....|....*....|....*....|...
gi 2087841467 346 KAMPLSITFDHRACTGGEAARFTKVLAEHLRKP 378
Cdd:PRK11855 510 LMLPLSLSYDHRVIDGATAARFTNYLKQLLADP 542
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
185-378 |
4.27e-70 |
|
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: 218.95 E-value: 4.27e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087841467 185 MAESHHNVAAVTITEEAVLEGW------------KQGEDISI--RLVQAIVHACQEEPAMNAWFDAETMTRCVHSTVNIG 250
Cdd:pfam00198 1 MTESKQTIPHFTLTDEVDVTELlalreelkedaaDEETKLTFlpFLVKAVALALKKFPELNASWDGEEGEIVYKKYVNIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087841467 251 IAVDSRHGLYVPVLRHADEYEPQEVRRWLDQTVQGIRERKIGREQLQHATITLSNFGAIAGIYATPVVTPPQVAIVGAGR 330
Cdd:pfam00198 81 IAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVGR 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2087841467 331 IIEKVVIRDGQAVAVKAMPLSITFDHRACTGGEAARFTKVLAEHLRKP 378
Cdd:pfam00198 161 IRKRPVVVDGEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENP 208
|
|
| PLN02528 |
PLN02528 |
2-oxoisovalerate dehydrogenase E2 component |
4-379 |
5.77e-55 |
|
2-oxoisovalerate dehydrogenase E2 component
Pssm-ID: 215289 [Multi-domain] Cd Length: 416 Bit Score: 186.08 E-value: 5.77e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087841467 4 FNLPDLGEGLAESEIVKWHISVGDMVKLDQVVLTVETAKATVDVPAPYGGRIVSRHGEEGDVINIGALLLEIdETGAEQT 83
Cdd:PLN02528 1 VPLAQTGEGIAECELLRWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGKVAQINFSPGDIVKVGETLLKI-MVEDSQH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087841467 84 VSEKKQTADaatvvgNVSQHAHSVNVDDfwigGEHNPSPDNLITalPSARLLAKKLGVDLELVKGSGPDGLIVDADIY-- 161
Cdd:PLN02528 80 LRSDSLLLP------TDSSNIVSLAESD----ERGSNLSGVLST--PAVRHLAKQYGIDLNDILGTGKDGRVLKEDVLky 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087841467 162 ---DEAGKQRPGTEV---------------------------LKGARRTMVSTMAES------HH----NVAAVTITEEA 201
Cdd:PLN02528 148 aaqKGVVKDSSSAEEatiaeqeefstsvstpteqsyedktipLRGFQRAMVKTMTAAakvphfHYveeiNVDALVELKAS 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087841467 202 VLEGWKQGEdISIR----LVQAIVHACQEEPAMNAWFDAETMTRCVHSTVNIGIAVDSRHGLYVPVLRHADEYEPQEVRR 277
Cdd:PLN02528 228 FQENNTDPT-VKHTflpfLIKSLSMALSKYPLLNSCFNEETSEIRLKGSHNIGVAMATEHGLVVPNIKNVQSLSLLEITK 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087841467 278 WLDQTVQGIRERKIGREQLQHATITLSNFGAIAGIYATPVVTPPQVAIVGAGRiIEKVV--IRDGQAVAVKAMPLSITFD 355
Cdd:PLN02528 307 ELSRLQHLAAENKLNPEDITGGTITLSNIGAIGGKFGSPVLNLPEVAIIALGR-IQKVPrfVDDGNVYPASIMTVTIGAD 385
|
410 420
....*....|....*....|....
gi 2087841467 356 HRACTGGEAARFTKVLAEHLRKPS 379
Cdd:PLN02528 386 HRVLDGATVARFCNEWKSYVEKPE 409
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
5-375 |
1.14e-49 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 176.73 E-value: 1.14e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087841467 5 NLPDLGEGlaESEIVKWHISVGDMVKLDQVVLTVETAKATVDVPAPYGGRIVSRHGEEGDVINIGALLLEIDETGAEQTV 84
Cdd:PRK11854 210 NVPDIGGD--EVEVTEVMVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVKTGSLIMRFEVEGAAPAA 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087841467 85 SEKKQTAdAATVVGNVSQHAHSVNVDDFWIGGEHNPSPDNLITALPSARLLAKKLGVDLELVKGSGPDGLIVDADI--YD 162
Cdd:PRK11854 288 APAKQEA-AAPAPAAAKAEAPAAAPAAKAEGKSEFAENDAYVHATPLVRRLAREFGVNLAKVKGTGRKGRILKEDVqaYV 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087841467 163 EAGKQRPGTEVLKGA------------------------------RRTMVSTMAESHHNVAAVT------ITEEAVL--- 203
Cdd:PRK11854 367 KDAVKRAEAAPAAAAaggggpgllpwpkvdfskfgeieevelgriQKISGANLHRNWVMIPHVTqfdkadITELEAFrkq 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087841467 204 ---EGWKQGEDISIR----LVQAIVHACQEEPAMNAWFDAETMTRCVHSTVNIGIAVDSRHGLYVPVLRHADEYEPQEVR 276
Cdd:PRK11854 447 qnaEAEKRKLGVKITplvfIMKAVAAALEQMPRFNSSLSEDGQRLTLKKYVNIGIAVDTPNGLVVPVFKDVNKKGIIELS 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087841467 277 RWLDQTVQGIRERKIGREQLQHATITLSNFGAIAGIYATPVVTPPQVAIVGAGRIIEKVViRDGQAVAVKAM-PLSITFD 355
Cdd:PRK11854 527 RELMDISKKARDGKLTAGDMQGGCFTISSIGGLGTTHFTPIVNAPEVAILGVSKSAMEPV-WNGKEFAPRLMlPLSLSYD 605
|
410 420
....*....|....*....|
gi 2087841467 356 HRACTGGEAARFTKVLAEHL 375
Cdd:PRK11854 606 HRVIDGADGARFITIINDRL 625
|
|
| sucB |
TIGR01347 |
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ... |
5-378 |
7.87e-49 |
|
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: 169.91 E-value: 7.87e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087841467 5 NLPDLGEGLAESEIVKWHISVGDMVKLDQVVLTVETAKATVDVPAPYGGRIVSRHGEEGDVINIGALLLEIDE-TGAEQT 83
Cdd:TIGR01347 4 KVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAILEEgNDATAA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087841467 84 VSEKKQTADAATVVGNVSQHahsvnvddfwiggehNPSPDNLITALPSARLLAKKLGVDLELVKGSGPDGLIVDADIyDE 163
Cdd:TIGR01347 84 PPAKSGEEKEETPAASAAAA---------------PTAAANRPSLSPAARRLAKEHGIDLSAVPGTGVTGRVTKEDI-IK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087841467 164 AGKQRPGTEVLKGA---------------------RRTMVSTMAESHHNVAAVTITEE----AVLEGWKQ-GEDI----S 213
Cdd:TIGR01347 148 KTEAPASAQPPAAAaaaaapaaatrpeervkmtrlRQRIAERLKEAQNSTAMLTTFNEvdmsAVMELRKRyKEEFekkhG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087841467 214 IRL------VQAIVHACQEEPAMNAWFDAETMTrcVHSTVNIGIAVDSRHGLYVPVLRHADEYEPQEVRRWLDQTVQGIR 287
Cdd:TIGR01347 228 VKLgfmsffVKAVVAALKRFPEVNAEIDGDDIV--YKDYYDISVAVSTDRGLVVPVVRNADRMSFADIEKEIADLGKKAR 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087841467 288 ERKIGREQLQHATITLSNFGAIAGIYATPVVTPPQVAIVGAGRIIEKVVIRDGQAVAVKAMPLSITFDHRACTGGEAARF 367
Cdd:TIGR01347 306 DGKLTLEDMTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHGIKERPVAVNGQIEIRPMMYLALSYDHRLIDGKEAVTF 385
|
410
....*....|.
gi 2087841467 368 TKVLAEHLRKP 378
Cdd:TIGR01347 386 LVTIKELLEDP 396
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
5-378 |
7.47e-47 |
|
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: 167.74 E-value: 7.47e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087841467 5 NLPDLGeGLAESEIVKWHISVGDMVKLDQVVLTVETAKATVDVPAPYGGRIVSRHGEEGDVINIGALLLEIDETGAEQTV 84
Cdd:TIGR01348 120 TVPDIG-DIEKVTVIEVLVKVGDTVSADQSLITLESDKASMEVPAPASGVVKSVKVKVGDSVPTGDLILTLSVAGSTPAT 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087841467 85 SEKKQTADAATVVGNVSQHAHS-----VNVDDFWIGGEHNPSPDNLITALPSARLLAKKLGVDLELVKGSGPDGLIVDAD 159
Cdd:TIGR01348 199 APAPASAQPAAQSPAATQPEPAaapaaAKAQAPAPQQAGTQNPAKVDHAAPAVRRLAREFGVDLSAVKGTGIKGRILRED 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087841467 160 IYDEAGKQ--------------RPG----------------TEVLKGARRTMVSTMAESHHNVAAVT------ITE-EAV 202
Cdd:TIGR01348 279 VQRFVKEPsvraqaaaasaaggAPGalpwpnvdfskfgeveEVDMSRIRKISGANLTRNWTMIPHVThfdkadITEmEAF 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087841467 203 ---LEGWKQGEDISIR----LVQAIVHACQEEPAMNAWFDAETMTRCVHSTVNIGIAVDSRHGLYVPVLRHADEYEPQEV 275
Cdd:TIGR01348 359 rkqQNAAVEKEGVKLTvlhiLMKAVAAALKKFPKFNASLDLGGEQLILKKYVNIGVAVDTPNGLLVPVIKDVDRKGITEL 438
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087841467 276 RRWLDQTVQGIRERKIGREQLQHATITLSNFGAIAGIYATPVVTPPQVAIVGAGR-IIEKVviRDGQAVAVKAM-PLSIT 353
Cdd:TIGR01348 439 ALELSDLAKKARDGKLTPDEMQGACFTISSLGGIGGTAFTPIVNAPEVAILGVSKsGMEPV--WNGKEFEPRLMlPLSLS 516
|
410 420
....*....|....*....|....*
gi 2087841467 354 FDHRACTGGEAARFTKVLAEHLRKP 378
Cdd:TIGR01348 517 YDHRVIDGADAARFTTYICESLADI 541
|
|
| PTZ00144 |
PTZ00144 |
dihydrolipoamide succinyltransferase; Provisional |
2-380 |
2.93e-46 |
|
dihydrolipoamide succinyltransferase; Provisional
Pssm-ID: 240289 [Multi-domain] Cd Length: 418 Bit Score: 163.31 E-value: 2.93e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087841467 2 KTFNLPDLGEGLAESEIVKWHISVGDMVKLDQVVLTVETAKATVDVPAPYGGRIVSRHGEEGDVINIGALLLEIDETGAE 81
Cdd:PTZ00144 45 KVIKVPTMGDSISEGTVVEWKKKVGDYVKEDEVICIIETDKVSVDIRAPASGVITKIFAEEGDTVEVGAPLSEIDTGGAP 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087841467 82 QTVSEKKQTADAATVVGNVSQHAHSvnvddfwiggehnPSPDNLITALPSARLLAKKLgvdlELVKGSGPDGLIVDADIY 161
Cdd:PTZ00144 125 PAAAPAAAAAAKAEKTTPEKPKAAA-------------PTPEPPAASKPTPPAAAKPP----EPAPAAKPPPTPVARADP 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087841467 162 DEAG------KQRPGtEVLKGARRT--MVSTMAEShhNVAAVTITEEAVLEGWKQGEDISIRLVQAIVHAC----QEEPA 229
Cdd:PTZ00144 188 RETRvpmsrmRQRIA-ERLKASQNTcaMLTTFNEC--DMSALMELRKEYKDDFQKKHGVKLGFMSAFVKAStialKKMPI 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087841467 230 MNAWFDAETMTrcVHSTVNIGIAVDSRHGLYVPVLRHADEYEPQEVRRWLDQTVQGIRERKIGREQLQHATITLSNFGAI 309
Cdd:PTZ00144 265 VNAYIDGDEIV--YRNYVDISVAVATPTGLVVPVIRNCENKSFAEIEKELADLAEKARNNKLTLEDMTGGTFTISNGGVF 342
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2087841467 310 AGIYATPVVTPPQVAIVGAGRIIEKVVIRDGQAVAVKAMPLSITFDHRACTGGEAARFTKVLAEHLRKPSV 380
Cdd:PTZ00144 343 GSLMGTPIINPPQSAILGMHAIKKRPVVVGNEIVIRPIMYLALTYDHRLIDGRDAVTFLKKIKDLIEDPAR 413
|
|
| PRK05704 |
PRK05704 |
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase; |
7-367 |
9.28e-44 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
Pssm-ID: 235571 [Multi-domain] Cd Length: 407 Bit Score: 156.53 E-value: 9.28e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087841467 7 PDLGEGLAESEIVKWHISVGDMVKLDQVVLTVETAKATVDVPAPYGGRIVSRHGEEGDVINIGALLLEIDETGAEQTVSE 86
Cdd:PRK05704 8 PTLPESVTEATIATWHKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGDTVTVGQVLGRIDEGAAAGAAAA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087841467 87 KKQTADAATVVGNVSQHAhsvnvddfwiggehNPSPDNLITALPSARLLAKKLGVDLELVKGSGPDGLIVDADIyDEAGK 166
Cdd:PRK05704 88 AAAAAAAAAAAPAQAQAA--------------AAAEQSNDALSPAARKLAAENGLDASAVKGTGKGGRVTKEDV-LAALA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087841467 167 QRPGTEVLKGA-----------------------RRTMVSTMAESHHNVAAVTITEE----AVLEGWKQGEDI-----SI 214
Cdd:PRK05704 153 AAAAAPAAPAAaapaaapaplgarpeervpmtrlRKTIAERLLEAQNTTAMLTTFNEvdmtPVMDLRKQYKDAfekkhGV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087841467 215 RL------VQAIVHACQEEPAMNAWFDAETMTrcVHSTVNIGIAVDSRHGLYVPVLRHADEYEPQEVRRWLDQTVQGIRE 288
Cdd:PRK05704 233 KLgfmsffVKAVVEALKRYPEVNASIDGDDIV--YHNYYDIGIAVGTPRGLVVPVLRDADQLSFAEIEKKIAELAKKARD 310
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2087841467 289 RKIGREQLQHATITLSNFGAIAGIYATPVVTPPQVAIVGAGRIIEKVVIRDGQAVAVKAMPLSITFDHRACTGGEAARF 367
Cdd:PRK05704 311 GKLSIEELTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHKIKERPVAVNGQIVIRPMMYLALSYDHRIIDGKEAVGF 389
|
|
| PRK11857 |
PRK11857 |
dihydrolipoamide acetyltransferase; Reviewed |
126-380 |
1.94e-42 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237002 [Multi-domain] Cd Length: 306 Bit Score: 150.33 E-value: 1.94e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087841467 126 ITALPSARLLAKKLGVDLELVKGSGPDGLIVDADI--YDEAGKQRPG-----------------------------TEVL 174
Cdd:PRK11857 2 ILATPIARALAKKLGIDISLLKGSGRDGKILAEDVenFIKSLKSAPTpaeaasvssaqqaaktaapaaappklegkREKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087841467 175 KGARRTMVSTMAESHHNVAAVTITEE-----------AVLEGWKQGEDISIR----LVQAIVHACQEEPAMNAWFDAETM 239
Cdd:PRK11857 82 APIRKAIARAMTNSWSNVAYVNLVNEidmtklwdlrkSVKDPVLKTEGVKLTflpfIAKAILIALKEFPIFAAKYDEATS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087841467 240 TRCVHSTVNIGIAVDSRHGLYVPVLRHADEYEPQEVRRWLDQTVQGIRERKIGREQLQHATITLSNFGAIAGIYATPVVT 319
Cdd:PRK11857 162 ELVYPDTLNLGIAVDTEAGLMVPVIKNAQKLSIVEIAKEISRLAKAARERKIKPDEMKGGSFTITNYGSVGSLYGVPVIN 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2087841467 320 PPQVAIVGAGRIIEKVVIRDGQAVAVKAMPLSITFDHRACTGGEAARFTKVLAEHLRKPSV 380
Cdd:PRK11857 242 YPELAIAGVGAIIDKAIVKNGQIVAGKVMHLTVAADHRWIDGATIGRFASRVKELLEKPEI 302
|
|
| PLN02744 |
PLN02744 |
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex |
6-378 |
5.62e-26 |
|
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
Pssm-ID: 215397 [Multi-domain] Cd Length: 539 Bit Score: 109.17 E-value: 5.62e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087841467 6 LPDLGEGLAESEIVKWHISVGDMVKLDQVVLTVETAKATVDVPA---PYGGRIVsrHGEEGDVINIGALL-LEIDETGAE 81
Cdd:PLN02744 117 MPSLSPTMTEGNIARWLKKEGDKVSPGEVLCEVETDKATVEMECmeeGYLAKIV--KGDGAKEIKVGEVIaITVEEEEDI 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087841467 82 QTVSEKKQTADAATVVGNVSQHAHSVNVDDF----------WIGGEHNPSPDNLITALPSARLLAKKLGVDLELVKGSGP 151
Cdd:PLN02744 195 GKFKDYKPSSSAAPAAPKAKPSPPPPKEEEVekpasspepkASKPSAPPSSGDRIFASPLARKLAEDNNVPLSSIKGTGP 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087841467 152 DGLIVDADIYD---EAGKQRPGTEVLKGA--------------RRTMVSTMAESHHNVAAVTITEEAVLEGWKQ------ 208
Cdd:PLN02744 275 DGRIVKADIEDylaSGGKGATAPPSTDSKapaldytdipntqiRKVTASRLLQSKQTIPHYYLTVDTRVDKLMAlrsqln 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087841467 209 -------GEDISIR--LVQAIVHACQEEPAMNA-WFDaeTMTRCVHStVNIGIAVDSRHGLYVPVLRHADEYEPQEVRRW 278
Cdd:PLN02744 355 slqeasgGKKISVNdlVIKAAALALRKVPQCNSsWTD--DYIRQYHN-VNINVAVQTENGLYVPVVKDADKKGLSTIAEE 431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087841467 279 LDQTVQGIRERKIGREQLQHATITLSNFGAIAGIYA-TPVVTPPQVAIVGAGRiIEKVVI---RDGQAVAVKAMPLSITF 354
Cdd:PLN02744 432 VKQLAQKARENSLKPEDYEGGTFTVSNLGGPFGIKQfCAIINPPQSAILAVGS-AEKRVIpgsGPDQYNFASFMSVTLSC 510
|
410 420
....*....|....*....|....
gi 2087841467 355 DHRACTGGEAARFTKVLAEHLRKP 378
Cdd:PLN02744 511 DHRVIDGAIGAEWLKAFKGYIENP 534
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
1-75 |
2.67e-25 |
|
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: 97.44 E-value: 2.67e-25
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2087841467 1 MKTFNLPDLGEGLAESEIVKWHISVGDMVKLDQVVLTVETAKATVDVPAPYGGRIVSRHGEEGDVINIGALLLEI 75
Cdd:COG0508 2 AIEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
|
|
| PLN02226 |
PLN02226 |
2-oxoglutarate dehydrogenase E2 component |
6-378 |
5.97e-25 |
|
2-oxoglutarate dehydrogenase E2 component
Pssm-ID: 177871 [Multi-domain] Cd Length: 463 Bit Score: 105.61 E-value: 5.97e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087841467 6 LPDLGEGLAESEIVKWHISVGDMVKLDQVVLTVETAKATVDVPAPYGGRIVSRHGEEGDVINIGallleidetgaeQTVS 85
Cdd:PLN02226 96 VPHMGESITDGTLATFLKKPGERVQADEAIAQIETDKVTIDIASPASGVIQEFLVKEGDTVEPG------------TKVA 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087841467 86 EKKQTADAAtvvgnvSQHAHSVNVDDFWIGGEHNPSPDNLITALPSARLLAKKLGvdlelvkGSGPDGLIVDADIYDEAG 165
Cdd:PLN02226 164 IISKSEDAA------SQVTPSQKIPETTDPKPSPPAEDKQKPKVESAPVAEKPKA-------PSSPPPPKQSAKEPQLPP 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087841467 166 KQRPGTEVLKGARRTMVSTMAESHHNVAAVTITEE---------------AVLEgwKQGEDISIR--LVQAIVHACQEEP 228
Cdd:PLN02226 231 KERERRVPMTRLRKRVATRLKDSQNTFALLTTFNEvdmtnlmklrsqykdAFYE--KHGVKLGLMsgFIKAAVSALQHQP 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087841467 229 AMNAWFDAETMTrcVHSTVNIGIAVDSRHGLYVPVLRHADEYEPQEVRRWLDQTVQGIRERKIGREQLQHATITLSNFGA 308
Cdd:PLN02226 309 VVNAVIDGDDII--YRDYVDISIAVGTSKGLVVPVIRGADKMNFAEIEKTINGLAKKANEGTISIDEMAGGSFTVSNGGV 386
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087841467 309 IAGIYATPVVTPPQVAIVGAGRIIEKVVIRDGQAVAVKAMPLSITFDHRACTGGEAARFTKVLAEHLRKP 378
Cdd:PLN02226 387 YGSLISTPIINPPQSAILGMHSIVSRPMVVGGSVVPRPMMYVALTYDHRLIDGREAVYFLRRVKDVVEDP 456
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
2-75 |
5.61e-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: 94.01 E-value: 5.61e-24
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2087841467 2 KTFNLPDLGEGLAESEIVKWHISVGDMVKLDQVVLTVETAKATVDVPAPYGGRIVSRHGEEGDVINIGALLLEI 75
Cdd:cd06849 1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
|
|
| PRK14843 |
PRK14843 |
dihydrolipoamide acetyltransferase; Provisional |
123-378 |
2.64e-18 |
|
dihydrolipoamide acetyltransferase; Provisional
Pssm-ID: 184847 [Multi-domain] Cd Length: 347 Bit Score: 84.96 E-value: 2.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087841467 123 DNLITALPSARLLAKKLGVDLELVKGSGPDGLIVDADI-----------YDEAGKQRPGTEVLK---------------G 176
Cdd:PRK14843 46 TNVVRISPLAKRIALEHNIAWQEIQGTGHRGKIMKKDVlallpeniendSIKSPAQIEKVEEVPdnvtpygeieripmtP 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087841467 177 ARRTMVSTMAESHHNVAAVTI------TE---------EAVLEGWKQGEDISIRLVQAIVHACQEEPAMNAWFDAETMTR 241
Cdd:PRK14843 126 MRKVIAQRMVESYLTAPTFTLnyevdmTEmlalrkkvlEPIMEATGKKTTVTDLLSLAVVKTLMKHPYINASLTEDGKTI 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087841467 242 CVHSTVNIGIAVDSRHGLYVPVLRHADEYEPQEVRRWLDQTVQGIRERKIGREQLQHATITLSNFGAIAGIYATPVVTPP 321
Cdd:PRK14843 206 ITHNYVNLAMAVGMDNGLMTPVVYNAEKMSLSELVVAFKDVIGRTLDGKLAPSELQNSTFTISNLGMFGVQSFGPIINQP 285
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 2087841467 322 QVAIVGAGRIIEKVVIRDGQAVAVKAMPLSITFDHRACTGGEAARFTKVLAEHLRKP 378
Cdd:PRK14843 286 NSAILGVSSTIEKPVVVNGEIVIRPIMSLGLTIDHRVVDGMAGAKFMKDLKELIETP 342
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
2-75 |
1.42e-13 |
|
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: 65.31 E-value: 1.42e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2087841467 2 KTFNLPDLGEGLAESeIVKWHISVGDMVKLDQVVLTVETAKATVDVPAPYGGRIVSRHGEEGDVINIGALLLEI 75
Cdd:pfam00364 1 TEIKSPMIGESVREG-VVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
|
|
| kgd |
PRK12270 |
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ... |
219-375 |
1.32e-11 |
|
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;
Pssm-ID: 237030 [Multi-domain] Cd Length: 1228 Bit Score: 66.45 E-value: 1.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087841467 219 AIVHACQEEPAMNAWFDAE--TMTRCVHSTVNIGIAVD------SRhGLYVPVLRHADEYEPQEVRRWLDQTVQGIRERK 290
Cdd:PRK12270 179 ALVQALKAFPNMNRHYAEVdgKPTLVTPAHVNLGLAIDlpkkdgSR-QLVVPAIKGAETMDFAQFWAAYEDIVRRARDGK 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087841467 291 IGREQLQHATITLSNFGAIAGIYATPVVTPPQVAIVGAGRI---------IEKVVIRDGqavAVKAMPLSITFDHRACTG 361
Cdd:PRK12270 258 LTADDFQGTTISLTNPGGIGTVHSVPRLMKGQGAIIGVGAMeypaefqgaSEERLAELG---ISKVMTLTSTYDHRIIQG 334
|
170
....*....|....
gi 2087841467 362 GEAARFTKVLAEHL 375
Cdd:PRK12270 335 AESGEFLRTIHQLL 348
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
6-72 |
1.96e-09 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 58.42 E-value: 1.96e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2087841467 6 LPDLGEGLAESEIVKWHISVGDMVKLDQVVLTVETAKATVDVPAPYGGRIVSRHGEEGDVINIGALL 72
Cdd:PRK14875 7 MPKWGLSMTEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGETLPVGALL 73
|
|
| E3_binding |
pfam02817 |
e3 binding domain; This family represents a small domain of the E2 subunit of 2-oxo-acid ... |
130-160 |
2.07e-08 |
|
e3 binding domain; This family represents a small domain of the E2 subunit of 2-oxo-acid dehydrogenases responsible for the binding of the E3 subunit.
Pssm-ID: 460710 [Multi-domain] Cd Length: 36 Bit Score: 49.61 E-value: 2.07e-08
10 20 30
....*....|....*....|....*....|.
gi 2087841467 130 PSARLLAKKLGVDLELVKGSGPDGLIVDADI 160
Cdd:pfam02817 5 PAARKLARELGIDLSDVKGTGPGGRITKEDV 35
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
6-75 |
2.44e-08 |
|
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: 50.52 E-value: 2.44e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087841467 6 LPDLGEGLAESEIVKWHISVGDMVKLDQVVLTVETAKATVDVPAPYGGRIVSRHGEEGDVINIGALLLEI 75
Cdd:cd06663 4 IPDLAQHLGDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKVEGDTPLVKI 73
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
18-75 |
1.13e-07 |
|
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: 48.18 E-value: 1.13e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 2087841467 18 IVKWHISVGDMVKLDQVVLTVETAKATVDVPAPYGGRIVSRHGEEGDVINIGALLLEI 75
Cdd:cd06850 10 VVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| PRK09282 |
PRK09282 |
pyruvate carboxylase subunit B; Validated |
18-75 |
4.25e-06 |
|
pyruvate carboxylase subunit B; Validated
Pssm-ID: 236449 [Multi-domain] Cd Length: 592 Bit Score: 48.69 E-value: 4.25e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 2087841467 18 IVKWHISVGDMVKLDQVVLTVETAKATVDVPAPYGGRIVSRHGEEGDVINIGALLLEI 75
Cdd:PRK09282 533 VVKVKVKEGDKVKAGDTVLVLEAMKMENEIQAPVDGTVKEILVKEGDRVNPGDVLMEI 590
|
|
| AccB |
COG0511 |
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ... |
23-76 |
1.06e-05 |
|
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: 44.50 E-value: 1.06e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 2087841467 23 ISVGDMVKLDQVVLTVETAKATVDVPAPYGGRIVSRHGEEGDVINIGALLLEID 76
Cdd:COG0511 83 VKVGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVVEILVENGQPVEYGQPLFVIE 136
|
|
| PRK14042 |
PRK14042 |
pyruvate carboxylase subunit B; Provisional |
18-76 |
3.45e-04 |
|
pyruvate carboxylase subunit B; Provisional
Pssm-ID: 172536 [Multi-domain] Cd Length: 596 Bit Score: 42.79 E-value: 3.45e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 2087841467 18 IVKWHISVGDMVKLDQVVLTVETAKATVDVPAPYGGRIVSRHGEEGDVINIGALLLEID 76
Cdd:PRK14042 536 IIAIHVSAGDEVKAGQAVLVIEAMKMETEIKAPANGVVAEILCQKGDKVTPGQVLIRVE 594
|
|
| PRK08225 |
PRK08225 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
20-76 |
5.41e-04 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 181304 [Multi-domain] Cd Length: 70 Bit Score: 38.23 E-value: 5.41e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 2087841467 20 KWHISVGDMVKLDQVVLTVETAKATVDVPAPYGGRIVSRHGEEGDVINIGALLLEID 76
Cdd:PRK08225 14 KIVVKVGDTVEEGQDVVILESMKMEIPIVAEEAGTVKKINVQEGDFVNEGDVLLEIE 70
|
|
| GCS_H |
cd06848 |
Glycine cleavage H-protein. Glycine cleavage H-proteins are part of the glycine cleavage ... |
25-61 |
6.07e-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: 6.07e-04
10 20 30
....*....|....*....|....*....|....*..
gi 2087841467 25 VGDMVKLDQVVLTVETAKATVDVPAPYGGRIVSRHGE 61
Cdd:cd06848 39 VGTEVKKGDPFGSVESVKAASDLYSPVSGEVVEVNEA 75
|
|
| GcvH |
COG0509 |
Glycine cleavage system protein H (lipoate-binding) [Amino acid transport and metabolism]; ... |
25-56 |
1.26e-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: 38.57 E-value: 1.26e-03
10 20 30
....*....|....*....|....*....|..
gi 2087841467 25 VGDMVKLDQVVLTVETAKATVDVPAPYGGRIV 56
Cdd:COG0509 47 VGTEVEAGEPFGVVESVKAVSDLYAPVSGEVV 78
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
18-94 |
1.64e-03 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 40.03 E-value: 1.64e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2087841467 18 IVKWHISVGDMVKLDQVVLTVETAKATVDVPAPYGGRIVSRHGEEGDVINIGALLLEIDETGAEQTVSEKKQTADAA 94
Cdd:COG1566 19 LGLALWAAGRNGPDEPVTADGRVEARVVTVAAKVSGRVTEVLVKEGDRVKKGQVLARLDPTDLQAALAQAEAQLAAA 95
|
|
| PRK05641 |
PRK05641 |
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
17-75 |
2.96e-03 |
|
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235540 [Multi-domain] Cd Length: 153 Bit Score: 37.92 E-value: 2.96e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 2087841467 17 EIVKWHISVGDMVKLDQVVLTVETAKATVDVPAPYGGRIVSRHGEEGDVINIGALLLEI 75
Cdd:PRK05641 94 KILRILVREGQQVKVGQGLLILEAMKMENEIPAPKDGVVKKILVKEGDTVDTGQPLIEL 152
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
18-75 |
3.16e-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: 39.68 E-value: 3.16e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 2087841467 18 IVKWHISVGDMVKLDQVVLTVETAKATVDVPAPYGGRIVSRHGEEGDVINIGALLLEI 75
Cdd:COG1038 1087 VVKVLVKEGDEVKKGDPLLTIEAMKMETTITAPRDGTVKEVLVKEGDQVEAGDLLIEL 1144
|
|
| PRK14040 |
PRK14040 |
oxaloacetate decarboxylase subunit alpha; |
18-75 |
3.81e-03 |
|
oxaloacetate decarboxylase subunit alpha;
Pssm-ID: 237592 [Multi-domain] Cd Length: 593 Bit Score: 39.14 E-value: 3.81e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 2087841467 18 IVKWHISVGDMVKLDQVVLTVETAKATVDVPAPYGGRIVSRHGEEGDVINIGALLLEI 75
Cdd:PRK14040 535 IFKVIVTEGQTVAEGDVLLILEAMKMETEIRAAQAGTVRGIAVKEGDAVAVGDTLLTL 592
|
|
| AcrA |
COG0845 |
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ... |
37-94 |
6.50e-03 |
|
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope biogenesis, Defense mechanisms];
Pssm-ID: 440606 [Multi-domain] Cd Length: 324 Bit Score: 38.00 E-value: 6.50e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 2087841467 37 TVEtAKATVDVPAPYGGRIVSRHGEEGDVINIGALLLEIDETGAEQTVSEKKQTADAA 94
Cdd:COG0845 17 TVE-ARREVEVRARVSGRVEEVLVDEGDRVKKGQVLARLDPPDLQAALAQAQAQLAAA 73
|
|
| |
