|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00144 |
PTZ00144 |
dihydrolipoamide succinyltransferase; Provisional |
158-519 |
0e+00 |
|
dihydrolipoamide succinyltransferase; Provisional
Pssm-ID: 240289 [Multi-domain] Cd Length: 418 Bit Score: 570.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517189665 158 KTISVPSMGDSITEGTVSTWTAAEGESVDADQVVCVIETDKVSVDVRAPEAGKIAKHLAASDEVVKVGSPLFELVPG--- 234
Cdd:PTZ00144 45 KVIKVPTMGDSISEGTVVEWKKKVGDYVKEDEVICIIETDKVSVDIRAPASGVITKIFAEEGDTVEVGAPLSEIDTGgap 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517189665 235 PGAGSAAKQSHSEGRPAPEAPKPAK----KQEASPKKAPAAKAPAETKPAKQATP-----GERTEKRVPMTRMRIRIAER 305
Cdd:PTZ00144 125 PAAAPAAAAAAKAEKTTPEKPKAAAptpePPAASKPTPPAAAKPPEPAPAAKPPPtpvarADPRETRVPMSRMRQRIAER 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517189665 306 LKDAQNTAASLTTFNEIDMSALMALRAKHKESFQEVHGVKLGFMSAFVKASVKALLDQPAVNAYIEGNEIVYHDYCDVSV 385
Cdd:PTZ00144 205 LKASQNTCAMLTTFNECDMSALMELRKEYKDDFQKKHGVKLGFMSAFVKASTIALKKMPIVNAYIDGDEIVYRNYVDISV 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517189665 386 AVATPTGLVVPVLRNCHQMSFAEVEQAIVTLGKKARDGQLALEDMAGGTFTISNGGVYGSLLGTPILNPPQSGILGMHGI 465
Cdd:PTZ00144 285 AVATPTGLVVPVIRNCENKSFAEIEKELADLAEKARNNKLTLEDMTGGTFTISNGGVFGSLMGTPIINPPQSAILGMHAI 364
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1517189665 466 FDRPVAVNGEIKIRPMMYVALTYDHRVIDGREAVTFLRKVKDCIEDPTRLLLDL 519
Cdd:PTZ00144 365 KKRPVVVGNEIVIRPIMYLALTYDHRLIDGRDAVTFLKKIKDLIEDPARMLLDL 418
|
|
| PRK05704 |
PRK05704 |
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase; |
54-519 |
0e+00 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
Pssm-ID: 235571 [Multi-domain] Cd Length: 407 Bit Score: 531.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517189665 54 INVPSMGDSITEGTISSWSVAEGDHVDADQVVCVIETDKVSVDVRAPEAGVVSKLLAKEGDEIAVGSPLFEISAGDSPAQ 133
Cdd:PRK05704 5 IKVPTLPESVTEATIATWHKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGDTVTVGQVLGRIDEGAAAGA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517189665 134 SKKSETKAAAPATNAPASSPGgpaktisvpsmgdsitegtvstwtAAEGESVDADqvvcvietdkvsvdvrAPEAGKIA- 212
Cdd:PRK05704 85 AAAAAAAAAAAAAAPAQAQAA------------------------AAAEQSNDAL----------------SPAARKLAa 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517189665 213 -KHLAASDevvkvgsplfelVPGPGA-GSAAKQSHSEGRPAPEAPKPAKKQEAspkkapaakapaetKPAKQATPGERTE 290
Cdd:PRK05704 125 eNGLDASA------------VKGTGKgGRVTKEDVLAALAAAAAAPAAPAAAA--------------PAAAPAPLGARPE 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517189665 291 KRVPMTRMRIRIAERLKDAQNTAASLTTFNEIDMSALMALRAKHKESFQEVHGVKLGFMSAFVKASVKALLDQPAVNAYI 370
Cdd:PRK05704 179 ERVPMTRLRKTIAERLLEAQNTTAMLTTFNEVDMTPVMDLRKQYKDAFEKKHGVKLGFMSFFVKAVVEALKRYPEVNASI 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517189665 371 EGNEIVYHDYCDVSVAVATPTGLVVPVLRNCHQMSFAEVEQAIVTLGKKARDGQLALEDMAGGTFTISNGGVYGSLLGTP 450
Cdd:PRK05704 259 DGDDIVYHNYYDIGIAVGTPRGLVVPVLRDADQLSFAEIEKKIAELAKKARDGKLSIEELTGGTFTITNGGVFGSLMSTP 338
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1517189665 451 ILNPPQSGILGMHGIFDRPVAVNGEIKIRPMMYVALTYDHRVIDGREAVTFLRKVKDCIEDPTRLLLDL 519
Cdd:PRK05704 339 IINPPQSAILGMHKIKERPVAVNGQIVIRPMMYLALSYDHRIIDGKEAVGFLVTIKELLEDPERLLLDL 407
|
|
| sucB |
TIGR01347 |
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ... |
53-519 |
0e+00 |
|
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: 517.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517189665 53 TINVPSMGDSITEGTISSWSVAEGDHVDADQVVCVIETDKVSVDVRAPEAGVVSKLLAKEGDEIAVGSPLFEISAGDSP- 131
Cdd:TIGR01347 2 EIKVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAILEEGNDAt 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517189665 132 -AQSKKSETKAAAPATNAPASSPGGPAKTISV-PSMGDSITEgtvstwtaaegESVDADQVVCVIETDKVSvdvrapeAG 209
Cdd:TIGR01347 82 aAPPAKSGEEKEETPAASAAAAPTAAANRPSLsPAARRLAKE-----------HGIDLSAVPGTGVTGRVT-------KE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517189665 210 KIAKHLAAsdevvkvgsplfelvpgpgagsaakqshsegRPAPEAPKPAKKqeaspkkapaakapaETKPAKQAtpgeRT 289
Cdd:TIGR01347 144 DIIKKTEA-------------------------------PASAQPPAAAAA---------------AAAPAAAT----RP 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517189665 290 EKRVPMTRMRIRIAERLKDAQNTAASLTTFNEIDMSALMALRAKHKESFQEVHGVKLGFMSAFVKASVKALLDQPAVNAY 369
Cdd:TIGR01347 174 EERVKMTRLRQRIAERLKEAQNSTAMLTTFNEVDMSAVMELRKRYKEEFEKKHGVKLGFMSFFVKAVVAALKRFPEVNAE 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517189665 370 IEGNEIVYHDYCDVSVAVATPTGLVVPVLRNCHQMSFAEVEQAIVTLGKKARDGQLALEDMAGGTFTISNGGVYGSLLGT 449
Cdd:TIGR01347 254 IDGDDIVYKDYYDISVAVSTDRGLVVPVVRNADRMSFADIEKEIADLGKKARDGKLTLEDMTGGTFTITNGGVFGSLMST 333
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517189665 450 PILNPPQSGILGMHGIFDRPVAVNGEIKIRPMMYVALTYDHRVIDGREAVTFLRKVKDCIEDPTRLLLDL 519
Cdd:TIGR01347 334 PIINPPQSAILGMHGIKERPVAVNGQIEIRPMMYLALSYDHRLIDGKEAVTFLVTIKELLEDPRRLLLDL 403
|
|
| PLN02226 |
PLN02226 |
2-oxoglutarate dehydrogenase E2 component |
151-519 |
3.37e-128 |
|
2-oxoglutarate dehydrogenase E2 component
Pssm-ID: 177871 [Multi-domain] Cd Length: 463 Bit Score: 381.80 E-value: 3.37e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517189665 151 SSPGGPAKTISVPSMGDSITEGTVSTWTAAEGESVDADQVVCVIETDKVSVDVRAPEAGKIAKHLAASDEVVKVGSPLFE 230
Cdd:PLN02226 85 SSESGDTVEAVVPHMGESITDGTLATFLKKPGERVQADEAIAQIETDKVTIDIASPASGVIQEFLVKEGDTVEPGTKVAI 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517189665 231 LvpGPGAGSAAKQSHSEGRPAPEAPKPAKKQEASPKKAPAAKAPAETK-------PAKQAT-----PGERTEKRVPMTRM 298
Cdd:PLN02226 165 I--SKSEDAASQVTPSQKIPETTDPKPSPPAEDKQKPKVESAPVAEKPkapssppPPKQSAkepqlPPKERERRVPMTRL 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517189665 299 RIRIAERLKDAQNTAASLTTFNEIDMSALMALRAKHKESFQEVHGVKLGFMSAFVKASVKALLDQPAVNAYIEGNEIVYH 378
Cdd:PLN02226 243 RKRVATRLKDSQNTFALLTTFNEVDMTNLMKLRSQYKDAFYEKHGVKLGLMSGFIKAAVSALQHQPVVNAVIDGDDIIYR 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517189665 379 DYCDVSVAVATPTGLVVPVLRNCHQMSFAEVEQAIVTLGKKARDGQLALEDMAGGTFTISNGGVYGSLLGTPILNPPQSG 458
Cdd:PLN02226 323 DYVDISIAVGTSKGLVVPVIRGADKMNFAEIEKTINGLAKKANEGTISIDEMAGGSFTVSNGGVYGSLISTPIINPPQSA 402
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1517189665 459 ILGMHGIFDRPVAVNGEIKIRPMMYVALTYDHRVIDGREAVTFLRKVKDCIEDPTRLLLDL 519
Cdd:PLN02226 403 ILGMHSIVSRPMVVGGSVVPRPMMYVALTYDHRLIDGREAVYFLRRVKDVVEDPQRLLLDI 463
|
|
| PRK11856 |
PRK11856 |
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed |
50-518 |
1.57e-114 |
|
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
Pssm-ID: 237001 [Multi-domain] Cd Length: 411 Bit Score: 344.85 E-value: 1.57e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517189665 50 GPKTINVPSMGDSITEGTISSWSVAEGDHVDADQVVCVIETDKVSVDVRAPEAGVVSKLLAKEGDEIAVGSPLFEISAGD 129
Cdd:PRK11856 1 MMFEFKMPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDVVPVGSVIAVIEEEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517189665 130 SPAQSKKSETKAAAPATNAPASSPGGPAKTisvpsmgdsitegtvstwTAAEGESVDADQVVCVIetdkvsvdvrAPEAG 209
Cdd:PRK11856 81 EAEAAAAAEAAPEAPAPEPAPAAAAAAAAA------------------PAAAAAPAAPAAAAAKA----------SPAVR 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517189665 210 KIAKHLaasdevvkvGSPLfELVPGPGAGSAAKQSHSEGRPAPEAPKPAkkqeaspkkapaakaPAETKPAKQATPGERT 289
Cdd:PRK11856 133 KLAREL---------GVDL-STVKGSGPGGRITKEDVEAAAAAAAPAAA---------------AAAAAAAAPPAAAAEG 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517189665 290 EKRVPMTRMRIRIAERLKDAQNTAASLTTFNEIDMSALMALRAKHKEsfqevHGVKLGFMSAFVKASVKALLDQPAVNAY 369
Cdd:PRK11856 188 EERVPLSGMRKAIAKRMVESKREIPHFTLTDEVDVTALLALRKQLKA-----IGVKLTVTDFLIKAVALALKKFPELNAS 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517189665 370 IEGNEIVYHDYCDVSVAVATPTGLVVPVLRNCHQMSFAEVEQAIVTLGKKARDGQLALEDMAGGTFTISNGGVYGSLLGT 449
Cdd:PRK11856 263 WDDDAIVLKKYVNIGIAVATDGGLIVPVIRDADKKSLFELAREIKDLAEKAREGKLKPEELQGGTFTISNLGMFGGDYFT 342
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1517189665 450 PILNPPQSGILGMHGIFDRPVAVNGEIKIRPMMYVALTYDHRVIDGREAVTFLRKVKDCIEDPTRLLLD 518
Cdd:PRK11856 343 PIINPPEVAILGVGAIVERPVVVDGEIVVRKVMPLSLSFDHRVIDGADAARFLKALKELLENPALLLLE 411
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
52-517 |
3.25e-113 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 346.04 E-value: 3.25e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517189665 52 KTINVPSMGDsITEGTISSWSVAEGDHVDADQVVCVIETDKVSVDVRAPEAGVVSKLLAKEGDEIAVGSPLFEISAGD-- 129
Cdd:PRK11855 3 IEFKVPDIGE-VVEVEVIEWLVKEGDTVEEDQPLVTVETDKATMEIPSPAAGVVKEIKVKVGDTVSVGGLLAVIEAAGaa 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517189665 130 ----------SPAQSKKSETKAAAPATNAPASSPGGPAKTISVPSMGDsITEGTVSTWTAAEGESVDADQVVCVIETDKV 199
Cdd:PRK11855 82 aaaaapaaaaAPAAAAAAAPAPAAAAPAAAAAAAGGGVVEVKVPDIGE-ITEVEVIEWLVKVGDTVEEDQSLITVETDKA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517189665 200 SVDVRAPEAGKIAKHLAASDEVVKVGSPLFEL-VPGPGAGSAAKQSHSEGRPAPEAPKPAKKQEASPKKAPAAKAPAETK 278
Cdd:PRK11855 161 TMEIPSPVAGVVKEIKVKVGDKVSVGSLLVVIeVAAAAPAAAAAPAAAAPAAAAAAAPAPAPAAAAAPAAAAPAAAAAPG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517189665 279 PAKQATPGER---------------TEK---------------------------------------------------- 291
Cdd:PRK11855 241 KAPHASPAVRrlarelgvdlsqvkgTGKkgritkedvqafvkgamsaaaaaaaaaaaagggglgllpwpkvdfskfgeie 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517189665 292 RVPMTRMRIRIAERLKDAQNTAASLTTFNEIDMSALMALRAKHKESFqEVHGVKLGFMSAFVKASVKALLDQPAVNAYI- 370
Cdd:PRK11855 321 TKPLSRIKKISAANLHRSWVTIPHVTQFDEADITDLEALRKQLKKEA-EKAGVKLTMLPFFIKAVVAALKEFPVFNASLd 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517189665 371 -EGNEIVYHDYCDVSVAVATPTGLVVPVLRNCHQMSFAEVEQAIVTLGKKARDGQLALEDMAGGTFTISNGGVYGSLLGT 449
Cdd:PRK11855 400 eDGDELTYKKYFNIGFAVDTPNGLVVPVIKDVDKKSLLEIAREIAELAKKARDGKLKPDDMQGGCFTISSLGGIGGTAFT 479
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1517189665 450 PILNPPQSGILGMHGIFDRPVAVNGEIKIRPMMYVALTYDHRVIDGREAVTFLRKVKDCIEDPTRLLL 517
Cdd:PRK11855 480 PIINAPEVAILGVGKSQMKPVWDGKEFVPRLMLPLSLSYDHRVIDGATAARFTNYLKQLLADPRRMLL 547
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
306-516 |
2.20e-95 |
|
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: 288.29 E-value: 2.20e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517189665 306 LKDAQNTAASLTTFNEIDMSALMALRAKHKESFQEvHGVKLGFMSAFVKASVKALLDQPAVNAYIEGN--EIVYHDYCDV 383
Cdd:pfam00198 1 MTESKQTIPHFTLTDEVDVTELLALREELKEDAAD-EETKLTFLPFLVKAVALALKKFPELNASWDGEegEIVYKKYVNI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517189665 384 SVAVATPTGLVVPVLRNCHQMSFAEVEQAIVTLGKKARDGQLALEDMAGGTFTISNGGVYGSLLGTPILNPPQSGILGMH 463
Cdd:pfam00198 80 GIAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVG 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1517189665 464 GIFDRPVAVNGEIKIRPMMYVALTYDHRVIDGREAVTFLRKVKDCIEDPTRLL 516
Cdd:pfam00198 160 RIRKRPVVVDGEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELLL 212
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
52-517 |
8.67e-94 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 298.45 E-value: 8.67e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517189665 52 KTINVPSMGDsiTEGTISSWSVAEGDHVDADQVVCVIETDKVSVDVRAPEAGVVSKLLAKEGDEIAVGSPL--FEIsAGD 129
Cdd:PRK11854 106 KDVHVPDIGS--DEVEVTEILVKVGDTVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVSTGSLImvFEV-AGE 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517189665 130 SPAqskkSETKAAAPATNAPASSPGGPAKTISVPSMGDsiTEGTVSTWTAAEGESVDADQVVCVIETDKVSVDVRAPEAG 209
Cdd:PRK11854 183 APA----AAPAAAEAAAPAAAPAAAAGVKDVNVPDIGG--DEVEVTEVMVKVGDKVEAEQSLITVEGDKASMEVPAPFAG 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517189665 210 KIAKHLAASDEVVKVGSPLFELVPGPGAGSAAKQSHSEGRPAPEAPKPAKKQEASPKKAPAAKAPAETKPAKQATP---- 285
Cdd:PRK11854 257 TVKEIKVNVGDKVKTGSLIMRFEVEGAAPAAAPAKQEAAAPAPAAAKAEAPAAAPAAKAEGKSEFAENDAYVHATPlvrr 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517189665 286 ----------------------------------------------------------------GERTEkrVPMTRMRIR 301
Cdd:PRK11854 337 larefgvnlakvkgtgrkgrilkedvqayvkdavkraeaapaaaaaggggpgllpwpkvdfskfGEIEE--VELGRIQKI 414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517189665 302 IAERLKDAQNTAASLTTFNEIDMSALMALR-AKHKESFQEVHGVKLGFMSAFVKASVKALLDQPAVNAYI--EGNEIVYH 378
Cdd:PRK11854 415 SGANLHRNWVMIPHVTQFDKADITELEAFRkQQNAEAEKRKLGVKITPLVFIMKAVAAALEQMPRFNSSLseDGQRLTLK 494
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517189665 379 DYCDVSVAVATPTGLVVPVLRNCHQMSFAEVEQAIVTLGKKARDGQLALEDMAGGTFTISNGGVYGSLLGTPILNPPQSG 458
Cdd:PRK11854 495 KYVNIGIAVDTPNGLVVPVFKDVNKKGIIELSRELMDISKKARDGKLTAGDMQGGCFTISSIGGLGTTHFTPIVNAPEVA 574
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1517189665 459 ILGMHGIFDRPVAVNGEIKIRPMMYVALTYDHRVIDGREAVTFLRKVKDCIEDPTRLLL 517
Cdd:PRK11854 575 ILGVSKSAMEPVWNGKEFAPRLMLPLSLSYDHRVIDGADGARFITIINDRLSDIRRLVL 633
|
|
| SucB_Actino |
TIGR02927 |
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model ... |
53-511 |
6.60e-93 |
|
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: 294.61 E-value: 6.60e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517189665 53 TINVPSMGDSITEGTISSWSVAEGDHVDADQVVCVIETDKVSVDVRAPEAGVVSKLLAKEGDEIAVGSPLFEI------- 125
Cdd:TIGR02927 4 SVKMPALGESVTEGTVTSWLKAVGDTVEADEPLLEVSTDKVDTEIPSPAAGVLLEIRAPEDDTVEVGGVLAIIgepgeag 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517189665 126 --SAGDSPAQSKKSETKAAAPATNAPASSP---------GGPAKTISVPSMGDSITEGTVSTWTAAEGESVDADQVVCVI 194
Cdd:TIGR02927 84 sePAPAAPEPEAAPEPEAPAPAPTPAAEAPapaapqaggSGEATEVKMPELGESVTEGTVTSWLKAVGDTVEVDEPLLEV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517189665 195 ETDKVSVDVRAPEAGKIAKHLAASDEVVKVGS---------------------PLFELVPGPGAGSAAKQSHSEGRPAPE 253
Cdd:TIGR02927 164 STDKVDTEIPSPVAGTLLEIRAPEDDTVEVGTvlaiigdanaapaepaeeeapAPSEAGSEPAPDPAARAPHAAPDPPAP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517189665 254 APKPAKK---------------------------------------------------------QEASPKKAPAAKAPAE 276
Cdd:TIGR02927 244 APAPAKTaapaaaapvssgdsgpyvtplvrklakdkgvdlstvkgtgvggrirkqdvlaaakaaEEARAAAAAPAAAAAP 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517189665 277 TKPAKQATPGE--------RTEKrvpMTRMRIRIAERLKDAQNTAASLTTFNEIDMSALMALRAKHKESFQEVHGVKLGF 348
Cdd:TIGR02927 324 AAPAAAAKPAEpdtaklrgTTQK---MNRIRQITADKTIESLQTSAQLTQVHEVDMTRVAALRARAKNDFLEKNGVNLTF 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517189665 349 MSAFVKASVKALLDQPAVNAYI--EGNEIVYHDYCDVSVAVATPTGLVVPVLRNCHQMSFAEVEQAIVTLGKKARDGQLA 426
Cdd:TIGR02927 401 LPFFVQAVTEALKAHPNVNASYnaETKEVTYHDVEHVGIAVDTPRGLLVPVIHNAGDLSLPGLAKAINDLAARARDNKLK 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517189665 427 LEDMAGGTFTISNGGVYGSLLGTPILNPPQSGILGMHGIFDRPVAVNGE-----IKIRPMMYVALTYDHRVIDGREAVTF 501
Cdd:TIGR02927 481 PDELSGGTFTITNIGSGGALFDTPILNPPQAAILGTGAIVKRPRVIKDEdggesIAIRSVCYLPLTYDHRLVDGADAGRF 560
|
570
....*....|
gi 1517189665 502 LRKVKDCIED 511
Cdd:TIGR02927 561 LTTIKKRLEE 570
|
|
| PDHac_trf_mito |
TIGR01349 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
54-517 |
1.42e-71 |
|
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: 234.69 E-value: 1.42e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517189665 54 INVPSMGDSITEGTISSWSVAEGDHVDADQVVCVIETDKVSVDVRAPEAGVVSKLLAKEGDE-IAVGSPLFEISAGDSPA 132
Cdd:TIGR01349 2 ITMPALSPTMTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEGTKdVPVNKPIAVLVEEKEDV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517189665 133 QSKKSETKAAAPATNAPASSPGGPAKTISVPSMGDSITEGTVSTWTAAEGESVDADQVVCVietdkvsvdvrAPEAGKIA 212
Cdd:TIGR01349 82 ADAFKNYKLESSASPAPKPSEIAPTAPPSAPKPSPAPQKQSPEPSSPAPLSDKESGDRIFA-----------SPLAKKLA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517189665 213 KHLAASDEVVKvGSplfelvpGPGaGSAAKQSHSEGRPAPEAPKPAKKQEASPKkapaakapaETKPAKQATPGERTEkr 292
Cdd:TIGR01349 151 KEKGIDLSAVA-GS-------GPN-GRIVKKDIESFVPQSPASANQQAAATTPA---------TYPAAAPVSTGSYED-- 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517189665 293 VPMTRMRIRIAERLKDAQNTAASLTTFNEIDMSALMALRAKHKESFQEVhgVKLGFMSAFVKASVKALLDQPAVNAYIEG 372
Cdd:TIGR01349 211 VPLSNIRKIIAKRLLESKQTIPHYYVSIECNVDKLLALRKELNAMASEV--YKLSVNDFIIKASALALREVPEANSSWTD 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517189665 373 NEIVYHDYCDVSVAVATPTGLVVPVLRNCHQMSFAEVEQAIVTLGKKARDGQLALEDMAGGTFTISNGGVYGSLLGTPIL 452
Cdd:TIGR01349 289 NFIRRYKNVDISVAVATPDGLITPIVRNADAKGLSTISNEIKDLAKRARNNKLKPEEFQGGTFTISNLGMFGIKDFTAII 368
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1517189665 453 NPPQSGILGMHGIFDRPVAVNGE---IKIRPMMYVALTYDHRVIDGREAVTFLRKVKDCIEDPTRLLL 517
Cdd:TIGR01349 369 NPPQACILAVGAVEDVAVVDNDEekgFAVASIMSVTLSCDHRVIDGAVGAEFLKSFKKYLENPIEMLL 436
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
52-517 |
5.41e-61 |
|
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: 209.73 E-value: 5.41e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517189665 52 KTINVPSMGDSiTEGTISSWSVAEGDHVDADQVVCVIETDKVSVDVRAPEAGVVSKLLAKEGDEIAVGSPLFEISAGD-- 129
Cdd:TIGR01348 1 TEIKVPDIGDN-EEGEVIEVLVKPGDKVEAGQSLITLESDKASMEVPSSAAGIIKEIKVKVGDTLPVGGVIATLEVGAga 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517189665 130 -SPAQSKKSETKAAAPATNAPASS--------PGGPAKTISVPSMGDsITEGTVSTWTAAEGESVDADQVVCVIETDKVS 200
Cdd:TIGR01348 80 qAQAEAKKEAAPAPTAGAPAPAAQaqaapaagQSSGVQEVTVPDIGD-IEKVTVIEVLVKVGDTVSADQSLITLESDKAS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517189665 201 VDVRAPEAGKIAKHLAASDEVVKVGSPLFEL---------VPGPGAGSAAKQSHSEGRPAPEAPKPAKKQEASPKKAPAA 271
Cdd:TIGR01348 159 MEVPAPASGVVKSVKVKVGDSVPTGDLILTLsvagstpatAPAPASAQPAAQSPAATQPEPAAAPAAAKAQAPAPQQAGT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517189665 272 KAPAETKPAKQA----------------------------------TPGERTE--------------------------- 290
Cdd:TIGR01348 239 QNPAKVDHAAPAvrrlarefgvdlsavkgtgikgrilredvqrfvkEPSVRAQaaaasaaggapgalpwpnvdfskfgev 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517189665 291 KRVPMTRMRIRIAERLKDAQNTAASLTTFNEIDMSALMALRAKHKESfQEVHGVKLGFMSAFVKASVKALLDQPAVNAYI 370
Cdd:TIGR01348 319 EEVDMSRIRKISGANLTRNWTMIPHVTHFDKADITEMEAFRKQQNAA-VEKEGVKLTVLHILMKAVAAALKKFPKFNASL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517189665 371 E--GNEIVYHDYCDVSVAVATPTGLVVPVLRNCHQMSFAEVEQAIVTLGKKARDGQLALEDMAGGTFTISNGGVYGSLLG 448
Cdd:TIGR01348 398 DlgGEQLILKKYVNIGVAVDTPNGLLVPVIKDVDRKGITELALELSDLAKKARDGKLTPDEMQGACFTISSLGGIGGTAF 477
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1517189665 449 TPILNPPQSGILGMHGIFDRPVAVNGEIKIRPMMYVALTYDHRVIDGREAVTFLRKVKDCIEDPTRLLL 517
Cdd:TIGR01348 478 TPIVNAPEVAILGVSKSGMEPVWNGKEFEPRLMLPLSLSYDHRVIDGADAARFTTYICESLADIRRLLL 546
|
|
| PRK14843 |
PRK14843 |
dihydrolipoamide acetyltransferase; Provisional |
258-517 |
2.62e-52 |
|
dihydrolipoamide acetyltransferase; Provisional
Pssm-ID: 184847 [Multi-domain] Cd Length: 347 Bit Score: 181.26 E-value: 2.62e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517189665 258 AKKQEASPKKAPAAKAPAETKPAKqATPGERTEkRVPMTRMRIRIAERLKDAQNTAASLTTFNEIDMSALMALRAKHKES 337
Cdd:PRK14843 88 PENIENDSIKSPAQIEKVEEVPDN-VTPYGEIE-RIPMTPMRKVIAQRMVESYLTAPTFTLNYEVDMTEMLALRKKVLEP 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517189665 338 FQEVHGVKLGFMSAFVKASVKALLDQPAVNAYI--EGNEIVYHDYCDVSVAVATPTGLVVPVLRNCHQMSFAEVEQAIVT 415
Cdd:PRK14843 166 IMEATGKKTTVTDLLSLAVVKTLMKHPYINASLteDGKTIITHNYVNLAMAVGMDNGLMTPVVYNAEKMSLSELVVAFKD 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517189665 416 LGKKARDGQLALEDMAGGTFTISNGGVYGSLLGTPILNPPQSGILGMHGIFDRPVAVNGEIKIRPMMYVALTYDHRVIDG 495
Cdd:PRK14843 246 VIGRTLDGKLAPSELQNSTFTISNLGMFGVQSFGPIINQPNSAILGVSSTIEKPVVVNGEIVIRPIMSLGLTIDHRVVDG 325
|
250 260
....*....|....*....|..
gi 1517189665 496 REAVTFLRKVKDCIEDPTRLLL 517
Cdd:PRK14843 326 MAGAKFMKDLKELIETPISMLI 347
|
|
| PRK11857 |
PRK11857 |
dihydrolipoamide acetyltransferase; Reviewed |
252-515 |
8.66e-45 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237002 [Multi-domain] Cd Length: 306 Bit Score: 159.96 E-value: 8.66e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517189665 252 PEAPKPAKKQEASPKKAPaakapaETKPAKQATPGERTEKRVPMTRMRIRIAERLKDAQNTAASLTTFNEIDMSALMALR 331
Cdd:PRK11857 44 KSAPTPAEAASVSSAQQA------AKTAAPAAAPPKLEGKREKVAPIRKAIARAMTNSWSNVAYVNLVNEIDMTKLWDLR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517189665 332 AKHKESFQEVHGVKLGFMSAFVKASVKALLDQPAVNA-YIEGN-EIVYHDYCDVSVAVATPTGLVVPVLRNCHQMSFAEV 409
Cdd:PRK11857 118 KSVKDPVLKTEGVKLTFLPFIAKAILIALKEFPIFAAkYDEATsELVYPDTLNLGIAVDTEAGLMVPVIKNAQKLSIVEI 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517189665 410 EQAIVTLGKKARDGQLALEDMAGGTFTISNGGVYGSLLGTPILNPPQSGILGMHGIFDRPVAVNGEIKIRPMMYVALTYD 489
Cdd:PRK11857 198 AKEISRLAKAARERKIKPDEMKGGSFTITNYGSVGSLYGVPVINYPELAIAGVGAIIDKAIVKNGQIVAGKVMHLTVAAD 277
|
250 260
....*....|....*....|....*.
gi 1517189665 490 HRVIDGREAVTFLRKVKDCIEDPTRL 515
Cdd:PRK11857 278 HRWIDGATIGRFASRVKELLEKPEIL 303
|
|
| PLN02528 |
PLN02528 |
2-oxoisovalerate dehydrogenase E2 component |
60-519 |
3.83e-43 |
|
2-oxoisovalerate dehydrogenase E2 component
Pssm-ID: 215289 [Multi-domain] Cd Length: 416 Bit Score: 158.34 E-value: 3.83e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517189665 60 GDSITEGTISSWSVAEGDHVDADQVVCVIETDKVSVDVRAPEAGVVSKLLAKEGDEIAVGSPLFEISAGDSPAQSKKSET 139
Cdd:PLN02528 7 GEGIAECELLRWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGKVAQINFSPGDIVKVGETLLKIMVEDSQHLRSDSLL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517189665 140 KaaapatnapaSSPGGPAKTISVPSMGDSITEGTVSTWTA---AEGESVDadqvvcvietdkVSVDVRAPEAGKIAKH-- 214
Cdd:PLN02528 87 L----------PTDSSNIVSLAESDERGSNLSGVLSTPAVrhlAKQYGID------------LNDILGTGKDGRVLKEdv 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517189665 215 --LAASDEVVKvgsplfelvpgpgagsaakqshsegrpapeapkpaKKQEASPKKAPAAKAPAETKPAKQATPGErtEKR 292
Cdd:PLN02528 145 lkYAAQKGVVK-----------------------------------DSSSAEEATIAEQEEFSTSVSTPTEQSYE--DKT 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517189665 293 VPmtrmrIRIAERLK-DAQNTAASLTTF---NEIDMSALMALRAKHKESfQEVHGVKLGFMSAFVKASVKALLDQPAVNA 368
Cdd:PLN02528 188 IP-----LRGFQRAMvKTMTAAAKVPHFhyvEEINVDALVELKASFQEN-NTDPTVKHTFLPFLIKSLSMALSKYPLLNS 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517189665 369 YIEG--NEIVYHDYCDVSVAVATPTGLVVPVLRNCHQMSFAEVEQAIVTLGKKARDGQLALEDMAGGTFTISNGGVYGSL 446
Cdd:PLN02528 262 CFNEetSEIRLKGSHNIGVAMATEHGLVVPNIKNVQSLSLLEITKELSRLQHLAAENKLNPEDITGGTITLSNIGAIGGK 341
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1517189665 447 LGTPILNPPQSGILGMHGIFDRPVAVN-GEIKIRPMMYVALTYDHRVIDGREAVTFLRKVKDCIEDPTRLLLDL 519
Cdd:PLN02528 342 FGSPVLNLPEVAIIALGRIQKVPRFVDdGNVYPASIMTVTIGADHRVLDGATVARFCNEWKSYVEKPELLMLHM 415
|
|
| PLN02744 |
PLN02744 |
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex |
39-517 |
2.78e-41 |
|
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
Pssm-ID: 215397 [Multi-domain] Cd Length: 539 Bit Score: 155.78 E-value: 2.78e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517189665 39 SSLPSARWLSTGP-----KTINVPSMGDSITEGTISSWSVAEGDHVDADQVVCVIETDKVSVDVRAPEAGVVSKLLAKEG 113
Cdd:PLN02744 95 SQMQSARGFSSSSdlpphQEIGMPSLSPTMTEGNIARWLKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVKGDG 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517189665 114 -DEIAVGSPL---------------FEISAGDSPAQSKKSET----KAAAPATNAPASSPGGPaKTISVPSMGDSITegt 173
Cdd:PLN02744 175 aKEIKVGEVIaitveeeedigkfkdYKPSSSAAPAAPKAKPSppppKEEEVEKPASSPEPKAS-KPSAPPSSGDRIF--- 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517189665 174 vstwtaaegesvdadqvvcvietdkvsvdvrapeAGKIAKHLAASDEVvkvgsPLfelvpgpgagSAAKQSHSEGRPApe 253
Cdd:PLN02744 251 ----------------------------------ASPLARKLAEDNNV-----PL----------SSIKGTGPDGRIV-- 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517189665 254 apkpakKQEASPKKAPAAKAPAETKPAKQATPG-ERTEkrVPMTRMRIRIAERLKDAQNTAAS--LTTFNEIDmsALMAL 330
Cdd:PLN02744 280 ------KADIEDYLASGGKGATAPPSTDSKAPAlDYTD--IPNTQIRKVTASRLLQSKQTIPHyyLTVDTRVD--KLMAL 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517189665 331 RAKhKESFQEVHGVKLGFMSAFV-KASVKALLDQPAVNAYIEGNEIVYHDYCDVSVAVATPTGLVVPVLRNCHQMSFAEV 409
Cdd:PLN02744 350 RSQ-LNSLQEASGGKKISVNDLViKAAALALRKVPQCNSSWTDDYIRQYHNVNINVAVQTENGLYVPVVKDADKKGLSTI 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517189665 410 EQAIVTLGKKARDGQLALEDMAGGTFTISN-GGVYGSLLGTPILNPPQSGILGMHGIFDR--PVAVNGEIKIRPMMYVAL 486
Cdd:PLN02744 429 AEEVKQLAQKARENSLKPEDYEGGTFTVSNlGGPFGIKQFCAIINPPQSAILAVGSAEKRviPGSGPDQYNFASFMSVTL 508
|
490 500 510
....*....|....*....|....*....|.
gi 1517189665 487 TYDHRVIDGREAVTFLRKVKDCIEDPTRLLL 517
Cdd:PLN02744 509 SCDHRVIDGAIGAEWLKAFKGYIENPESMLL 539
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
52-125 |
1.04e-29 |
|
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: 110.96 E-value: 1.04e-29
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1517189665 52 KTINVPSMGDSITEGTISSWSVAEGDHVDADQVVCVIETDKVSVDVRAPEAGVVSKLLAKEGDEIAVGSPLFEI 125
Cdd:cd06849 1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
51-125 |
2.55e-27 |
|
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: 104.76 E-value: 2.55e-27
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1517189665 51 PKTINVPSMGDSITEGTISSWSVAEGDHVDADQVVCVIETDKVSVDVRAPEAGVVSKLLAKEGDEIAVGSPLFEI 125
Cdd:COG0508 2 AIEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
158-231 |
1.66e-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: 96.70 E-value: 1.66e-24
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1517189665 158 KTISVPSMGDSITEGTVSTWTAAEGESVDADQVVCVIETDKVSVDVRAPEAGKIAKHLAASDEVVKVGSPLFEL 231
Cdd:cd06849 1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
157-232 |
1.44e-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: 91.28 E-value: 1.44e-22
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1517189665 157 AKTISVPSMGDSITEGTVSTWTAAEGESVDADQVVCVIETDKVSVDVRAPEAGKIAKHLAASDEVVKVGSPLFELV 232
Cdd:COG0508 2 AIEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVIA 77
|
|
| kgd |
PRK12270 |
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ... |
233-505 |
2.28e-22 |
|
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;
Pssm-ID: 237030 [Multi-domain] Cd Length: 1228 Bit Score: 101.51 E-value: 2.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517189665 233 PGPGAGSAAKQSHSEGRPAPEAPKPAKKQEASPKKAPAAKAPAETKPAKQATPGERTEKRVPMTRMRIRIAErlkdaqNT 312
Cdd:PRK12270 58 PAAAPAAKAPAAPAPAPPAAAAPAAPPKPAAAAAAAAAPAAPPAAAAAAAPAAAAVEDEVTPLRGAAAAVAK------NM 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517189665 313 AASL-----TTFNEIDMSALMALRAKHKESFQEVHGVKLGFMSAFVKASVKALLDQPAVNAY---IEGN-EIVYHDYCDV 383
Cdd:PRK12270 132 DASLevptaTSVRAVPAKLLIDNRIVINNHLKRTRGGKVSFTHLIGYALVQALKAFPNMNRHyaeVDGKpTLVTPAHVNL 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517189665 384 SVA--VATPTG---LVVPVLRNCHQMSFAEVEQAIVTLGKKARDGQLALEDMAGGTFTISNGGVYGSLLGTPILNPPQSG 458
Cdd:PRK12270 212 GLAidLPKKDGsrqLVVPAIKGAETMDFAQFWAAYEDIVRRARDGKLTADDFQGTTISLTNPGGIGTVHSVPRLMKGQGA 291
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1517189665 459 ILGMhGIFDRPVAVNG-------EIKIRPMMYVALTYDHRVIDGREAVTFLRKV 505
Cdd:PRK12270 292 IIGV-GAMEYPAEFQGaseerlaELGISKVMTLTSTYDHRIIQGAESGEFLRTI 344
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
52-125 |
8.25e-20 |
|
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: 83.42 E-value: 8.25e-20
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1517189665 52 KTINVPSMGDSITEGtISSWSVAEGDHVDADQVVCVIETDKVSVDVRAPEAGVVSKLLAKEGDEIAVGSPLFEI 125
Cdd:pfam00364 1 TEIKSPMIGESVREG-VVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
158-231 |
1.95e-14 |
|
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: 68.01 E-value: 1.95e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1517189665 158 KTISVPSMGDSITEGtVSTWTAAEGESVDADQVVCVIETDKVSVDVRAPEAGKIAKHLAASDEVVKVGSPLFEL 231
Cdd:pfam00364 1 TEIKSPMIGESVREG-VVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
66-125 |
2.30e-14 |
|
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: 67.83 E-value: 2.30e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517189665 66 GTISSWSVAEGDHVDADQVVCVIETDKVSVDVRAPEAGVVSKLLAKEGDEIAVGSPLFEI 125
Cdd:cd06850 8 GTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
52-131 |
4.72e-14 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 73.82 E-value: 4.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517189665 52 KTINVPSMGDSITEGTISSWSVAEGDHVDADQVVCVIETDKVSVDVRAPEAGVVSKLLAKEGDEIAVGSPLFEISAGDSP 131
Cdd:PRK14875 3 TPITMPKWGLSMTEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGETLPVGALLAVVADAEVS 82
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
53-125 |
1.13e-12 |
|
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases, and the H-protein of the glycine cleavage system (GCS). These domains transport CO2, acyl, or methylamine, respectively, between components of the complex/protein via a biotinyl or lipoyl group, which is covalently attached to a highly conserved lysine residue.
Pssm-ID: 133456 [Multi-domain] Cd Length: 73 Bit Score: 63.23 E-value: 1.13e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1517189665 53 TINVPSMGDSITEGTISSWSVAEGDHVDADQVVCVIETDKVSVDVRAPEAGVVSKLLAKEGDEIAVGSPLFEI 125
Cdd:cd06663 1 TILIPDLAQHLGDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKVEGDTPLVKI 73
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
160-309 |
2.39e-11 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 65.71 E-value: 2.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517189665 160 ISVPSMGDSITEGTVSTWTAAEGESVDADQVVCVIETDKVSVDVRAPEAGKIAKHL-AASDEVVKVGSPLFELVpgpGAG 238
Cdd:PRK11892 5 ILMPALSPTMEEGTLAKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKILvPEGTEGVKVNTPIAVLL---EEG 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1517189665 239 SAAKQSHSEGRPAPEAPKPAKKQEASPKKAPAAKAPAETKPAKQATPGERTEKR-VPMTRMRIRiaERLKDA 309
Cdd:PRK11892 82 ESASDAGAAPAAAAEAAAAAPAAAAAAAAKKAAPAPAAPAAPAAEVAADPDIPAgTEMVTMTVR--EALRDA 151
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
156-241 |
3.98e-11 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 64.58 E-value: 3.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517189665 156 PAKTISVPSMGDSITEGTVSTWTAAEGESVDADQVVCVIETDKVSVDVRAPEAGKIAKHLAASDEVVKVGSPLFELVPGP 235
Cdd:PRK14875 1 SITPITMPKWGLSMTEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGETLPVGALLAVVADAE 80
|
....*.
gi 1517189665 236 GAGSAA 241
Cdd:PRK14875 81 VSDAEI 86
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
159-231 |
1.09e-10 |
|
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: 57.45 E-value: 1.09e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1517189665 159 TISVPSMGDSITEGTVSTWTAAEGESVDADQVVCVIETDKVSVDVRAPEAGKIAKHLAASDEVVKVGSPLFEL 231
Cdd:cd06663 1 TILIPDLAQHLGDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKVEGDTPLVKI 73
|
|
| AccB |
COG0511 |
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ... |
73-125 |
1.25e-10 |
|
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: 59.14 E-value: 1.25e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1517189665 73 VAEGDHVDADQVVCVIETDKVSVDVRAPEAGVVSKLLAKEGDEIAVGSPLFEI 125
Cdd:COG0511 83 VKVGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVVEILVENGQPVEYGQPLFVI 135
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
54-163 |
5.48e-10 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 61.47 E-value: 5.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517189665 54 INVPSMGDSITEGTISSWSVAEGDHVDADQVVCVIETDKVSVDVRAPEAGVVSKLLAKEGDE-IAVGSPLFEI-----SA 127
Cdd:PRK11892 5 ILMPALSPTMEEGTLAKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKILVPEGTEgVKVNTPIAVLleegeSA 84
|
90 100 110
....*....|....*....|....*....|....*.
gi 1517189665 128 GDSPAQSKKSETKAAAPATNAPASSPGGPAKTISVP 163
Cdd:PRK11892 85 SDAGAAPAAAAEAAAAAPAAAAAAAAKKAAPAPAAP 120
|
|
| PRK09282 |
PRK09282 |
pyruvate carboxylase subunit B; Validated |
66-125 |
8.49e-10 |
|
pyruvate carboxylase subunit B; Validated
Pssm-ID: 236449 [Multi-domain] Cd Length: 592 Bit Score: 61.01 E-value: 8.49e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517189665 66 GTISSWSVAEGDHVDADQVVCVIETDKVSVDVRAPEAGVVSKLLAKEGDEIAVGSPLFEI 125
Cdd:PRK09282 531 GTVVKVKVKEGDKVKAGDTVLVLEAMKMENEIQAPVDGTVKEILVKEGDRVNPGDVLMEI 590
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
172-231 |
3.92e-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: 52.80 E-value: 3.92e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517189665 172 GTVSTWTAAEGESVDADQVVCVIETDKVSVDVRAPEAGKIAKHLAASDEVVKVGSPLFEL 231
Cdd:cd06850 8 GTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| PRK14040 |
PRK14040 |
oxaloacetate decarboxylase subunit alpha; |
66-126 |
9.30e-09 |
|
oxaloacetate decarboxylase subunit alpha;
Pssm-ID: 237592 [Multi-domain] Cd Length: 593 Bit Score: 58.02 E-value: 9.30e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1517189665 66 GTISSWSVAEGDHVDADQVVCVIETDKVSVDVRAPEAGVVSKLLAKEGDEIAVGSPLFEIS 126
Cdd:PRK14040 533 GNIFKVIVTEGQTVAEGDVLLILEAMKMETEIRAAQAGTVRGIAVKEGDAVAVGDTLLTLA 593
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
66-125 |
2.50e-07 |
|
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: 53.54 E-value: 2.50e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517189665 66 GTISSWSVAEGDHVDADQVVCVIETDKVSVDVRAPEAGVVSKLLAKEGDEIAVGSPLFEI 125
Cdd:COG1038 1085 GTVVKVLVKEGDEVKKGDPLLTIEAMKMETTITAPRDGTVKEVLVKEGDQVEAGDLLIEL 1144
|
|
| PRK05641 |
PRK05641 |
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
34-125 |
8.70e-07 |
|
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235540 [Multi-domain] Cd Length: 153 Bit Score: 48.71 E-value: 8.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517189665 34 PRAVRSSLPSARWLSTGPKTINVPsmgdsiTEGTISSWSVAEGDHVDADQVVCVIETDKVSVDVRAPEAGVVSKLLAKEG 113
Cdd:PRK05641 67 PTPVAPAAPAPAPASAGENVVTAP------MPGKILRILVREGQQVKVGQGLLILEAMKMENEIPAPKDGVVKKILVKEG 140
|
90
....*....|..
gi 1517189665 114 DEIAVGSPLFEI 125
Cdd:PRK05641 141 DTVDTGQPLIEL 152
|
|
| PRK07051 |
PRK07051 |
biotin carboxyl carrier domain-containing protein; |
73-127 |
1.12e-06 |
|
biotin carboxyl carrier domain-containing protein;
Pssm-ID: 180811 [Multi-domain] Cd Length: 80 Bit Score: 46.54 E-value: 1.12e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1517189665 73 VAEGDHVDADQVVCVIETDKVSVDVRAPEAGVVSKLLAKEGDEIAVGSPLFEISA 127
Cdd:PRK07051 26 VEVGDAVAAGDVVGLIEVMKQFTEVEAEAAGRVVEFLVEDGEPVEAGQVLARIEE 80
|
|
| AccB |
COG0511 |
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ... |
181-231 |
1.33e-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: 1.33e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1517189665 181 EGESVDADQVVCVIETDKVSVDVRAPEAGKIAKHLAASDEVVKVGSPLFEL 231
Cdd:COG0511 85 VGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVVEILVENGQPVEYGQPLFVI 135
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
66-126 |
6.84e-06 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 48.98 E-value: 6.84e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1517189665 66 GTISSWSVAEGDHVDADQVVCVIETDKVSVDVRAPEAGVVSKLLAKEGDEIAVGSPLFEIS 126
Cdd:PRK12999 1085 GSVVTVLVKEGDEVKAGDPLAVIEAMKMETTITAPVDGTVKRVLVKAGDQVEAGDLLVELE 1145
|
|
| PRK14042 |
PRK14042 |
pyruvate carboxylase subunit B; Provisional |
66-125 |
1.11e-05 |
|
pyruvate carboxylase subunit B; Provisional
Pssm-ID: 172536 [Multi-domain] Cd Length: 596 Bit Score: 48.18 E-value: 1.11e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517189665 66 GTISSWSVAEGDHVDADQVVCVIETDKVSVDVRAPEAGVVSKLLAKEGDEIAVGSPLFEI 125
Cdd:PRK14042 534 GSIIAIHVSAGDEVKAGQAVLVIEAMKMETEIKAPANGVVAEILCQKGDKVTPGQVLIRV 593
|
|
| PLN02983 |
PLN02983 |
biotin carboxyl carrier protein of acetyl-CoA carboxylase |
73-125 |
1.05e-04 |
|
biotin carboxyl carrier protein of acetyl-CoA carboxylase
Pssm-ID: 215533 [Multi-domain] Cd Length: 274 Bit Score: 44.06 E-value: 1.05e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1517189665 73 VAEGDHVDADQVVCVIETDKVSVDVRAPEAGVVSKLLAKEGDEIAVGSPLFEI 125
Cdd:PLN02983 220 VKVGDKVQKGQVVCIIEAMKLMNEIEADQSGTIVEILAEDGKPVSVDTPLFVI 272
|
|
| PRK08225 |
PRK08225 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
73-126 |
1.18e-04 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 181304 [Multi-domain] Cd Length: 70 Bit Score: 40.54 E-value: 1.18e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1517189665 73 VAEGDHVDADQVVCVIETDKVSVDVRAPEAGVVSKLLAKEGDEIAVGSPLFEIS 126
Cdd:PRK08225 17 VKVGDTVEEGQDVVILESMKMEIPIVAEEAGTVKKINVQEGDFVNEGDVLLEIE 70
|
|
| PRK09282 |
PRK09282 |
pyruvate carboxylase subunit B; Validated |
172-233 |
2.70e-04 |
|
pyruvate carboxylase subunit B; Validated
Pssm-ID: 236449 [Multi-domain] Cd Length: 592 Bit Score: 43.68 E-value: 2.70e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1517189665 172 GTVSTWTAAEGESVDADQVVCVIETDKVSVDVRAPEAGKIAKHLAASDEVVKVGSPLFELVP 233
Cdd:PRK09282 531 GTVVKVKVKEGDKVKAGDTVLVLEAMKMENEIQAPVDGTVKEILVKEGDRVNPGDVLMEIEP 592
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
96-194 |
4.48e-04 |
|
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: 43.14 E-value: 4.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517189665 96 DVRAPEAGVVSKLLAKEGDEIAVGSPLFEISAgdspaqsKKSETkaaapatnapasspggpakTISVPsmgdsiTEGTVS 175
Cdd:COG1038 1078 HIGAPMPGTVVKVLVKEGDEVKKGDPLLTIEA-------MKMET-------------------TITAP------RDGTVK 1125
|
90
....*....|....*....
gi 1517189665 176 TWTAAEGESVDADQVVCVI 194
Cdd:COG1038 1126 EVLVKEGDQVEAGDLLIEL 1144
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
172-231 |
7.83e-04 |
|
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: 42.37 E-value: 7.83e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517189665 172 GTVSTWTAAEGESVDADQVVCVIETDKVSVDVRAPEAGKIAKHLAASDEVVKVGSPLFEL 231
Cdd:COG1038 1085 GTVVKVLVKEGDEVKKGDPLLTIEAMKMETTITAPRDGTVKEVLVKEGDQVEAGDLLIEL 1144
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
65-138 |
8.92e-04 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 41.64 E-value: 8.92e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1517189665 65 EGTISSWSVAEGDhvdadqvvcvIETDKVSVDVRAPEAGVVSKLLAKEGDEIAVGSPLFEISAGDSPAQSKKSE 138
Cdd:pfam00529 1 LAPLTKGVEAPGR----------VVVSGNAKAVQPQVSGIVTRVLVKEGDRVKAGDVLFQLDPTDYQAALDSAE 64
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
97-194 |
1.17e-03 |
|
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: 37.40 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517189665 97 VRAPEAGVVSKLLAKEGDEIAVGSPLFEISAGdspaqskKSETkaaapatnapasspggpakTISVPsmgdsiTEGTVST 176
Cdd:cd06850 2 VTAPMPGTVVKVLVKEGDKVEAGQPLAVLEAM-------KMEN-------------------EVTAP------VAGVVKE 49
|
90
....*....|....*...
gi 1517189665 177 WTAAEGESVDADQVVCVI 194
Cdd:cd06850 50 ILVKEGDQVEAGQLLVVI 67
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
172-233 |
1.28e-03 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 41.66 E-value: 1.28e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1517189665 172 GTVSTWTAAEGESVDADQVVCVIETDKVSVDVRAPEAGKIAKHLAASDEVVKVGSPLFELVP 233
Cdd:PRK12999 1085 GSVVTVLVKEGDEVKAGDPLAVIEAMKMETTITAPVDGTVKRVLVKAGDQVEAGDLLVELEP 1146
|
|
| AcrA |
COG0845 |
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ... |
73-133 |
1.36e-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: 41.08 E-value: 1.36e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1517189665 73 VAEGDHVDADQVVCVIETDKvSVDVRAPEAGVVSKLLAKEGDEIAVGSPLFEISAGDSPAQ 133
Cdd:COG0845 3 VERGDVPETVEATGTVEARR-EVEVRARVSGRVEEVLVDEGDRVKKGQVLARLDPPDLQAA 62
|
|
| PRK14040 |
PRK14040 |
oxaloacetate decarboxylase subunit alpha; |
151-232 |
2.34e-03 |
|
oxaloacetate decarboxylase subunit alpha;
Pssm-ID: 237592 [Multi-domain] Cd Length: 593 Bit Score: 40.68 E-value: 2.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517189665 151 SSPGGPAKTISVPSMGDSIT---EGTVSTWTAAEGESVDADQVVCVIETDKVSVDVRAPEAGKIAKHLAASDEVVKVGSP 227
Cdd:PRK14040 509 AAPAAAAAAAPAAAAGEPVTaplAGNIFKVIVTEGQTVAEGDVLLILEAMKMETEIRAAQAGTVRGIAVKEGDAVAVGDT 588
|
....*
gi 1517189665 228 LFELV 232
Cdd:PRK14040 589 LLTLA 593
|
|
| PRK07051 |
PRK07051 |
biotin carboxyl carrier domain-containing protein; |
179-231 |
2.34e-03 |
|
biotin carboxyl carrier domain-containing protein;
Pssm-ID: 180811 [Multi-domain] Cd Length: 80 Bit Score: 36.91 E-value: 2.34e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1517189665 179 AAEGESVDADQVVCVIETDKVSVDVRAPEAGKIAKHLAASDEVVKVGSPLFEL 231
Cdd:PRK07051 26 VEVGDAVAAGDVVGLIEVMKQFTEVEAEAAGRVVEFLVEDGEPVEAGQVLARI 78
|
|
| PLN02983 |
PLN02983 |
biotin carboxyl carrier protein of acetyl-CoA carboxylase |
182-233 |
3.15e-03 |
|
biotin carboxyl carrier protein of acetyl-CoA carboxylase
Pssm-ID: 215533 [Multi-domain] Cd Length: 274 Bit Score: 39.44 E-value: 3.15e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1517189665 182 GESVDADQVVCVIETDKVSVDVRAPEAGKIAKHLAASDEVVKVGSPLFELVP 233
Cdd:PLN02983 223 GDKVQKGQVVCIIEAMKLMNEIEADQSGTIVEILAEDGKPVSVDTPLFVIEP 274
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