|
Name |
Accession |
Description |
Interval |
E-value |
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
1-720 |
0e+00 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 713.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516651833 1 MAYSVEMPELGesVTEGTITQWLKEVGDTVEADEPLLEVSTDKVDTEIPSPAAGVLLEIKAEEDDTIDVGTVIAIIGEEg 80
Cdd:PRK11854 1 MAIEIKVPDIG--ADEVEVTEILVKVGDKVEAEQSLITVEGDKASMEVPSPQAGVVKEIKVKVGDKVETGALIMIFESA- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516651833 81 edsgsassedkDDAPAEDEAPAEDAKETETEAKPKAepkkgsgGTATDVQMPELGesVTEGTITQWLKQVGDEVEVDEPL 160
Cdd:PRK11854 78 -----------DGAADAAPAQAEEKKEAAPAAAPAA-------AAAKDVHVPDIG--SDEVEVTEILVKVGDTVEAEQSL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516651833 161 LEVSTDKVDTEIPSPVAGTIVEILADEDDTIDVGAVIARIGDGNAAtdneaedsdtssessessdekeepkkeEPKKDEK 240
Cdd:PRK11854 138 ITVEGDKASMEVPAPFAGTVKEIKVNVGDKVSTGSLIMVFEVAGEA---------------------------PAAAPAA 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516651833 241 QEAPKAEAKKSSGGSATDVQMPELGesVTEGTITQWLKQVGDEVEVDEPLLEVSTDKVDTEIPSPVAGTIVEILADEDDT 320
Cdd:PRK11854 191 AEAAAPAAAPAAAAGVKDVNVPDIG--GDEVEVTEVMVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDK 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516651833 321 IDVGAVIARIGDADAASEEATEATEPAEseeerdvpseeaieeaeskdenatvdeakkdPKAEEAEEPKKSPAAekseeP 400
Cdd:PRK11854 269 VKTGSLIMRFEVEGAAPAAAPAKQEAAA-------------------------------PAPAAAKAEAPAAAP-----A 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516651833 401 KKSSATEKIDNNGNVPYVTPLVRKLADKHGVDLNSIEGTGVGGRIRKQDVLAAAEGGSA---EGSAEQASGKSTDARANW 477
Cdd:PRK11854 313 AKAEGKSEFAENDAYVHATPLVRRLAREFGVNLAKVKGTGRKGRILKEDVQAYVKDAVKraeAAPAAAAAGGGGPGLLPW 392
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516651833 478 STksVDPEKAELIGTTQkVNRIRQITAEKMVESLQTSAQLTHVQEVDMSKVWDLRKS-NKQAFVDKHGANPTFLGFIVKA 556
Cdd:PRK11854 393 PK--VDFSKFGEIEEVE-LGRIQKISGANLHRNWVMIPHVTQFDKADITELEAFRKQqNAEAEKRKLGVKITPLVFIMKA 469
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516651833 557 AAEALVSHPNVNASYNAETKEMTYHADVNIGIAVDTPQGLLVPVVKKAQDKSLVEIVKDIADLADRARNRKLRPDDLTGG 636
Cdd:PRK11854 470 VAAALEQMPRFNSSLSEDGQRLTLKKYVNIGIAVDTPNGLVVPVFKDVNKKGIIELSRELMDISKKARDGKLTAGDMQGG 549
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516651833 637 TFTVSNIGSEGALLDTPVLTPPQAGILGTAAIEKRPVvvteDGADAIAIRYMCYLPFTYDHQVVDGADAGRFITTIKDRL 716
Cdd:PRK11854 550 CFTISSIGGLGTTHFTPIVNAPEVAILGVSKSAMEPV----WNGKEFAPRLMLPLSLSYDHRVIDGADGARFITIINDRL 625
|
....
gi 516651833 717 ETAD 720
Cdd:PRK11854 626 SDIR 629
|
|
| SucB_Actino |
TIGR02927 |
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model ... |
126-727 |
0e+00 |
|
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: 673.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516651833 126 ATDVQMPELGESVTEGTITQWLKQVGDEVEVDEPLLEVSTDKVDTEIPSPVAGTIVEILADEDDTIDVGAVIARIGDgna 205
Cdd:TIGR02927 2 AESVKMPALGESVTEGTVTSWLKAVGDTVEADEPLLEVSTDKVDTEIPSPAAGVLLEIRAPEDDTVEVGGVLAIIGE--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516651833 206 atdnEAEDSDTSSESSESSDEKEEPKKEEPKKDEKQEAP-KAEAKKSSGGSATDVQMPELGESVTEGTITQWLKQVGDEV 284
Cdd:TIGR02927 79 ----PGEAGSEPAPAAPEPEAAPEPEAPAPAPTPAAEAPaPAAPQAGGSGEATEVKMPELGESVTEGTVTSWLKAVGDTV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516651833 285 EVDEPLLEVSTDKVDTEIPSPVAGTIVEILADEDDTIDVGAVIARIGDADAASEEATEATEPAESEEErdvpseeaieea 364
Cdd:TIGR02927 155 EVDEPLLEVSTDKVDTEIPSPVAGTLLEIRAPEDDTVEVGTVLAIIGDANAAPAEPAEEEAPAPSEAG------------ 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516651833 365 eskdeNATVDEAKKDPKAEEAEEPKKSPAAEKSEEPKkssATEKIDNNGNVPYVTPLVRKLADKHGVDLNSIEGTGVGGR 444
Cdd:TIGR02927 223 -----SEPAPDPAARAPHAAPDPPAPAPAPAKTAAPA---AAAPVSSGDSGPYVTPLVRKLAKDKGVDLSTVKGTGVGGR 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516651833 445 IRKQDVLAAAEGGSAEGSAEQASGKSTDARANW-STKSVDPEKAELIGTTQKVNRIRQITAEKMVESLQTSAQLTHVQEV 523
Cdd:TIGR02927 295 IRKQDVLAAAKAAEEARAAAAAPAAAAAPAAPAaAAKPAEPDTAKLRGTTQKMNRIRQITADKTIESLQTSAQLTQVHEV 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516651833 524 DMSKVWDLRKSNKQAFVDKHGANPTFLGFIVKAAAEALVSHPNVNASYNAETKEMTYHADVNIGIAVDTPQGLLVPVVKK 603
Cdd:TIGR02927 375 DMTRVAALRARAKNDFLEKNGVNLTFLPFFVQAVTEALKAHPNVNASYNAETKEVTYHDVEHVGIAVDTPRGLLVPVIHN 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516651833 604 AQDKSLVEIVKDIADLADRARNRKLRPDDLTGGTFTVSNIGSEGALLDTPVLTPPQAGILGTAAIEKRPVVVT-EDGADA 682
Cdd:TIGR02927 455 AGDLSLPGLAKAINDLAARARDNKLKPDELSGGTFTITNIGSGGALFDTPILNPPQAAILGTGAIVKRPRVIKdEDGGES 534
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 516651833 683 IAIRYMCYLPFTYDHQVVDGADAGRFITTIKDRLETADFAADLEV 727
Cdd:TIGR02927 535 IAIRSVCYLPLTYDHRLVDGADAGRFLTTIKKRLEEGDFEGDLGL 579
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
126-724 |
0e+00 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 551.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516651833 126 ATDVQMPELGEsVTEGTITQWLKQVGDEVEVDEPLLEVSTDKVDTEIPSPVAGTIVEILADEDDTIDVGAVIARIGDGNA 205
Cdd:PRK11855 2 AIEFKVPDIGE-VVEVEVIEWLVKEGDTVEEDQPLVTVETDKATMEIPSPAAGVVKEIKVKVGDTVSVGGLLAVIEAAGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516651833 206 ATDNEAEDSDTSSESSESSDEKEepkkeepkkdekQEAPKAEAKKSSGGSATDVQMPELGEsVTEGTITQWLKQVGDEVE 285
Cdd:PRK11855 81 AAAAAAPAAAAAPAAAAAAAPAP------------AAAAPAAAAAAAGGGVVEVKVPDIGE-ITEVEVIEWLVKVGDTVE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516651833 286 VDEPLLEVSTDKVDTEIPSPVAGTIVEILADEDDTIDVGAVIARIGDADAASEEATEATEPAeseeerdvpseeaieeae 365
Cdd:PRK11855 148 EDQSLITVETDKATMEIPSPVAGVVKEIKVKVGDKVSVGSLLVVIEVAAAAPAAAAAPAAAA------------------ 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516651833 366 skdenatvdeakkdPKAEEAEEPKKSPAAEKSEEPKKSSATEKidnNGNVPYVTPLVRKLADKHGVDLNSIEGTGVGGRI 445
Cdd:PRK11855 210 --------------PAAAAAAAPAPAPAAAAAPAAAAPAAAAA---PGKAPHASPAVRRLARELGVDLSQVKGTGKKGRI 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516651833 446 RKQDVLAAAEGGSAEGSAEQASGKSTDARanwSTKSVDPEKAELI--GTTQKV--NRIRQITAEKMVESLQTSAQLTHVQ 521
Cdd:PRK11855 273 TKEDVQAFVKGAMSAAAAAAAAAAAAGGG---GLGLLPWPKVDFSkfGEIETKplSRIKKISAANLHRSWVTIPHVTQFD 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516651833 522 EVDMSKVWDLRKSNKQAFvDKHGANPTFLGFIVKAAAEALVSHPNVNASYNAETKEMTYHADVNIGIAVDTPQGLLVPVV 601
Cdd:PRK11855 350 EADITDLEALRKQLKKEA-EKAGVKLTMLPFFIKAVVAALKEFPVFNASLDEDGDELTYKKYFNIGFAVDTPNGLVVPVI 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516651833 602 KKAQDKSLVEIVKDIADLADRARNRKLRPDDLTGGTFTVSNIGSEGALLDTPVLTPPQAGILGTAAIEKRPVvvteDGAD 681
Cdd:PRK11855 429 KDVDKKSLLEIAREIAELAKKARDGKLKPDDMQGGCFTISSLGGIGGTAFTPIINAPEVAILGVGKSQMKPV----WDGK 504
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 516651833 682 AIAIRYMCYLPFTYDHQVVDGADAGRFITTIKDRLETADFAAD 724
Cdd:PRK11855 505 EFVPRLMLPLSLSYDHRVIDGATAARFTNYLKQLLADPRRMLL 547
|
|
| PRK11856 |
PRK11856 |
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed |
256-718 |
5.49e-137 |
|
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
Pssm-ID: 237001 [Multi-domain] Cd Length: 411 Bit Score: 409.18 E-value: 5.49e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516651833 256 ATDVQMPELGESVTEGTITQWLKQVGDEVEVDEPLLEVSTDKVDTEIPSPVAGTIVEILADEDDTIDVGAVIARIGDADA 335
Cdd:PRK11856 2 MFEFKMPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDVVPVGSVIAVIEEEGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516651833 336 ASEEATEATEPAESEEErdvpseeaieeaeskdenatvdeakkdpKAEEAEEPKKSPAAEKSEEPKKSSATEKIdnngnv 415
Cdd:PRK11856 82 AEAAAAAEAAPEAPAPE----------------------------PAPAAAAAAAAAPAAAAAPAAPAAAAAKA------ 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516651833 416 pyvTPLVRKLADKHGVDLNSIEGTGVGGRIRKQDVLAAAEGGSAEGSAEQASGKSTDARAnwstksvdPEKAELIgttqK 495
Cdd:PRK11856 128 ---SPAVRKLARELGVDLSTVKGSGPGGRITKEDVEAAAAAAAPAAAAAAAAAAAPPAAA--------AEGEERV----P 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516651833 496 VNRIRQITAEKMVESLQTSAQLTHVQEVDMSKVWDLRKSnkqafVDKHGANPTFLGFIVKAAAEALVSHPNVNASYNAET 575
Cdd:PRK11856 193 LSGMRKAIAKRMVESKREIPHFTLTDEVDVTALLALRKQ-----LKAIGVKLTVTDFLIKAVALALKKFPELNASWDDDA 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516651833 576 keMTYHADVNIGIAVDTPQGLLVPVVKKAQDKSLVEIVKDIADLADRARNRKLRPDDLTGGTFTVSNIGSEGALLDTPVL 655
Cdd:PRK11856 268 --IVLKKYVNIGIAVATDGGLIVPVIRDADKKSLFELAREIKDLAEKAREGKLKPEELQGGTFTISNLGMFGGDYFTPII 345
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 516651833 656 TPPQAGILGTAAIEKRPVVVteDGadAIAIRYMCYLPFTYDHQVVDGADAGRFITTIKDRLET 718
Cdd:PRK11856 346 NPPEVAILGVGAIVERPVVV--DG--EIVVRKVMPLSLSFDHRVIDGADAARFLKALKELLEN 404
|
|
| PRK05704 |
PRK05704 |
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase; |
255-717 |
4.10e-124 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
Pssm-ID: 235571 [Multi-domain] Cd Length: 407 Bit Score: 376.10 E-value: 4.10e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516651833 255 SATDVQMPELGESVTEGTITQWLKQVGDEVEVDEPLLEVSTDKVDTEIPSPVAGTIVEILADEDDTIDVGAVIARIGDAD 334
Cdd:PRK05704 1 MMVEIKVPTLPESVTEATIATWHKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGDTVTVGQVLGRIDEGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516651833 335 AASEEAteatepaeseeerdvpseeaieeaeskdenatvdeAKKDPKAEEAEEPKKSPAAEKSEEPKKSSAtekidnngn 414
Cdd:PRK05704 81 AAGAAA-----------------------------------AAAAAAAAAAAAPAQAQAAAAAEQSNDALS--------- 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516651833 415 vpyvtPLVRKLADKHGVDLNSIEGTGVGGRIRKQDVLAAAEGGSAEGSAEQASGKStdaranwSTKSVDPEKAEligTTQ 494
Cdd:PRK05704 117 -----PAARKLAAENGLDASAVKGTGKGGRVTKEDVLAALAAAAAAPAAPAAAAPA-------AAPAPLGARPE---ERV 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516651833 495 KVNRIRQITAEKMVESLQTSAQLTHVQEVDMSKVWDLRKSNKQAFVDKHGANPTFLGFIVKAAAEALVSHPNVNASYNAE 574
Cdd:PRK05704 182 PMTRLRKTIAERLLEAQNTTAMLTTFNEVDMTPVMDLRKQYKDAFEKKHGVKLGFMSFFVKAVVEALKRYPEVNASIDGD 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516651833 575 tkEMTYHADVNIGIAVDTPQGLLVPVVKKAQDKSLVEIVKDIADLADRARNRKLRPDDLTGGTFTVSNIGSEGALLDTPV 654
Cdd:PRK05704 262 --DIVYHNYYDIGIAVGTPRGLVVPVLRDADQLSFAEIEKKIAELAKKARDGKLSIEELTGGTFTITNGGVFGSLMSTPI 339
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 516651833 655 LTPPQAGILGTAAIEKRPVVVTEDgadaIAIRYMCYLPFTYDHQVVDGADAGRFITTIKDRLE 717
Cdd:PRK05704 340 INPPQSAILGMHKIKERPVAVNGQ----IVIRPMMYLALSYDHRIIDGKEAVGFLVTIKELLE 398
|
|
| sucB |
TIGR01347 |
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ... |
257-717 |
8.89e-110 |
|
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: 339.02 E-value: 8.89e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516651833 257 TDVQMPELGESVTEGTITQWLKQVGDEVEVDEPLLEVSTDKVDTEIPSPVAGTIVEILADEDDTIDVGAVIARIGDADAA 336
Cdd:TIGR01347 1 IEIKVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAILEEGNDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516651833 337 SEEATEATEPaeseeerdvpseeaieeaeskdenatvdeakkdpkaEEAEEPKKSPAAEKSEEPKKSSAtekidnngnvp 416
Cdd:TIGR01347 81 TAAPPAKSGE------------------------------------EKEETPAASAAAAPTAAANRPSL----------- 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516651833 417 yvTPLVRKLADKHGVDLNSIEGTGVGGRIRKQDVLAAAEggsAEGSAEQASGKSTDARANWSTKSVDPEkaeligttqKV 496
Cdd:TIGR01347 114 --SPAARRLAKEHGIDLSAVPGTGVTGRVTKEDIIKKTE---APASAQPPAAAAAAAAPAAATRPEERV---------KM 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516651833 497 NRIRQITAEKMVESLQTSAQLTHVQEVDMSKVWDLRKSNKQAFVDKHGANPTFLGFIVKAAAEALVSHPNVNASynAETK 576
Cdd:TIGR01347 180 TRLRQRIAERLKEAQNSTAMLTTFNEVDMSAVMELRKRYKEEFEKKHGVKLGFMSFFVKAVVAALKRFPEVNAE--IDGD 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516651833 577 EMTYHADVNIGIAVDTPQGLLVPVVKKAQDKSLVEIVKDIADLADRARNRKLRPDDLTGGTFTVSNIGSEGALLDTPVLT 656
Cdd:TIGR01347 258 DIVYKDYYDISVAVSTDRGLVVPVVRNADRMSFADIEKEIADLGKKARDGKLTLEDMTGGTFTITNGGVFGSLMSTPIIN 337
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 516651833 657 PPQAGILGTAAIEKRPVVVTedgaDAIAIRYMCYLPFTYDHQVVDGADAGRFITTIKDRLE 717
Cdd:TIGR01347 338 PPQSAILGMHGIKERPVAVN----GQIEIRPMMYLALSYDHRLIDGKEAVTFLVTIKELLE 394
|
|
| PTZ00144 |
PTZ00144 |
dihydrolipoamide succinyltransferase; Provisional |
245-717 |
1.49e-94 |
|
dihydrolipoamide succinyltransferase; Provisional
Pssm-ID: 240289 [Multi-domain] Cd Length: 418 Bit Score: 299.68 E-value: 1.49e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516651833 245 KAEAKKSSGGSATDVQMPELGESVTEGTITQWLKQVGDEVEVDEPLLEVSTDKVDTEIPSPVAGTIVEILADEDDTIDVG 324
Cdd:PTZ00144 33 CSAHFSKSYFSIKVIKVPTMGDSISEGTVVEWKKKVGDYVKEDEVICIIETDKVSVDIRAPASGVITKIFAEEGDTVEVG 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516651833 325 AVIARIGDADAASEEATEATEPAEseeerdvpseeaieeaeskdenatvdEAKKDPKAEEAEEPKKSPAAEKSEEPKKSS 404
Cdd:PTZ00144 113 APLSEIDTGGAPPAAAPAAAAAAK--------------------------AEKTTPEKPKAAAPTPEPPAASKPTPPAAA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516651833 405 ATEKIDNNGNVPYvtplvrkladkhgvdlnsiegtgvggrirkqdvlaaaeggsaegsaeqasgkSTDARANWSTKSVdp 484
Cdd:PTZ00144 167 KPPEPAPAAKPPP----------------------------------------------------TPVARADPRETRV-- 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516651833 485 ekaeligttqKVNRIRQITAEKMVESLQTSAQLTHVQEVDMSKVWDLRKSNKQAFVDKHGANPTFLGFIVKAAAEALVSH 564
Cdd:PTZ00144 193 ----------PMSRMRQRIAERLKASQNTCAMLTTFNECDMSALMELRKEYKDDFQKKHGVKLGFMSAFVKASTIALKKM 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516651833 565 PNVNASYnaETKEMTYHADVNIGIAVDTPQGLLVPVVKKAQDKSLVEIVKDIADLADRARNRKLRPDDLTGGTFTVSNIG 644
Cdd:PTZ00144 263 PIVNAYI--DGDEIVYRNYVDISVAVATPTGLVVPVIRNCENKSFAEIEKELADLAEKARNNKLTLEDMTGGTFTISNGG 340
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 516651833 645 SEGALLDTPVLTPPQAGILGTAAIEKRPVVVTedgaDAIAIRYMCYLPFTYDHQVVDGADAGRFITTIKDRLE 717
Cdd:PTZ00144 341 VFGSLMGTPIINPPQSAILGMHAIKKRPVVVG----NEIVIRPIMYLALTYDHRLIDGRDAVTFLKKIKDLIE 409
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
127-717 |
1.29e-93 |
|
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: 301.79 E-value: 1.29e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516651833 127 TDVQMPELGESvTEGTITQWLKQVGDEVEVDEPLLEVSTDKVDTEIPSPVAGTIVEILADEDDTIDVGAVIARIGDGNAA 206
Cdd:TIGR01348 1 TEIKVPDIGDN-EEGEVIEVLVKPGDKVEAGQSLITLESDKASMEVPSSAAGIIKEIKVKVGDTLPVGGVIATLEVGAGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516651833 207 tdneaedsdtSSESSESSDEKEEPKKEEPKKDEKQEAPKAEAKKSSGgsaTDVQMPELGeSVTEGTITQWLKQVGDEVEV 286
Cdd:TIGR01348 80 ----------QAQAEAKKEAAPAPTAGAPAPAAQAQAAPAAGQSSGV---QEVTVPDIG-DIEKVTVIEVLVKVGDTVSA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516651833 287 DEPLLEVSTDKVDTEIPSPVAGTIVEILADEDDTIDVGAVIARIgdadaASEEATEATEPAeseeerdvpseeaieeaes 366
Cdd:TIGR01348 146 DQSLITLESDKASMEVPAPASGVVKSVKVKVGDSVPTGDLILTL-----SVAGSTPATAPA------------------- 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516651833 367 kdeNATVDEAKKDPkAEEAEEPKKSPAAEKSEEPkkSSATEKIDNNGNVPYVTPLVRKLADKHGVDLNSIEGTGVGGRIR 446
Cdd:TIGR01348 202 ---PASAQPAAQSP-AATQPEPAAAPAAAKAQAP--APQQAGTQNPAKVDHAAPAVRRLAREFGVDLSAVKGTGIKGRIL 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516651833 447 KQDVLAAAegGSAEGSAEQASGKSTDARANWST-KSVDPEKAELIgTTQKVNRIRQITAEKMVESLQTSAQLTHVQEVDM 525
Cdd:TIGR01348 276 REDVQRFV--KEPSVRAQAAAASAAGGAPGALPwPNVDFSKFGEV-EEVDMSRIRKISGANLTRNWTMIPHVTHFDKADI 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516651833 526 SKVWDLRKSNKQAfVDKHGANPTFLGFIVKAAAEALVSHPNVNASYNAETKEMTYHADVNIGIAVDTPQGLLVPVVKKAQ 605
Cdd:TIGR01348 353 TEMEAFRKQQNAA-VEKEGVKLTVLHILMKAVAAALKKFPKFNASLDLGGEQLILKKYVNIGVAVDTPNGLLVPVIKDVD 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516651833 606 DKSLVEIVKDIADLADRARNRKLRPDDLTGGTFTVSNIGSEGALLDTPVLTPPQAGILGTAAIEKRPVvvtEDGaDAIAI 685
Cdd:TIGR01348 432 RKGITELALELSDLAKKARDGKLTPDEMQGACFTISSLGGIGGTAFTPIVNAPEVAILGVSKSGMEPV---WNG-KEFEP 507
|
570 580 590
....*....|....*....|....*....|..
gi 516651833 686 RYMCYLPFTYDHQVVDGADAGRFITTIKDRLE 717
Cdd:TIGR01348 508 RLMLPLSLSYDHRVIDGADAARFTTYICESLA 539
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
507-717 |
5.23e-88 |
|
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: 275.19 E-value: 5.23e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516651833 507 MVESLQTSAQLTHVQEVDMSKVWDLRKSNKQAFVDKHGaNPTFLGFIVKAAAEALVSHPNVNASYNAETKEMTYHADVNI 586
Cdd:pfam00198 1 MTESKQTIPHFTLTDEVDVTELLALREELKEDAADEET-KLTFLPFLVKAVALALKKFPELNASWDGEEGEIVYKKYVNI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516651833 587 GIAVDTPQGLLVPVVKKAQDKSLVEIVKDIADLADRARNRKLRPDDLTGGTFTVSNIGSEGALLDTPVLTPPQAGILGTA 666
Cdd:pfam00198 80 GIAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVG 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 516651833 667 AIEKRPVVVtedgADAIAIRYMCYLPFTYDHQVVDGADAGRFITTIKDRLE 717
Cdd:pfam00198 160 RIRKRPVVV----DGEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLE 206
|
|
| PDHac_trf_mito |
TIGR01349 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
259-717 |
4.36e-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: 238.54 E-value: 4.36e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516651833 259 VQMPELGESVTEGTITQWLKQVGDEVEVDEPLLEVSTDKVDTEIPSPVAGTIVEILADED-DTIDVGAVIARIGDADAAS 337
Cdd:TIGR01349 2 ITMPALSPTMTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEGtKDVPVNKPIAVLVEEKEDV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516651833 338 EEATEATEPAESEEERDVPseeaieeaeskdenatvdeAKKDPKAEEAEEPKKSPAAEKSEEPKKSSATEKIDNNGNVpY 417
Cdd:TIGR01349 82 ADAFKNYKLESSASPAPKP-------------------SEIAPTAPPSAPKPSPAPQKQSPEPSSPAPLSDKESGDRI-F 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516651833 418 VTPLVRKLADKHGVDLNSIEGTGVGGRIRKQDVLAAAEGgSAEGSAEQASGKSTDARAnwSTKSVDPEKAELIgttqKVN 497
Cdd:TIGR01349 142 ASPLAKKLAKEKGIDLSAVAGSGPNGRIVKKDIESFVPQ-SPASANQQAAATTPATYP--AAAPVSTGSYEDV----PLS 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516651833 498 RIRQITAEKMVESLQTSAQLTHVQEVDMSKVWDLRKS-NKQAF-VDKHGANptflGFIVKAAAEALVSHPNVNASYNAET 575
Cdd:TIGR01349 215 NIRKIIAKRLLESKQTIPHYYVSIECNVDKLLALRKElNAMASeVYKLSVN----DFIIKASALALREVPEANSSWTDNF 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516651833 576 keMTYHADVNIGIAVDTPQGLLVPVVKKAQDKSLVEIVKDIADLADRARNRKLRPDDLTGGTFTVSNIGSEGALLDTPVL 655
Cdd:TIGR01349 291 --IRRYKNVDISVAVATPDGLITPIVRNADAKGLSTISNEIKDLAKRARNNKLKPEEFQGGTFTISNLGMFGIKDFTAII 368
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 516651833 656 TPPQAGILGTAAIEKRPvVVTEDGADAIAIRYMCYLPFTYDHQVVDGADAGRFITTIKDRLE 717
Cdd:TIGR01349 369 NPPQACILAVGAVEDVA-VVDNDEEKGFAVASIMSVTLSCDHRVIDGAVGAEFLKSFKKYLE 429
|
|
| PRK11857 |
PRK11857 |
dihydrolipoamide acetyltransferase; Reviewed |
418-720 |
8.95e-68 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237002 [Multi-domain] Cd Length: 306 Bit Score: 225.44 E-value: 8.95e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516651833 418 VTPLVRKLADKHGVDLNSIEGTGVGGRIRKQDVLA-AAEGGSAEGSAEQASGKSTDARAnwSTKSVDPEKAELIGTTQKV 496
Cdd:PRK11857 4 ATPIARALAKKLGIDISLLKGSGRDGKILAEDVENfIKSLKSAPTPAEAASVSSAQQAA--KTAAPAAAPPKLEGKREKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516651833 497 NRIRQITAEKMVESLQTSAQLTHVQEVDMSKVWDLRKSNKQAFVDKHGANPTFLGFIVKAAAEALVSHPNVNASYNAETK 576
Cdd:PRK11857 82 APIRKAIARAMTNSWSNVAYVNLVNEIDMTKLWDLRKSVKDPVLKTEGVKLTFLPFIAKAILIALKEFPIFAAKYDEATS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516651833 577 EMTYHADVNIGIAVDTPQGLLVPVVKKAQDKSLVEIVKDIADLADRARNRKLRPDDLTGGTFTVSNIGSEGALLDTPVLT 656
Cdd:PRK11857 162 ELVYPDTLNLGIAVDTEAGLMVPVIKNAQKLSIVEIAKEISRLAKAARERKIKPDEMKGGSFTITNYGSVGSLYGVPVIN 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 516651833 657 PPQAGILGTAAIEKRPVVvtEDGAdAIAIRYMcYLPFTYDHQVVDGADAGRFITTIKDRLETAD 720
Cdd:PRK11857 242 YPELAIAGVGAIIDKAIV--KNGQ-IVAGKVM-HLTVAADHRWIDGATIGRFASRVKELLEKPE 301
|
|
| PLN02528 |
PLN02528 |
2-oxoisovalerate dehydrogenase E2 component |
259-717 |
1.33e-59 |
|
2-oxoisovalerate dehydrogenase E2 component
Pssm-ID: 215289 [Multi-domain] Cd Length: 416 Bit Score: 206.88 E-value: 1.33e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516651833 259 VQMPELGESVTEGTITQWLKQVGDEVEVDEPLLEVSTDKVDTEIPSPVAGTIVEILADEDDTIDVGAVIARIGDADAASE 338
Cdd:PLN02528 1 VPLAQTGEGIAECELLRWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGKVAQINFSPGDIVKVGETLLKIMVEDSQHL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516651833 339 EATEATEPAESEEErdvpseeaieeaeskdenatvdeakkdpkaeeaeepkkSPAAEKSEEPKKSSATekidnngnvpYV 418
Cdd:PLN02528 81 RSDSLLLPTDSSNI--------------------------------------VSLAESDERGSNLSGV----------LS 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516651833 419 TPLVRKLADKHGVDLNSIEGTGVGGRIRKQDVLA-AAEGGSAEGSAEQASGKStDARANWSTKSVDPEKAELIGTTQKVN 497
Cdd:PLN02528 113 TPAVRHLAKQYGIDLNDILGTGKDGRVLKEDVLKyAAQKGVVKDSSSAEEATI-AEQEEFSTSVSTPTEQSYEDKTIPLR 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516651833 498 RIRQItaekMVESLQTSAQLTH---VQEVDMSKVWDLRKSNKQAFVDkHGANPTFLGFIVKAAAEALVSHPNVNASYNAE 574
Cdd:PLN02528 192 GFQRA----MVKTMTAAAKVPHfhyVEEINVDALVELKASFQENNTD-PTVKHTFLPFLIKSLSMALSKYPLLNSCFNEE 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516651833 575 TKEMTYHADVNIGIAVDTPQGLLVPVVKKAQDKSLVEIVKDIADLADRARNRKLRPDDLTGGTFTVSNIGSEGALLDTPV 654
Cdd:PLN02528 267 TSEIRLKGSHNIGVAMATEHGLVVPNIKNVQSLSLLEITKELSRLQHLAAENKLNPEDITGGTITLSNIGAIGGKFGSPV 346
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 516651833 655 LTPPQAGILGTAAIEKRPVVVTEDGADAIAIrymcyLPFTY--DHQVVDGADAGRFITTIKDRLE 717
Cdd:PLN02528 347 LNLPEVAIIALGRIQKVPRFVDDGNVYPASI-----MTVTIgaDHRVLDGATVARFCNEWKSYVE 406
|
|
| PLN02744 |
PLN02744 |
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex |
261-718 |
3.76e-59 |
|
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
Pssm-ID: 215397 [Multi-domain] Cd Length: 539 Bit Score: 208.94 E-value: 3.76e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516651833 261 MPELGESVTEGTITQWLKQVGDEVEVDEPLLEVSTDKVDTEIPSPVAGTIVEIL-ADEDDTIDVGAVIArigdadaasee 339
Cdd:PLN02744 117 MPSLSPTMTEGNIARWLKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVkGDGAKEIKVGEVIA----------- 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516651833 340 ateatepAESEEERDVpseeaieeAESKDENATVDEAKKDPKAEEAEEPKKSPAAEKSEEP--KKSSATEKIDNNGNVPY 417
Cdd:PLN02744 186 -------ITVEEEEDI--------GKFKDYKPSSSAAPAAPKAKPSPPPPKEEEVEKPASSpePKASKPSAPPSSGDRIF 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516651833 418 VTPLVRKLADKHGVDLNSIEGTGVGGRIRKQDVLAAAEGGSAEGSAEqasgKSTDARANwSTKSVDpekaelIGTTQkvn 497
Cdd:PLN02744 251 ASPLARKLAEDNNVPLSSIKGTGPDGRIVKADIEDYLASGGKGATAP----PSTDSKAP-ALDYTD------IPNTQ--- 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516651833 498 rIRQITAEKMVESLQTSAQLTHVQEVDMSKVWDLRkSNKQAFVDKHGANPTFLG-FIVKAAAEALVSHPNVNASYNAETK 576
Cdd:PLN02744 317 -IRKVTASRLLQSKQTIPHYYLTVDTRVDKLMALR-SQLNSLQEASGGKKISVNdLVIKAAALALRKVPQCNSSWTDDYI 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516651833 577 EMtYHaDVNIGIAVDTPQGLLVPVVKKAQDKSLVEIVKDIADLADRARNRKLRPDDLTGGTFTVSNIGSE-GALLDTPVL 655
Cdd:PLN02744 395 RQ-YH-NVNINVAVQTENGLYVPVVKDADKKGLSTIAEEVKQLAQKARENSLKPEDYEGGTFTVSNLGGPfGIKQFCAII 472
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 516651833 656 TPPQAGILGTAAIEKRpvVVTEDGADaiAIRYMCYLPFTY--DHQVVDGADAGRFITTIKDRLET 718
Cdd:PLN02744 473 NPPQSAILAVGSAEKR--VIPGSGPD--QYNFASFMSVTLscDHRVIDGAIGAEWLKAFKGYIEN 533
|
|
| PLN02226 |
PLN02226 |
2-oxoglutarate dehydrogenase E2 component |
251-717 |
6.14e-58 |
|
2-oxoglutarate dehydrogenase E2 component
Pssm-ID: 177871 [Multi-domain] Cd Length: 463 Bit Score: 203.83 E-value: 6.14e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516651833 251 SSGGSATDVQMPELGESVTEGTITQWLKQVGDEVEVDEPLLEVSTDKVDTEIPSPVAGTIVEILADEDDTIDVGAVIARI 330
Cdd:PLN02226 86 SESGDTVEAVVPHMGESITDGTLATFLKKPGERVQADEAIAQIETDKVTIDIASPASGVIQEFLVKEGDTVEPGTKVAII 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516651833 331 gdadAASEEATEATEPAEseeerdvpseeaieeaeskdenatvdeakkdpKAEEAEEPKKSPAAEKSEEPKKSSAteKID 410
Cdd:PLN02226 166 ----SKSEDAASQVTPSQ--------------------------------KIPETTDPKPSPPAEDKQKPKVESA--PVA 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516651833 411 NNGNVPYVTPLVRKLADKhgvdlnsiegtgvggrirkqdvlaaaeggsaegsaEQASGKSTDARAnwstksvdpekaeli 490
Cdd:PLN02226 208 EKPKAPSSPPPPKQSAKE-----------------------------------PQLPPKERERRV--------------- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516651833 491 gttqKVNRIRQITAEKMVESLQTSAQLTHVQEVDMSKVWDLRKSNKQAFVDKHGANPTFLGFIVKAAAEALVSHPNVNAS 570
Cdd:PLN02226 238 ----PMTRLRKRVATRLKDSQNTFALLTTFNEVDMTNLMKLRSQYKDAFYEKHGVKLGLMSGFIKAAVSALQHQPVVNAV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516651833 571 YNAEtkEMTYHADVNIGIAVDTPQGLLVPVVKKAQDKSLVEIVKDIADLADRARNRKLRPDDLTGGTFTVSNIGSEGALL 650
Cdd:PLN02226 314 IDGD--DIIYRDYVDISIAVGTSKGLVVPVIRGADKMNFAEIEKTINGLAKKANEGTISIDEMAGGSFTVSNGGVYGSLI 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 516651833 651 DTPVLTPPQAGILGTAAIEKRPVVVtedgADAIAIRYMCYLPFTYDHQVVDGADAGRFITTIKDRLE 717
Cdd:PLN02226 392 STPIINPPQSAILGMHSIVSRPMVV----GGSVVPRPMMYVALTYDHRLIDGREAVYFLRRVKDVVE 454
|
|
| PRK14843 |
PRK14843 |
dihydrolipoamide acetyltransferase; Provisional |
414-718 |
5.92e-44 |
|
dihydrolipoamide acetyltransferase; Provisional
Pssm-ID: 184847 [Multi-domain] Cd Length: 347 Bit Score: 161.61 E-value: 5.92e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516651833 414 NVPYVTPLVRKLADKHGVDLNSIEGTGVGGRIRKQDVLAAAeggsaegsAEQASGKSTDARANWSTKSVDPEKAELIGTT 493
Cdd:PRK14843 47 NVVRISPLAKRIALEHNIAWQEIQGTGHRGKIMKKDVLALL--------PENIENDSIKSPAQIEKVEEVPDNVTPYGEI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516651833 494 QKV--NRIRQITAEKMVESLQTSAQLTHVQEVDMSKVWDLRKSNKQAFVDKHGANPTFLGFIVKAAAEALVSHPNVNASY 571
Cdd:PRK14843 119 ERIpmTPMRKVIAQRMVESYLTAPTFTLNYEVDMTEMLALRKKVLEPIMEATGKKTTVTDLLSLAVVKTLMKHPYINASL 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516651833 572 NAETKEMTYHADVNIGIAVDTPQGLLVPVVKKAQDKSLVEIVKDIADLADRARNRKLRPDDLTGGTFTVSNIGSEGALLD 651
Cdd:PRK14843 199 TEDGKTIITHNYVNLAMAVGMDNGLMTPVVYNAEKMSLSELVVAFKDVIGRTLDGKLAPSELQNSTFTISNLGMFGVQSF 278
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 516651833 652 TPVLTPPQAGILGTAAIEKRPVVVTEDgadaIAIRYMCYLPFTYDHQVVDGADAGRFITTIKDRLET 718
Cdd:PRK14843 279 GPIINQPNSAILGVSSTIEKPVVVNGE----IVIRPIMSLGLTIDHRVVDGMAGAKFMKDLKELIET 341
|
|
| PRK11856 |
PRK11856 |
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed |
1-118 |
7.89e-35 |
|
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
Pssm-ID: 237001 [Multi-domain] Cd Length: 411 Bit Score: 137.23 E-value: 7.89e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516651833 1 MAYSVEMPELGESVTEGTITQWLKEVGDTVEADEPLLEVSTDKVDTEIPSPAAGVLLEIKAEEDDTIDVGTVIAIIGEEG 80
Cdd:PRK11856 1 MMFEFKMPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDVVPVGSVIAVIEEEG 80
|
90 100 110
....*....|....*....|....*....|....*...
gi 516651833 81 EDSGSASSEDKDDAPAEDEAPAEDAKETETEAKPKAEP 118
Cdd:PRK11856 81 EAEAAAAAEAAPEAPAPEPAPAAAAAAAAAPAAAAAPA 118
|
|
| PRK05704 |
PRK05704 |
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase; |
1-116 |
3.49e-30 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
Pssm-ID: 235571 [Multi-domain] Cd Length: 407 Bit Score: 123.41 E-value: 3.49e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516651833 1 MAYSVEMPELGESVTEGTITQWLKEVGDTVEADEPLLEVSTDKVDTEIPSPAAGVLLEIKAEEDDTIDVGTVIAIIGEEG 80
Cdd:PRK05704 1 MMVEIKVPTLPESVTEATIATWHKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGDTVTVGQVLGRIDEGA 80
|
90 100 110
....*....|....*....|....*....|....*.
gi 516651833 81 EDSGSASSEDKDDAPAEDEAPAEDAKETETEAKPKA 116
Cdd:PRK05704 81 AAGAAAAAAAAAAAAAAAPAQAQAAAAAEQSNDALS 116
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
1-76 |
1.10e-29 |
|
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: 112.08 E-value: 1.10e-29
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 516651833 1 MAYSVEMPELGESVTEGTITQWLKEVGDTVEADEPLLEVSTDKVDTEIPSPAAGVLLEIKAEEDDTIDVGTVIAII 76
Cdd:COG0508 1 MAIEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
255-330 |
4.91e-29 |
|
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: 110.16 E-value: 4.91e-29
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 516651833 255 SATDVQMPELGESVTEGTITQWLKQVGDEVEVDEPLLEVSTDKVDTEIPSPVAGTIVEILADEDDTIDVGAVIARI 330
Cdd:COG0508 1 MAIEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
126-200 |
5.68e-29 |
|
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: 110.16 E-value: 5.68e-29
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 516651833 126 ATDVQMPELGESVTEGTITQWLKQVGDEVEVDEPLLEVSTDKVDTEIPSPVAGTIVEILADEDDTIDVGAVIARI 200
Cdd:COG0508 2 AIEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
|
|
| sucB |
TIGR01347 |
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ... |
4-118 |
1.39e-27 |
|
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: 115.60 E-value: 1.39e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516651833 4 SVEMPELGESVTEGTITQWLKEVGDTVEADEPLLEVSTDKVDTEIPSPAAGVLLEIKAEEDDTIDVGTVIAIIgEEGEDS 83
Cdd:TIGR01347 2 EIKVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAIL-EEGNDA 80
|
90 100 110
....*....|....*....|....*....|....*
gi 516651833 84 GSASSEDKDDAPAEDEAPAEDAKETETEAKPKAEP 118
Cdd:TIGR01347 81 TAAPPAKSGEEKEETPAASAAAAPTAAANRPSLSP 115
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
257-330 |
1.63e-27 |
|
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: 105.95 E-value: 1.63e-27
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 516651833 257 TDVQMPELGESVTEGTITQWLKQVGDEVEVDEPLLEVSTDKVDTEIPSPVAGTIVEILADEDDTIDVGAVIARI 330
Cdd:cd06849 1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
127-200 |
1.63e-27 |
|
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: 105.95 E-value: 1.63e-27
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 516651833 127 TDVQMPELGESVTEGTITQWLKQVGDEVEVDEPLLEVSTDKVDTEIPSPVAGTIVEILADEDDTIDVGAVIARI 200
Cdd:cd06849 1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
5-76 |
4.58e-27 |
|
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: 104.41 E-value: 4.58e-27
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 516651833 5 VEMPELGESVTEGTITQWLKEVGDTVEADEPLLEVSTDKVDTEIPSPAAGVLLEIKAEEDDTIDVGTVIAII 76
Cdd:cd06849 3 IKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
|
|
| kgd |
PRK12270 |
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ... |
452-720 |
3.39e-22 |
|
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;
Pssm-ID: 237030 [Multi-domain] Cd Length: 1228 Bit Score: 102.66 E-value: 3.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516651833 452 AAAEGGSAEGSAEQASGKSTDARANWSTKSVDPEKAELIGTTQKVNRIRQITAEKMVESLQ--TSaqlTHVQEVDMSKVW 529
Cdd:PRK12270 76 AAAAPAAPPKPAAAAAAAAAPAAPPAAAAAAAPAAAAVEDEVTPLRGAAAAVAKNMDASLEvpTA---TSVRAVPAKLLI 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516651833 530 DLRksnkqAFVDKH-----GANPTFLGFIVKAAAEALVSHPNVNASYnAETK---EMTYHADVNIGIAVDTPQ-----GL 596
Cdd:PRK12270 153 DNR-----IVINNHlkrtrGGKVSFTHLIGYALVQALKAFPNMNRHY-AEVDgkpTLVTPAHVNLGLAIDLPKkdgsrQL 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516651833 597 LVPVVKKAQDKSLVEIVKDIADLADRARNRKLRPDDLTGGTFTVSNIGSEGALLDTPVLTPPQAGILGTAAIEKRPVV-- 674
Cdd:PRK12270 227 VVPAIKGAETMDFAQFWAAYEDIVRRARDGKLTADDFQGTTISLTNPGGIGTVHSVPRLMKGQGAIIGVGAMEYPAEFqg 306
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 516651833 675 VTEDGADAIAIRYMCYLPFTYDHQVVDGADAGRFITTIKDRLETAD 720
Cdd:PRK12270 307 ASEERLAELGISKVMTLTSTYDHRIIQGAESGEFLRTIHQLLLGED 352
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
255-354 |
3.68e-22 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 98.86 E-value: 3.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516651833 255 SATDVQMPELGESVTEGTITQWLKQVGDEVEVDEPLLEVSTDKVDTEIPSPVAGTIVEILADEDDTIDVGAVIARIGDAD 334
Cdd:PRK14875 1 SITPITMPKWGLSMTEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGETLPVGALLAVVADAE 80
|
90 100
....*....|....*....|
gi 516651833 335 AASEEATEATEPAESEEERD 354
Cdd:PRK14875 81 VSDAEIDAFIAPFARRFAPE 100
|
|
| PTZ00144 |
PTZ00144 |
dihydrolipoamide succinyltransferase; Provisional |
4-120 |
5.63e-22 |
|
dihydrolipoamide succinyltransferase; Provisional
Pssm-ID: 240289 [Multi-domain] Cd Length: 418 Bit Score: 98.99 E-value: 5.63e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516651833 4 SVEMPELGESVTEGTITQWLKEVGDTVEADEPLLEVSTDKVDTEIPSPAAGVLLEIKAEEDDTIDVGTVIAII--GEEGE 81
Cdd:PTZ00144 46 VIKVPTMGDSISEGTVVEWKKKVGDYVKEDEVICIIETDKVSVDIRAPASGVITKIFAEEGDTVEVGAPLSEIdtGGAPP 125
|
90 100 110
....*....|....*....|....*....|....*....
gi 516651833 82 DSGSASSEDKDDAPAEDEAPAEDAKETETEAKPKAEPKK 120
Cdd:PTZ00144 126 AAAPAAAAAAKAEKTTPEKPKAAAPTPEPPAASKPTPPA 164
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
1-136 |
3.29e-20 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 93.08 E-value: 3.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516651833 1 MAYSVEMPELGESVTEGTITQWLKEVGDTVEADEPLLEVSTDKVDTEIPSPAAGVLLEIKAEEDDTIDVGTVIAIIGEEG 80
Cdd:PRK14875 1 SITPITMPKWGLSMTEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGETLPVGALLAVVADAE 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 516651833 81 edsgsASSEDKDDAPAEDEAPAEDAKETETEAKPkaEPKKGSGGtATDVQMPELGE 136
Cdd:PRK14875 81 -----VSDAEIDAFIAPFARRFAPEGIDEEDAGP--APRKARIG-GRTVRYLRLGE 128
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
125-209 |
3.24e-19 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 90.00 E-value: 3.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516651833 125 TATDVQMPELGESVTEGTITQWLKQVGDEVEVDEPLLEVSTDKVDTEIPSPVAGTIVEILADEDDTIDVGAVIARIGDGN 204
Cdd:PRK14875 1 SITPITMPKWGLSMTEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGETLPVGALLAVVADAE 80
|
....*
gi 516651833 205 AATDN 209
Cdd:PRK14875 81 VSDAE 85
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
5-76 |
4.18e-19 |
|
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue binds biotin in one group and lipoic acid in the other. Note that the HMM does not currently recognize the Glycine cleavage system H proteins.
Pssm-ID: 395290 [Multi-domain] Cd Length: 73 Bit Score: 81.88 E-value: 4.18e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 516651833 5 VEMPELGESVTEGtITQWLKEVGDTVEADEPLLEVSTDKVDTEIPSPAAGVLLEIKAEEDDTIDVGTVIAII 76
Cdd:pfam00364 3 IKSPMIGESVREG-VVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
127-200 |
4.39e-19 |
|
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue binds biotin in one group and lipoic acid in the other. Note that the HMM does not currently recognize the Glycine cleavage system H proteins.
Pssm-ID: 395290 [Multi-domain] Cd Length: 73 Bit Score: 81.88 E-value: 4.39e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 516651833 127 TDVQMPELGESVTEGtITQWLKQVGDEVEVDEPLLEVSTDKVDTEIPSPVAGTIVEILADEDDTIDVGAVIARI 200
Cdd:pfam00364 1 TEIKSPMIGESVREG-VVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
257-330 |
4.39e-19 |
|
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue binds biotin in one group and lipoic acid in the other. Note that the HMM does not currently recognize the Glycine cleavage system H proteins.
Pssm-ID: 395290 [Multi-domain] Cd Length: 73 Bit Score: 81.88 E-value: 4.39e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 516651833 257 TDVQMPELGESVTEGtITQWLKQVGDEVEVDEPLLEVSTDKVDTEIPSPVAGTIVEILADEDDTIDVGAVIARI 330
Cdd:pfam00364 1 TEIKSPMIGESVREG-VVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
|
|
| PLN02226 |
PLN02226 |
2-oxoglutarate dehydrogenase E2 component |
7-121 |
3.31e-17 |
|
2-oxoglutarate dehydrogenase E2 component
Pssm-ID: 177871 [Multi-domain] Cd Length: 463 Bit Score: 85.19 E-value: 3.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516651833 7 MPELGESVTEGTITQWLKEVGDTVEADEPLLEVSTDKVDTEIPSPAAGVLLEIKAEEDDTIDVGTVIAIIgEEGEDSGS- 85
Cdd:PLN02226 96 VPHMGESITDGTLATFLKKPGERVQADEAIAQIETDKVTIDIASPASGVIQEFLVKEGDTVEPGTKVAII-SKSEDAASq 174
|
90 100 110
....*....|....*....|....*....|....*...
gi 516651833 86 -ASSEDKDDAPA-EDEAPAEDAKETETEAKPKAEPKKG 121
Cdd:PLN02226 175 vTPSQKIPETTDpKPSPPAEDKQKPKVESAPVAEKPKA 212
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
1-139 |
1.24e-16 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 83.04 E-value: 1.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516651833 1 MAYSVEMPELGESVTEGTITQWLKEVGDTVEADEPLLEVSTDKVDTEIPSPAAGVLLEIKAEE-DDTIDVGTVIAIIGEE 79
Cdd:PRK11892 1 MAIEILMPALSPTMEEGTLAKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKILVPEgTEGVKVNTPIAVLLEE 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 516651833 80 GEDSGSASSEDKDDAPAEDEAPAEDAKETE-TEAKPKAEPKKGSGGTATDVQMPELGESVT 139
Cdd:PRK11892 81 GESASDAGAAPAAAAEAAAAAPAAAAAAAAkKAAPAPAAPAAPAAEVAADPDIPAGTEMVT 141
|
|
| PLN02744 |
PLN02744 |
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex |
7-119 |
1.23e-14 |
|
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
Pssm-ID: 215397 [Multi-domain] Cd Length: 539 Bit Score: 77.20 E-value: 1.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516651833 7 MPELGESVTEGTITQWLKEVGDTVEADEPLLEVSTDKVDTEIPSPAAGVLLEI-KAEEDDTIDVGTVIAIIGEEGEDSGS 85
Cdd:PLN02744 117 MPSLSPTMTEGNIARWLKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIvKGDGAKEIKVGEVIAITVEEEEDIGK 196
|
90 100 110
....*....|....*....|....*....|....*....
gi 516651833 86 -----ASSEDKDDAPAEDEAPAEDAKETETEAKPKAEPK 119
Cdd:PLN02744 197 fkdykPSSSAAPAAPKAKPSPPPPKEEEVEKPASSPEPK 235
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
5-119 |
6.48e-14 |
|
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: 74.91 E-value: 6.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516651833 5 VEMPELGeSVTEGTITQWLKEVGDTVEADEPLLEVSTDKVDTEIPSPAAGVLLEIKAEEDDTIDVGTVIAIIgeEGEDSG 84
Cdd:TIGR01348 119 VTVPDIG-DIEKVTVIEVLVKVGDTVSADQSLITLESDKASMEVPAPASGVVKSVKVKVGDSVPTGDLILTL--SVAGST 195
|
90 100 110
....*....|....*....|....*....|....*.
gi 516651833 85 SASSEDKDDAPAEDEAPAEDAKE-TETEAKPKAEPK 119
Cdd:TIGR01348 196 PATAPAPASAQPAAQSPAATQPEpAAAPAAAKAQAP 231
|
|
| PDHac_trf_mito |
TIGR01349 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
5-119 |
8.22e-13 |
|
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: 70.98 E-value: 8.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516651833 5 VEMPELGESVTEGTITQWLKEVGDTVEADEPLLEVSTDKVDTEIPSPAAGVLLEIKAEED-DTIDVGTVIAIIGEEGEDS 83
Cdd:TIGR01349 2 ITMPALSPTMTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEGtKDVPVNKPIAVLVEEKEDV 81
|
90 100 110
....*....|....*....|....*....|....*.
gi 516651833 84 GSAsseDKDDAPAEDEAPAEDAKETETEAKPKAEPK 119
Cdd:TIGR01349 82 ADA---FKNYKLESSASPAPKPSEIAPTAPPSAPKP 114
|
|
| E3_binding |
pfam02817 |
e3 binding domain; This family represents a small domain of the E2 subunit of 2-oxo-acid ... |
416-451 |
1.03e-11 |
|
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: 59.62 E-value: 1.03e-11
10 20 30
....*....|....*....|....*....|....*.
gi 516651833 416 PYVTPLVRKLADKHGVDLNSIEGTGVGGRIRKQDVL 451
Cdd:pfam02817 1 VLASPAARKLARELGIDLSDVKGTGPGGRITKEDVE 36
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
256-384 |
3.93e-11 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 65.71 E-value: 3.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516651833 256 ATDVQMPELGESVTEGTITQWLKQVGDEVEVDEPLLEVSTDKVDTEIPSPVAGTIVEILADE-DDTIDVGAVIARI-GDA 333
Cdd:PRK11892 2 AIEILMPALSPTMEEGTLAKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKILVPEgTEGVKVNTPIAVLlEEG 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 516651833 334 DAASEEATEATEPAESEEERDVPSEEAIEEAESKDENATVDEAKKDPKAEE 384
Cdd:PRK11892 82 ESASDAGAAPAAAAEAAAAAPAAAAAAAAKKAAPAPAAPAAPAAEVAADPD 132
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
141-200 |
8.77e-11 |
|
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all biotin-dependent enzymes, such as acetyl-CoA carboxylase, pyruvate carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA carboxylase, geranyl-CoA carboxylase, oxaloacetate decarboxylase, methylmalonyl-CoA decarboxylase, transcarboxylase and urea amidolyase. This domain functions in transferring CO2 from one subsite to another, allowing carboxylation, decarboxylation, or transcarboxylation. During this process, biotin is covalently attached to a specific lysine.
Pssm-ID: 133459 [Multi-domain] Cd Length: 67 Bit Score: 57.81 E-value: 8.77e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 516651833 141 GTITQWLKQVGDEVEVDEPLLEVSTDKVDTEIPSPVAGTIVEILADEDDTIDVGAVIARI 200
Cdd:cd06850 8 GTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
271-330 |
8.77e-11 |
|
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all biotin-dependent enzymes, such as acetyl-CoA carboxylase, pyruvate carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA carboxylase, geranyl-CoA carboxylase, oxaloacetate decarboxylase, methylmalonyl-CoA decarboxylase, transcarboxylase and urea amidolyase. This domain functions in transferring CO2 from one subsite to another, allowing carboxylation, decarboxylation, or transcarboxylation. During this process, biotin is covalently attached to a specific lysine.
Pssm-ID: 133459 [Multi-domain] Cd Length: 67 Bit Score: 57.81 E-value: 8.77e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 516651833 271 GTITQWLKQVGDEVEVDEPLLEVSTDKVDTEIPSPVAGTIVEILADEDDTIDVGAVIARI 330
Cdd:cd06850 8 GTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| PRK09282 |
PRK09282 |
pyruvate carboxylase subunit B; Validated |
84-200 |
1.08e-10 |
|
pyruvate carboxylase subunit B; Validated
Pssm-ID: 236449 [Multi-domain] Cd Length: 592 Bit Score: 64.86 E-value: 1.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516651833 84 GSASSEDKDDAPAEDEAPAEDAKETETEAKPKAEPKKGSGGTATdVQMPelgesvteGTITQWLKQVGDEVEVDEPLLEV 163
Cdd:PRK09282 483 GVKAEGKRPFYLRVDGMPEEVVVEPLKEIVVGGRPRASAPGAVT-SPMP--------GTVVKVKVKEGDKVKAGDTVLVL 553
|
90 100 110
....*....|....*....|....*....|....*..
gi 516651833 164 STDKVDTEIPSPVAGTIVEILADEDDTIDVGAVIARI 200
Cdd:PRK09282 554 EAMKMENEIQAPVDGTVKEILVKEGDRVNPGDVLMEI 590
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
126-269 |
3.68e-10 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 62.63 E-value: 3.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516651833 126 ATDVQMPELGESVTEGTITQWLKQVGDEVEVDEPLLEVSTDKVDTEIPSPVAGTIVEILADE-DDTIDVGAVIARI-GDG 203
Cdd:PRK11892 2 AIEILMPALSPTMEEGTLAKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKILVPEgTEGVKVNTPIAVLlEEG 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 516651833 204 NAATDNE-AEDSDTSSESSESSDEKEEPKKEEPKKDEKQEAPKAEAkkssggsATDVQMPELGESVT 269
Cdd:PRK11892 82 ESASDAGaAPAAAAEAAAAAPAAAAAAAAKKAAPAPAAPAAPAAEV-------AADPDIPAGTEMVT 141
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
17-76 |
4.62e-10 |
|
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all biotin-dependent enzymes, such as acetyl-CoA carboxylase, pyruvate carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA carboxylase, geranyl-CoA carboxylase, oxaloacetate decarboxylase, methylmalonyl-CoA decarboxylase, transcarboxylase and urea amidolyase. This domain functions in transferring CO2 from one subsite to another, allowing carboxylation, decarboxylation, or transcarboxylation. During this process, biotin is covalently attached to a specific lysine.
Pssm-ID: 133459 [Multi-domain] Cd Length: 67 Bit Score: 55.89 E-value: 4.62e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 516651833 17 GTITQWLKEVGDTVEADEPLLEVSTDKVDTEIPSPAAGVLLEIKAEEDDTIDVGTVIAII 76
Cdd:cd06850 8 GTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
258-330 |
1.00e-09 |
|
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: 55.14 E-value: 1.00e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 516651833 258 DVQMPELGESVTEGTITQWLKQVGDEVEVDEPLLEVSTDKVDTEIPSPVAGTIVEILADEDDTIDVGAVIARI 330
Cdd:cd06663 1 TILIPDLAQHLGDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKVEGDTPLVKI 73
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
128-200 |
1.00e-09 |
|
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: 55.14 E-value: 1.00e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 516651833 128 DVQMPELGESVTEGTITQWLKQVGDEVEVDEPLLEVSTDKVDTEIPSPVAGTIVEILADEDDTIDVGAVIARI 200
Cdd:cd06663 1 TILIPDLAQHLGDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKVEGDTPLVKI 73
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
5-76 |
6.68e-09 |
|
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: 52.83 E-value: 6.68e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 516651833 5 VEMPELGESVTEGTITQWLKEVGDTVEADEPLLEVSTDKVDTEIPSPAAGVLLEIKAEEDDTIDVGTVIAII 76
Cdd:cd06663 2 ILIPDLAQHLGDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKVEGDTPLVKI 73
|
|
| PRK09282 |
PRK09282 |
pyruvate carboxylase subunit B; Validated |
241-330 |
2.93e-08 |
|
pyruvate carboxylase subunit B; Validated
Pssm-ID: 236449 [Multi-domain] Cd Length: 592 Bit Score: 57.16 E-value: 2.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516651833 241 QEAPKAEAKKSSGGSATDVQMPelgesvteGTITQWLKQVGDEVEVDEPLLEVSTDKVDTEIPSPVAGTIVEILADEDDT 320
Cdd:PRK09282 509 KEIVVGGRPRASAPGAVTSPMP--------GTVVKVKVKEGDKVKAGDTVLVLEAMKMENEIQAPVDGTVKEILVKEGDR 580
|
90
....*....|
gi 516651833 321 IDVGAVIARI 330
Cdd:PRK09282 581 VNPGDVLMEI 590
|
|
| AccB |
COG0511 |
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ... |
94-201 |
7.73e-07 |
|
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440277 [Multi-domain] Cd Length: 136 Bit Score: 48.74 E-value: 7.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516651833 94 APAEDEAPAEDAKETETEAKPKAEPKKGSGGTATdvqmpelgeSVTEGTITQW-------LKQVGDEVEVDEPLLEVSTD 166
Cdd:COG0511 31 AAAPVAAPAAAAPAAAAPAAAAAAAAASGGGAVK---------SPMVGTFYRApspgakpFVKVGDKVKAGDTLCIIEAM 101
|
90 100 110
....*....|....*....|....*....|....*
gi 516651833 167 KVDTEIPSPVAGTIVEILADEDDTIDVGAVIARIG 201
Cdd:COG0511 102 KMMNEIEAPVSGTVVEILVENGQPVEYGQPLFVIE 136
|
|
| AccB |
COG0511 |
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ... |
279-331 |
1.70e-06 |
|
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440277 [Multi-domain] Cd Length: 136 Bit Score: 47.97 E-value: 1.70e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 516651833 279 QVGDEVEVDEPLLEVSTDKVDTEIPSPVAGTIVEILADEDDTIDVGAVIARIG 331
Cdd:COG0511 84 KVGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVVEILVENGQPVEYGQPLFVIE 136
|
|
| PRK05641 |
PRK05641 |
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
94-201 |
2.22e-06 |
|
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235540 [Multi-domain] Cd Length: 153 Bit Score: 47.93 E-value: 2.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516651833 94 APAEDEAPAEDAKETETEAKPKAEPKKGSGGTATDVQMPelgesvteGTITQWLKQVGDEVEVDEPLLEVSTDKVDTEIP 173
Cdd:PRK05641 54 TPAPAPAPAVPSAPTPVAPAAPAPAPASAGENVVTAPMP--------GKILRILVREGQQVKVGQGLLILEAMKMENEIP 125
|
90 100
....*....|....*....|....*...
gi 516651833 174 SPVAGTIVEILADEDDTIDVGAVIARIG 201
Cdd:PRK05641 126 APKDGVVKKILVKEGDTVDTGQPLIELG 153
|
|
| PRK06549 |
PRK06549 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
79-194 |
2.74e-06 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235826 [Multi-domain] Cd Length: 130 Bit Score: 47.11 E-value: 2.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516651833 79 EGEDSGSASSEDKDDAPAEDEAPAEDAKETETEAKPKAePKKGSGGTATDVQMPelgesvteGTITQWLKQVGDEVEVDE 158
Cdd:PRK06549 17 EMEEIGAPAQAAAPAQPASTPVPVPTEASPQVEAQAPQ-PAAAAGADAMPSPMP--------GTILKVLVAVGDQVTENQ 87
|
90 100 110
....*....|....*....|....*....|....*.
gi 516651833 159 PLLEVSTDKVDTEIPSPVAGTIVEILADEDDTIDVG 194
Cdd:PRK06549 88 PLLILEAMKMENEIVASSAGTVTAIHVTPGQVVNPG 123
|
|
| PRK09282 |
PRK09282 |
pyruvate carboxylase subunit B; Validated |
17-76 |
1.38e-05 |
|
pyruvate carboxylase subunit B; Validated
Pssm-ID: 236449 [Multi-domain] Cd Length: 592 Bit Score: 48.30 E-value: 1.38e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 516651833 17 GTITQWLKEVGDTVEADEPLLEVSTDKVDTEIPSPAAGVLLEIKAEEDDTIDVGTVIAII 76
Cdd:PRK09282 531 GTVVKVKVKEGDKVKAGDTVLVLEAMKMENEIQAPVDGTVKEILVKEGDRVNPGDVLMEI 590
|
|
| PRK05641 |
PRK05641 |
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
241-331 |
6.55e-05 |
|
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235540 [Multi-domain] Cd Length: 153 Bit Score: 43.70 E-value: 6.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516651833 241 QEAPKAEAKKSSGGSATDVQMPelgesvteGTITQWLKQVGDEVEVDEPLLEVSTDKVDTEIPSPVAGTIVEILADEDDT 320
Cdd:PRK05641 71 APAAPAPAPASAGENVVTAPMP--------GKILRILVREGQQVKVGQGLLILEAMKMENEIPAPKDGVVKKILVKEGDT 142
|
90
....*....|.
gi 516651833 321 IDVGAVIARIG 331
Cdd:PRK05641 143 VDTGQPLIELG 153
|
|
| GCS_H |
cd06848 |
Glycine cleavage H-protein. Glycine cleavage H-proteins are part of the glycine cleavage ... |
146-183 |
8.19e-05 |
|
Glycine cleavage H-protein. Glycine cleavage H-proteins are part of the glycine cleavage system (GCS) found in bacteria, archea and the mitochondria of eukaryotes. GCS is a multienzyme complex consisting of 4 different components (P-, H-, T- and L-proteins) which catalyzes the oxidative cleavage of glycine. The H-protein shuttles the methylamine group of glycine from the P-protein (glycine dehydrogenase) to the T-protein (aminomethyltransferase) via a lipoyl group, attached to a completely conserved lysine residue.
Pssm-ID: 133457 [Multi-domain] Cd Length: 96 Bit Score: 42.14 E-value: 8.19e-05
10 20 30
....*....|....*....|....*....|....*...
gi 516651833 146 WLKQVGDEVEVDEPLLEVSTDKVDTEIPSPVAGTIVEI 183
Cdd:cd06848 35 ELPEVGTEVKKGDPFGSVESVKAASDLYSPVSGEVVEV 72
|
|
| GCS_H |
cd06848 |
Glycine cleavage H-protein. Glycine cleavage H-proteins are part of the glycine cleavage ... |
276-313 |
8.19e-05 |
|
Glycine cleavage H-protein. Glycine cleavage H-proteins are part of the glycine cleavage system (GCS) found in bacteria, archea and the mitochondria of eukaryotes. GCS is a multienzyme complex consisting of 4 different components (P-, H-, T- and L-proteins) which catalyzes the oxidative cleavage of glycine. The H-protein shuttles the methylamine group of glycine from the P-protein (glycine dehydrogenase) to the T-protein (aminomethyltransferase) via a lipoyl group, attached to a completely conserved lysine residue.
Pssm-ID: 133457 [Multi-domain] Cd Length: 96 Bit Score: 42.14 E-value: 8.19e-05
10 20 30
....*....|....*....|....*....|....*...
gi 516651833 276 WLKQVGDEVEVDEPLLEVSTDKVDTEIPSPVAGTIVEI 313
Cdd:cd06848 35 ELPEVGTEVKKGDPFGSVESVKAASDLYSPVSGEVVEV 72
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
333-537 |
8.23e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.29 E-value: 8.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516651833 333 ADAASEEATEATEPAESEEERDVPSEEAIEEAESKDENATVDEAKKDPKAEEAEEPKKSPAAEKSEEPKKSSATEKIDNN 412
Cdd:PTZ00121 1472 ADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADEL 1551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516651833 413 GNVPYvtplVRKLADKHGVDLNSIEGTGVGGRIRKQDVLAAAEGGSAEGS----AEQASGKSTDARANWSTKSvdpeKAE 488
Cdd:PTZ00121 1552 KKAEE----LKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVmklyEEEKKMKAEEAKKAEEAKI----KAE 1623
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 516651833 489 LIGTTQKVNRIRQITAEKMVESLQTSAQLTHVQEVDMSKVWDLRKSNKQ 537
Cdd:PTZ00121 1624 ELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEE 1672
|
|
| AccB |
COG0511 |
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ... |
25-77 |
1.11e-04 |
|
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: 42.57 E-value: 1.11e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 516651833 25 EVGDTVEADEPLLEVSTDKVDTEIPSPAAGVLLEIKAEEDDTIDVGTVIAIIG 77
Cdd:COG0511 84 KVGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVVEILVENGQPVEYGQPLFVIE 136
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
107-194 |
1.90e-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: 45.07 E-value: 1.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516651833 107 ETETEAKPKAEPkkgsgGTATDV--QMPelgesvteGTITQWLKQVGDEVEVDEPLLEVSTDKVDTEIPSPVAGTIVEIL 184
Cdd:COG1038 1062 KVTVASREKADP-----GNPGHIgaPMP--------GTVVKVLVKEGDEVKKGDPLLTIEAMKMETTITAPRDGTVKEVL 1128
|
90
....*....|
gi 516651833 185 ADEDDTIDVG 194
Cdd:COG1038 1129 VKEGDQVEAG 1138
|
|
| PLN02528 |
PLN02528 |
2-oxoisovalerate dehydrogenase E2 component |
5-118 |
2.06e-04 |
|
2-oxoisovalerate dehydrogenase E2 component
Pssm-ID: 215289 [Multi-domain] Cd Length: 416 Bit Score: 44.33 E-value: 2.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516651833 5 VEMPELGESVTEGTITQWLKEVGDTVEADEPLLEVSTDKVDTEIPSPAAGVLLEIKAEEDDTIDVGTVIAIIGEEGEDSG 84
Cdd:PLN02528 1 VPLAQTGEGIAECELLRWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGKVAQINFSPGDIVKVGETLLKIMVEDSQHL 80
|
90 100 110
....*....|....*....|....*....|....
gi 516651833 85 SASSEDKDDAPAEDEAPAEDAKETETEAKPKAEP 118
Cdd:PLN02528 81 RSDSLLLPTDSSNIVSLAESDERGSNLSGVLSTP 114
|
|
| GcvH |
COG0509 |
Glycine cleavage system protein H (lipoate-binding) [Amino acid transport and metabolism]; ... |
147-183 |
3.29e-04 |
|
Glycine cleavage system protein H (lipoate-binding) [Amino acid transport and metabolism]; Glycine cleavage system protein H (lipoate-binding) is part of the Pathway/BioSystem: Glycine cleavage
Pssm-ID: 440275 Cd Length: 128 Bit Score: 41.26 E-value: 3.29e-04
10 20 30
....*....|....*....|....*....|....*..
gi 516651833 147 LKQVGDEVEVDEPLLEVSTDKVDTEIPSPVAGTIVEI 183
Cdd:COG0509 44 LPEVGTEVEAGEPFGVVESVKAVSDLYAPVSGEVVEV 80
|
|
| GcvH |
COG0509 |
Glycine cleavage system protein H (lipoate-binding) [Amino acid transport and metabolism]; ... |
277-313 |
3.29e-04 |
|
Glycine cleavage system protein H (lipoate-binding) [Amino acid transport and metabolism]; Glycine cleavage system protein H (lipoate-binding) is part of the Pathway/BioSystem: Glycine cleavage
Pssm-ID: 440275 Cd Length: 128 Bit Score: 41.26 E-value: 3.29e-04
10 20 30
....*....|....*....|....*....|....*..
gi 516651833 277 LKQVGDEVEVDEPLLEVSTDKVDTEIPSPVAGTIVEI 313
Cdd:COG0509 44 LPEVGTEVEAGEPFGVVESVKAVSDLYAPVSGEVVEV 80
|
|
| PRK14040 |
PRK14040 |
oxaloacetate decarboxylase subunit alpha; |
246-327 |
4.34e-04 |
|
oxaloacetate decarboxylase subunit alpha;
Pssm-ID: 237592 [Multi-domain] Cd Length: 593 Bit Score: 43.77 E-value: 4.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516651833 246 AEAKKSSGGSATDVQMPELGESVT---EGTITQWLKQVGDEVEVDEPLLEVSTDKVDTEIPSPVAGTIVEILADEDDTID 322
Cdd:PRK14040 505 AAPAAAPAAAAAAAPAAAAGEPVTaplAGNIFKVIVTEGQTVAEGDVLLILEAMKMETEIRAAQAGTVRGIAVKEGDAVA 584
|
....*
gi 516651833 323 VGAVI 327
Cdd:PRK14040 585 VGDTL 589
|
|
| PRK07051 |
PRK07051 |
biotin carboxyl carrier domain-containing protein; |
278-332 |
4.39e-04 |
|
biotin carboxyl carrier domain-containing protein;
Pssm-ID: 180811 [Multi-domain] Cd Length: 80 Bit Score: 39.61 E-value: 4.39e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 516651833 278 KQVGDEVEVDEPLLEVSTDKVDTEIPSPVAGTIVEILADEDDTIDVGAVIARIGD 332
Cdd:PRK07051 26 VEVGDAVAAGDVVGLIEVMKQFTEVEAEAAGRVVEFLVEDGEPVEAGQVLARIEE 80
|
|
| PRK07051 |
PRK07051 |
biotin carboxyl carrier domain-containing protein; |
148-202 |
4.39e-04 |
|
biotin carboxyl carrier domain-containing protein;
Pssm-ID: 180811 [Multi-domain] Cd Length: 80 Bit Score: 39.61 E-value: 4.39e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 516651833 148 KQVGDEVEVDEPLLEVSTDKVDTEIPSPVAGTIVEILADEDDTIDVGAVIARIGD 202
Cdd:PRK07051 26 VEVGDAVAAGDVVGLIEVMKQFTEVEAEAAGRVVEFLVEDGEPVEAGQVLARIEE 80
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
107-194 |
8.31e-04 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 42.82 E-value: 8.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516651833 107 ETETEAKPKAEPkkgsgGTATDV--QMPelgesvteGTITQWLKQVGDEVEVDEPLLEVSTDKVDTEIPSPVAGTIVEIL 184
Cdd:PRK12999 1062 KSTVAAREKADP-----GNPGHVgaPMP--------GSVVTVLVKEGDEVKAGDPLAVIEAMKMETTITAPVDGTVKRVL 1128
|
90
....*....|
gi 516651833 185 ADEDDTIDVG 194
Cdd:PRK12999 1129 VKAGDQVEAG 1138
|
|
| PRK13108 |
PRK13108 |
prolipoprotein diacylglyceryl transferase; Reviewed |
281-440 |
1.33e-03 |
|
prolipoprotein diacylglyceryl transferase; Reviewed
Pssm-ID: 237284 [Multi-domain] Cd Length: 460 Bit Score: 41.89 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516651833 281 GDEVEVDEPLLevstdkvdteiPSPVAGTIVEILADEDDTIDVGAVIARIGDADAASEEAT----EATEPAESEEERDVP 356
Cdd:PRK13108 287 GSEYVVDEALE-----------REPAELAAAAVASAASAVGPVGPGEPNQPDDVAEAVKAEvaevTDEVAAESVVQVADR 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516651833 357 SEEAIEEAESKDENATVDEAKKDPKAEEAEEPKKSpAAEKSEEPKKSSATEKIDNNGNVPYVTPLVRKLADKHGVDLNSI 436
Cdd:PRK13108 356 DGESTPAVEETSEADIEREQPGDLAGQAPAAHQVD-AEAASAAPEEPAALASEAHDETEPEVPEKAAPIPDPAKPDELAV 434
|
....
gi 516651833 437 EGTG 440
Cdd:PRK13108 435 AGPG 438
|
|
| PRK14040 |
PRK14040 |
oxaloacetate decarboxylase subunit alpha; |
122-197 |
1.46e-03 |
|
oxaloacetate decarboxylase subunit alpha;
Pssm-ID: 237592 [Multi-domain] Cd Length: 593 Bit Score: 41.84 E-value: 1.46e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 516651833 122 SGGTATDVQMPELGESVT---EGTITQWLKQVGDEVEVDEPLLEVSTDKVDTEIPSPVAGTIVEILADEDDTIDVGAVI 197
Cdd:PRK14040 511 PAAAAAAAPAAAAGEPVTaplAGNIFKVIVTEGQTVAEGDVLLILEAMKMETEIRAAQAGTVRGIAVKEGDAVAVGDTL 589
|
|
| PRK14042 |
PRK14042 |
pyruvate carboxylase subunit B; Provisional |
271-330 |
1.49e-03 |
|
pyruvate carboxylase subunit B; Provisional
Pssm-ID: 172536 [Multi-domain] Cd Length: 596 Bit Score: 42.02 E-value: 1.49e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 516651833 271 GTITQWLKQVGDEVEVDEPLLEVSTDKVDTEIPSPVAGTIVEILADEDDTIDVGAVIARI 330
Cdd:PRK14042 534 GSIIAIHVSAGDEVKAGQAVLVIEAMKMETEIKAPANGVVAEILCQKGDKVTPGQVLIRV 593
|
|
| PRK14042 |
PRK14042 |
pyruvate carboxylase subunit B; Provisional |
141-200 |
1.49e-03 |
|
pyruvate carboxylase subunit B; Provisional
Pssm-ID: 172536 [Multi-domain] Cd Length: 596 Bit Score: 42.02 E-value: 1.49e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 516651833 141 GTITQWLKQVGDEVEVDEPLLEVSTDKVDTEIPSPVAGTIVEILADEDDTIDVGAVIARI 200
Cdd:PRK14042 534 GSIIAIHVSAGDEVKAGQAVLVIEAMKMETEIKAPANGVVAEILCQKGDKVTPGQVLIRV 593
|
|
| PRK06549 |
PRK06549 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
242-324 |
1.65e-03 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235826 [Multi-domain] Cd Length: 130 Bit Score: 39.02 E-value: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516651833 242 EAPKAEAKKSSGGSATDVQMPelgesvteGTITQWLKQVGDEVEVDEPLLEVSTDKVDTEIPSPVAGTIVEILADEDDTI 321
Cdd:PRK06549 49 EAQAPQPAAAAGADAMPSPMP--------GTILKVLVAVGDQVTENQPLLILEAMKMENEIVASSAGTVTAIHVTPGQVV 120
|
...
gi 516651833 322 DVG 324
Cdd:PRK06549 121 NPG 123
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
271-324 |
2.42e-03 |
|
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the Pathway/BioSystem: Urea cycle
Pssm-ID: 440660 [Multi-domain] Cd Length: 1144 Bit Score: 41.22 E-value: 2.42e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 516651833 271 GTITQWLKQVGDEVEVDEPLLEVSTDKVDTEIPSPVAGTIVEILADEDDTIDVG 324
Cdd:COG1038 1085 GTVVKVLVKEGDEVKKGDPLLTIEAMKMETTITAPRDGTVKEVLVKEGDQVEAG 1138
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
271-324 |
3.65e-03 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 40.89 E-value: 3.65e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 516651833 271 GTITQWLKQVGDEVEVDEPLLEVSTDKVDTEIPSPVAGTIVEILADEDDTIDVG 324
Cdd:PRK12999 1085 GSVVTVLVKEGDEVKAGDPLAVIEAMKMETTITAPVDGTVKRVLVKAGDQVEAG 1138
|
|
| PRK05641 |
PRK05641 |
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
17-77 |
4.02e-03 |
|
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235540 [Multi-domain] Cd Length: 153 Bit Score: 38.69 E-value: 4.02e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 516651833 17 GTITQWLKEVGDTVEADEPLLEVSTDKVDTEIPSPAAGVLLEIKAEEDDTIDVGTVIAIIG 77
Cdd:PRK05641 93 GKILRILVREGQQVKVGQGLLILEAMKMENEIPAPKDGVVKKILVKEGDTVDTGQPLIELG 153
|
|
| PRK14040 |
PRK14040 |
oxaloacetate decarboxylase subunit alpha; |
2-77 |
4.92e-03 |
|
oxaloacetate decarboxylase subunit alpha;
Pssm-ID: 237592 [Multi-domain] Cd Length: 593 Bit Score: 40.30 E-value: 4.92e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 516651833 2 AYSVEMPELGESVT---EGTITQWLKEVGDTVEADEPLLEVSTDKVDTEIPSPAAGVLLEIKAEEDDTIDVGTVIAIIG 77
Cdd:PRK14040 515 AAAAPAAAAGEPVTaplAGNIFKVIVTEGQTVAEGDVLLILEAMKMETEIRAAQAGTVRGIAVKEGDAVAVGDTLLTLA 593
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
337-538 |
5.07e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.51 E-value: 5.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516651833 337 SEEATEATEPAESEEERDVPSEEAIEEAESKDENATVDEAKKDPKAEEAEEPKKSPAAEKSEEPKKSSATEKIDNNGNVP 416
Cdd:PTZ00121 1136 AEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAE 1215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516651833 417 YV--------TPLVRKL--ADKHGVDLNSIEGTGVGGRIRKQDvlaaaEGGSAEGSAEQASGKSTDAR-ANWSTKSVDPE 485
Cdd:PTZ00121 1216 EArkaedakkAEAVKKAeeAKKDAEEAKKAEEERNNEEIRKFE-----EARMAHFARRQAAIKAEEARkADELKKAEEKK 1290
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 516651833 486 KAELIGTTQKVNRIRQitAEKMVESLQTSAQLTHVQEVDMSKVWDLRKSNKQA 538
Cdd:PTZ00121 1291 KADEAKKAEEKKKADE--AKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEA 1341
|
|
| GCS_H |
cd06848 |
Glycine cleavage H-protein. Glycine cleavage H-proteins are part of the glycine cleavage ... |
22-59 |
7.41e-03 |
|
Glycine cleavage H-protein. Glycine cleavage H-proteins are part of the glycine cleavage system (GCS) found in bacteria, archea and the mitochondria of eukaryotes. GCS is a multienzyme complex consisting of 4 different components (P-, H-, T- and L-proteins) which catalyzes the oxidative cleavage of glycine. The H-protein shuttles the methylamine group of glycine from the P-protein (glycine dehydrogenase) to the T-protein (aminomethyltransferase) via a lipoyl group, attached to a completely conserved lysine residue.
Pssm-ID: 133457 [Multi-domain] Cd Length: 96 Bit Score: 36.36 E-value: 7.41e-03
10 20 30
....*....|....*....|....*....|....*...
gi 516651833 22 WLKEVGDTVEADEPLLEVSTDKVDTEIPSPAAGVLLEI 59
Cdd:cd06848 35 ELPEVGTEVKKGDPFGSVESVKAASDLYSPVSGEVVEV 72
|
|
| |
