|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11856 |
PRK11856 |
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed |
4-472 |
2.25e-129 |
|
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
Pssm-ID: 237001 [Multi-domain] Cd Length: 411 Bit Score: 381.45 E-value: 2.25e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239651286 4 AKNFHLPDLGEGLPDATIVEWFVKEGDSVRLDDPLVSMETAKAVVEVPSPFSGTVTKLAGAAGDIIVTGAVLAQFAldas 83
Cdd:PRK11856 2 MFEFKMPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDVVPVGSVIAVIE---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239651286 84 qpqrADGQDTGHSHGPAPTHTPSTSDSAAGNTARVVASdnggeiadadstsngesdrddagtvvgamqssNAVQSEQAIA 163
Cdd:PRK11856 78 ----EEGEAEAAAAAEAAPEAPAPEPAPAAAAAAAAAP--------------------------------AAAAAPAAPA 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239651286 164 VGGVRAMPAVRALARKLRVELAQVRATGPDGTVTMADVKQAAAAGSAPVSATRATASVTPingnnanagaqhaaantqaa 243
Cdd:PRK11856 122 AAAAKASPAVRKLARELGVDLSTVKGSGPGGRITKEDVEAAAAAAAPAAAAAAAAAAAPP-------------------- 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239651286 244 nasasdtqqrsalsasgkpmrtqsPSVVAKGQPEQLKGVRRNMARVMADAHSKVVPTTLNDDADIHAW----------QP 313
Cdd:PRK11856 182 ------------------------AAAAEGEERVPLSGMRKAIAKRMVESKREIPHFTLTDEVDVTALlalrkqlkaiGV 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239651286 314 GNDVTVRLVRGIVRACQAVPALNAWFDGEALsrTLHTQVDIGIAVDTEEGLFVPALRNADMLDAHGIRESVNRLRQQVEN 393
Cdd:PRK11856 238 KLTVTDFLIKAVALALKKFPELNASWDDDAI--VLKKYVNIGIAVATDGGLIVPVIRDADKKSLFELAREIKDLAEKARE 315
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1239651286 394 RSIAASELSGYTISLSNFGMFAGRYATPVVVPPCVAIVAAGRARYQLTPVMGSVETHKVMPLSLTFDHRAATGGEAARF 472
Cdd:PRK11856 316 GKLKPEELQGGTFTISNLGMFGGDYFTPIINPPEVAILGVGAIVERPVVVDGEIVVRKVMPLSLSFDHRVIDGADAARF 394
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
2-472 |
1.45e-60 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 207.37 E-value: 1.45e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239651286 2 SQAKNFHLPDLGEgLPDATIVEWFVKEGDSVRLDDPLVSMETAKAVVEVPSPFSGTVTKLAGAAGDIIVTGAVLAQFALD 81
Cdd:PRK11855 117 GGVVEVKVPDIGE-ITEVEVIEWLVKVGDTVEEDQSLITVETDKATMEIPSPVAGVVKEIKVKVGDKVSVGSLLVVIEVA 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239651286 82 ASQPQRAdgqdtghshgPAPTHTPSTSDSAAGNTARVVASDNGGEIADADSTSNGesdrddagtvvgamqssnavqseqa 161
Cdd:PRK11855 196 AAAPAAA----------AAPAAAAPAAAAAAAPAPAPAAAAAPAAAAPAAAAAPG------------------------- 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239651286 162 iavGGVRAMPAVRALARKLRVELAQVRATGPDGTVTMADVKQAAAAGSAPVSATRATASVTPINGnnanagaqhaaantq 241
Cdd:PRK11855 241 ---KAPHASPAVRRLARELGVDLSQVKGTGKKGRITKEDVQAFVKGAMSAAAAAAAAAAAAGGGG--------------- 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239651286 242 aanasasdtqqrSALSASGKPMRTQSPSVvakgQPEQLKGVRRNMARVMADAHSKVVPTTLNDDADI------------H 309
Cdd:PRK11855 303 ------------LGLLPWPKVDFSKFGEI----ETKPLSRIKKISAANLHRSWVTIPHVTQFDEADItdlealrkqlkkE 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239651286 310 AWQPGNDVTVR--LVRGIVRACQAVPALNAWFDGEALSRTLHTQVDIGIAVDTEEGLFVPALRNADMLDAHGIRESVNRL 387
Cdd:PRK11855 367 AEKAGVKLTMLpfFIKAVVAALKEFPVFNASLDEDGDELTYKKYFNIGFAVDTPNGLVVPVIKDVDKKSLLEIAREIAEL 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239651286 388 RQQVENRSIAASELSGYTISLSNFGMFAGRYATPVVVPPCVAIVAAGRAryQLTPVM--GSVETHKVMPLSLTFDHRAAT 465
Cdd:PRK11855 447 AKKARDGKLKPDDMQGGCFTISSLGGIGGTAFTPIINAPEVAILGVGKS--QMKPVWdgKEFVPRLMLPLSLSYDHRVID 524
|
....*..
gi 1239651286 466 GGEAARF 472
Cdd:PRK11855 525 GATAARF 531
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
290-472 |
7.31e-50 |
|
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: 169.26 E-value: 7.31e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239651286 290 MADAHSKVVPTTLNDDADI------------HAWQPGNDVTV--RLVRGIVRACQAVPALNAWFDGEALSRTLHTQVDIG 355
Cdd:pfam00198 1 MTESKQTIPHFTLTDEVDVtellalreelkeDAADEETKLTFlpFLVKAVALALKKFPELNASWDGEEGEIVYKKYVNIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239651286 356 IAVDTEEGLFVPALRNADMLDAHGIRESVNRLRQQVENRSIAASELSGYTISLSNFGMFAGRYATPVVVPPCVAIVAAGR 435
Cdd:pfam00198 81 IAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVGR 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 1239651286 436 ARyqLTPVM--GSVETHKVMPLSLTFDHRAATGGEAARF 472
Cdd:pfam00198 161 IR--KRPVVvdGEIVVRKVMPLSLSFDHRVIDGAEAARF 197
|
|
| PLN02528 |
PLN02528 |
2-oxoisovalerate dehydrogenase E2 component |
7-472 |
7.70e-48 |
|
2-oxoisovalerate dehydrogenase E2 component
Pssm-ID: 215289 [Multi-domain] Cd Length: 416 Bit Score: 170.29 E-value: 7.70e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239651286 7 FHLPDLGEGLPDATIVEWFVKEGDSVRLDDPLVSMETAKAVVEVPSPFSGTVTKLAGAAGDIIVTGAVLAQFALDASQpq 86
Cdd:PLN02528 1 VPLAQTGEGIAECELLRWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGKVAQINFSPGDIVKVGETLLKIMVEDSQ-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239651286 87 radgqdtGHSHGPAPTHTPSTSDSAAgntarvvasdnggeiadADSTSNGESdrddagtvvgamqssnavqseqaiaVGG 166
Cdd:PLN02528 79 -------HLRSDSLLLPTDSSNIVSL-----------------AESDERGSN-------------------------LSG 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239651286 167 VRAMPAVRALARKLRVELAQVRATGPDGTVTMADV-KQAAAAGsapvsatratasvtpingnnanagaqhaaantqaanA 245
Cdd:PLN02528 110 VLSTPAVRHLAKQYGIDLNDILGTGKDGRVLKEDVlKYAAQKG------------------------------------V 153
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239651286 246 SASDTQQRSALSASGKPMRTQSPSVVAKGQPEQ---LKGVRRNMARVMADAHSkvVP-----TTLNDDADIH---AWQPG 314
Cdd:PLN02528 154 VKDSSSAEEATIAEQEEFSTSVSTPTEQSYEDKtipLRGFQRAMVKTMTAAAK--VPhfhyvEEINVDALVElkaSFQEN 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239651286 315 N-DVTVR------LVRGIVRACQAVPALNAWFDGEALSRTLHTQVDIGIAVDTEEGLFVPALRNADMLDAHGIRESVNRL 387
Cdd:PLN02528 232 NtDPTVKhtflpfLIKSLSMALSKYPLLNSCFNEETSEIRLKGSHNIGVAMATEHGLVVPNIKNVQSLSLLEITKELSRL 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239651286 388 RQQVENRSIAASELSGYTISLSNFGMFAGRYATPVVVPPCVAIVAAGR----ARYQLTpvmGSVETHKVMPLSLTFDHRA 463
Cdd:PLN02528 312 QHLAAENKLNPEDITGGTITLSNIGAIGGKFGSPVLNLPEVAIIALGRiqkvPRFVDD---GNVYPASIMTVTIGADHRV 388
|
....*....
gi 1239651286 464 ATGGEAARF 472
Cdd:PLN02528 389 LDGATVARF 397
|
|
| PRK05704 |
PRK05704 |
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase; |
10-472 |
2.19e-42 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
Pssm-ID: 235571 [Multi-domain] Cd Length: 407 Bit Score: 155.38 E-value: 2.19e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239651286 10 PDLGEGLPDATIVEWFVKEGDSVRLDDPLVSMETAKAVVEVPSPFSGTVTKLAGAAGDIIVTGAVLAQFaldasqpqrad 89
Cdd:PRK05704 8 PTLPESVTEATIATWHKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGDTVTVGQVLGRI----------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239651286 90 gqDTGHSHGPAPTHTPSTSDSAAGNTARVVASDnggeiadadstsngESDRDDAgtvvgamqssnavqseqaiavggvrA 169
Cdd:PRK05704 77 --DEGAAAGAAAAAAAAAAAAAAAPAQAQAAAA--------------AEQSNDA-------------------------L 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239651286 170 MPAVRALARKLRVELAQVRATGPDGTVTMADVKQAAAAGSAPVSATRATAsvtpingnnanagaqhaaantqaanasasd 249
Cdd:PRK05704 116 SPAARKLAAENGLDASAVKGTGKGGRVTKEDVLAALAAAAAAPAAPAAAA------------------------------ 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239651286 250 tQQRSALSASGKPMRTQSPSVVAKGQPEQLKGVRR-----------NMARVMA------DAHSKVvpttlnddadiHAwq 312
Cdd:PRK05704 166 -PAAAPAPLGARPEERVPMTRLRKTIAERLLEAQNttamlttfnevDMTPVMDlrkqykDAFEKK-----------HG-- 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239651286 313 pgndvtVRL------VRGIVRACQAVPALNAWFDGEALsrTLHTQVDIGIAVDTEEGLFVPALRNADMLDAHGIRESVNR 386
Cdd:PRK05704 232 ------VKLgfmsffVKAVVEALKRYPEVNASIDGDDI--VYHNYYDIGIAVGTPRGLVVPVLRDADQLSFAEIEKKIAE 303
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239651286 387 LRQQVENRSIAASELSGYTISLSNFGMFAGRYATPVVVPPCVAIVaaGRARYQLTPVM--GSVETHKVMPLSLTFDHRAA 464
Cdd:PRK05704 304 LAKKARDGKLSIEELTGGTFTITNGGVFGSLMSTPIINPPQSAIL--GMHKIKERPVAvnGQIVIRPMMYLALSYDHRII 381
|
....*...
gi 1239651286 465 TGGEAARF 472
Cdd:PRK05704 382 DGKEAVGF 389
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
2-472 |
6.95e-41 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 155.16 E-value: 6.95e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239651286 2 SQAKNFHLPDLGEGlpDATIVEWFVKEGDSVRLDDPLVSMETAKAVVEVPSPFSGTVTKLAGAAGDIIVTGAVLAQFALD 81
Cdd:PRK11854 204 AGVKDVNVPDIGGD--EVEVTEVMVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVKTGSLIMRFEVE 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239651286 82 ASQPQRADGQDtghshgPAPTHTPSTSDSAAGNTARVVASDNGGEIADADSTsngesdrddagtvvgamqssnavqseqa 161
Cdd:PRK11854 282 GAAPAAAPAKQ------EAAAPAPAAAKAEAPAAAPAAKAEGKSEFAENDAY---------------------------- 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239651286 162 iavggVRAMPAVRALARKLRVELAQVRATGPDGTVTMADVKQAAAAGSAPVSATRATASvtpingnnanagaqhaaantq 241
Cdd:PRK11854 328 -----VHATPLVRRLAREFGVNLAKVKGTGRKGRILKEDVQAYVKDAVKRAEAAPAAAA--------------------- 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239651286 242 aanasasdtqqrsalSASGKPMRTQSPSVVAKGQPE----QLKGVRRNMARVMADAHSKVVPTTLNDDADI--------- 308
Cdd:PRK11854 382 ---------------AGGGGPGLLPWPKVDFSKFGEieevELGRIQKISGANLHRNWVMIPHVTQFDKADIteleafrkq 446
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239651286 309 ---HAWQPGNDVT----VRLVRGIVRACQAVPALNAWFDGEALSRTLHTQVDIGIAVDTEEGLFVPALRNADMLDAHGIR 381
Cdd:PRK11854 447 qnaEAEKRKLGVKitplVFIMKAVAAALEQMPRFNSSLSEDGQRLTLKKYVNIGIAVDTPNGLVVPVFKDVNKKGIIELS 526
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239651286 382 ESVNRLRQQVENRSIAASELSGYTISLSNFGMFAGRYATPVVVPPCVAIVAAGRAryQLTPVMG--SVETHKVMPLSLTF 459
Cdd:PRK11854 527 RELMDISKKARDGKLTAGDMQGGCFTISSIGGLGTTHFTPIVNAPEVAILGVSKS--AMEPVWNgkEFAPRLMLPLSLSY 604
|
490
....*....|...
gi 1239651286 460 DHRAATGGEAARF 472
Cdd:PRK11854 605 DHRVIDGADGARF 617
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
2-472 |
1.56e-38 |
|
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: 147.33 E-value: 1.56e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239651286 2 SQAKNFHLPDLGeGLPDATIVEWFVKEGDSVRLDDPLVSMETAKAVVEVPSPFSGTVTKLAGAAGDIIVTGAVLAQFALD 81
Cdd:TIGR01348 114 SGVQEVTVPDIG-DIEKVTVIEVLVKVGDTVSADQSLITLESDKASMEVPAPASGVVKSVKVKVGDSVPTGDLILTLSVA 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239651286 82 ASQPQRADGqdtghshgPAPTHTPSTSDSAagnTARVVASDNGGEIADADSTSngesdrdDAGTVVGAMQSsnavqseqa 161
Cdd:TIGR01348 193 GSTPATAPA--------PASAQPAAQSPAA---TQPEPAAAPAAAKAQAPAPQ-------QAGTQNPAKVD--------- 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239651286 162 iavggvRAMPAVRALARKLRVELAQVRATGPDGTVTMADVKQAAAAGSApvsatRATASvtpingnnanagaqhaaantq 241
Cdd:TIGR01348 246 ------HAAPAVRRLAREFGVDLSAVKGTGIKGRILREDVQRFVKEPSV-----RAQAA--------------------- 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239651286 242 aanasasdtqqrSALSASGKPMRTQSPSV----VAKGQPEQLKGVRRNMARVMADAHSKVVPTTLNDDADIHAWQPGN-- 315
Cdd:TIGR01348 294 ------------AASAAGGAPGALPWPNVdfskFGEVEEVDMSRIRKISGANLTRNWTMIPHVTHFDKADITEMEAFRkq 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239651286 316 ------------DVTVRLVRGIVRACQAVPALNAWFDGEALSRTLHTQVDIGIAVDTEEGLFVPALRNADMLDAHGIRES 383
Cdd:TIGR01348 362 qnaavekegvklTVLHILMKAVAAALKKFPKFNASLDLGGEQLILKKYVNIGVAVDTPNGLLVPVIKDVDRKGITELALE 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239651286 384 VNRLRQQVENRSIAASELSGYTISLSNFGMFAGRYATPVVVPPCVAIVAAGRARYQltPVMGSVE--THKVMPLSLTFDH 461
Cdd:TIGR01348 442 LSDLAKKARDGKLTPDEMQGACFTISSLGGIGGTAFTPIVNAPEVAILGVSKSGME--PVWNGKEfePRLMLPLSLSYDH 519
|
490
....*....|.
gi 1239651286 462 RAATGGEAARF 472
Cdd:TIGR01348 520 RVIDGADAARF 530
|
|
| sucB |
TIGR01347 |
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ... |
10-472 |
2.69e-37 |
|
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: 141.41 E-value: 2.69e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239651286 10 PDLGEGLPDATIVEWFVKEGDSVRLDDPLVSMETAKAVVEVPSPFSGTVTKLAGAAGDIIVTGAVLAQFAldasqpqrad 89
Cdd:TIGR01347 6 PELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAILE---------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239651286 90 gqdtghshgpapthtpstsdsaagntarvvasdnggEIADADSTSNGESDRDDAGTVVGAMQSSNAVQSEQAIAVggvra 169
Cdd:TIGR01347 76 ------------------------------------EGNDATAAPPAKSGEEKEETPAASAAAAPTAAANRPSLS----- 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239651286 170 mPAVRALARKLRVELAQVRATGPDGTVTMADVKQAAAAGSAPVSATRATASVTPINgnnanagaqhaaANTQAANASASD 249
Cdd:TIGR01347 115 -PAARRLAKEHGIDLSAVPGTGVTGRVTKEDIIKKTEAPASAQPPAAAAAAAAPAA------------ATRPEERVKMTR 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239651286 250 TQQRSAlsasgkpmrtqspsvvakgqpEQLKGVRRNMArvMADAHSKVVPTTLNDDADIHAWQPGNDVTVRL------VR 323
Cdd:TIGR01347 182 LRQRIA---------------------ERLKEAQNSTA--MLTTFNEVDMSAVMELRKRYKEEFEKKHGVKLgfmsffVK 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239651286 324 GIVRACQAVPALNAWFDGEALsrTLHTQVDIGIAVDTEEGLFVPALRNADMLDAHGIRESVNRLRQQVENRSIAASELSG 403
Cdd:TIGR01347 239 AVVAALKRFPEVNAEIDGDDI--VYKDYYDISVAVSTDRGLVVPVVRNADRMSFADIEKEIADLGKKARDGKLTLEDMTG 316
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1239651286 404 YTISLSNFGMFAGRYATPVVVPPCVAIVaaGRARYQLTPVM--GSVETHKVMPLSLTFDHRAATGGEAARF 472
Cdd:TIGR01347 317 GTFTITNGGVFGSLMSTPIINPPQSAIL--GMHGIKERPVAvnGQIEIRPMMYLALSYDHRLIDGKEAVTF 385
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
4-79 |
1.14e-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: 105.15 E-value: 1.14e-27
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1239651286 4 AKNFHLPDLGEGLPDATIVEWFVKEGDSVRLDDPLVSMETAKAVVEVPSPFSGTVTKLAGAAGDIIVTGAVLAQFA 79
Cdd:COG0508 2 AIEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVIA 77
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
5-76 |
1.39e-26 |
|
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: 102.10 E-value: 1.39e-26
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1239651286 5 KNFHLPDLGEGLPDATIVEWFVKEGDSVRLDDPLVSMETAKAVVEVPSPFSGTVTKLAGAAGDIIVTGAVLA 76
Cdd:cd06849 1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIA 72
|
|
| PRK11857 |
PRK11857 |
dihydrolipoamide acetyltransferase; Reviewed |
167-472 |
7.54e-25 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237002 [Multi-domain] Cd Length: 306 Bit Score: 104.49 E-value: 7.54e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239651286 167 VRAMPAVRALARKLRVELAQVRATGPDGTVTMADVKQ-AAAAGSAPVSATRATAsvtpingnnanagaqhaaantqaana 245
Cdd:PRK11857 2 ILATPIARALAKKLGIDISLLKGSGRDGKILAEDVENfIKSLKSAPTPAEAASV-------------------------- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239651286 246 sasdtqqrSALSASGKPMRTQSPSVVAKGQPEQLKGVRRNMARVMADAHSKVVPTTLNDDADIHA-W----------QPG 314
Cdd:PRK11857 56 --------SSAQQAAKTAAPAAAPPKLEGKREKVAPIRKAIARAMTNSWSNVAYVNLVNEIDMTKlWdlrksvkdpvLKT 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239651286 315 NDVTVR----LVRGIVRACQAVPALNAWFDgEALSRTLHTQ-VDIGIAVDTEEGLFVPALRNADMLDAHGIRESVNRLRQ 389
Cdd:PRK11857 128 EGVKLTflpfIAKAILIALKEFPIFAAKYD-EATSELVYPDtLNLGIAVDTEAGLMVPVIKNAQKLSIVEIAKEISRLAK 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239651286 390 QVENRSIAASELSGYTISLSNFGMFAGRYATPVVVPPCVAIVAAGRARYQLTPVMGSVETHKVMPLSLTFDHRAATGGEA 469
Cdd:PRK11857 207 AARERKIKPDEMKGGSFTITNYGSVGSLYGVPVINYPELAIAGVGAIIDKAIVKNGQIVAGKVMHLTVAADHRWIDGATI 286
|
...
gi 1239651286 470 ARF 472
Cdd:PRK11857 287 GRF 289
|
|
| PTZ00144 |
PTZ00144 |
dihydrolipoamide succinyltransferase; Provisional |
9-472 |
3.86e-23 |
|
dihydrolipoamide succinyltransferase; Provisional
Pssm-ID: 240289 [Multi-domain] Cd Length: 418 Bit Score: 101.30 E-value: 3.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239651286 9 LPDLGEGLPDATIVEWFVKEGDSVRLDDPLVSMETAKAVVEVPSPFSGTVTKLAGAAGDIIVTGAVLAQFaldasqpqra 88
Cdd:PTZ00144 49 VPTMGDSISEGTVVEWKKKVGDYVKEDEVICIIETDKVSVDIRAPASGVITKIFAEEGDTVEVGAPLSEI---------- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239651286 89 dgqDTGhshGPAPTHTPSTSDSAAGNTARVVASDNGGEIADADSTSNgesdrddagtvvgamqssnavqseqaiavggvr 168
Cdd:PTZ00144 119 ---DTG---GAPPAAAPAAAAAAKAEKTTPEKPKAAAPTPEPPAASK--------------------------------- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239651286 169 amPAVRALARKlrvelaqvratgpdgtvtmadVKQAAAAGSAPVSATRATASVTpingnnanagaqhaaantqaanasas 248
Cdd:PTZ00144 160 --PTPPAAAKP---------------------PEPAPAAKPPPTPVARADPRET-------------------------- 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239651286 249 dtqqRSALSasgkPMRTQspsvVAkgqpEQLKGVRR-----------NMARVMAdahskvVPTTLNDDadihaWQPGNDV 317
Cdd:PTZ00144 191 ----RVPMS----RMRQR----IA----ERLKASQNtcamlttfnecDMSALME------LRKEYKDD-----FQKKHGV 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239651286 318 TVRLVRGIVRAC----QAVPALNAWFDGEALSrtLHTQVDIGIAVDTEEGLFVPALRNADMLDAHGIRESVNRLRQQVEN 393
Cdd:PTZ00144 244 KLGFMSAFVKAStialKKMPIVNAYIDGDEIV--YRNYVDISVAVATPTGLVVPVIRNCENKSFAEIEKELADLAEKARN 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239651286 394 RSIAASELSGYTISLSNFGMFAGRYATPVVVPPCVAIVaaGRARYQLTPVM--GSVETHKVMPLSLTFDHRAATGGEAAR 471
Cdd:PTZ00144 322 NKLTLEDMTGGTFTISNGGVFGSLMGTPIINPPQSAIL--GMHAIKKRPVVvgNEIVIRPIMYLALTYDHRLIDGRDAVT 399
|
.
gi 1239651286 472 F 472
Cdd:PTZ00144 400 F 400
|
|
| PLN02744 |
PLN02744 |
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex |
9-472 |
5.02e-19 |
|
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
Pssm-ID: 215397 [Multi-domain] Cd Length: 539 Bit Score: 89.91 E-value: 5.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239651286 9 LPDLGEGLPDATIVEWFVKEGDSVRLDDPLVSMETAKAVVEVPSPFSGTVTKLAGAAG--DIIVtGAVLAQFALDASQPQ 86
Cdd:PLN02744 117 MPSLSPTMTEGNIARWLKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVKGDGakEIKV-GEVIAITVEEEEDIG 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239651286 87 RADGqdtghshgpaptHTPSTSDSAAGNTARVVASDNGGEIADADSTSngesdrddagtvvgamQSSNAVQSEQAIAVGG 166
Cdd:PLN02744 196 KFKD------------YKPSSSAAPAAPKAKPSPPPPKEEEVEKPASS----------------PEPKASKPSAPPSSGD 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239651286 167 -VRAMPAVRALARKLRVELAQVRATGPDGTVTMADVKQAAAAGSAPVSATRATASVTPingnnanagaqHAAANTQAANA 245
Cdd:PLN02744 248 rIFASPLARKLAEDNNVPLSSIKGTGPDGRIVKADIEDYLASGGKGATAPPSTDSKAP-----------ALDYTDIPNTQ 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239651286 246 SASDTQQRSALSASGKPMRTQSPSVVAkgqpEQLKGVRRNMARVMADAHSKVVptTLNDdadihawqpgndvtvRLVRGI 325
Cdd:PLN02744 317 IRKVTASRLLQSKQTIPHYYLTVDTRV----DKLMALRSQLNSLQEASGGKKI--SVND---------------LVIKAA 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239651286 326 VRACQAVPALNA-WFDgeALSRTLHtQVDIGIAVDTEEGLFVPALRNADMLDAHGIRESVNRLRQQVENRSIAASELSGY 404
Cdd:PLN02744 376 ALALRKVPQCNSsWTD--DYIRQYH-NVNINVAVQTENGLYVPVVKDADKKGLSTIAEEVKQLAQKARENSLKPEDYEGG 452
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1239651286 405 TISLSNF-GMFAGRYATPVVVPPCVAIVAAGRARYQLTP--VMGSVETHKVMPLSLTFDHRAATGGEAARF 472
Cdd:PLN02744 453 TFTVSNLgGPFGIKQFCAIINPPQSAILAVGSAEKRVIPgsGPDQYNFASFMSVTLSCDHRVIDGAIGAEW 523
|
|
| PLN02226 |
PLN02226 |
2-oxoglutarate dehydrogenase E2 component |
321-472 |
4.61e-18 |
|
2-oxoglutarate dehydrogenase E2 component
Pssm-ID: 177871 [Multi-domain] Cd Length: 463 Bit Score: 86.35 E-value: 4.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239651286 321 LVRGIVRACQAVPALNAWFDGEALsrTLHTQVDIGIAVDTEEGLFVPALRNADMLDAHGIRESVNRLRQQVENRSIAASE 400
Cdd:PLN02226 296 FIKAAVSALQHQPVVNAVIDGDDI--IYRDYVDISIAVGTSKGLVVPVIRGADKMNFAEIEKTINGLAKKANEGTISIDE 373
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1239651286 401 LSGYTISLSNFGMFAGRYATPVVVPPCVAIVAAGRARYQLTPVMGSVETHKVMPLSLTFDHRAATGGEAARF 472
Cdd:PLN02226 374 MAGGSFTVSNGGVYGSLISTPIINPPQSAILGMHSIVSRPMVVGGSVVPRPMMYVALTYDHRLIDGREAVYF 445
|
|
| PRK14843 |
PRK14843 |
dihydrolipoamide acetyltransferase; Provisional |
167-472 |
7.90e-16 |
|
dihydrolipoamide acetyltransferase; Provisional
Pssm-ID: 184847 [Multi-domain] Cd Length: 347 Bit Score: 78.79 E-value: 7.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239651286 167 VRAMPAVRALARKLRVELAQVRATGPDGTVTMADVKQAAAAGSAPVSA-TRATASVTPINGNNANAGAQHAAANTQAANA 245
Cdd:PRK14843 6 LRATPAARKLADDLGINLYDVSGSGANGRVHKEDVETYKDTNVVRISPlAKRIALEHNIAWQEIQGTGHRGKIMKKDVLA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239651286 246 SASDTQQRSALSASGKPMRTQ--SPSVVAKGQPEQ--LKGVRRNMARVMADAHSKVVPTTLNDDADIHAW---------- 311
Cdd:PRK14843 86 LLPENIENDSIKSPAQIEKVEevPDNVTPYGEIERipMTPMRKVIAQRMVESYLTAPTFTLNYEVDMTEMlalrkkvlep 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239651286 312 ---QPGNDVTVR--LVRGIVRACQAVPALNAWFDGEALSRTLHTQVDIGIAVDTEEGLFVPALRNADMLDAHGIRESVNR 386
Cdd:PRK14843 166 imeATGKKTTVTdlLSLAVVKTLMKHPYINASLTEDGKTIITHNYVNLAMAVGMDNGLMTPVVYNAEKMSLSELVVAFKD 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239651286 387 LRQQVENRSIAASELSGYTISLSNFGMFAGRYATPVVVPPCVAIVAAGRARYQLTPVMGSVETHKVMPLSLTFDHRAATG 466
Cdd:PRK14843 246 VIGRTLDGKLAPSELQNSTFTISNLGMFGVQSFGPIINQPNSAILGVSSTIEKPVVVNGEIVIRPIMSLGLTIDHRVVDG 325
|
....*.
gi 1239651286 467 GEAARF 472
Cdd:PRK14843 326 MAGAKF 331
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
7-76 |
3.84e-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: 67.24 E-value: 3.84e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239651286 7 FHLPDLGEGLpDATIVEWFVKEGDSVRLDDPLVSMETAKAVVEVPSPFSGTVTKLAGAAGDIIVTGAVLA 76
Cdd:pfam00364 3 IKSPMIGESV-REGVVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLA 71
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
20-78 |
1.06e-10 |
|
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all biotin-dependent enzymes, such as acetyl-CoA carboxylase, pyruvate carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA carboxylase, geranyl-CoA carboxylase, oxaloacetate decarboxylase, methylmalonyl-CoA decarboxylase, transcarboxylase and urea amidolyase. This domain functions in transferring CO2 from one subsite to another, allowing carboxylation, decarboxylation, or transcarboxylation. During this process, biotin is covalently attached to a specific lysine.
Pssm-ID: 133459 [Multi-domain] Cd Length: 67 Bit Score: 57.43 E-value: 1.06e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1239651286 20 TIVEWFVKEGDSVRLDDPLVSMETAKAVVEVPSPFSGTVTKLAGAAGDIIVTGAVLAQF 78
Cdd:cd06850 9 TVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
9-60 |
1.33e-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: 57.07 E-value: 1.33e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1239651286 9 LPDLGEGLPDATIVEWFVKEGDSVRLDDPLVSMETAKAVVEVPSPFSGTVTK 60
Cdd:cd06663 4 IPDLAQHLGDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKK 55
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
9-76 |
1.22e-09 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 59.96 E-value: 1.22e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1239651286 9 LPDLGEGLPDATIVEWFVKEGDSVRLDDPLVSMETAKAVVEVPSPFSGTVTKLAGAAGDIIVTGAVLA 76
Cdd:PRK14875 7 MPKWGLSMTEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGETLPVGALLA 74
|
|
| E3_binding |
pfam02817 |
e3 binding domain; This family represents a small domain of the E2 subunit of 2-oxo-acid ... |
167-202 |
4.13e-09 |
|
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: 51.92 E-value: 4.13e-09
10 20 30
....*....|....*....|....*....|....*.
gi 1239651286 167 VRAMPAVRALARKLRVELAQVRATGPDGTVTMADVK 202
Cdd:pfam02817 1 VLASPAARKLARELGIDLSDVKGTGPGGRITKEDVE 36
|
|
| kgd |
PRK12270 |
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ... |
325-472 |
1.16e-07 |
|
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;
Pssm-ID: 237030 [Multi-domain] Cd Length: 1228 Bit Score: 54.51 E-value: 1.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239651286 325 IVRACQAVPALNAWF---DGEAlSRTLHTQVDIGIAVDTEE-----GLFVPALRNADMLDAHGIRESVNRLRQQVENRSI 396
Cdd:PRK12270 180 LVQALKAFPNMNRHYaevDGKP-TLVTPAHVNLGLAIDLPKkdgsrQLVVPAIKGAETMDFAQFWAAYEDIVRRARDGKL 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239651286 397 AASELSGYTISLSNFGMFAGRYATPVVVPPCVAIVAAG----RARYQLTpvmgSVET------HKVMPLSLTFDHRAATG 466
Cdd:PRK12270 259 TADDFQGTTISLTNPGGIGTVHSVPRLMKGQGAIIGVGameyPAEFQGA----SEERlaelgiSKVMTLTSTYDHRIIQG 334
|
....*.
gi 1239651286 467 GEAARF 472
Cdd:PRK12270 335 AESGEF 340
|
|
| GCS_H |
cd06848 |
Glycine cleavage H-protein. Glycine cleavage H-proteins are part of the glycine cleavage ... |
16-60 |
2.01e-06 |
|
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: 45.99 E-value: 2.01e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1239651286 16 LPDATIVEwFVKEGDSVRLDDPLVSMETAKAVVEVPSPFSGTVTK 60
Cdd:cd06848 28 LGDIVFVE-LPEVGTEVKKGDPFGSVESVKAASDLYSPVSGEVVE 71
|
|
| GcvH |
COG0509 |
Glycine cleavage system protein H (lipoate-binding) [Amino acid transport and metabolism]; ... |
16-59 |
9.81e-05 |
|
Glycine cleavage system protein H (lipoate-binding) [Amino acid transport and metabolism]; Glycine cleavage system protein H (lipoate-binding) is part of the Pathway/BioSystem: Glycine cleavage
Pssm-ID: 440275 Cd Length: 128 Bit Score: 42.03 E-value: 9.81e-05
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1239651286 16 LPDATIVEWfVKEGDSVRLDDPLVSMETAKAVVEVPSPFSGTVT 59
Cdd:COG0509 36 LGDIVFVEL-PEVGTEVEAGEPFGVVESVKAVSDLYAPVSGEVV 78
|
|
| PRK09282 |
PRK09282 |
pyruvate carboxylase subunit B; Validated |
20-75 |
1.10e-04 |
|
pyruvate carboxylase subunit B; Validated
Pssm-ID: 236449 [Multi-domain] Cd Length: 592 Bit Score: 44.83 E-value: 1.10e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1239651286 20 TIVEWFVKEGDSVRLDDPLVSMETAKAVVEVPSPFSGTVTKLAGAAGDIIVTGAVL 75
Cdd:PRK09282 532 TVVKVKVKEGDKVKAGDTVLVLEAMKMENEIQAPVDGTVKEILVKEGDRVNPGDVL 587
|
|
| AccB |
COG0511 |
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ... |
17-75 |
1.22e-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: 41.80 E-value: 1.22e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1239651286 17 PDATIvewFVKEGDSVRLDDPLVSMETAKAVVEVPSPFSGTVTKLAGAAGDIIVTGAVL 75
Cdd:COG0511 77 PGAKP---FVKVGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVVEILVENGQPVEYGQPL 132
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
20-72 |
7.12e-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: 7.12e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1239651286 20 TIVEWFVKEGDSVRLDDPLVS-----METAkavveVPSPFSGTVTKLAGAAGDIIVTG 72
Cdd:COG1038 1086 TVVKVLVKEGDEVKKGDPLLTieamkMETT-----ITAPRDGTVKEVLVKEGDQVEAG 1138
|
|
| GCV_H |
pfam01597 |
Glycine cleavage H-protein; This is a family of glycine cleavage H-proteins, part of the ... |
27-59 |
9.25e-04 |
|
Glycine cleavage H-protein; This is a family of glycine cleavage H-proteins, part of the glycine cleavage multienzyme complex (GCV) found in bacteria and the mitochondria of eukaryotes. GCV catalyzes the catabolism of glycine in eukaryotes. A lipoyl group is attached to a completely conserved lysine residue. The H protein shuttles the methylamine group of glycine from the P protein to the T protein.
Pssm-ID: 396258 Cd Length: 122 Bit Score: 39.24 E-value: 9.25e-04
10 20 30
....*....|....*....|....*....|...
gi 1239651286 27 KEGDSVRLDDPLVSMETAKAVVEVPSPFSGTVT 59
Cdd:pfam01597 40 EVGTKVKKGESLAAIESVKAASPIYAPVSGEVV 72
|
|
| PRK05889 |
PRK05889 |
biotin/lipoyl-binding carrier protein; |
19-76 |
1.66e-03 |
|
biotin/lipoyl-binding carrier protein;
Pssm-ID: 180306 [Multi-domain] Cd Length: 71 Bit Score: 37.10 E-value: 1.66e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1239651286 19 ATIVEWFVKEGDSVRLDDPLVSMETAKAVVEVPSPFSGTVTKLAGAAGDIIVTGAVLA 76
Cdd:PRK05889 11 ASVLEVVVNEGDQIGKGDTLVLLESMKMEIPVLAEVAGTVSKVSVSVGDVIQAGDLIA 68
|
|
| PRK14040 |
PRK14040 |
oxaloacetate decarboxylase subunit alpha; |
20-79 |
3.15e-03 |
|
oxaloacetate decarboxylase subunit alpha;
Pssm-ID: 237592 [Multi-domain] Cd Length: 593 Bit Score: 39.91 E-value: 3.15e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239651286 20 TIVEWFVKEGDSVRLDDPLVSMETAKAVVEVPSPFSGTVTKLAGAAGDIIVTGAVLAQFA 79
Cdd:PRK14040 534 NIFKVIVTEGQTVAEGDVLLILEAMKMETEIRAAQAGTVRGIAVKEGDAVAVGDTLLTLA 593
|
|
| PRK05641 |
PRK05641 |
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
21-75 |
4.22e-03 |
|
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235540 [Multi-domain] Cd Length: 153 Bit Score: 37.92 E-value: 4.22e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1239651286 21 IVEWFVKEGDSVRLDDPLVSMETAKAVVEVPSPFSGTVTKLAGAAGDIIVTGAVL 75
Cdd:PRK05641 95 ILRILVREGQQVKVGQGLLILEAMKMENEIPAPKDGVVKKILVKEGDTVDTGQPL 149
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
20-72 |
7.95e-03 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 38.97 E-value: 7.95e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1239651286 20 TIVEWFVKEGDSVRLDDPLVS-----METAkavveVPSPFSGTVTKLAGAAGDIIVTG 72
Cdd:PRK12999 1086 SVVTVLVKEGDEVKAGDPLAVieamkMETT-----ITAPVDGTVKRVLVKAGDQVEAG 1138
|
|
| |
