|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02528 |
PLN02528 |
2-oxoisovalerate dehydrogenase E2 component |
66-492 |
1.41e-177 |
|
2-oxoisovalerate dehydrogenase E2 component
Pssm-ID: 215289 [Multi-domain] Cd Length: 416 Bit Score: 504.64 E-value: 1.41e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556990772 66 FKLSDIGEGITEVTVKEWYVKEGDSVSQFDSICEVQSDKASVTITSRYDGVIRKLYYNVDDMAFVGKPLVDIETDAVKDV 145
Cdd:PLN02528 1 VPLAQTGEGIAECELLRWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGKVAQINFSPGDIVKVGETLLKIMVEDSQHL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556990772 146 asEQDVVETPAVSHEEHTHQEIKGHK-----TLATPAVRRLAMENNIKLSEVVGTGKDGRILKEDILNYLAkQTGAIIPP 220
Cdd:PLN02528 81 --RSDSLLLPTDSSNIVSLAESDERGsnlsgVLSTPAVRHLAKQYGIDLNDILGTGKDGRVLKEDVLKYAA-QKGVVKDS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556990772 221 SPKLEIIPPApqpvaipakpkDREPGDPKPIVKPAVFIgkDKTEPVKGFQKAMVKTMSAALKIPHFGYCDEVDLTQLNQF 300
Cdd:PLN02528 158 SSAEEATIAE-----------QEEFSTSVSTPTEQSYE--DKTIPLRGFQRAMVKTMTAAAKVPHFHYVEEINVDALVEL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556990772 301 REELKSMANAQGVRISFMPFFLKAASLGLLHYPILNASVDENCQNITYKAAHNIGIAMDTQQGLIVPNVKNVQALSIFEI 380
Cdd:PLN02528 225 KASFQENNTDPTVKHTFLPFLIKSLSMALSKYPLLNSCFNEETSEIRLKGSHNIGVAMATEHGLVVPNIKNVQSLSLLEI 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556990772 381 AAELNRLQTLGSTGQLGTTDLTNGTFTLSNIGSIGGTYAKPVILPPEVAIGALGKIQLVPRFNDIGEVVKASVMNVSWSA 460
Cdd:PLN02528 305 TKELSRLQHLAAENKLNPEDITGGTITLSNIGAIGGKFGSPVLNLPEVAIIALGRIQKVPRFVDDGNVYPASIMTVTIGA 384
|
410 420 430
....*....|....*....|....*....|..
gi 556990772 461 DHRIIDGATMARFSNLWKSYLEHPASMLLDLK 492
Cdd:PLN02528 385 DHRVLDGATVARFCNEWKSYVEKPELLMLHMR 416
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
277-488 |
7.83e-95 |
|
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to three copies of a lipoyl binding domain followed by the catalytic domain.
Pssm-ID: 425518 [Multi-domain] Cd Length: 212 Bit Score: 285.98 E-value: 7.83e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556990772 277 MSAAL-KIPHFGYCDEVDLTQLNQFREELKSMANAQGVRISFMPFFLKAASLGLLHYPILNASVDENCQNITYKAAHNIG 355
Cdd:pfam00198 1 MTESKqTIPHFTLTDEVDVTELLALREELKEDAADEETKLTFLPFLVKAVALALKKFPELNASWDGEEGEIVYKKYVNIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556990772 356 IAMDTQQGLIVPNVKNVQALSIFEIAAELNRLQTLGSTGQLGTTDLTNGTFTLSNIGSIGGTYAKPVILPPEVAIGALGK 435
Cdd:pfam00198 81 IAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVGR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 556990772 436 IQLVPRFNDiGEVVKASVMNVSWSADHRIIDGATMARFSNLWKSYLEHPASML 488
Cdd:pfam00198 161 IRKRPVVVD-GEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELLL 212
|
|
| sucB |
TIGR01347 |
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ... |
64-491 |
3.78e-73 |
|
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: 236.94 E-value: 3.78e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556990772 64 VQFKLSDIGEGITEVTVKEWYVKEGDSVSQFDSICEVQSDKASVTITSRYDGVIRKLYYNVDDMAFVGKPLVDIETDAVK 143
Cdd:TIGR01347 1 IEIKVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAILEEGNDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556990772 144 DVAS--EQDVVETPAVSHEEHTHQEIKGHKTLATPAVRRLAMENNIKLSEVVGTGKDGRILKEDILNYLAKQTGAIIPPS 221
Cdd:TIGR01347 81 TAAPpaKSGEEKEETPAASAAAAPTAAANRPSLSPAARRLAKEHGIDLSAVPGTGVTGRVTKEDIIKKTEAPASAQPPAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556990772 222 PKLEIIPPAPqpvaipAKPKDREPgdpkpivkpAVFIGKDKTEPVKGFQK--AMVKTMsaalkiphfgycDEVDLTQLNQ 299
Cdd:TIGR01347 161 AAAAAAPAAA------TRPEERVK---------MTRLRQRIAERLKEAQNstAMLTTF------------NEVDMSAVME 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556990772 300 FREELK-SMANAQGVRISFMPFFLKAASLGLLHYPILNASVDENcqNITYKAAHNIGIAMDTQQGLIVPNVKNVQALSIF 378
Cdd:TIGR01347 214 LRKRYKeEFEKKHGVKLGFMSFFVKAVVAALKRFPEVNAEIDGD--DIVYKDYYDISVAVSTDRGLVVPVVRNADRMSFA 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556990772 379 EIAAELNRLQTLGSTGQLGTTDLTNGTFTLSNIGSIGGTYAKPVILPPEVAIGALGKIQLVPRFNDiGEVVKASVMNVSW 458
Cdd:TIGR01347 292 DIEKEIADLGKKARDGKLTLEDMTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHGIKERPVAVN-GQIEIRPMMYLAL 370
|
410 420 430
....*....|....*....|....*....|...
gi 556990772 459 SADHRIIDGATMARFSNLWKSYLEHPASMLLDL 491
Cdd:TIGR01347 371 SYDHRLIDGKEAVTFLVTIKELLEDPRRLLLDL 403
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
64-137 |
7.23e-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: 100.17 E-value: 7.23e-26
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 556990772 64 VQFKLSDIGEGITEVTVKEWYVKEGDSVSQFDSICEVQSDKASVTITSRYDGVIRKLYYNVDDMAFVGKPLVDI 137
Cdd:cd06849 1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
64-137 |
1.45e-21 |
|
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: 88.20 E-value: 1.45e-21
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 556990772 64 VQFKLSDIGEGITEVTVKEWYVKEGDSVSQFDSICEVQSDKASVTITSRYDGVIRKLYYNVDDMAFVGKPLVDI 137
Cdd:COG0508 3 IEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02528 |
PLN02528 |
2-oxoisovalerate dehydrogenase E2 component |
66-492 |
1.41e-177 |
|
2-oxoisovalerate dehydrogenase E2 component
Pssm-ID: 215289 [Multi-domain] Cd Length: 416 Bit Score: 504.64 E-value: 1.41e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556990772 66 FKLSDIGEGITEVTVKEWYVKEGDSVSQFDSICEVQSDKASVTITSRYDGVIRKLYYNVDDMAFVGKPLVDIETDAVKDV 145
Cdd:PLN02528 1 VPLAQTGEGIAECELLRWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGKVAQINFSPGDIVKVGETLLKIMVEDSQHL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556990772 146 asEQDVVETPAVSHEEHTHQEIKGHK-----TLATPAVRRLAMENNIKLSEVVGTGKDGRILKEDILNYLAkQTGAIIPP 220
Cdd:PLN02528 81 --RSDSLLLPTDSSNIVSLAESDERGsnlsgVLSTPAVRHLAKQYGIDLNDILGTGKDGRVLKEDVLKYAA-QKGVVKDS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556990772 221 SPKLEIIPPApqpvaipakpkDREPGDPKPIVKPAVFIgkDKTEPVKGFQKAMVKTMSAALKIPHFGYCDEVDLTQLNQF 300
Cdd:PLN02528 158 SSAEEATIAE-----------QEEFSTSVSTPTEQSYE--DKTIPLRGFQRAMVKTMTAAAKVPHFHYVEEINVDALVEL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556990772 301 REELKSMANAQGVRISFMPFFLKAASLGLLHYPILNASVDENCQNITYKAAHNIGIAMDTQQGLIVPNVKNVQALSIFEI 380
Cdd:PLN02528 225 KASFQENNTDPTVKHTFLPFLIKSLSMALSKYPLLNSCFNEETSEIRLKGSHNIGVAMATEHGLVVPNIKNVQSLSLLEI 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556990772 381 AAELNRLQTLGSTGQLGTTDLTNGTFTLSNIGSIGGTYAKPVILPPEVAIGALGKIQLVPRFNDIGEVVKASVMNVSWSA 460
Cdd:PLN02528 305 TKELSRLQHLAAENKLNPEDITGGTITLSNIGAIGGKFGSPVLNLPEVAIIALGRIQKVPRFVDDGNVYPASIMTVTIGA 384
|
410 420 430
....*....|....*....|....*....|..
gi 556990772 461 DHRIIDGATMARFSNLWKSYLEHPASMLLDLK 492
Cdd:PLN02528 385 DHRVLDGATVARFCNEWKSYVEKPELLMLHMR 416
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
55-489 |
1.88e-155 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 453.13 E-value: 1.88e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556990772 55 TTVVTSGQLVQFKLSDIGEgITEVTVKEWYVKEGDSVSQFDSICEVQSDKASVTITSRYDGVIRKLYYNVDDMAFVGKPL 134
Cdd:PRK11855 111 AAAAAGGGVVEVKVPDIGE-ITEVEVIEWLVKVGDTVEEDQSLITVETDKATMEIPSPVAGVVKEIKVKVGDKVSVGSLL 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556990772 135 VDIETDAVKDVASEQDVVETPAVSHEEH---------------THQEIKGHK-TLATPAVRRLAMENNIKLSEVVGTGKD 198
Cdd:PRK11855 190 VVIEVAAAAPAAAAAPAAAAPAAAAAAApapapaaaaapaaaaPAAAAAPGKaPHASPAVRRLARELGVDLSQVKGTGKK 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556990772 199 GRILKEDILNYL-AKQTGAIippspkleiiPPAPQPVAIPAKPKDREPgdpKPIVKPAVFiGKDKTEPVKGFQKAMVKTM 277
Cdd:PRK11855 270 GRITKEDVQAFVkGAMSAAA----------AAAAAAAAAGGGGLGLLP---WPKVDFSKF-GEIETKPLSRIKKISAANL 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556990772 278 SAAL-KIPHFGYCDEVDLTQLNQFREELKSMANAQGVRISFMPFFLKAASLGLLHYPILNASVDENCQNITYKAAHNIGI 356
Cdd:PRK11855 336 HRSWvTIPHVTQFDEADITDLEALRKQLKKEAEKAGVKLTMLPFFIKAVVAALKEFPVFNASLDEDGDELTYKKYFNIGF 415
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556990772 357 AMDTQQGLIVPNVKNVQALSIFEIAAELNRLQTLGSTGQLGTTDLTNGTFTLSNIGSIGGTYAKPVILPPEVAIGALGKI 436
Cdd:PRK11855 416 AVDTPNGLVVPVIKDVDKKSLLEIAREIAELAKKARDGKLKPDDMQGGCFTISSLGGIGGTAFTPIINAPEVAILGVGKS 495
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 556990772 437 QLVPrFNDIGEVVKASVMNVSWSADHRIIDGATMARFSNLWKSYLEHPASMLL 489
Cdd:PRK11855 496 QMKP-VWDGKEFVPRLMLPLSLSYDHRVIDGATAARFTNYLKQLLADPRRMLL 547
|
|
| PRK11856 |
PRK11856 |
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed |
64-490 |
2.43e-131 |
|
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
Pssm-ID: 237001 [Multi-domain] Cd Length: 411 Bit Score: 386.84 E-value: 2.43e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556990772 64 VQFKLSDIGEGITEVTVKEWYVKEGDSVSQFDSICEVQSDKASVTITSRYDGVIRKLYYNVDDMAFVGKPLVDIETDAVK 143
Cdd:PRK11856 3 FEFKMPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDVVPVGSVIAVIEEEGEA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556990772 144 DVASEQDVVET--------------PAVSHEEHTHQEIKGHKTLATPAVRRLAMENNIKLSEVVGTGKDGRILKEDILNY 209
Cdd:PRK11856 83 EAAAAAEAAPEapapepapaaaaaaAAAPAAAAAPAAPAAAAAKASPAVRKLARELGVDLSTVKGSGPGGRITKEDVEAA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556990772 210 LAKQTgaiippspkleiiPPAPQPVAIPAKPKDREPGDpkpivkpavfigkDKTEPVKGFQKAMVKTMSAA-LKIPHFGY 288
Cdd:PRK11856 163 AAAAA-------------PAAAAAAAAAAAPPAAAAEG-------------EERVPLSGMRKAIAKRMVESkREIPHFTL 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556990772 289 CDEVDLTQLNQFREELKsmanAQGVRISFMPFFLKAASLGLLHYPILNASVDEncQNITYKAAHNIGIAMDTQQGLIVPN 368
Cdd:PRK11856 217 TDEVDVTALLALRKQLK----AIGVKLTVTDFLIKAVALALKKFPELNASWDD--DAIVLKKYVNIGIAVATDGGLIVPV 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556990772 369 VKNVQALSIFEIAAELNRLQTLGSTGQLGTTDLTNGTFTLSNIGSIGGTYAKPVILPPEVAIGALGKIQLVPRFNDiGEV 448
Cdd:PRK11856 291 IRDADKKSLFELAREIKDLAEKAREGKLKPEELQGGTFTISNLGMFGGDYFTPIINPPEVAILGVGAIVERPVVVD-GEI 369
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 556990772 449 VKASVMNVSWSADHRIIDGATMARFSNLWKSYLEHPASMLLD 490
Cdd:PRK11856 370 VVRKVMPLSLSFDHRVIDGADAARFLKALKELLENPALLLLE 411
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
277-488 |
7.83e-95 |
|
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to three copies of a lipoyl binding domain followed by the catalytic domain.
Pssm-ID: 425518 [Multi-domain] Cd Length: 212 Bit Score: 285.98 E-value: 7.83e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556990772 277 MSAAL-KIPHFGYCDEVDLTQLNQFREELKSMANAQGVRISFMPFFLKAASLGLLHYPILNASVDENCQNITYKAAHNIG 355
Cdd:pfam00198 1 MTESKqTIPHFTLTDEVDVTELLALREELKEDAADEETKLTFLPFLVKAVALALKKFPELNASWDGEEGEIVYKKYVNIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556990772 356 IAMDTQQGLIVPNVKNVQALSIFEIAAELNRLQTLGSTGQLGTTDLTNGTFTLSNIGSIGGTYAKPVILPPEVAIGALGK 435
Cdd:pfam00198 81 IAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVGR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 556990772 436 IQLVPRFNDiGEVVKASVMNVSWSADHRIIDGATMARFSNLWKSYLEHPASML 488
Cdd:pfam00198 161 IRKRPVVVD-GEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELLL 212
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
74-482 |
1.36e-79 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 260.32 E-value: 1.36e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556990772 74 GITEVTVKEWYVKEGDSVSQFDSICEVQSDKASVTITSRYDGVIRKLYYNVDDMAFVGKPLVDIETDAVKDVASEQDV-- 151
Cdd:PRK11854 215 GGDEVEVTEVMVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVKTGSLIMRFEVEGAAPAAAPAKQea 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556990772 152 -------------VETPAVSHEEHTHQEIKGHKTLATPAVRRLAMENNIKLSEVVGTGKDGRILKEDILNYlAKQTgaii 218
Cdd:PRK11854 295 aapapaaakaeapAAAPAAKAEGKSEFAENDAYVHATPLVRRLAREFGVNLAKVKGTGRKGRILKEDVQAY-VKDA---- 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556990772 219 ppSPKLEIIPPAPqpvaipAKPKDREPGDPKPIVKPAVFiGKDKTEPVKGFQKAMVKTMSAAL-KIPHFGYCDEVDLTQL 297
Cdd:PRK11854 370 --VKRAEAAPAAA------AAGGGGPGLLPWPKVDFSKF-GEIEEVELGRIQKISGANLHRNWvMIPHVTQFDKADITEL 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556990772 298 NQFREELKSMANAQ--GVRISFMPFFLKAASLGLLHYPILNASVDENCQNITYKAAHNIGIAMDTQQGLIVPNVKNVQAL 375
Cdd:PRK11854 441 EAFRKQQNAEAEKRklGVKITPLVFIMKAVAAALEQMPRFNSSLSEDGQRLTLKKYVNIGIAVDTPNGLVVPVFKDVNKK 520
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556990772 376 SIFEIAAELNRLQTLGSTGQLGTTDLTNGTFTLSNIGSIGGTYAKPVILPPEVAIGALGKIQLVPRFNdIGEVVKASVMN 455
Cdd:PRK11854 521 GIIELSRELMDISKKARDGKLTAGDMQGGCFTISSIGGLGTTHFTPIVNAPEVAILGVSKSAMEPVWN-GKEFAPRLMLP 599
|
410 420
....*....|....*....|....*..
gi 556990772 456 VSWSADHRIIDGATMARFSNLWKSYLE 482
Cdd:PRK11854 600 LSLSYDHRVIDGADGARFITIINDRLS 626
|
|
| sucB |
TIGR01347 |
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ... |
64-491 |
3.78e-73 |
|
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: 236.94 E-value: 3.78e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556990772 64 VQFKLSDIGEGITEVTVKEWYVKEGDSVSQFDSICEVQSDKASVTITSRYDGVIRKLYYNVDDMAFVGKPLVDIETDAVK 143
Cdd:TIGR01347 1 IEIKVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAILEEGNDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556990772 144 DVAS--EQDVVETPAVSHEEHTHQEIKGHKTLATPAVRRLAMENNIKLSEVVGTGKDGRILKEDILNYLAKQTGAIIPPS 221
Cdd:TIGR01347 81 TAAPpaKSGEEKEETPAASAAAAPTAAANRPSLSPAARRLAKEHGIDLSAVPGTGVTGRVTKEDIIKKTEAPASAQPPAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556990772 222 PKLEIIPPAPqpvaipAKPKDREPgdpkpivkpAVFIGKDKTEPVKGFQK--AMVKTMsaalkiphfgycDEVDLTQLNQ 299
Cdd:TIGR01347 161 AAAAAAPAAA------TRPEERVK---------MTRLRQRIAERLKEAQNstAMLTTF------------NEVDMSAVME 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556990772 300 FREELK-SMANAQGVRISFMPFFLKAASLGLLHYPILNASVDENcqNITYKAAHNIGIAMDTQQGLIVPNVKNVQALSIF 378
Cdd:TIGR01347 214 LRKRYKeEFEKKHGVKLGFMSFFVKAVVAALKRFPEVNAEIDGD--DIVYKDYYDISVAVSTDRGLVVPVVRNADRMSFA 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556990772 379 EIAAELNRLQTLGSTGQLGTTDLTNGTFTLSNIGSIGGTYAKPVILPPEVAIGALGKIQLVPRFNDiGEVVKASVMNVSW 458
Cdd:TIGR01347 292 DIEKEIADLGKKARDGKLTLEDMTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHGIKERPVAVN-GQIEIRPMMYLAL 370
|
410 420 430
....*....|....*....|....*....|...
gi 556990772 459 SADHRIIDGATMARFSNLWKSYLEHPASMLLDL 491
Cdd:TIGR01347 371 SYDHRLIDGKEAVTFLVTIKELLEDPRRLLLDL 403
|
|
| PRK05704 |
PRK05704 |
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase; |
67-491 |
2.75e-71 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
Pssm-ID: 235571 [Multi-domain] Cd Length: 407 Bit Score: 232.03 E-value: 2.75e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556990772 67 KLSDIGEGITEVTVKEWYVKEGDSVSQFDSICEVQSDKASVTITSRYDGVIRKLYYNVDDMAFVGKPLVDIETDAV--KD 144
Cdd:PRK05704 6 KVPTLPESVTEATIATWHKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGDTVTVGQVLGRIDEGAAagAA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556990772 145 VASEQDVVETPAVSHEEHTHQEIKGHKTLATPAVRRLAMENNIKLSEVVGTGKDGRILKEDILNYLAKQTGAIIPPSPKl 224
Cdd:PRK05704 86 AAAAAAAAAAAAAPAQAQAAAAAEQSNDALSPAARKLAAENGLDASAVKGTGKGGRVTKEDVLAALAAAAAAPAAPAAA- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556990772 225 eiiPPAPQPVAIPAKPKDREPgdpkpivkpAVFIGKDKTEPVKGFQK--AMVKTmsaalkiphFgycDEVDLTQLNQFRE 302
Cdd:PRK05704 165 ---APAAAPAPLGARPEERVP---------MTRLRKTIAERLLEAQNttAMLTT---------F---NEVDMTPVMDLRK 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556990772 303 ELKSMANAQ-GVRISFMPFFLKAASLGLLHYPILNASVDENcqNITYKAAHNIGIAMDTQQGLIVPNVKNVQALSIFEIA 381
Cdd:PRK05704 221 QYKDAFEKKhGVKLGFMSFFVKAVVEALKRYPEVNASIDGD--DIVYHNYYDIGIAVGTPRGLVVPVLRDADQLSFAEIE 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556990772 382 AELNRLQTLGSTGQLGTTDLTNGTFTLSNigsiGGTY----AKPVILPPEVAIgaLG--KIQLVPRFNDiGEVVKASVMN 455
Cdd:PRK05704 299 KKIAELAKKARDGKLSIEELTGGTFTITN----GGVFgslmSTPIINPPQSAI--LGmhKIKERPVAVN-GQIVIRPMMY 371
|
410 420 430
....*....|....*....|....*....|....*.
gi 556990772 456 VSWSADHRIIDGATMARFSNLWKSYLEHPASMLLDL 491
Cdd:PRK05704 372 LALSYDHRIIDGKEAVGFLVTIKELLEDPERLLLDL 407
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
60-489 |
6.02e-70 |
|
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: 232.46 E-value: 6.02e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556990772 60 SGQLVQFKLSDIGeGITEVTVKEWYVKEGDSVSQFDSICEVQSDKASVTITSRYDGVIRKLYYNVDDMAFVGKPLVDIET 139
Cdd:TIGR01348 113 SSGVQEVTVPDIG-DIEKVTVIEVLVKVGDTVSADQSLITLESDKASMEVPAPASGVVKSVKVKVGDSVPTGDLILTLSV 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556990772 140 DAVKDVASEQDVVETPAVSHEEHTHQE--------------------IKGHKTL-ATPAVRRLAMENNIKLSEVVGTGKD 198
Cdd:TIGR01348 192 AGSTPATAPAPASAQPAAQSPAATQPEpaaapaaakaqapapqqagtQNPAKVDhAAPAVRRLAREFGVDLSAVKGTGIK 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556990772 199 GRILKEDILNYLAKQTGAiippSPKLEIIPPAPQPVAIPAKPKDREPgdpkpivkpavfIGKDKTEPVKGFQKAMVKTMS 278
Cdd:TIGR01348 272 GRILREDVQRFVKEPSVR----AQAAAASAAGGAPGALPWPNVDFSK------------FGEVEEVDMSRIRKISGANLT 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556990772 279 AA-LKIPHFGYCDEVDLTQLNQFREELKSMANAQGVRISFMPFFLKAASLGLLHYPILNASVDENCQNITYKAAHNIGIA 357
Cdd:TIGR01348 336 RNwTMIPHVTHFDKADITEMEAFRKQQNAAVEKEGVKLTVLHILMKAVAAALKKFPKFNASLDLGGEQLILKKYVNIGVA 415
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556990772 358 MDTQQGLIVPNVKNVQALSIFEIAAELNRLQTLGSTGQLGTTDLTNGTFTLSNIGSIGGTYAKPVILPPEVAIGALGKIQ 437
Cdd:TIGR01348 416 VDTPNGLLVPVIKDVDRKGITELALELSDLAKKARDGKLTPDEMQGACFTISSLGGIGGTAFTPIVNAPEVAILGVSKSG 495
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 556990772 438 LVPRFNDiGEVVKASVMNVSWSADHRIIDGATMARFSNLWKSYLEHPASMLL 489
Cdd:TIGR01348 496 MEPVWNG-KEFEPRLMLPLSLSYDHRVIDGADAARFTTYICESLADIRRLLL 546
|
|
| PRK11857 |
PRK11857 |
dihydrolipoamide acetyltransferase; Reviewed |
171-484 |
4.62e-67 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237002 [Multi-domain] Cd Length: 306 Bit Score: 217.74 E-value: 4.62e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556990772 171 KTLATPAVRRLAMENNIKLSEVVGTGKDGRILKEDILNYLAKQTGAiipPSPKleiiPPAPQPVAIPAKPKdrepgdPKP 250
Cdd:PRK11857 1 KILATPIARALAKKLGIDISLLKGSGRDGKILAEDVENFIKSLKSA---PTPA----EAASVSSAQQAAKT------AAP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556990772 251 IVKPAVFIGKdkTEPVKGFQKAMVKTMSAALK-IPHFGYCDEVDLTQLNQFREELK-SMANAQGVRISFMPFFLKAASLG 328
Cdd:PRK11857 68 AAAPPKLEGK--REKVAPIRKAIARAMTNSWSnVAYVNLVNEIDMTKLWDLRKSVKdPVLKTEGVKLTFLPFIAKAILIA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556990772 329 LLHYPILNASVDENCQNITYKAAHNIGIAMDTQQGLIVPNVKNVQALSIFEIAAELNRLQTLGSTGQLGTTDLTNGTFTL 408
Cdd:PRK11857 146 LKEFPIFAAKYDEATSELVYPDTLNLGIAVDTEAGLMVPVIKNAQKLSIVEIAKEISRLAKAARERKIKPDEMKGGSFTI 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 556990772 409 SNIGSIGGTYAKPVILPPEVAIGALGKIQLVPRFNDiGEVVKASVMNVSWSADHRIIDGATMARFSNLWKSYLEHP 484
Cdd:PRK11857 226 TNYGSVGSLYGVPVINYPELAIAGVGAIIDKAIVKN-GQIVAGKVMHLTVAADHRWIDGATIGRFASRVKELLEKP 300
|
|
| SucB_Actino |
TIGR02927 |
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model ... |
60-482 |
3.75e-63 |
|
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: 215.26 E-value: 3.75e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556990772 60 SGQLVQFKLSDIGEGITEVTVKEWYVKEGDSVSQFDSICEVQSDKASVTITSRYDGVIRKLYYNVDDMAFVGKPLVDI-- 137
Cdd:TIGR02927 123 SGEATEVKMPELGESVTEGTVTSWLKAVGDTVEVDEPLLEVSTDKVDTEIPSPVAGTLLEIRAPEDDTVEVGTVLAIIgd 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556990772 138 -------ETDAVKDVASEQDVVETPAVSHEEHTHQEIKGHKTLA----------------------TPAVRRLAMENNIK 188
Cdd:TIGR02927 203 anaapaePAEEEAPAPSEAGSEPAPDPAARAPHAAPDPPAPAPApaktaapaaaapvssgdsgpyvTPLVRKLAKDKGVD 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556990772 189 LSEVVGTGKDGRILKEDILnylAKQTGAIIPPSPkleiiPPAPQPVAIPAKPkdrePGDPKPiVKPAVFIGKDKTEPVKG 268
Cdd:TIGR02927 283 LSTVKGTGVGGRIRKQDVL---AAAKAAEEARAA-----AAAPAAAAAPAAP----AAAAKP-AEPDTAKLRGTTQKMNR 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556990772 269 FQKAMVKTMSAALKI-PHFGYCDEVDLTQLNQFREELKS-MANAQGVRISFMPFFLKAASLGLLHYPILNASVDENCQNI 346
Cdd:TIGR02927 350 IRQITADKTIESLQTsAQLTQVHEVDMTRVAALRARAKNdFLEKNGVNLTFLPFFVQAVTEALKAHPNVNASYNAETKEV 429
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556990772 347 TYKAAHNIGIAMDTQQGLIVPNVKNVQALSIFEIAAELNRLQTLGSTGQLGTTDLTNGTFTLSNIGSIGGTYAKPVILPP 426
Cdd:TIGR02927 430 TYHDVEHVGIAVDTPRGLLVPVIHNAGDLSLPGLAKAINDLAARARDNKLKPDELSGGTFTITNIGSGGALFDTPILNPP 509
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 556990772 427 EVAIGALGKIQLVPRF---NDIGEVVKA-SVMNVSWSADHRIIDGATMARFSNLWKSYLE 482
Cdd:TIGR02927 510 QAAILGTGAIVKRPRVikdEDGGESIAIrSVCYLPLTYDHRLVDGADAGRFLTTIKKRLE 569
|
|
| PTZ00144 |
PTZ00144 |
dihydrolipoamide succinyltransferase; Provisional |
36-491 |
1.24e-59 |
|
dihydrolipoamide succinyltransferase; Provisional
Pssm-ID: 240289 [Multi-domain] Cd Length: 418 Bit Score: 201.83 E-value: 1.24e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556990772 36 YPVVKKPFLKYSDQHRYFRTTVVTSGQLVQFKLS----------DIGEGITEVTVKEWYVKEGDSVSQFDSICEVQSDKA 105
Cdd:PTZ00144 7 KRLNKPLLSSVKGMFRRFSLRKLQPACSAHFSKSyfsikvikvpTMGDSISEGTVVEWKKKVGDYVKEDEVICIIETDKV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556990772 106 SVTITSRYDGVIRKLYYNVDDMAFVGKPLVDIETDAVKDVASeqdvVETPAVSHEEHTHQEikghktlatpavrrlamen 185
Cdd:PTZ00144 87 SVDIRAPASGVITKIFAEEGDTVEVGAPLSEIDTGGAPPAAA----PAAAAAAKAEKTTPE------------------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556990772 186 niklsevvgtgkdgrilkedilnylAKQTGAIIPPSPKleiippAPQPVAIPAKPKDREPGDPKPIVKPAVFIGKDKT-- 263
Cdd:PTZ00144 144 -------------------------KPKAAAPTPEPPA------ASKPTPPAAAKPPEPAPAAKPPPTPVARADPRETrv 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556990772 264 ----------EPVKGFQK--AMVKTMsaalkiphfgycDEVDLTQLNQFREELK-SMANAQGVRISFMPFFLKAASLGLL 330
Cdd:PTZ00144 193 pmsrmrqriaERLKASQNtcAMLTTF------------NECDMSALMELRKEYKdDFQKKHGVKLGFMSAFVKASTIALK 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556990772 331 HYPILNASVDENCqnITYKAAHNIGIAMDTQQGLIVPNVKNVQALSIFEIAAELNRLQTLGSTGQLGTTDLTNGTFTLSN 410
Cdd:PTZ00144 261 KMPIVNAYIDGDE--IVYRNYVDISVAVATPTGLVVPVIRNCENKSFAEIEKELADLAEKARNNKLTLEDMTGGTFTISN 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556990772 411 IGSIGGTYAKPVILPPEVAIGALGKIQLVPRFNDiGEVVKASVMNVSWSADHRIIDGATMARFSNLWKSYLEHPASMLLD 490
Cdd:PTZ00144 339 GGVFGSLMGTPIINPPQSAILGMHAIKKRPVVVG-NEIVIRPIMYLALTYDHRLIDGRDAVTFLKKIKDLIEDPARMLLD 417
|
.
gi 556990772 491 L 491
Cdd:PTZ00144 418 L 418
|
|
| PDHac_trf_mito |
TIGR01349 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
75-489 |
1.87e-55 |
|
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: 191.16 E-value: 1.87e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556990772 75 ITEVTVKEWYVKEGDSVSQFDSICEVQSDKASVTITSRYDGVIRKLYY--NVDDMAfVGKPLV-------DIEtDAVKDV 145
Cdd:TIGR01349 11 MTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVpeGTKDVP-VNKPIAvlveekeDVA-DAFKNY 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556990772 146 ASEQDVVETPAVSHEEHTHQEI-------------------------KGHKTLATPAVRRLAMENNIKLSEVVGTGKDGR 200
Cdd:TIGR01349 89 KLESSASPAPKPSEIAPTAPPSapkpspapqkqspepsspaplsdkeSGDRIFASPLAKKLAKEKGIDLSAVAGSGPNGR 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556990772 201 ILKEDILNYLakqtgaiippspkleiiPPAPQPVAIPAKPKDREPGDPKPIVKPAVFigkdKTEPVKGFQKAMVKTMSAA 280
Cdd:TIGR01349 169 IVKKDIESFV-----------------PQSPASANQQAAATTPATYPAAAPVSTGSY----EDVPLSNIRKIIAKRLLES 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556990772 281 LK-IPHFGYCDEVDLTQLNQFREELKSMANAQgVRISFMPFFLKAASLGLLHYPILNASVDENcqNITYKAAHNIGIAMD 359
Cdd:TIGR01349 228 KQtIPHYYVSIECNVDKLLALRKELNAMASEV-YKLSVNDFIIKASALALREVPEANSSWTDN--FIRRYKNVDISVAVA 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556990772 360 TQQGLIVPNVKNVQALSIFEIAAELNRLQTLGSTGQLGTTDLTNGTFTLSNIGSIGGTYAKPVILPPEVAIGALG---KI 436
Cdd:TIGR01349 305 TPDGLITPIVRNADAKGLSTISNEIKDLAKRARNNKLKPEEFQGGTFTISNLGMFGIKDFTAIINPPQACILAVGaveDV 384
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 556990772 437 QLVPRFNDIGEVVkASVMNVSWSADHRIIDGATMARFSNLWKSYLEHPASMLL 489
Cdd:TIGR01349 385 AVVDNDEEKGFAV-ASIMSVTLSCDHRVIDGAVGAEFLKSFKKYLENPIEMLL 436
|
|
| PLN02744 |
PLN02744 |
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex |
75-489 |
3.91e-46 |
|
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
Pssm-ID: 215397 [Multi-domain] Cd Length: 539 Bit Score: 168.49 E-value: 3.91e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556990772 75 ITEVTVKEWYVKEGDSVSQFDSICEVQSDKASVTITSRYDGVIRKLYY---------------NVDDMAFVGKpLVDIET 139
Cdd:PLN02744 124 MTEGNIARWLKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVKgdgakeikvgeviaiTVEEEEDIGK-FKDYKP 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556990772 140 DAVKDVA----------SEQDVVETPAVSHEEHTHQE----IKGHKTLATPAVRRLAMENNIKLSEVVGTGKDGRILKED 205
Cdd:PLN02744 203 SSSAAPAapkakpspppPKEEEVEKPASSPEPKASKPsappSSGDRIFASPLARKLAEDNNVPLSSIKGTGPDGRIVKAD 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556990772 206 ILNYLAKQTGaiippspklEIIPPAPQPVAIPakpkdrepgdpkpivkpavfiGKDKTE-PVKGFQKAMVKTM-SAALKI 283
Cdd:PLN02744 283 IEDYLASGGK---------GATAPPSTDSKAP---------------------ALDYTDiPNTQIRKVTASRLlQSKQTI 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556990772 284 PHFGYCDEVDLTQLNQFREELKSMANAQG-VRISFMPFFLKAASLGLLHYPILNAS-VDENCQNitYKAAhNIGIAMDTQ 361
Cdd:PLN02744 333 PHYYLTVDTRVDKLMALRSQLNSLQEASGgKKISVNDLVIKAAALALRKVPQCNSSwTDDYIRQ--YHNV-NINVAVQTE 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556990772 362 QGLIVPNVKNVQALSIFEIAAELNRLQTLGSTGQLGTTDLTNGTFTLSNIGS-IGGTYAKPVILPPEVAIGALGKIQ--L 438
Cdd:PLN02744 410 NGLYVPVVKDADKKGLSTIAEEVKQLAQKARENSLKPEDYEGGTFTVSNLGGpFGIKQFCAIINPPQSAILAVGSAEkrV 489
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 556990772 439 VPRFNDiGEVVKASVMNVSWSADHRIIDGATMARFSNLWKSYLEHPASMLL 489
Cdd:PLN02744 490 IPGSGP-DQYNFASFMSVTLSCDHRVIDGAIGAEWLKAFKGYIENPESMLL 539
|
|
| PLN02226 |
PLN02226 |
2-oxoglutarate dehydrogenase E2 component |
50-491 |
5.61e-39 |
|
2-oxoglutarate dehydrogenase E2 component
Pssm-ID: 177871 [Multi-domain] Cd Length: 463 Bit Score: 147.21 E-value: 5.61e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556990772 50 HRYFRTTVVTSGQLVQFKLSDIGEGITEVTVKEWYVKEGDSVSQFDSICEVQSDKASVTITSRYDGVIRKLYYNVDDMAF 129
Cdd:PLN02226 78 QRWVRPFSSESGDTVEAVVPHMGESITDGTLATFLKKPGERVQADEAIAQIETDKVTIDIASPASGVIQEFLVKEGDTVE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556990772 130 VGKPLVDIET--DAVKDVASEQDVVETPAVSHEEHTHQEIKGhKTLATPavrrlamenniklsevvgtgkdgrilkedil 207
Cdd:PLN02226 158 PGTKVAIISKseDAASQVTPSQKIPETTDPKPSPPAEDKQKP-KVESAP------------------------------- 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556990772 208 nyLAKQTGAIIPPspkleiiPPAPQPVAIPA-KPKDREPGDPKPIVKPAVfigkdkTEPVKGFQK--AMVKTMsaalkip 284
Cdd:PLN02226 206 --VAEKPKAPSSP-------PPPKQSAKEPQlPPKERERRVPMTRLRKRV------ATRLKDSQNtfALLTTF------- 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556990772 285 hfgycDEVDLTQLNQFREELK-SMANAQGVRISFMPFFLKAASLGLLHYPILNASVDENcqNITYKAAHNIGIAMDTQQG 363
Cdd:PLN02226 264 -----NEVDMTNLMKLRSQYKdAFYEKHGVKLGLMSGFIKAAVSALQHQPVVNAVIDGD--DIIYRDYVDISIAVGTSKG 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556990772 364 LIVPNVKNVQALSIFEIAAELNRLQTLGSTGQLGTTDLTNGTFTLSNIGSIGGTYAKPVILPPEVAIgaLGKIQLVPRFN 443
Cdd:PLN02226 337 LVVPVIRGADKMNFAEIEKTINGLAKKANEGTISIDEMAGGSFTVSNGGVYGSLISTPIINPPQSAI--LGMHSIVSRPM 414
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 556990772 444 DI-GEVVKASVMNVSWSADHRIIDGATMARFSNLWKSYLEHPASMLLDL 491
Cdd:PLN02226 415 VVgGSVVPRPMMYVALTYDHRLIDGREAVYFLRRVKDVVEDPQRLLLDI 463
|
|
| PRK14843 |
PRK14843 |
dihydrolipoamide acetyltransferase; Provisional |
175-489 |
7.44e-35 |
|
dihydrolipoamide acetyltransferase; Provisional
Pssm-ID: 184847 [Multi-domain] Cd Length: 347 Bit Score: 133.49 E-value: 7.44e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556990772 175 TPAVRRLAMENNIKLSEVVGTGKDGRILKEDILnylakqtgAIIPPSPKLEIIPPAPQPVAIPAKPKDREPgdpkpivkp 254
Cdd:PRK14843 52 SPLAKRIALEHNIAWQEIQGTGHRGKIMKKDVL--------ALLPENIENDSIKSPAQIEKVEEVPDNVTP--------- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556990772 255 avfIGKDKTEPVKGFQKAMVKTMSAA-LKIPHFGYCDEVDLTQLNQFREE-LKSMANAQGVRISFMPFFLKAASLGLLHY 332
Cdd:PRK14843 115 ---YGEIERIPMTPMRKVIAQRMVESyLTAPTFTLNYEVDMTEMLALRKKvLEPIMEATGKKTTVTDLLSLAVVKTLMKH 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556990772 333 PILNASVDENCQNITYKAAHNIGIAMDTQQGLIVPNVKNVQALSIFEIAAELNRLQTLGSTGQLGTTDLTNGTFTLSNIG 412
Cdd:PRK14843 192 PYINASLTEDGKTIITHNYVNLAMAVGMDNGLMTPVVYNAEKMSLSELVVAFKDVIGRTLDGKLAPSELQNSTFTISNLG 271
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 556990772 413 SIGGTYAKPVILPPEVAI-GALGKIQLVPRFNdiGEVVKASVMNVSWSADHRIIDGATMARFSNLWKSYLEHPASMLL 489
Cdd:PRK14843 272 MFGVQSFGPIINQPNSAIlGVSSTIEKPVVVN--GEIVIRPIMSLGLTIDHRVVDGMAGAKFMKDLKELIETPISMLI 347
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
64-137 |
7.23e-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: 100.17 E-value: 7.23e-26
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 556990772 64 VQFKLSDIGEGITEVTVKEWYVKEGDSVSQFDSICEVQSDKASVTITSRYDGVIRKLYYNVDDMAFVGKPLVDI 137
Cdd:cd06849 1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
64-137 |
1.45e-21 |
|
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: 88.20 E-value: 1.45e-21
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 556990772 64 VQFKLSDIGEGITEVTVKEWYVKEGDSVSQFDSICEVQSDKASVTITSRYDGVIRKLYYNVDDMAFVGKPLVDI 137
Cdd:COG0508 3 IEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
64-137 |
3.70e-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: 81.49 E-value: 3.70e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 556990772 64 VQFKLSDIGEGITEVtVKEWYVKEGDSVSQFDSICEVQSDKASVTITSRYDGVIRKLYYNVDDMAFVGKPLVDI 137
Cdd:pfam00364 1 TEIKSPMIGESVREG-VVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
|
|
| kgd |
PRK12270 |
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ... |
219-473 |
5.89e-16 |
|
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;
Pssm-ID: 237030 [Multi-domain] Cd Length: 1228 Bit Score: 81.09 E-value: 5.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556990772 219 PPSPKLEIIPPAPQPVAIPAKPKDRePGDPKPIVKPAVFIGKDKTEPVKGFQKAMVKTMSAALKIPhfgycdevdlT--- 295
Cdd:PRK12270 74 PPAAAAPAAPPKPAAAAAAAAAPAA-PPAAAAAAAPAAAAVEDEVTPLRGAAAAVAKNMDASLEVP----------Tats 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556990772 296 --------------QLNQFreelksMANAQGVRISFMPFFLKAASLGLLHYPILNASVDE-NCQNITYKAAH-NIGIAMD 359
Cdd:PRK12270 143 vravpakllidnriVINNH------LKRTRGGKVSFTHLIGYALVQALKAFPNMNRHYAEvDGKPTLVTPAHvNLGLAID 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556990772 360 TQQ-----GLIVPNVKNVQALSIFEIAAELNRLQTLGSTGQLGTTDLTNGTFTLSNIGSIGGTYAKPVILPPEVAIGALG 434
Cdd:PRK12270 217 LPKkdgsrQLVVPAIKGAETMDFAQFWAAYEDIVRRARDGKLTADDFQGTTISLTNPGGIGTVHSVPRLMKGQGAIIGVG 296
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 556990772 435 KIQLVPRF--------NDIGeVVKasVMNVSWSADHRIIDGATMARF 473
Cdd:PRK12270 297 AMEYPAEFqgaseerlAELG-ISK--VMTLTSTYDHRIIQGAESGEF 340
|
|
| E3_binding |
pfam02817 |
e3 binding domain; This family represents a small domain of the E2 subunit of 2-oxo-acid ... |
173-207 |
3.44e-14 |
|
e3 binding domain; This family represents a small domain of the E2 subunit of 2-oxo-acid dehydrogenases responsible for the binding of the E3 subunit.
Pssm-ID: 460710 [Multi-domain] Cd Length: 36 Bit Score: 66.17 E-value: 3.44e-14
10 20 30
....*....|....*....|....*....|....*
gi 556990772 173 LATPAVRRLAMENNIKLSEVVGTGKDGRILKEDIL 207
Cdd:pfam02817 2 LASPAARKLARELGIDLSDVKGTGPGGRITKEDVE 36
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
72-219 |
2.29e-10 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 62.27 E-value: 2.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556990772 72 GEGITEVTVKEWYVKEGDSVSQFDSICEVQSDKASVTITSRYDGVIRKLYYNVDDMAFVGKPLVDIETDAVKDvaSEQDV 151
Cdd:PRK14875 11 GLSMTEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGETLPVGALLAVVADAEVSD--AEIDA 88
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 556990772 152 VetpavsheehthqeikghktlATPAVRRLAMEnNIKLSEVVGTGKDGRILKEDIlNYLAKQTGAIIP 219
Cdd:PRK14875 89 F---------------------IAPFARRFAPE-GIDEEDAGPAPRKARIGGRTV-RYLRLGEGDGTP 133
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
68-137 |
2.06e-07 |
|
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: 48.21 E-value: 2.06e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556990772 68 LSDIGEGITEVTVKEWYVKEGDSVSQFDSICEVQSDKASVTITSRYDGVIRKLYYNVDDMAFVGKPLVDI 137
Cdd:cd06663 4 IPDLAQHLGDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKVEGDTPLVKI 73
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
79-137 |
7.30e-05 |
|
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: 40.86 E-value: 7.30e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 556990772 79 TVKEWYVKEGDSVSQFDSICEVQSDKASVTITSRYDGVIRKLYYNVDDMAFVGKPLVDI 137
Cdd:cd06850 9 TVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
76-143 |
4.99e-03 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 39.13 E-value: 4.99e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 556990772 76 TEVTVKEWYVKEGDSVSQFDSICEVQSDKASVTITSRYDGVIrklyynvddmafvGKPLVDIETDAVK 143
Cdd:PRK11892 15 EEGTLAKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTL-------------GKILVPEGTEGVK 69
|
|
| |
