|
Name |
Accession |
Description |
Interval |
E-value |
| sucB |
TIGR01347 |
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ... |
74-463 |
0e+00 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This model describes the TCA cycle 2-oxoglutarate system E2 component, dihydrolipoamide succinyltransferase. It is closely related to the pyruvate dehydrogenase E2 component, dihydrolipoamide acetyltransferase. The seed for this model includes mitochondrial and Gram-negative bacterial forms. Mycobacterial candidates are highly derived, differ in having and extra copy of the lipoyl-binding domain at the N-terminus. They score below the trusted cutoff, but above the noise cutoff and above all examples of dihydrolipoamide acetyltransferase. [Energy metabolism, TCA cycle]
Pssm-ID: 273565 [Multi-domain] Cd Length: 403 Bit Score: 615.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365855 74 TSIEVPPMAESLTEGSLKEYTKNVGDFIKEDELLATIETDKIDIEVNSPVSGTVTKLNFKPEDTVTVGEELAQVE----P 149
Cdd:TIGR01347 1 IEIKVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAILEegndA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365855 150 GEAPAEGSGESKPE-PTEQAEPSQGVAARENSSEETASK--KEAAPKKEAAPKKEVTEPK-KADQPKKTVS--KAQEPPV 223
Cdd:TIGR01347 81 TAAPPAKSGEEKEEtPAASAAAAPTAAANRPSLSPAARRlaKEHGIDLSAVPGTGVTGRVtKEDIIKKTEApaSAQPPAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365855 224 ASNSFTP--FPRTETRVKMNRMRLRIAERLKESQNTAASLTTFNEVDMSALMEMRKLYKDEIIKKTGTKFGFMGLFSKAC 301
Cdd:TIGR01347 161 AAAAAAPaaATRPEERVKMTRLRQRIAERLKEAQNSTAMLTTFNEVDMSAVMELRKRYKEEFEKKHGVKLGFMSFFVKAV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365855 302 TLAAKDIPAVNGAIEGDQIVYRDYTDISVAVATPKGLVTPVVRNAESLSVLDIENEIVRLSHKARDGKLTLEDMTGGTFT 381
Cdd:TIGR01347 241 VAALKRFPEVNAEIDGDDIVYKDYYDISVAVSTDRGLVVPVVRNADRMSFADIEKEIADLGKKARDGKLTLEDMTGGTFT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365855 382 ISNGGVFGSLYGTPIINSPQTAVLGLHGVKERPVTVNGQIVSRPMMYLALTYDHRLLDGREAVTFLKTVKELIEDPRKML 461
Cdd:TIGR01347 321 ITNGGVFGSLMSTPIINPPQSAILGMHGIKERPVAVNGQIEIRPMMYLALSYDHRLIDGKEAVTFLVTIKELLEDPRRLL 400
|
..
gi 398365855 462 LW 463
Cdd:TIGR01347 401 LD 402
|
|
| PTZ00144 |
PTZ00144 |
dihydrolipoamide succinyltransferase; Provisional |
62-462 |
0e+00 |
|
dihydrolipoamide succinyltransferase; Provisional
Pssm-ID: 240289 [Multi-domain] Cd Length: 418 Bit Score: 523.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365855 62 NPFSITSNR---FKSTSIEVPPMAESLTEGSLKEYTKNVGDFIKEDELLATIETDKIDIEVNSPVSGTVTKLNFKPEDTV 138
Cdd:PTZ00144 30 QPACSAHFSksyFSIKVIKVPTMGDSISEGTVVEWKKKVGDYVKEDEVICIIETDKVSVDIRAPASGVITKIFAEEGDTV 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365855 139 TVGEELAQVEPGEAPaegsgeskpepteqaePSQGVAARENSSEETASKKEAAPKKEAAPKKEVTEPKKAdQPKKTVSKA 218
Cdd:PTZ00144 110 EVGAPLSEIDTGGAP----------------PAAAPAAAAAAKAEKTTPEKPKAAAPTPEPPAASKPTPP-AAAKPPEPA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365855 219 QEPPVASNSFTPFPRTETRVKMNRMRLRIAERLKESQNTAASLTTFNEVDMSALMEMRKLYKDEIIKKTGTKFGFMGLFS 298
Cdd:PTZ00144 173 PAAKPPPTPVARADPRETRVPMSRMRQRIAERLKASQNTCAMLTTFNECDMSALMELRKEYKDDFQKKHGVKLGFMSAFV 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365855 299 KACTLAAKDIPAVNGAIEGDQIVYRDYTDISVAVATPKGLVTPVVRNAESLSVLDIENEIVRLSHKARDGKLTLEDMTGG 378
Cdd:PTZ00144 253 KASTIALKKMPIVNAYIDGDEIVYRNYVDISVAVATPTGLVVPVIRNCENKSFAEIEKELADLAEKARNNKLTLEDMTGG 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365855 379 TFTISNGGVFGSLYGTPIINSPQTAVLGLHGVKERPVTVNGQIVSRPMMYLALTYDHRLLDGREAVTFLKTVKELIEDPR 458
Cdd:PTZ00144 333 TFTISNGGVFGSLMGTPIINPPQSAILGMHAIKKRPVVVGNEIVIRPIMYLALTYDHRLIDGRDAVTFLKKIKDLIEDPA 412
|
....
gi 398365855 459 KMLL 462
Cdd:PTZ00144 413 RMLL 416
|
|
| PRK05704 |
PRK05704 |
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase; |
73-462 |
2.44e-174 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
Pssm-ID: 235571 [Multi-domain] Cd Length: 407 Bit Score: 494.74 E-value: 2.44e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365855 73 STSIEVPPMAESLTEGSLKEYTKNVGDFIKEDELLATIETDKIDIEVNSPVSGTVTKLNFKPEDTVTVGEELAQVEPGEA 152
Cdd:PRK05704 2 MVEIKVPTLPESVTEATIATWHKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGDTVTVGQVLGRIDEGAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365855 153 paegSGESKPEPTEQAEPSQGVAARENSSEETASKKEAAP--KKEAAPKK-------------EVTEPKKADQPKKTVSK 217
Cdd:PRK05704 82 ----AGAAAAAAAAAAAAAAAPAQAQAAAAAEQSNDALSPaaRKLAAENGldasavkgtgkggRVTKEDVLAALAAAAAA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365855 218 AQEPPVASNSFTPFP---RTETRVKMNRMRLRIAERLKESQNTAASLTTFNEVDMSALMEMRKLYKDEIIKKTGTKFGFM 294
Cdd:PRK05704 158 PAAPAAAAPAAAPAPlgaRPEERVPMTRLRKTIAERLLEAQNTTAMLTTFNEVDMTPVMDLRKQYKDAFEKKHGVKLGFM 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365855 295 GLFSKACTLAAKDIPAVNGAIEGDQIVYRDYTDISVAVATPKGLVTPVVRNAESLSVLDIENEIVRLSHKARDGKLTLED 374
Cdd:PRK05704 238 SFFVKAVVEALKRYPEVNASIDGDDIVYHNYYDIGIAVGTPRGLVVPVLRDADQLSFAEIEKKIAELAKKARDGKLSIEE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365855 375 MTGGTFTISNGGVFGSLYGTPIINSPQTAVLGLHGVKERPVTVNGQIVSRPMMYLALTYDHRLLDGREAVTFLKTVKELI 454
Cdd:PRK05704 318 LTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHKIKERPVAVNGQIVIRPMMYLALSYDHRIIDGKEAVGFLVTIKELL 397
|
....*...
gi 398365855 455 EDPRKMLL 462
Cdd:PRK05704 398 EDPERLLL 405
|
|
| PRK11856 |
PRK11856 |
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed |
76-463 |
1.44e-119 |
|
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
Pssm-ID: 237001 [Multi-domain] Cd Length: 411 Bit Score: 355.64 E-value: 1.44e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365855 76 IEVPPMAESLTEGSLKEYTKNVGDFIKEDELLATIETDKIDIEVNSPVSGTVTKLNFKPEDTVTVGEELAQV-EPGEAPA 154
Cdd:PRK11856 5 FKMPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDVVPVGSVIAVIeEEGEAEA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365855 155 EGSGESKPEPTEQAEPSQGVAARENSSEETASKKEAAPKKE-AAPK------------KEV--TEPK----KAD----QP 211
Cdd:PRK11856 85 AAAAEAAPEAPAPEPAPAAAAAAAAAPAAAAAPAAPAAAAAkASPAvrklarelgvdlSTVkgSGPGgritKEDveaaAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365855 212 KKTVSKAQEPPVASNSFTPFPRTETRVKMNRMRLRIAERLKESQNTAASLTTFNEVDMSALMEMRKLYKDEIIKKTgtkf 291
Cdd:PRK11856 165 AAAPAAAAAAAAAAAPPAAAAEGEERVPLSGMRKAIAKRMVESKREIPHFTLTDEVDVTALLALRKQLKAIGVKLT---- 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365855 292 gFMGLFSKACTLAAKDIPAVNGAIEGDQIVYRDYTDISVAVATPKGLVTPVVRNAESLSVLDIENEIVRLSHKARDGKLT 371
Cdd:PRK11856 241 -VTDFLIKAVALALKKFPELNASWDDDAIVLKKYVNIGIAVATDGGLIVPVIRDADKKSLFELAREIKDLAEKAREGKLK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365855 372 LEDMTGGTFTISNGGVFGSLYGTPIINSPQTAVLGLHGVKERPVTVNGQIVSRPMMYLALTYDHRLLDGREAVTFLKTVK 451
Cdd:PRK11856 320 PEELQGGTFTISNLGMFGGDYFTPIINPPEVAILGVGAIVERPVVVDGEIVVRKVMPLSLSFDHRVIDGADAARFLKALK 399
|
410
....*....|..
gi 398365855 452 ELIEDPRKMLLW 463
Cdd:PRK11856 400 ELLENPALLLLE 411
|
|
| PLN02226 |
PLN02226 |
2-oxoglutarate dehydrogenase E2 component |
11-462 |
4.20e-117 |
|
2-oxoglutarate dehydrogenase E2 component
Pssm-ID: 177871 [Multi-domain] Cd Length: 463 Bit Score: 351.36 E-value: 4.20e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365855 11 AKSLVKSKVArnVMAASFVKRHASTSLFKQANKVESLG------------SIYLSGKKISVAANPFSITSNrfKSTSIEV 78
Cdd:PLN02226 21 GKSLQSSRVA--ASSPSLLSGSETGALLHRGNHAHSFHnlalpgnsgisrSASLVSSTLQRWVRPFSSESG--DTVEAVV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365855 79 PPMAESLTEGSLKEYTKNVGDFIKEDELLATIETDKIDIEVNSPVSGTVTKLNFKPEDTVTVGEELAQVEPGEapaegsg 158
Cdd:PLN02226 97 PHMGESITDGTLATFLKKPGERVQADEAIAQIETDKVTIDIASPASGVIQEFLVKEGDTVEPGTKVAIISKSE------- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365855 159 eskpEPTEQAEPSQGVAARENSSEETASKKEAAPKKEAAPKKEvtEPKKADQPKKTVSKAQEPPVasnsftPFPRTETRV 238
Cdd:PLN02226 170 ----DAASQVTPSQKIPETTDPKPSPPAEDKQKPKVESAPVAE--KPKAPSSPPPPKQSAKEPQL------PPKERERRV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365855 239 KMNRMRLRIAERLKESQNTAASLTTFNEVDMSALMEMRKLYKDEIIKKTGTKFGFMGLFSKACTLAAKDIPAVNGAIEGD 318
Cdd:PLN02226 238 PMTRLRKRVATRLKDSQNTFALLTTFNEVDMTNLMKLRSQYKDAFYEKHGVKLGLMSGFIKAAVSALQHQPVVNAVIDGD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365855 319 QIVYRDYTDISVAVATPKGLVTPVVRNAESLSVLDIENEIVRLSHKARDGKLTLEDMTGGTFTISNGGVFGSLYGTPIIN 398
Cdd:PLN02226 318 DIIYRDYVDISIAVGTSKGLVVPVIRGADKMNFAEIEKTINGLAKKANEGTISIDEMAGGSFTVSNGGVYGSLISTPIIN 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 398365855 399 SPQTAVLGLHGVKERPVTVNGQIVSRPMMYLALTYDHRLLDGREAVTFLKTVKELIEDPRKMLL 462
Cdd:PLN02226 398 PPQSAILGMHSIVSRPMVVGGSVVPRPMMYVALTYDHRLIDGREAVYFLRRVKDVVEDPQRLLL 461
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
76-462 |
4.37e-97 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 302.51 E-value: 4.37e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365855 76 IEVPPMAEsLTEGSLKEYTKNVGDFIKEDELLATIETDKIDIEVNSPVSGTVTKLNFKPEDTVTVGEELAQVEPGEAPAE 155
Cdd:PRK11855 122 VKVPDIGE-ITEVEVIEWLVKVGDTVEEDQSLITVETDKATMEIPSPVAGVVKEIKVKVGDKVSVGSLLVVIEVAAAAPA 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365855 156 GSGESKPEPTEQAEPSQGVAARENSSEETASKKEAAPKKEAAP------------------------------KKEVTEP 205
Cdd:PRK11855 201 AAAAPAAAAPAAAAAAAPAPAPAAAAAPAAAAPAAAAAPGKAPhaspavrrlarelgvdlsqvkgtgkkgritKEDVQAF 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365855 206 KKADQPKKTVSKAQEPPVASNS----------FTPFPRTETrVKMNRMRLRIAERLKESQNTAASLTTFNEVDMSALMEM 275
Cdd:PRK11855 281 VKGAMSAAAAAAAAAAAAGGGGlgllpwpkvdFSKFGEIET-KPLSRIKKISAANLHRSWVTIPHVTQFDEADITDLEAL 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365855 276 RKLYKDEIiKKTGTKFGFMGLFSKACTLAAKDIPAVNGAI--EGDQIVYRDYTDISVAVATPKGLVTPVVRNAESLSVLD 353
Cdd:PRK11855 360 RKQLKKEA-EKAGVKLTMLPFFIKAVVAALKEFPVFNASLdeDGDELTYKKYFNIGFAVDTPNGLVVPVIKDVDKKSLLE 438
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365855 354 IENEIVRLSHKARDGKLTLEDMTGGTFTISNGGVFGSLYGTPIINSPQTAVLGLHGVKERPVTVNGQIVSRPMMYLALTY 433
Cdd:PRK11855 439 IAREIAELAKKARDGKLKPDDMQGGCFTISSLGGIGGTAFTPIINAPEVAILGVGKSQMKPVWDGKEFVPRLMLPLSLSY 518
|
410 420
....*....|....*....|....*....
gi 398365855 434 DHRLLDGREAVTFLKTVKELIEDPRKMLL 462
Cdd:PRK11855 519 DHRVIDGATAARFTNYLKQLLADPRRMLL 547
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
251-461 |
1.48e-96 |
|
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: 289.44 E-value: 1.48e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365855 251 LKESQNTAASLTTFNEVDMSALMEMRKLYKdEIIKKTGTKFGFMGLFSKACTLAAKDIPAVNGAIEGD--QIVYRDYTDI 328
Cdd:pfam00198 1 MTESKQTIPHFTLTDEVDVTELLALREELK-EDAADEETKLTFLPFLVKAVALALKKFPELNASWDGEegEIVYKKYVNI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365855 329 SVAVATPKGLVTPVVRNAESLSVLDIENEIVRLSHKARDGKLTLEDMTGGTFTISNGGVFGSLYGTPIINSPQTAVLGLH 408
Cdd:pfam00198 80 GIAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVG 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 398365855 409 GVKERPVTVNGQIVSRPMMYLALTYDHRLLDGREAVTFLKTVKELIEDPRKML 461
Cdd:pfam00198 160 RIRKRPVVVDGEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELLL 212
|
|
| SucB_Actino |
TIGR02927 |
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model ... |
73-456 |
2.05e-77 |
|
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: 252.24 E-value: 2.05e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365855 73 STSIEVPPMAESLTEGSLKEYTKNVGDFIKEDELLATIETDKIDIEVNSPVSGTVTKLNFKPEDTVTVGEELAQVEPGEA 152
Cdd:TIGR02927 126 ATEVKMPELGESVTEGTVTSWLKAVGDTVEVDEPLLEVSTDKVDTEIPSPVAGTLLEIRAPEDDTVEVGTVLAIIGDANA 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365855 153 PAEGSGESKPEPTEQA--EPSQGVAARE-----------NSSEETASKKEAAPKK------------------------- 194
Cdd:TIGR02927 206 APAEPAEEEAPAPSEAgsEPAPDPAARAphaapdppapaPAPAKTAAPAAAAPVSsgdsgpyvtplvrklakdkgvdlst 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365855 195 ---------------EAAPKKEvTEPKKADQPKKTVSKAQEPPVASNSFTP---FPRTETRvKMNRMRLRIAERLKESQN 256
Cdd:TIGR02927 286 vkgtgvggrirkqdvLAAAKAA-EEARAAAAAPAAAAAPAAPAAAAKPAEPdtaKLRGTTQ-KMNRIRQITADKTIESLQ 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365855 257 TAASLTTFNEVDMSALMEMRKLYKDEIIKKTGTKFGFMGLFSKACTLAAKDIPAVNGAI--EGDQIVYRDYTDISVAVAT 334
Cdd:TIGR02927 364 TSAQLTQVHEVDMTRVAALRARAKNDFLEKNGVNLTFLPFFVQAVTEALKAHPNVNASYnaETKEVTYHDVEHVGIAVDT 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365855 335 PKGLVTPVVRNAESLSVLDIENEIVRLSHKARDGKLTLEDMTGGTFTISNGGVFGSLYGTPIINSPQTAVLGLHGVKERP 414
Cdd:TIGR02927 444 PRGLLVPVIHNAGDLSLPGLAKAINDLAARARDNKLKPDELSGGTFTITNIGSGGALFDTPILNPPQAAILGTGAIVKRP 523
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 398365855 415 VTV-----NGQIVSRPMMYLALTYDHRLLDGREAVTFLKTVKELIED 456
Cdd:TIGR02927 524 RVIkdedgGESIAIRSVCYLPLTYDHRLVDGADAGRFLTTIKKRLEE 570
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
86-462 |
5.28e-74 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 244.53 E-value: 5.28e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365855 86 TEGSLKEYTKNVGDFIKEDELLATIETDKIDIEVNSPVSGTVTKLNFKPEDTVTVGEELAQVE-PGEAPAegsgeSKPEP 164
Cdd:PRK11854 217 DEVEVTEVMVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVKTGSLIMRFEvEGAAPA-----AAPAK 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365855 165 TEQAEPSQGVAArensseetASKKEAAPKKEAAPKKEVTEPK---------------------------------KAD-- 209
Cdd:PRK11854 292 QEAAAPAPAAAK--------AEAPAAAPAAKAEGKSEFAENDayvhatplvrrlarefgvnlakvkgtgrkgrilKEDvq 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365855 210 -QPKKTVSKAQEPPVASNS--------------FTPFPRTETrVKMNRMRLRIAERLKESQNTAASLTTFNEVDMSALME 274
Cdd:PRK11854 364 aYVKDAVKRAEAAPAAAAAggggpgllpwpkvdFSKFGEIEE-VELGRIQKISGANLHRNWVMIPHVTQFDKADITELEA 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365855 275 MRKLYKDE-IIKKTGTKFGFMGLFSKACTLAAKDIPAVNGAI--EGDQIVYRDYTDISVAVATPKGLVTPVVRNAESLSV 351
Cdd:PRK11854 443 FRKQQNAEaEKRKLGVKITPLVFIMKAVAAALEQMPRFNSSLseDGQRLTLKKYVNIGIAVDTPNGLVVPVFKDVNKKGI 522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365855 352 LDIENEIVRLSHKARDGKLTLEDMTGGTFTISNGGVFGSLYGTPIINSPQTAVLGLHGVKERPVTVNGQIVSRPMMYLAL 431
Cdd:PRK11854 523 IELSRELMDISKKARDGKLTAGDMQGGCFTISSIGGLGTTHFTPIVNAPEVAILGVSKSAMEPVWNGKEFAPRLMLPLSL 602
|
410 420 430
....*....|....*....|....*....|.
gi 398365855 432 TYDHRLLDGREAVTFLKTVKELIEDPRKMLL 462
Cdd:PRK11854 603 SYDHRVIDGADGARFITIINDRLSDIRRLVL 633
|
|
| PDHac_trf_mito |
TIGR01349 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
76-462 |
1.59e-63 |
|
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: 211.96 E-value: 1.59e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365855 76 IEVPPMAESLTEGSLKEYTKNVGDFIKEDELLATIETDKIDIEVNSPVSGTVTKLnFKPEDT--VTVGEELA-QVEPGEA 152
Cdd:TIGR01349 2 ITMPALSPTMTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKI-LVPEGTkdVPVNKPIAvLVEEKED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365855 153 --------PAEGSGESKPEPTEQAEPSQGVA----------ARENSSEETASKKEAAPKKEAAP---------------- 198
Cdd:TIGR01349 81 vadafknyKLESSASPAPKPSEIAPTAPPSApkpspapqkqSPEPSSPAPLSDKESGDRIFASPlakklakekgidlsav 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365855 199 ----------KKEVTE-PKKADQPKKTVSKAQEPPvASNSFTPFPRTE-TRVKMNRMRLRIAERLKESQNTAASLTTFNE 266
Cdd:TIGR01349 161 agsgpngrivKKDIESfVPQSPASANQQAAATTPA-TYPAAAPVSTGSyEDVPLSNIRKIIAKRLLESKQTIPHYYVSIE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365855 267 VDMSALMEMRKlyKDEIIKKTGTKFGFMGLFSKACTLAAKDIPAVNGAIEGDQIVYRDYTDISVAVATPKGLVTPVVRNA 346
Cdd:TIGR01349 240 CNVDKLLALRK--ELNAMASEVYKLSVNDFIIKASALALREVPEANSSWTDNFIRRYKNVDISVAVATPDGLITPIVRNA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365855 347 ESLSVLDIENEIVRLSHKARDGKLTLEDMTGGTFTISNGGVFGSLYGTPIINSPQTAVLGLHGVKERPVTVNGQ---IVS 423
Cdd:TIGR01349 318 DAKGLSTISNEIKDLAKRARNNKLKPEEFQGGTFTISNLGMFGIKDFTAIINPPQACILAVGAVEDVAVVDNDEekgFAV 397
|
410 420 430
....*....|....*....|....*....|....*....
gi 398365855 424 RPMMYLALTYDHRLLDGREAVTFLKTVKELIEDPRKMLL 462
Cdd:TIGR01349 398 ASIMSVTLSCDHRVIDGAVGAEFLKSFKKYLENPIEMLL 436
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
76-462 |
4.92e-57 |
|
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: 197.40 E-value: 4.92e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365855 76 IEVPPMAeSLTEGSLKEYTKNVGDFIKEDELLATIETDKIDIEVNSPVSGTVTKLNFKPEDTVTVGEEL----------- 144
Cdd:TIGR01348 119 VTVPDIG-DIEKVTVIEVLVKVGDTVSADQSLITLESDKASMEVPAPASGVVKSVKVKVGDSVPTGDLIltlsvagstpa 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365855 145 --AQVEPGEAPAEGSGESKPEPTEQ--AEPSQGVAARENSSEETASKKEAAPK---------------KEAAPKKEVTEP 205
Cdd:TIGR01348 198 taPAPASAQPAAQSPAATQPEPAAApaAAKAQAPAPQQAGTQNPAKVDHAAPAvrrlarefgvdlsavKGTGIKGRILRE 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365855 206 KKADQPKKTVSKAQEPPVASNS----FTPFPRTE-------TRVKMNRMRLRIAERLKESQNTAASLTTFNEVDMSALME 274
Cdd:TIGR01348 278 DVQRFVKEPSVRAQAAAASAAGgapgALPWPNVDfskfgevEEVDMSRIRKISGANLTRNWTMIPHVTHFDKADITEMEA 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365855 275 MRKLYKDEIiKKTGTKFGFMGLFSKACTLAAKDIPAVNGAIE--GDQIVYRDYTDISVAVATPKGLVTPVVRNAESLSVL 352
Cdd:TIGR01348 358 FRKQQNAAV-EKEGVKLTVLHILMKAVAAALKKFPKFNASLDlgGEQLILKKYVNIGVAVDTPNGLLVPVIKDVDRKGIT 436
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365855 353 DIENEIVRLSHKARDGKLTLEDMTGGTFTISNGGVFGSLYGTPIINSPQTAVLGLHGVKERPVTVNGQIVSRPMMYLALT 432
Cdd:TIGR01348 437 ELALELSDLAKKARDGKLTPDEMQGACFTISSLGGIGGTAFTPIVNAPEVAILGVSKSGMEPVWNGKEFEPRLMLPLSLS 516
|
410 420 430
....*....|....*....|....*....|
gi 398365855 433 YDHRLLDGREAVTFLKTVKELIEDPRKMLL 462
Cdd:TIGR01348 517 YDHRVIDGADAARFTTYICESLADIRRLLL 546
|
|
| PRK11857 |
PRK11857 |
dihydrolipoamide acetyltransferase; Reviewed |
196-457 |
7.29e-53 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237002 [Multi-domain] Cd Length: 306 Bit Score: 179.99 E-value: 7.29e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365855 196 AAPKKEVTEPKKADQPKKTVSKAQEPPVAsnsftPFPRTETRV-KMNRMRLRIAERLKESQNTAASLTTFNEVDMSALME 274
Cdd:PRK11857 41 KSLKSAPTPAEAASVSSAQQAAKTAAPAA-----APPKLEGKReKVAPIRKAIARAMTNSWSNVAYVNLVNEIDMTKLWD 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365855 275 MRKLYKDEIIKKTGTKFGFMGLFSKACTLAAKDIPAVNGAIE--GDQIVYRDYTDISVAVATPKGLVTPVVRNAESLSVL 352
Cdd:PRK11857 116 LRKSVKDPVLKTEGVKLTFLPFIAKAILIALKEFPIFAAKYDeaTSELVYPDTLNLGIAVDTEAGLMVPVIKNAQKLSIV 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365855 353 DIENEIVRLSHKARDGKLTLEDMTGGTFTISNGGVFGSLYGTPIINSPQTAVLGLHGVKERPVTVNGQIVSRPMMYLALT 432
Cdd:PRK11857 196 EIAKEISRLAKAARERKIKPDEMKGGSFTITNYGSVGSLYGVPVINYPELAIAGVGAIIDKAIVKNGQIVAGKVMHLTVA 275
|
250 260
....*....|....*....|....*
gi 398365855 433 YDHRLLDGREAVTFLKTVKELIEDP 457
Cdd:PRK11857 276 ADHRWIDGATIGRFASRVKELLEKP 300
|
|
| PRK14843 |
PRK14843 |
dihydrolipoamide acetyltransferase; Provisional |
202-462 |
5.09e-52 |
|
dihydrolipoamide acetyltransferase; Provisional
Pssm-ID: 184847 [Multi-domain] Cd Length: 347 Bit Score: 178.95 E-value: 5.09e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365855 202 VTEPKKAD--QPKKTVSKAQEPPvasNSFTPFPRTEtRVKMNRMRLRIAERLKESQNTAASLTTFNEVDMSALMEMRKLY 279
Cdd:PRK14843 87 LPENIENDsiKSPAQIEKVEEVP---DNVTPYGEIE-RIPMTPMRKVIAQRMVESYLTAPTFTLNYEVDMTEMLALRKKV 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365855 280 KDEIIKKTGTKFGFMGLFSKACTLAAKDIPAVNGAI--EGDQIVYRDYTDISVAVATPKGLVTPVVRNAESLSVLDIENE 357
Cdd:PRK14843 163 LEPIMEATGKKTTVTDLLSLAVVKTLMKHPYINASLteDGKTIITHNYVNLAMAVGMDNGLMTPVVYNAEKMSLSELVVA 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365855 358 IVRLSHKARDGKLTLEDMTGGTFTISNGGVFGSLYGTPIINSPQTAVLGLHGVKERPVTVNGQIVSRPMMYLALTYDHRL 437
Cdd:PRK14843 243 FKDVIGRTLDGKLAPSELQNSTFTISNLGMFGVQSFGPIINQPNSAILGVSSTIEKPVVVNGEIVIRPIMSLGLTIDHRV 322
|
250 260
....*....|....*....|....*
gi 398365855 438 LDGREAVTFLKTVKELIEDPRKMLL 462
Cdd:PRK14843 323 VDGMAGAKFMKDLKELIETPISMLI 347
|
|
| PLN02528 |
PLN02528 |
2-oxoisovalerate dehydrogenase E2 component |
80-462 |
1.07e-46 |
|
2-oxoisovalerate dehydrogenase E2 component
Pssm-ID: 215289 [Multi-domain] Cd Length: 416 Bit Score: 166.82 E-value: 1.07e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365855 80 PMA---ESLTEGSLKEYTKNVGDFIKEDELLATIETDKIDIEVNSPVSGTVTKLNFKPEDTVTVGEELAQVEPGEAPAEg 156
Cdd:PLN02528 2 PLAqtgEGIAECELLRWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGKVAQINFSPGDIVKVGETLLKIMVEDSQHL- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365855 157 SGESKPEPTEQAEPSQGVAARENSSEETASKKEAAPKKEAapkKEV---------TEPK----KADQPKKTVSKA--QEP 221
Cdd:PLN02528 81 RSDSLLLPTDSSNIVSLAESDERGSNLSGVLSTPAVRHLA---KQYgidlndilgTGKDgrvlKEDVLKYAAQKGvvKDS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365855 222 PVASNSFTP-----FPRTETRVKMNRMRLRIAER-----LKESQNTAASLTTF---NEVDMSALMEMRKLYKDEIiKKTG 288
Cdd:PLN02528 158 SSAEEATIAeqeefSTSVSTPTEQSYEDKTIPLRgfqraMVKTMTAAAKVPHFhyvEEINVDALVELKASFQENN-TDPT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365855 289 TKFGFMGLFSKACTLAAKDIPAVNGAIEGD--QIVYRDYTDISVAVATPKGLVTPVVRNAESLSVLDIENEIVRLSHKAR 366
Cdd:PLN02528 237 VKHTFLPFLIKSLSMALSKYPLLNSCFNEEtsEIRLKGSHNIGVAMATEHGLVVPNIKNVQSLSLLEITKELSRLQHLAA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365855 367 DGKLTLEDMTGGTFTISNGGVFGSLYGTPIINSPQTAVLGLHGVKERPVTVN-GQIVSRPMMYLALTYDHRLLDGREAVT 445
Cdd:PLN02528 317 ENKLNPEDITGGTITLSNIGAIGGKFGSPVLNLPEVAIIALGRIQKVPRFVDdGNVYPASIMTVTIGADHRVLDGATVAR 396
|
410
....*....|....*..
gi 398365855 446 FLKTVKELIEDPRKMLL 462
Cdd:PLN02528 397 FCNEWKSYVEKPELLML 413
|
|
| PLN02744 |
PLN02744 |
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex |
59-462 |
3.11e-38 |
|
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
Pssm-ID: 215397 [Multi-domain] Cd Length: 539 Bit Score: 145.77 E-value: 3.11e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365855 59 VAANPFSITSNRFKSTSIEVPPMAESLTEGSLKEYTKNVGDFIKEDELLATIETDKIDIEVNSPVSGTVTKLNFKP-EDT 137
Cdd:PLN02744 98 QSARGFSSSSDLPPHQEIGMPSLSPTMTEGNIARWLKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVKGDgAKE 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365855 138 VTVGEELA-QVEPGE--------APAEGSGESKPEPTEQAEPSQGVAARENSS--EETASKKEAAPKKE----AAP--KK 200
Cdd:PLN02744 178 IKVGEVIAiTVEEEEdigkfkdyKPSSSAAPAAPKAKPSPPPPKEEEVEKPASspEPKASKPSAPPSSGdrifASPlaRK 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365855 201 ------------EVTEPK----KADQPKKTVSKAQEPPVASNSFTPFPRTE-TRVKMNRMRLRIAERLKESQNTAAS--L 261
Cdd:PLN02744 258 laednnvplssiKGTGPDgrivKADIEDYLASGGKGATAPPSTDSKAPALDyTDIPNTQIRKVTASRLLQSKQTIPHyyL 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365855 262 TTFNEVDmsALMEMRKLYKDEIIKKTGTKFGFMGLFSKACTLAAKDIPAVNGAIEGDQIVYRDYTDISVAVATPKGLVTP 341
Cdd:PLN02744 338 TVDTRVD--KLMALRSQLNSLQEASGGKKISVNDLVIKAAALALRKVPQCNSSWTDDYIRQYHNVNINVAVQTENGLYVP 415
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365855 342 VVRNAESLSVLDIENEIVRLSHKARDGKLTLEDMTGGTFTISN-GGVFGSLYGTPIINSPQTAVLGLHGVKER--PVTVN 418
Cdd:PLN02744 416 VVKDADKKGLSTIAEEVKQLAQKARENSLKPEDYEGGTFTVSNlGGPFGIKQFCAIINPPQSAILAVGSAEKRviPGSGP 495
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 398365855 419 GQIVSRPMMYLALTYDHRLLDGREAVTFLKTVKELIEDPRKMLL 462
Cdd:PLN02744 496 DQYNFASFMSVTLSCDHRVIDGAIGAEWLKAFKGYIENPESMLL 539
|
|
| kgd |
PRK12270 |
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ... |
135-453 |
1.93e-22 |
|
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;
Pssm-ID: 237030 [Multi-domain] Cd Length: 1228 Bit Score: 100.74 E-value: 1.93e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365855 135 EDTVTVGEE----LAQVEPGEAPAegsGESKPEPTEQAEPSQGVAARENSSEETASKKEAAPKKEAAPKKEVTEPKKADQ 210
Cdd:PRK12270 20 ADPNSVDPSwrefFADYGPGSTAA---PTAAAAAAAAAASAPAAAPAAKAPAAPAPAPPAAAAPAAPPKPAAAAAAAAAP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365855 211 PKKTVSKAQEPPVASnsftpfPRTETRVKMNRMRLRIAErlkesqNTAASL-----TTFNEVDMSALMEMRKLYKDEIIK 285
Cdd:PRK12270 97 AAPPAAAAAAAPAAA------AVEDEVTPLRGAAAAVAK------NMDASLevptaTSVRAVPAKLLIDNRIVINNHLKR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365855 286 KTGTKFGFMGLFSKACTLAAKDIPAVN---GAIEGD-QIVYRDYTDISVAVATPK-----GLVTPVVRNAESLS---VLD 353
Cdd:PRK12270 165 TRGGKVSFTHLIGYALVQALKAFPNMNrhyAEVDGKpTLVTPAHVNLGLAIDLPKkdgsrQLVVPAIKGAETMDfaqFWA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365855 354 IENEIVRlshKARDGKLTLEDMTGGTFTISNGGVFGSLYGTPIINSPQTAVLGLhGVKERPV--------TVNGQIVSRp 425
Cdd:PRK12270 245 AYEDIVR---RARDGKLTADDFQGTTISLTNPGGIGTVHSVPRLMKGQGAIIGV-GAMEYPAefqgaseeRLAELGISK- 319
|
330 340
....*....|....*....|....*...
gi 398365855 426 MMYLALTYDHRLLDGREAVTFLKTVKEL 453
Cdd:PRK12270 320 VMTLTSTYDHRIIQGAESGEFLRTIHQL 347
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
74-145 |
3.96e-21 |
|
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: 86.69 E-value: 3.96e-21
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 398365855 74 TSIEVPPMAESLTEGSLKEYTKNVGDFIKEDELLATIETDKIDIEVNSPVSGTVTKLNFKPEDTVTVGEELA 145
Cdd:cd06849 1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIA 72
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
73-147 |
2.79e-19 |
|
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: 81.65 E-value: 2.79e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 398365855 73 STSIEVPPMAESLTEGSLKEYTKNVGDFIKEDELLATIETDKIDIEVNSPVSGTVTKLNFKPEDTVTVGEELAQV 147
Cdd:COG0508 2 AIEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
80-145 |
6.36e-11 |
|
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: 57.99 E-value: 6.36e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 398365855 80 PMAESLTEGSLKEYTKNVGDFIKEDELLATIETDKIDIEVNSPVSGTVTKLNFKPEDTVTVGEELA 145
Cdd:pfam00364 6 PMIGESVREGVVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLA 71
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
73-204 |
9.10e-10 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 60.70 E-value: 9.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365855 73 STSIEVPPMAESLTEGSLKEYTKNVGDFIKEDELLATIETDKIDIEVNSPVSGTVTKLnFKPEDT--VTVGEELAQ-VEP 149
Cdd:PRK11892 2 AIEILMPALSPTMEEGTLAKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKI-LVPEGTegVKVNTPIAVlLEE 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 398365855 150 GEAPAEGSGESKPEPTEQAEPSQGVAARENSSEETASKKEAAPKKEAAPKKEVTE 204
Cdd:PRK11892 81 GESASDAGAAPAAAAEAAAAAPAAAAAAAAKKAAPAPAAPAAPAAEVAADPDIPA 135
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
74-215 |
1.14e-08 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 56.88 E-value: 1.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365855 74 TSIEVPPMAESLTEGSLKEYTKNVGDFIKEDELLATIETDKIDIEVNSPVSGTVTKLNFKPEDTVTVGEELAQVEPGEAP 153
Cdd:PRK14875 3 TPITMPKWGLSMTEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGETLPVGALLAVVADAEVS 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 398365855 154 AEgsgeskpEPTEQAEPSQGVAARENSSEEtaskkEAAPkkeaapkkevtEPKKADQPKKTV 215
Cdd:PRK14875 83 DA-------EIDAFIAPFARRFAPEGIDEE-----DAGP-----------APRKARIGGRTV 121
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
76-144 |
1.14e-08 |
|
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases, and the H-protein of the glycine cleavage system (GCS). These domains transport CO2, acyl, or methylamine, respectively, between components of the complex/protein via a biotinyl or lipoyl group, which is covalently attached to a highly conserved lysine residue.
Pssm-ID: 133456 [Multi-domain] Cd Length: 73 Bit Score: 51.67 E-value: 1.14e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 398365855 76 IEVPPMAESLTEGSLKEYTKNVGDFIKEDELLATIETDKIDIEVNSPVSGTVTKLNFKPEDTVTVGEEL 144
Cdd:cd06663 2 ILIPDLAQHLGDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKVEGDTPL 70
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
80-147 |
1.32e-08 |
|
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: 51.26 E-value: 1.32e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 398365855 80 PMAeslteGSLKEYTKNVGDFIKEDELLATIETDKIDIEVNSPVSGTVTKLNFKPEDTVTVGEELAQV 147
Cdd:cd06850 5 PMP-----GTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| AccB |
COG0511 |
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ... |
96-148 |
2.53e-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: 46.81 E-value: 2.53e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 398365855 96 NVGDFIKEDELLATIETDKIDIEVNSPVSGTVTKLNFKPEDTVTVGEELAQVE 148
Cdd:COG0511 84 KVGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVVEILVENGQPVEYGQPLFVIE 136
|
|
| PRK09282 |
PRK09282 |
pyruvate carboxylase subunit B; Validated |
96-149 |
5.69e-06 |
|
pyruvate carboxylase subunit B; Validated
Pssm-ID: 236449 [Multi-domain] Cd Length: 592 Bit Score: 48.69 E-value: 5.69e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 398365855 96 NVGDFIKEDELLATIETDKIDIEVNSPVSGTVTKLNFKPEDTVTVGEELAQVEP 149
Cdd:PRK09282 539 KEGDKVKAGDTVLVLEAMKMENEIQAPVDGTVKEILVKEGDRVNPGDVLMEIEP 592
|
|
| GCS_H |
cd06848 |
Glycine cleavage H-protein. Glycine cleavage H-proteins are part of the glycine cleavage ... |
95-131 |
3.12e-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: 42.52 E-value: 3.12e-05
10 20 30
....*....|....*....|....*....|....*..
gi 398365855 95 KNVGDFIKEDELLATIETDKIDIEVNSPVSGTVTKLN 131
Cdd:cd06848 37 PEVGTEVKKGDPFGSVESVKAASDLYSPVSGEVVEVN 73
|
|
| PRK00624 |
PRK00624 |
glycine cleavage system protein H; Provisional |
97-138 |
9.02e-05 |
|
glycine cleavage system protein H; Provisional
Pssm-ID: 167014 Cd Length: 114 Bit Score: 41.74 E-value: 9.02e-05
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 398365855 97 VGDFIKEDELLATIETDKIDIEVNSPVSGTVTKLNFKPEDTV 138
Cdd:PRK00624 42 VGSFCKEGEVLVILESSKSAIEVLSPVSGEVIEVNTALEDDI 83
|
|
| AcrA |
COG0845 |
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ... |
98-155 |
3.89e-04 |
|
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope biogenesis, Defense mechanisms];
Pssm-ID: 440606 [Multi-domain] Cd Length: 324 Bit Score: 42.24 E-value: 3.89e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 398365855 98 GDFIKEDELLATIETDKiDIEVNSPVSGTVTKLNFKPEDTVTVGEELAQVEPGEAPAE 155
Cdd:COG0845 6 GDVPETVEATGTVEARR-EVEVRARVSGRVEEVLVDEGDRVKKGQVLARLDPPDLQAA 62
|
|
| PRK14040 |
PRK14040 |
oxaloacetate decarboxylase subunit alpha; |
97-144 |
1.65e-03 |
|
oxaloacetate decarboxylase subunit alpha;
Pssm-ID: 237592 [Multi-domain] Cd Length: 593 Bit Score: 40.68 E-value: 1.65e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 398365855 97 VGDFIKEDELLATIETDKIDIEVNSPVSGTVTKLNFKPEDTVTVGEEL 144
Cdd:PRK14040 542 EGQTVAEGDVLLILEAMKMETEIRAAQAGTVRGIAVKEGDAVAVGDTL 589
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
80-149 |
2.13e-03 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 40.51 E-value: 2.13e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365855 80 PMAeslteGSLKEYTKNVGDFIKEDELLATIETDKIDIEVNSPVSGTVTKLNFKPEDTVTVGEELAQVEP 149
Cdd:PRK12999 1082 PMP-----GSVVTVLVKEGDEVKAGDPLAVIEAMKMETTITAPVDGTVKRVLVKAGDQVEAGDLLVELEP 1146
|
|
| GcvH |
COG0509 |
Glycine cleavage system protein H (lipoate-binding) [Amino acid transport and metabolism]; ... |
95-131 |
3.47e-03 |
|
Glycine cleavage system protein H (lipoate-binding) [Amino acid transport and metabolism]; Glycine cleavage system protein H (lipoate-binding) is part of the Pathway/BioSystem: Glycine cleavage
Pssm-ID: 440275 Cd Length: 128 Bit Score: 37.41 E-value: 3.47e-03
10 20 30
....*....|....*....|....*....|....*..
gi 398365855 95 KNVGDFIKEDELLATIETDKIDIEVNSPVSGTVTKLN 131
Cdd:COG0509 45 PEVGTEVEAGEPFGVVESVKAVSDLYAPVSGEVVEVN 81
|
|
| motB |
PRK05996 |
MotB family protein; |
148-210 |
8.66e-03 |
|
MotB family protein;
Pssm-ID: 235665 [Multi-domain] Cd Length: 423 Bit Score: 38.53 E-value: 8.66e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 398365855 148 EPGEAPAEGSGESKPEPTEQAEPSQGVAARENSSEETASKKEAAPKKEAAPKKEVTEPKKADQ 210
Cdd:PRK05996 223 QAAPLPQAQPKKAATEEELIADAKKAATGEPAANAAKAAKPEPMPDDQQKEAEQLQAAIAQAI 285
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
133-220 |
9.43e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 38.58 E-value: 9.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365855 133 KPEDTVTVGEELAQVEPGEAPAEgSGESKPEPTEQAEPSQGVAARENSSEETASKKEAAPKKEAAPKKeVTEPKKADQPK 212
Cdd:PTZ00121 1399 KAEEDKKKADELKKAAAAKKKAD-EAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKK-AEEAKKADEAK 1476
|
....*...
gi 398365855 213 KtvsKAQE 220
Cdd:PTZ00121 1477 K---KAEE 1481
|
|
| |
