|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11856 |
PRK11856 |
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed |
9-499 |
2.46e-155 |
|
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
Pssm-ID: 237001 [Multi-domain] Cd Length: 411 Bit Score: 448.09 E-value: 2.46e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751461977 9 VREFKMPDVGEGLTEAEILKWYVQPGDTVTDGQVVCEVETAKAAVELPIPYDGVVRALHFPEGTTVDVGTSIIAVDVSGG 88
Cdd:PRK11856 2 MFEFKMPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDVVPVGSVIAVIEEEGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751461977 89 AAPepeapaaaeavpaaaapapavavpaeqPAEAEPAAVGSGRQPVLVGYGVSTSATRRRPRKPAPDGFArqtlegdrte 168
Cdd:PRK11856 82 AEA---------------------------AAAAEAAPEAPAPEPAPAAAAAAAAAPAAAAAPAAPAAAA---------- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751461977 169 lnghaqatptapapaapvagalrPLAKPPVRKLAKDLGVDLATVTATGPDGIVTREDVHAAVAAEPKTSEEPAAVPapva 248
Cdd:PRK11856 125 -----------------------AKASPAVRKLARELGVDLSTVKGSGPGGRITKEDVEAAAAAAAPAAAAAAAAA---- 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751461977 249 ppaptaaatpvtaSAPVSYDTARETRIPVKGVRKATAAAMVGSAFTAPHVTEFVTVDVTRTMKLVEELKQDKEftglRVN 328
Cdd:PRK11856 178 -------------AAPPAAAAEGEERVPLSGMRKAIAKRMVESKREIPHFTLTDEVDVTALLALRKQLKAIGV----KLT 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751461977 329 PLLLIAKALLVAIRRNPDVNASWDEAAqeIVVKHYVNLGIAAATPRGLIVPNIKDAHAKTLPQLAESLGELVSTARDGKT 408
Cdd:PRK11856 241 VTDFLIKAVALALKKFPELNASWDDDA--IVLKKYVNIGIAVATDGGLIVPVIRDADKKSLFELAREIKDLAEKAREGKL 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751461977 409 SPSAMQAGTVTITNVGVFGVDTGTPILNPGESAILAVGAIKLQPWVHKGKVKPRQVTTLALSFDHRLVDGELGSRVLADV 488
Cdd:PRK11856 319 KPEELQGGTFTISNLGMFGGDYFTPIINPPEVAILGVGAIVERPVVVDGEIVVRKVMPLSLSFDHRVIDGADAARFLKAL 398
|
490
....*....|.
gi 1751461977 489 AAILEQPKRLI 499
Cdd:PRK11856 399 KELLENPALLL 409
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
288-499 |
6.96e-87 |
|
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: 265.95 E-value: 6.96e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751461977 288 MVGSAFTAPHVTEFVTVDVTRTMKLVEELKQDKEFTGLRVNPLLLIAKALLVAIRRNPDVNASWDEAAQEIVVKHYVNLG 367
Cdd:pfam00198 1 MTESKQTIPHFTLTDEVDVTELLALREELKEDAADEETKLTFLPFLVKAVALALKKFPELNASWDGEEGEIVYKKYVNIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751461977 368 IAAATPRGLIVPNIKDAHAKTLPQLAESLGELVSTARDGKTSPSAMQAGTVTITNVGVFGVDTGTPILNPGESAILAVGA 447
Cdd:pfam00198 81 IAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVGR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1751461977 448 IKLQPWVHKGKVKPRQVTTLALSFDHRLVDGELGSRVLADVAAILEQPKRLI 499
Cdd:pfam00198 161 IRKRPVVVDGEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELLL 212
|
|
| sucB |
TIGR01347 |
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ... |
11-501 |
6.16e-70 |
|
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: 228.85 E-value: 6.16e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751461977 11 EFKMPDVGEGLTEAEILKWYVQPGDTVTDGQVVCEVETAKAAVELPIPYDGVVRALHFPEGTTVDVGTSIIAVDVSGGaa 90
Cdd:TIGR01347 2 EIKVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAILEEGND-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751461977 91 pepeapaaaeavpaaaapapavavpaeqPAEAEPAAVGSGRQPVLVgygvstsatrrRPRKPAPDGFARqtlegdrteln 170
Cdd:TIGR01347 80 ----------------------------ATAAPPAKSGEEKEETPA-----------ASAAAAPTAAAN----------- 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751461977 171 ghaqatptapapaapvagalRPLAKPPVRKLAKDLGVDLATVTATGPDGIVTREDVHAAVAAEPKTSEEPAAVPAPvapp 250
Cdd:TIGR01347 110 --------------------RPSLSPAARRLAKEHGIDLSAVPGTGVTGRVTKEDIIKKTEAPASAQPPAAAAAAA---- 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751461977 251 aptaaatpvtasAPVSYdTARETRIPVKGVRKATAAAMVGSAFTAPHVTEFVTVDVTRTMKLVEELKQD-KEFTGLRVNP 329
Cdd:TIGR01347 166 ------------APAAA-TRPEERVKMTRLRQRIAERLKEAQNSTAMLTTFNEVDMSAVMELRKRYKEEfEKKHGVKLGF 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751461977 330 LLLIAKALLVAIRRNPDVNASWDeaAQEIVVKHYVNLGIAAATPRGLIVPNIKDAHAKTLPQLAESLGELVSTARDGKTS 409
Cdd:TIGR01347 233 MSFFVKAVVAALKRFPEVNAEID--GDDIVYKDYYDISVAVSTDRGLVVPVVRNADRMSFADIEKEIADLGKKARDGKLT 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751461977 410 PSAMQAGTVTITNVGVFGVDTGTPILNPGESAILAVGAIKLQPWVHKGKVKPRQVTTLALSFDHRLVDGELGSRVLADVA 489
Cdd:TIGR01347 311 LEDMTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHGIKERPVAVNGQIEIRPMMYLALSYDHRLIDGKEAVTFLVTIK 390
|
490
....*....|..
gi 1751461977 490 AILEQPKRLISW 501
Cdd:TIGR01347 391 ELLEDPRRLLLD 402
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
11-83 |
3.73e-26 |
|
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: 101.30 E-value: 3.73e-26
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1751461977 11 EFKMPDVGEGLTEAEILKWYVQPGDTVTDGQVVCEVETAKAAVELPIPYDGVVRALHFPEGTTVDVGTsIIAV 83
Cdd:COG0508 4 EIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGA-VIAV 75
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
11-83 |
7.03e-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: 100.56 E-value: 7.03e-26
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1751461977 11 EFKMPDVGEGLTEAEILKWYVQPGDTVTDGQVVCEVETAKAAVELPIPYDGVVRALHFPEGTTVDVGTsIIAV 83
Cdd:cd06849 2 EIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQ-VIAV 73
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11856 |
PRK11856 |
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed |
9-499 |
2.46e-155 |
|
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
Pssm-ID: 237001 [Multi-domain] Cd Length: 411 Bit Score: 448.09 E-value: 2.46e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751461977 9 VREFKMPDVGEGLTEAEILKWYVQPGDTVTDGQVVCEVETAKAAVELPIPYDGVVRALHFPEGTTVDVGTSIIAVDVSGG 88
Cdd:PRK11856 2 MFEFKMPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDVVPVGSVIAVIEEEGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751461977 89 AAPepeapaaaeavpaaaapapavavpaeqPAEAEPAAVGSGRQPVLVGYGVSTSATRRRPRKPAPDGFArqtlegdrte 168
Cdd:PRK11856 82 AEA---------------------------AAAAEAAPEAPAPEPAPAAAAAAAAAPAAAAAPAAPAAAA---------- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751461977 169 lnghaqatptapapaapvagalrPLAKPPVRKLAKDLGVDLATVTATGPDGIVTREDVHAAVAAEPKTSEEPAAVPapva 248
Cdd:PRK11856 125 -----------------------AKASPAVRKLARELGVDLSTVKGSGPGGRITKEDVEAAAAAAAPAAAAAAAAA---- 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751461977 249 ppaptaaatpvtaSAPVSYDTARETRIPVKGVRKATAAAMVGSAFTAPHVTEFVTVDVTRTMKLVEELKQDKEftglRVN 328
Cdd:PRK11856 178 -------------AAPPAAAAEGEERVPLSGMRKAIAKRMVESKREIPHFTLTDEVDVTALLALRKQLKAIGV----KLT 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751461977 329 PLLLIAKALLVAIRRNPDVNASWDEAAqeIVVKHYVNLGIAAATPRGLIVPNIKDAHAKTLPQLAESLGELVSTARDGKT 408
Cdd:PRK11856 241 VTDFLIKAVALALKKFPELNASWDDDA--IVLKKYVNIGIAVATDGGLIVPVIRDADKKSLFELAREIKDLAEKAREGKL 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751461977 409 SPSAMQAGTVTITNVGVFGVDTGTPILNPGESAILAVGAIKLQPWVHKGKVKPRQVTTLALSFDHRLVDGELGSRVLADV 488
Cdd:PRK11856 319 KPEELQGGTFTISNLGMFGGDYFTPIINPPEVAILGVGAIVERPVVVDGEIVVRKVMPLSLSFDHRVIDGADAARFLKAL 398
|
490
....*....|.
gi 1751461977 489 AAILEQPKRLI 499
Cdd:PRK11856 399 KELLENPALLL 409
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
9-499 |
1.32e-97 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 305.21 E-value: 1.32e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751461977 9 VREFKMPDVGEgLTEAEILKWYVQPGDTVTDGQVVCEVETAKAAVELPIPYDGVVRALHFPEGTTVDVGTSIIAVDVSGG 88
Cdd:PRK11855 119 VVEVKVPDIGE-ITEVEVIEWLVKVGDTVEEDQSLITVETDKATMEIPSPVAGVVKEIKVKVGDKVSVGSLLVVIEVAAA 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751461977 89 AAPEPEAPAAAEAVPAAAAPAPAVAVPAEQPAEAEPAAvgsgrqpvlvgygvstsatrrrprkPAPDGFArqtlegdrte 168
Cdd:PRK11855 198 APAAAAAPAAAAPAAAAAAAPAPAPAAAAAPAAAAPAA-------------------------AAAPGKA---------- 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751461977 169 lnghaqatptapapaapvagalrPLAKPPVRKLAKDLGVDLATVTATGPDGIVTREDVHAAVAAEPKTSEepaavpAPVA 248
Cdd:PRK11855 243 -----------------------PHASPAVRRLARELGVDLSQVKGTGKKGRITKEDVQAFVKGAMSAAA------AAAA 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751461977 249 PPAPTAAATPVTASAP-VSYDTARETRI-PVKGVRKATAAAMVGSAFTAPHVTEFVTVDVTRTMKLVEELKQDKEFTGLR 326
Cdd:PRK11855 294 AAAAAGGGGLGLLPWPkVDFSKFGEIETkPLSRIKKISAANLHRSWVTIPHVTQFDEADITDLEALRKQLKKEAEKAGVK 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751461977 327 VNPLLLIAKALLVAIRRNPDVNASWDEAAQEIVVKHYVNLGIAAATPRGLIVPNIKDAHAKTLPQLAESLGELVSTARDG 406
Cdd:PRK11855 374 LTMLPFFIKAVVAALKEFPVFNASLDEDGDELTYKKYFNIGFAVDTPNGLVVPVIKDVDKKSLLEIAREIAELAKKARDG 453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751461977 407 KTSPSAMQAGTVTITNVGVFGVDTGTPILNPGESAILAVGAIKLQPWVHKGKVKPRQVTTLALSFDHRLVDGELGSRVLA 486
Cdd:PRK11855 454 KLKPDDMQGGCFTISSLGGIGGTAFTPIINAPEVAILGVGKSQMKPVWDGKEFVPRLMLPLSLSYDHRVIDGATAARFTN 533
|
490
....*....|...
gi 1751461977 487 DVAAILEQPKRLI 499
Cdd:PRK11855 534 YLKQLLADPRRML 546
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
288-499 |
6.96e-87 |
|
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: 265.95 E-value: 6.96e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751461977 288 MVGSAFTAPHVTEFVTVDVTRTMKLVEELKQDKEFTGLRVNPLLLIAKALLVAIRRNPDVNASWDEAAQEIVVKHYVNLG 367
Cdd:pfam00198 1 MTESKQTIPHFTLTDEVDVTELLALREELKEDAADEETKLTFLPFLVKAVALALKKFPELNASWDGEEGEIVYKKYVNIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751461977 368 IAAATPRGLIVPNIKDAHAKTLPQLAESLGELVSTARDGKTSPSAMQAGTVTITNVGVFGVDTGTPILNPGESAILAVGA 447
Cdd:pfam00198 81 IAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVGR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1751461977 448 IKLQPWVHKGKVKPRQVTTLALSFDHRLVDGELGSRVLADVAAILEQPKRLI 499
Cdd:pfam00198 161 IRKRPVVVDGEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELLL 212
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
9-499 |
1.48e-75 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 249.92 E-value: 1.48e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751461977 9 VREFKMPDVGegLTEAEILKWYVQPGDTVTDGQVVCEVETAKAAVELPIPYDGVVRALHFPEGTTVDVGTSIIAVDVSGG 88
Cdd:PRK11854 206 VKDVNVPDIG--GDEVEVTEVMVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVKTGSLIMRFEVEGA 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751461977 89 AAPEPEApaaaeavpaaaapapavavpaeQPAEAEPAAVgsgrqpvlvgygvstsatrrRPRKPAPDGFARQTLEGDRTE 168
Cdd:PRK11854 284 APAAAPA----------------------KQEAAAPAPA--------------------AAKAEAPAAAPAAKAEGKSEF 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751461977 169 LNGHAQatptapapaapvagalrPLAKPPVRKLAKDLGVDLATVTATGPDGIVTREDVHAAVAAEPKTSEEPAAVPAPVA 248
Cdd:PRK11854 322 AENDAY-----------------VHATPLVRRLAREFGVNLAKVKGTGRKGRILKEDVQAYVKDAVKRAEAAPAAAAAGG 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751461977 249 PPAPTAAATpvtasaPVSYDTARETR-IPVKGVRKATAAAMVGSAFTAPHVTEFVTVDVTRtmklVEELKQD------KE 321
Cdd:PRK11854 385 GGPGLLPWP------KVDFSKFGEIEeVELGRIQKISGANLHRNWVMIPHVTQFDKADITE----LEAFRKQqnaeaeKR 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751461977 322 FTGLRVNPLLLIAKALLVAIRRNPDVNASWDEAAQEIVVKHYVNLGIAAATPRGLIVPNIKDAHAKTLPQLAESLGELVS 401
Cdd:PRK11854 455 KLGVKITPLVFIMKAVAAALEQMPRFNSSLSEDGQRLTLKKYVNIGIAVDTPNGLVVPVFKDVNKKGIIELSRELMDISK 534
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751461977 402 TARDGKTSPSAMQAGTVTITNVGVFGVDTGTPILNPGESAILAVGAIKLQPwVHKGK-VKPRQVTTLALSFDHRLVDGEL 480
Cdd:PRK11854 535 KARDGKLTAGDMQGGCFTISSIGGLGTTHFTPIVNAPEVAILGVSKSAMEP-VWNGKeFAPRLMLPLSLSYDHRVIDGAD 613
|
490
....*....|....*....
gi 1751461977 481 GSRVLADVAAILEQPKRLI 499
Cdd:PRK11854 614 GARFITIINDRLSDIRRLV 632
|
|
| sucB |
TIGR01347 |
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ... |
11-501 |
6.16e-70 |
|
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: 228.85 E-value: 6.16e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751461977 11 EFKMPDVGEGLTEAEILKWYVQPGDTVTDGQVVCEVETAKAAVELPIPYDGVVRALHFPEGTTVDVGTSIIAVDVSGGaa 90
Cdd:TIGR01347 2 EIKVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAILEEGND-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751461977 91 pepeapaaaeavpaaaapapavavpaeqPAEAEPAAVGSGRQPVLVgygvstsatrrRPRKPAPDGFARqtlegdrteln 170
Cdd:TIGR01347 80 ----------------------------ATAAPPAKSGEEKEETPA-----------ASAAAAPTAAAN----------- 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751461977 171 ghaqatptapapaapvagalRPLAKPPVRKLAKDLGVDLATVTATGPDGIVTREDVHAAVAAEPKTSEEPAAVPAPvapp 250
Cdd:TIGR01347 110 --------------------RPSLSPAARRLAKEHGIDLSAVPGTGVTGRVTKEDIIKKTEAPASAQPPAAAAAAA---- 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751461977 251 aptaaatpvtasAPVSYdTARETRIPVKGVRKATAAAMVGSAFTAPHVTEFVTVDVTRTMKLVEELKQD-KEFTGLRVNP 329
Cdd:TIGR01347 166 ------------APAAA-TRPEERVKMTRLRQRIAERLKEAQNSTAMLTTFNEVDMSAVMELRKRYKEEfEKKHGVKLGF 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751461977 330 LLLIAKALLVAIRRNPDVNASWDeaAQEIVVKHYVNLGIAAATPRGLIVPNIKDAHAKTLPQLAESLGELVSTARDGKTS 409
Cdd:TIGR01347 233 MSFFVKAVVAALKRFPEVNAEID--GDDIVYKDYYDISVAVSTDRGLVVPVVRNADRMSFADIEKEIADLGKKARDGKLT 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751461977 410 PSAMQAGTVTITNVGVFGVDTGTPILNPGESAILAVGAIKLQPWVHKGKVKPRQVTTLALSFDHRLVDGELGSRVLADVA 489
Cdd:TIGR01347 311 LEDMTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHGIKERPVAVNGQIEIRPMMYLALSYDHRLIDGKEAVTFLVTIK 390
|
490
....*....|..
gi 1751461977 490 AILEQPKRLISW 501
Cdd:TIGR01347 391 ELLEDPRRLLLD 402
|
|
| PRK05704 |
PRK05704 |
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase; |
11-499 |
2.59e-68 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
Pssm-ID: 235571 [Multi-domain] Cd Length: 407 Bit Score: 224.71 E-value: 2.59e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751461977 11 EFKMPDVGEGLTEAEILKWYVQPGDTVTDGQVVCEVETAKAAVELPIPYDGVVRALHFPEGTTVDVGtSIIAVDVSGGAA 90
Cdd:PRK05704 4 EIKVPTLPESVTEATIATWHKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGDTVTVG-QVLGRIDEGAAA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751461977 91 PEPeapaaaeavpaaaapapavavpaeQPAEAEPAAvgsgrqpvlvgygvstSATRRRPRKPAPDGFARQtlegdrteln 170
Cdd:PRK05704 83 GAA------------------------AAAAAAAAA----------------AAAAPAQAQAAAAAEQSN---------- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751461977 171 ghaqatptapapaapvagalrPLAKPPVRKLAKDLGVDLATVTATGPDGIVTREDVHAAVAAEPKTSEEPAAVPAPvapp 250
Cdd:PRK05704 113 ---------------------DALSPAARKLAAENGLDASAVKGTGKGGRVTKEDVLAALAAAAAAPAAPAAAAPA---- 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751461977 251 aptaaatpvtaSAPVSYDTARETRIPVKGVRKATAAAMVGSAFTAPHVTEFVTVDVTRTMKLVEELKQDKE--------F 322
Cdd:PRK05704 168 -----------AAPAPLGARPEERVPMTRLRKTIAERLLEAQNTTAMLTTFNEVDMTPVMDLRKQYKDAFEkkhgvklgF 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751461977 323 TGLRVnpllliaKALLVAIRRNPDVNASWDeaAQEIVVKHYVNLGIAAATPRGLIVPNIKDAHAKTLPQLAESLGELVST 402
Cdd:PRK05704 237 MSFFV-------KAVVEALKRYPEVNASID--GDDIVYHNYYDIGIAVGTPRGLVVPVLRDADQLSFAEIEKKIAELAKK 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751461977 403 ARDGKTSPSAMQAGTVTITNVGVFGVDTGTPILNPGESAILAVGAIKLQPWVHKGKVKPRQVTTLALSFDHRLVDGELGS 482
Cdd:PRK05704 308 ARDGKLSIEELTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHKIKERPVAVNGQIVIRPMMYLALSYDHRIIDGKEAV 387
|
490
....*....|....*..
gi 1751461977 483 RVLADVAAILEQPKRLI 499
Cdd:PRK05704 388 GFLVTIKELLEDPERLL 404
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
7-499 |
1.94e-66 |
|
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: 223.60 E-value: 1.94e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751461977 7 APVREFKMPDVGeGLTEAEILKWYVQPGDTVTDGQVVCEVETAKAAVELPIPYDGVVRALHFPEGTTVDVGTSIIAVDVS 86
Cdd:TIGR01348 114 SGVQEVTVPDIG-DIEKVTVIEVLVKVGDTVSADQSLITLESDKASMEVPAPASGVVKSVKVKVGDSVPTGDLILTLSVA 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751461977 87 GgaapepeapaaaeavpaaaapapAVAVPAEQPAEAEPAAvgsgrqpvlvgygvsTSATRRRPRKPAPDGFARQTlegdr 166
Cdd:TIGR01348 193 G-----------------------STPATAPAPASAQPAA---------------QSPAATQPEPAAAPAAAKAQ----- 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751461977 167 telnghaqatPTAPAPAAPVAGALRPLAKPPVRKLAKDLGVDLATVTATGPDGIVTREDVHAAVAAEPKTSEEPAAVPAP 246
Cdd:TIGR01348 230 ----------APAPQQAGTQNPAKVDHAAPAVRRLAREFGVDLSAVKGTGIKGRILREDVQRFVKEPSVRAQAAAASAAG 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751461977 247 VAPPAPTAAATPVTASAPVSydtaretRIPVKGVRKATAAAMVGSAFTAPHVTEFVTVDVTRTMKLVEELKQDKEFTGLR 326
Cdd:TIGR01348 300 GAPGALPWPNVDFSKFGEVE-------EVDMSRIRKISGANLTRNWTMIPHVTHFDKADITEMEAFRKQQNAAVEKEGVK 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751461977 327 VNPLLLIAKALLVAIRRNPDVNASWDEAAQEIVVKHYVNLGIAAATPRGLIVPNIKDAHAKTLPQLAESLGELVSTARDG 406
Cdd:TIGR01348 373 LTVLHILMKAVAAALKKFPKFNASLDLGGEQLILKKYVNIGVAVDTPNGLLVPVIKDVDRKGITELALELSDLAKKARDG 452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751461977 407 KTSPSAMQAGTVTITNVGVFGVDTGTPILNPGESAILAVGAIKLQPWVHKGKVKPRQVTTLALSFDHRLVDGELGSRVLA 486
Cdd:TIGR01348 453 KLTPDEMQGACFTISSLGGIGGTAFTPIVNAPEVAILGVSKSGMEPVWNGKEFEPRLMLPLSLSYDHRVIDGADAARFTT 532
|
490
....*....|...
gi 1751461977 487 DVAAILEQPKRLI 499
Cdd:TIGR01348 533 YICESLADIRRLL 545
|
|
| PLN02528 |
PLN02528 |
2-oxoisovalerate dehydrogenase E2 component |
12-499 |
3.11e-61 |
|
2-oxoisovalerate dehydrogenase E2 component
Pssm-ID: 215289 [Multi-domain] Cd Length: 416 Bit Score: 206.49 E-value: 3.11e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751461977 12 FKMPDVGEGLTEAEILKWYVQPGDTVTDGQVVCEVETAKAAVELPIPYDGVVRALHFPEGTTVDVGTSIIAVDVSGGAAP 91
Cdd:PLN02528 1 VPLAQTGEGIAECELLRWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGKVAQINFSPGDIVKVGETLLKIMVEDSQHL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751461977 92 EPEAPAAAEAvpaaaapapavavpaeqPAEAEPAAVGSGRqpvlvgyGVSTSATrrrprkpapdgfarqtlegdrtelng 171
Cdd:PLN02528 81 RSDSLLLPTD-----------------SSNIVSLAESDER-------GSNLSGV-------------------------- 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751461977 172 haqatptapapaapvagalrpLAKPPVRKLAKDLGVDLATVTATGPDGIVTREDV--HAA---VAAEPKTSEEPAAVPAP 246
Cdd:PLN02528 111 ---------------------LSTPAVRHLAKQYGIDLNDILGTGKDGRVLKEDVlkYAAqkgVVKDSSSAEEATIAEQE 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751461977 247 VAPPAPTAAATPvtasapvSYDtarETRIPVKGVRKATAAAMVGSAfTAPHvteFVTVDVTRTMKLVE---ELKQDKEFT 323
Cdd:PLN02528 170 EFSTSVSTPTEQ-------SYE---DKTIPLRGFQRAMVKTMTAAA-KVPH---FHYVEEINVDALVElkaSFQENNTDP 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751461977 324 GLRVNPLLLIAKALLVAIRRNPDVNASWDEAAQEIVVKHYVNLGIAAATPRGLIVPNIKDAHAKTLPQLAESLGELVSTA 403
Cdd:PLN02528 236 TVKHTFLPFLIKSLSMALSKYPLLNSCFNEETSEIRLKGSHNIGVAMATEHGLVVPNIKNVQSLSLLEITKELSRLQHLA 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751461977 404 RDGKTSPSAMQAGTVTITNVGVFGVDTGTPILNPGESAILAVGAI-KLQPWVHKGKVKPRQVTTLALSFDHRLVDGELGS 482
Cdd:PLN02528 316 AENKLNPEDITGGTITLSNIGAIGGKFGSPVLNLPEVAIIALGRIqKVPRFVDDGNVYPASIMTVTIGADHRVLDGATVA 395
|
490
....*....|....*..
gi 1751461977 483 RVLADVAAILEQPKRLI 499
Cdd:PLN02528 396 RFCNEWKSYVEKPELLM 412
|
|
| PTZ00144 |
PTZ00144 |
dihydrolipoamide succinyltransferase; Provisional |
13-499 |
1.26e-55 |
|
dihydrolipoamide succinyltransferase; Provisional
Pssm-ID: 240289 [Multi-domain] Cd Length: 418 Bit Score: 191.43 E-value: 1.26e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751461977 13 KMPDVGEGLTEAEILKWYVQPGDTVTDGQVVCEVETAKAAVELPIPYDGVVRALHFPEGTTVDVGTSIIAVDVSGgaape 92
Cdd:PTZ00144 48 KVPTMGDSISEGTVVEWKKKVGDYVKEDEVICIIETDKVSVDIRAPASGVITKIFAEEGDTVEVGAPLSEIDTGG----- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751461977 93 peapaaaeavpaaaapapavavpaeQPAEAEPAAVGSGRQPvlvgygvSTSATRRRPRKPAPDGFARQTlegdrtelngh 172
Cdd:PTZ00144 123 -------------------------APPAAAPAAAAAAKAE-------KTTPEKPKAAAPTPEPPAASK----------- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751461977 173 aqatptapapaapvagalrPLAKPPVRKlakdlgvdlatvtatgpdgivtredvhAAVAAEPKTSEEpaavpapvappap 252
Cdd:PTZ00144 160 -------------------PTPPAAAKP---------------------------PEPAPAAKPPPT------------- 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751461977 253 taaatpvtasaPVSYDTARETRIPVKGVRKATAAAMVGSAFTAPHVTEFVTVDVTRTMKLVEELKQD-KEFTGLRVNPLL 331
Cdd:PTZ00144 181 -----------PVARADPRETRVPMSRMRQRIAERLKASQNTCAMLTTFNECDMSALMELRKEYKDDfQKKHGVKLGFMS 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751461977 332 LIAKALLVAIRRNPDVNASWDEaaQEIVVKHYVNLGIAAATPRGLIVPNIKDAHAKTLPQLAESLGELVSTARDGKTSPS 411
Cdd:PTZ00144 250 AFVKASTIALKKMPIVNAYIDG--DEIVYRNYVDISVAVATPTGLVVPVIRNCENKSFAEIEKELADLAEKARNNKLTLE 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751461977 412 AMQAGTVTITNVGVFGVDTGTPILNPGESAILAVGAIKLQPWVHKGKVKPRQVTTLALSFDHRLVDGELGSRVLADVAAI 491
Cdd:PTZ00144 328 DMTGGTFTISNGGVFGSLMGTPIINPPQSAILGMHAIKKRPVVVGNEIVIRPIMYLALTYDHRLIDGRDAVTFLKKIKDL 407
|
....*...
gi 1751461977 492 LEQPKRLI 499
Cdd:PTZ00144 408 IEDPARML 415
|
|
| SucB_Actino |
TIGR02927 |
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model ... |
13-494 |
4.39e-51 |
|
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: 183.29 E-value: 4.39e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751461977 13 KMPDVGEGLTEAEILKWYVQPGDTVTDGQVVCEVETAKAAVELPIPYDGVVRALHFPEGTTVDVGTSIIAVDVSGGAAPE 92
Cdd:TIGR02927 6 KMPALGESVTEGTVTSWLKAVGDTVEADEPLLEVSTDKVDTEIPSPAAGVLLEIRAPEDDTVEVGGVLAIIGEPGEAGSE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751461977 93 PEAPAAAEAVPAAAAPAPAVAVPAEQ-PAEAEPAAVGSGR--------------------------------QPVL---- 135
Cdd:TIGR02927 86 PAPAAPEPEAAPEPEAPAPAPTPAAEaPAPAAPQAGGSGEatevkmpelgesvtegtvtswlkavgdtvevdEPLLevst 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751461977 136 ----------------------------------VGYGVSTSATRRRPR---------KPAPDGFARQTLEGDRTELNGH 172
Cdd:TIGR02927 166 dkvdteipspvagtlleirapeddtvevgtvlaiIGDANAAPAEPAEEEapapseagsEPAPDPAARAPHAAPDPPAPAP 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751461977 173 AQATPTAPAPAAPVAGALR-PLAKPPVRKLAKDLGVDLATVTATGPDGIVTREDVHAAVAAEPKTSEepaavpAPVAPPA 251
Cdd:TIGR02927 246 APAKTAAPAAAAPVSSGDSgPYVTPLVRKLAKDKGVDLSTVKGTGVGGRIRKQDVLAAAKAAEEARA------AAAAPAA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751461977 252 PTAAATPVTASAPVSYDTA--RETRIPVKGVRKATAAAMVGSAFTAPHVTEFVTVDVTRTMKLVEELKQD-KEFTGLRVN 328
Cdd:TIGR02927 320 AAAPAAPAAAAKPAEPDTAklRGTTQKMNRIRQITADKTIESLQTSAQLTQVHEVDMTRVAALRARAKNDfLEKNGVNLT 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751461977 329 PLLLIAKALLVAIRRNPDVNASWDEAAQEIVVKHYVNLGIAAATPRGLIVPNIKDAHAKTLPQLAESLGELVSTARDGKT 408
Cdd:TIGR02927 400 FLPFFVQAVTEALKAHPNVNASYNAETKEVTYHDVEHVGIAVDTPRGLLVPVIHNAGDLSLPGLAKAINDLAARARDNKL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751461977 409 SPSAMQAGTVTITNVGVFGVDTGTPILNPGESAILAVGAIKLQPWVHKGK-----VKPRQVTTLALSFDHRLVDGELGSR 483
Cdd:TIGR02927 480 KPDELSGGTFTITNIGSGGALFDTPILNPPQAAILGTGAIVKRPRVIKDEdggesIAIRSVCYLPLTYDHRLVDGADAGR 559
|
570
....*....|.
gi 1751461977 484 VLADVAAILEQ 494
Cdd:TIGR02927 560 FLTTIKKRLEE 570
|
|
| PRK11857 |
PRK11857 |
dihydrolipoamide acetyltransferase; Reviewed |
193-498 |
9.10e-48 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237002 [Multi-domain] Cd Length: 306 Bit Score: 167.28 E-value: 9.10e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751461977 193 LAKPPVRKLAKDLGVDLATVTATGPDGIVTREDVHaavaaepKTSEEPAAVPAPVAPPAPTAAATPVTASAPVSYDTARE 272
Cdd:PRK11857 3 LATPIARALAKKLGIDISLLKGSGRDGKILAEDVE-------NFIKSLKSAPTPAEAASVSSAQQAAKTAAPAAAPPKLE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751461977 273 TRI-PVKGVRKATAAAMVGSAFTAPHVTEFVTVDVTRTMKLVEELKQD-KEFTGLRVNPLLLIAKALLVAIRRNPDVNAS 350
Cdd:PRK11857 76 GKReKVAPIRKAIARAMTNSWSNVAYVNLVNEIDMTKLWDLRKSVKDPvLKTEGVKLTFLPFIAKAILIALKEFPIFAAK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751461977 351 WDEAAQEIVVKHYVNLGIAAATPRGLIVPNIKDAHAKTLPQLAESLGELVSTARDGKTSPSAMQAGTVTITNVGVFGVDT 430
Cdd:PRK11857 156 YDEATSELVYPDTLNLGIAVDTEAGLMVPVIKNAQKLSIVEIAKEISRLAKAARERKIKPDEMKGGSFTITNYGSVGSLY 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1751461977 431 GTPILNPGESAILAVGAIKLQPWVHKGKVKPRQVTTLALSFDHRLVDGELGSRVLADVAAILEQPKRL 498
Cdd:PRK11857 236 GVPVINYPELAIAGVGAIIDKAIVKNGQIVAGKVMHLTVAADHRWIDGATIGRFASRVKELLEKPEIL 303
|
|
| PLN02744 |
PLN02744 |
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex |
8-499 |
6.79e-47 |
|
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
Pssm-ID: 215397 [Multi-domain] Cd Length: 539 Bit Score: 170.80 E-value: 6.79e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751461977 8 PVREFKMPDVGEGLTEAEILKWYVQPGDTVTDGQVVCEVETAKAAVELPIPYDGVVRALHFPEGTT-VDVGtSIIAVDVS 86
Cdd:PLN02744 111 PHQEIGMPSLSPTMTEGNIARWLKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVKGDGAKeIKVG-EVIAITVE 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751461977 87 ggaapepEAPAAAEAVPAAAAPAPAVAVPAEQPAEAEPAaVGSGRQPvlvgygvSTSATRRRPRKPAPdgfarqTLEGDR 166
Cdd:PLN02744 190 -------EEEDIGKFKDYKPSSSAAPAAPKAKPSPPPPK-EEEVEKP-------ASSPEPKASKPSAP------PSSGDR 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751461977 167 TelnghaqatptapapaapvagalrpLAKPPVRKLAKDLGVDLATVTATGPDGIVTREDVHAAVAAEPKtseepaavpap 246
Cdd:PLN02744 249 I-------------------------FASPLARKLAEDNNVPLSSIKGTGPDGRIVKADIEDYLASGGK----------- 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751461977 247 vappAPTAAATPVTASAPVSYdtareTRIPVKGVRKATAAAMVGSAFTAPHVteFVTVD--VTRTMKLVEELKQDKEFTG 324
Cdd:PLN02744 293 ----GATAPPSTDSKAPALDY-----TDIPNTQIRKVTASRLLQSKQTIPHY--YLTVDtrVDKLMALRSQLNSLQEASG 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751461977 325 ---LRVNPLLLIAKALlvAIRRNPDVNASW-DEAAQEIvvkHYVNLGIAAATPRGLIVPNIKDAHAKTLPQLAESLGELV 400
Cdd:PLN02744 362 gkkISVNDLVIKAAAL--ALRKVPQCNSSWtDDYIRQY---HNVNINVAVQTENGLYVPVVKDADKKGLSTIAEEVKQLA 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751461977 401 STARDGKTSPSAMQAGTVTITNV-GVFGVDTGTPILNPGESAILAVGAI--KLQPWVHKGKVKPRQVTTLALSFDHRLVD 477
Cdd:PLN02744 437 QKARENSLKPEDYEGGTFTVSNLgGPFGIKQFCAIINPPQSAILAVGSAekRVIPGSGPDQYNFASFMSVTLSCDHRVID 516
|
490 500
....*....|....*....|..
gi 1751461977 478 GELGSRVLADVAAILEQPKRLI 499
Cdd:PLN02744 517 GAIGAEWLKAFKGYIENPESML 538
|
|
| PRK14843 |
PRK14843 |
dihydrolipoamide acetyltransferase; Provisional |
194-495 |
4.33e-42 |
|
dihydrolipoamide acetyltransferase; Provisional
Pssm-ID: 184847 [Multi-domain] Cd Length: 347 Bit Score: 153.52 E-value: 4.33e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751461977 194 AKPPVRKLAKDLGVDLATVTATGPDGIVTREDV---------------------HAAVAAEPKTSEEPAAVPAPVAPPAP 252
Cdd:PRK14843 8 ATPAARKLADDLGINLYDVSGSGANGRVHKEDVetykdtnvvrisplakrialeHNIAWQEIQGTGHRGKIMKKDVLALL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751461977 253 TAAATPVTASAPVSYDTARET-----------RIPVKGVRKATAAAMVGSAFTAPHVTEFVTVDVTRTMKLVEE-LKQDK 320
Cdd:PRK14843 88 PENIENDSIKSPAQIEKVEEVpdnvtpygeieRIPMTPMRKVIAQRMVESYLTAPTFTLNYEVDMTEMLALRKKvLEPIM 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751461977 321 EFTGLRVNPLLLIAKALLVAIRRNPDVNASWDEAAQEIVVKHYVNLGIAAATPRGLIVPNIKDAHAKTLPQLAESLGELV 400
Cdd:PRK14843 168 EATGKKTTVTDLLSLAVVKTLMKHPYINASLTEDGKTIITHNYVNLAMAVGMDNGLMTPVVYNAEKMSLSELVVAFKDVI 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751461977 401 STARDGKTSPSAMQAGTVTITNVGVFGVDTGTPILNPGESAILAVGAIKLQPWVHKGKVKPRQVTTLALSFDHRLVDGEL 480
Cdd:PRK14843 248 GRTLDGKLAPSELQNSTFTISNLGMFGVQSFGPIINQPNSAILGVSSTIEKPVVVNGEIVIRPIMSLGLTIDHRVVDGMA 327
|
330
....*....|....*
gi 1751461977 481 GSRVLADVAAILEQP 495
Cdd:PRK14843 328 GAKFMKDLKELIETP 342
|
|
| PLN02226 |
PLN02226 |
2-oxoglutarate dehydrogenase E2 component |
271-499 |
2.21e-34 |
|
2-oxoglutarate dehydrogenase E2 component
Pssm-ID: 177871 [Multi-domain] Cd Length: 463 Bit Score: 134.88 E-value: 2.21e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751461977 271 RETRIPVKGVRKATAAAMVGSAFTAPHVTEFVTVDVTRTMKLVEELKQD-KEFTGLRVNPLLLIAKALLVAIRRNPDVNA 349
Cdd:PLN02226 233 RERRVPMTRLRKRVATRLKDSQNTFALLTTFNEVDMTNLMKLRSQYKDAfYEKHGVKLGLMSGFIKAAVSALQHQPVVNA 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751461977 350 SWDeaAQEIVVKHYVNLGIAAATPRGLIVPNIKDAHAKTLPQLAESLGELVSTARDGKTSPSAMQAGTVTITNVGVFGVD 429
Cdd:PLN02226 313 VID--GDDIIYRDYVDISIAVGTSKGLVVPVIRGADKMNFAEIEKTINGLAKKANEGTISIDEMAGGSFTVSNGGVYGSL 390
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751461977 430 TGTPILNPGESAILAVGAIKLQPWVHKGKVKPRQVTTLALSFDHRLVDGELGSRVLADVAAILEQPKRLI 499
Cdd:PLN02226 391 ISTPIINPPQSAILGMHSIVSRPMVVGGSVVPRPMMYVALTYDHRLIDGREAVYFLRRVKDVVEDPQRLL 460
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
11-83 |
3.73e-26 |
|
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: 101.30 E-value: 3.73e-26
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1751461977 11 EFKMPDVGEGLTEAEILKWYVQPGDTVTDGQVVCEVETAKAAVELPIPYDGVVRALHFPEGTTVDVGTsIIAV 83
Cdd:COG0508 4 EIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGA-VIAV 75
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
11-83 |
7.03e-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: 100.56 E-value: 7.03e-26
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1751461977 11 EFKMPDVGEGLTEAEILKWYVQPGDTVTDGQVVCEVETAKAAVELPIPYDGVVRALHFPEGTTVDVGTsIIAV 83
Cdd:cd06849 2 EIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQ-VIAV 73
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
11-81 |
8.32e-18 |
|
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: 77.64 E-value: 8.32e-18
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1751461977 11 EFKMPDVGEGLTEAeILKWYVQPGDTVTDGQVVCEVETAKAAVELPIPYDGVVRALHFPEGTTVDVGTSII 81
Cdd:pfam00364 2 EIKSPMIGESVREG-VVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLA 71
|
|
| kgd |
PRK12270 |
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ... |
210-478 |
5.79e-15 |
|
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;
Pssm-ID: 237030 [Multi-domain] Cd Length: 1228 Bit Score: 78.01 E-value: 5.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751461977 210 ATVTATGPDGIVTREDVHAAVAAEPKTSEEPAAVPAPVAPPAPTAAATPVTASAPVSY----DTARETRIPVKGVRKATA 285
Cdd:PRK12270 49 AAAAAAASAPAAAPAAKAPAAPAPAPPAAAAPAAPPKPAAAAAAAAAPAAPPAAAAAAapaaAAVEDEVTPLRGAAAAVA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751461977 286 AAMVGSaFTAPHVTEFVTVdvtrTMKLVEE--------LKQDKeftGLRVNPLLLIAKALLVAIRRNPDVNASWDEAA-- 355
Cdd:PRK12270 129 KNMDAS-LEVPTATSVRAV----PAKLLIDnrivinnhLKRTR---GGKVSFTHLIGYALVQALKAFPNMNRHYAEVDgk 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751461977 356 QEIVVKHYVNLGIAAATP-----RGLIVPNIKDAHAKTLPQLAESLGELVSTARDGKTSPSAMQAGTVTITNVGVFGVDT 430
Cdd:PRK12270 201 PTLVTPAHVNLGLAIDLPkkdgsRQLVVPAIKGAETMDFAQFWAAYEDIVRRARDGKLTADDFQGTTISLTNPGGIGTVH 280
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1751461977 431 GTPILNPGESAILAVGAIKLqPWVHKGKVKPR-------QVTTLALSFDHRLVDG 478
Cdd:PRK12270 281 SVPRLMKGQGAIIGVGAMEY-PAEFQGASEERlaelgisKVMTLTSTYDHRIIQG 334
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
8-80 |
2.29e-12 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 68.43 E-value: 2.29e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1751461977 8 PVREFKMPDVGEGLTEAEILKWYVQPGDTVTDGQVVCEVETAKAAVELPIPYDGVVRALHFPEGTTVDVGTSI 80
Cdd:PRK14875 1 SITPITMPKWGLSMTEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGETLPVGALL 73
|
|
| E3_binding |
pfam02817 |
e3 binding domain; This family represents a small domain of the E2 subunit of 2-oxo-acid ... |
192-226 |
4.76e-12 |
|
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: 60.39 E-value: 4.76e-12
10 20 30
....*....|....*....|....*....|....*
gi 1751461977 192 PLAKPPVRKLAKDLGVDLATVTATGPDGIVTREDV 226
Cdd:pfam02817 1 VLASPAARKLARELGIDLSDVKGTGPGGRITKEDV 35
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
15-81 |
8.53e-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: 55.14 E-value: 8.53e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1751461977 15 PDVGEGLTEAEILKWYVQPGDTVTDGQVVCEVETAKAAVELPIPYDGVVRALHFPEGTTVDVGTSII 81
Cdd:cd06663 5 PDLAQHLGDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKVEGDTPLV 71
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
26-83 |
1.61e-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: 1.61e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751461977 26 ILKWYVQPGDTVTDGQVVCEVETAKaaVELPI--PYDGVVRALHFPEGTTVDVGTSIIAV 83
Cdd:cd06850 10 VVKVLVKEGDKVEAGQPLAVLEAMK--MENEVtaPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
11-127 |
9.86e-07 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 51.07 E-value: 9.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751461977 11 EFKMPDVGEGLTEAEILKWYVQPGDTVTDGQVVCEVETAKAAVELPIPYDGVVRALHFPEGTT-VDVGTsIIAV------ 83
Cdd:PRK11892 4 EILMPALSPTMEEGTLAKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKILVPEGTEgVKVNT-PIAVlleege 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1751461977 84 DVSGGAAPEPEAPAAAEAVPAAAAPAPAVAVPAEQPAEAEPAAV 127
Cdd:PRK11892 83 SASDAGAAPAAAAEAAAAAPAAAAAAAAKKAAPAPAAPAAPAAE 126
|
|
| PRK05641 |
PRK05641 |
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
15-81 |
5.87e-06 |
|
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235540 [Multi-domain] Cd Length: 153 Bit Score: 46.39 E-value: 5.87e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1751461977 15 PDVGEGLTEA----EILKWYVQPGDTVTDGQVVCEVETAKAAVELPIPYDGVVRALHFPEGTTVDVGTSII 81
Cdd:PRK05641 80 ASAGENVVTApmpgKILRILVREGQQVKVGQGLLILEAMKMENEIPAPKDGVVKKILVKEGDTVDTGQPLI 150
|
|
| PRK09282 |
PRK09282 |
pyruvate carboxylase subunit B; Validated |
26-83 |
1.74e-05 |
|
pyruvate carboxylase subunit B; Validated
Pssm-ID: 236449 [Multi-domain] Cd Length: 592 Bit Score: 47.53 E-value: 1.74e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1751461977 26 ILKWYVQPGDTVTDGQVVCEVETAKAAVELPIPYDGVVRALHFPEGTTVDVGTSIIAV 83
Cdd:PRK09282 533 VVKVKVKEGDKVKAGDTVLVLEAMKMENEIQAPVDGTVKEILVKEGDRVNPGDVLMEI 590
|
|
| AccB |
COG0511 |
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ... |
30-84 |
2.42e-05 |
|
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: 44.12 E-value: 2.42e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1751461977 30 YVQPGDTVTDGQVVCEVETAKAAVELPIPYDGVVRALHFPEGTTVDVGTSIIAVD 84
Cdd:COG0511 82 FVKVGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVVEILVENGQPVEYGQPLFVIE 136
|
|
| PRK14040 |
PRK14040 |
oxaloacetate decarboxylase subunit alpha; |
26-83 |
4.29e-05 |
|
oxaloacetate decarboxylase subunit alpha;
Pssm-ID: 237592 [Multi-domain] Cd Length: 593 Bit Score: 46.08 E-value: 4.29e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1751461977 26 ILKWYVQPGDTVTDGQVVCEVETAKAAVELPIPYDGVVRALHFPEGTTVDVGTSIIAV 83
Cdd:PRK14040 535 IFKVIVTEGQTVAEGDVLLILEAMKMETEIRAAQAGTVRGIAVKEGDAVAVGDTLLTL 592
|
|
| PRK08225 |
PRK08225 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
28-77 |
1.15e-03 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 181304 [Multi-domain] Cd Length: 70 Bit Score: 37.46 E-value: 1.15e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1751461977 28 KWYVQPGDTVTDGQVVCEVETAKaaVELPIPYD--GVVRALHFPEGTTVDVG 77
Cdd:PRK08225 14 KIVVKVGDTVEEGQDVVILESMK--MEIPIVAEeaGTVKKINVQEGDFVNEG 63
|
|
| GcvH |
COG0509 |
Glycine cleavage system protein H (lipoate-binding) [Amino acid transport and metabolism]; ... |
32-63 |
2.12e-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: 38.18 E-value: 2.12e-03
10 20 30
....*....|....*....|....*....|..
gi 1751461977 32 QPGDTVTDGQVVCEVETAKAAVELPIPYDGVV 63
Cdd:COG0509 46 EVGTEVEAGEPFGVVESVKAVSDLYAPVSGEV 77
|
|
| |
