|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02528 |
PLN02528 |
2-oxoisovalerate dehydrogenase E2 component |
66-495 |
1.58e-170 |
|
2-oxoisovalerate dehydrogenase E2 component
Pssm-ID: 215289 [Multi-domain] Cd Length: 416 Bit Score: 486.92 E-value: 1.58e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185134993 66 FKLSDIGEGIMEVTVKEWYVKEGDKVSQFDSICEVQSDKASVTITSRYDGVIKKLYYEVDATALVGTPLVDIETEPGPEV 145
Cdd:PLN02528 1 VPLAQTGEGIAECELLRWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGKVAQINFSPGDIVKVGETLLKIMVEDSQHL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185134993 146 VHEEDVVETPAMSNDEHTHQEIKGHKT---QATPAVRRLAMENNIKLSEVVGTGRDGRILKEDILNFLAkQTGAILPPTP 222
Cdd:PLN02528 81 RSDSLLLPTDSSNIVSLAESDERGSNLsgvLSTPAVRHLAKQYGIDLNDILGTGKDGRVLKEDVLKYAA-QKGVVKDSSS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185134993 223 FHEiqppppaASAPSSASMPKMKPTPSVQLpvvsrpvftGKDSTEPLKGFHKAMVKTMTAALKIPHFGYKDEVDLTRLVQ 302
Cdd:PLN02528 160 AEE-------ATIAEQEEFSTSVSTPTEQS---------YEDKTIPLRGFQRAMVKTMTAAAKVPHFHYVEEINVDALVE 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185134993 303 LRKELKGLSEARGVKLSYMPFFIKAASLGLLHFPILNASVDEAVQNITYKASHNIGLAMDTSQGLLVPNVKNVQLLSVFE 382
Cdd:PLN02528 224 LKASFQENNTDPTVKHTFLPFLIKSLSMALSKYPLLNSCFNEETSEIRLKGSHNIGVAMATEHGLVVPNIKNVQSLSLLE 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185134993 383 IAVELNRMQTLGATGQLGTADLTGGTFTLSNIGSIGGTYAKPVILPPEVAIGALGKIQVLPRFNSRDEVVKAHVMNVSWS 462
Cdd:PLN02528 304 ITKELSRLQHLAAENKLNPEDITGGTITLSNIGAIGGKFGSPVLNLPEVAIIALGRIQKVPRFVDDGNVYPASIMTVTIG 383
|
410 420 430
....*....|....*....|....*....|...
gi 185134993 463 ADHRIIDGATMARFSNLWRDYLENPASMVLDLK 495
Cdd:PLN02528 384 ADHRVLDGATVARFCNEWKSYVEKPELLMLHMR 416
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
280-490 |
2.16e-93 |
|
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: 282.51 E-value: 2.16e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185134993 280 MTAAL-KIPHFGYKDEVDLTRLVQLRKELKGLSEARGVKLSYMPFFIKAASLGLLHFPILNASVDEAVQNITYKASHNIG 358
Cdd:pfam00198 1 MTESKqTIPHFTLTDEVDVTELLALREELKEDAADEETKLTFLPFLVKAVALALKKFPELNASWDGEEGEIVYKKYVNIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185134993 359 LAMDTSQGLLVPNVKNVQLLSVFEIAVELNRMQTLGATGQLGTADLTGGTFTLSNIGSIGGTYAKPVILPPEVAIGALGK 438
Cdd:pfam00198 81 IAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVGR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 185134993 439 IQVLPRFNsRDEVVKAHVMNVSWSADHRIIDGATMARFSNLWRDYLENPASM 490
Cdd:pfam00198 161 IRKRPVVV-DGEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELL 211
|
|
| sucB |
TIGR01347 |
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ... |
67-494 |
2.65e-71 |
|
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: 232.32 E-value: 2.65e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185134993 67 KLSDIGEGIMEVTVKEWYVKEGDKVSQFDSICEVQSDKASVTITSRYDGVIKKLYYEVDATALVGTPLVDIE--TEPGPE 144
Cdd:TIGR01347 4 KVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAILEegNDATAA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185134993 145 VVHEEDVVETPAMSNDEHTHQEIKGHKTQATPAVRRLAMENNIKLSEVVGTGRDGRILKEDILNFLAKQTGAiLPPTPFH 224
Cdd:TIGR01347 84 PPAKSGEEKEETPAASAAAAPTAAANRPSLSPAARRLAKEHGIDLSAVPGTGVTGRVTKEDIIKKTEAPASA-QPPAAAA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185134993 225 EIQPPPPAASAPSSASMPKMKPTpsvqlpvVSRPVFTGKDSTEPLKGFHkamvktmtaalkiphfgykdEVDLTRLVQLR 304
Cdd:TIGR01347 163 AAAAPAAATRPEERVKMTRLRQR-------IAERLKEAQNSTAMLTTFN--------------------EVDMSAVMELR 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185134993 305 KELKGLSEAR-GVKLSYMPFFIKAASLGLLHFPILNASVDEavQNITYKASHNIGLAMDTSQGLLVPNVKNVQLLSVFEI 383
Cdd:TIGR01347 216 KRYKEEFEKKhGVKLGFMSFFVKAVVAALKRFPEVNAEIDG--DDIVYKDYYDISVAVSTDRGLVVPVVRNADRMSFADI 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185134993 384 AVELNRMQTLGATGQLGTADLTGGTFTLSNIGSIGGTYAKPVILPPEVAIGALGKIQVLPrFNSRDEVVKAHVMNVSWSA 463
Cdd:TIGR01347 294 EKEIADLGKKARDGKLTLEDMTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHGIKERP-VAVNGQIEIRPMMYLALSY 372
|
410 420 430
....*....|....*....|....*....|.
gi 185134993 464 DHRIIDGATMARFSNLWRDYLENPASMVLDL 494
Cdd:TIGR01347 373 DHRLIDGKEAVTFLVTIKELLEDPRRLLLDL 403
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
65-137 |
2.48e-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: 101.71 E-value: 2.48e-26
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 185134993 65 PFKLSDIGEGIMEVTVKEWYVKEGDKVSQFDSICEVQSDKASVTITSRYDGVIKKLYYEVDATALVGTPLVDI 137
Cdd:cd06849 2 EIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
66-137 |
3.41e-22 |
|
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: 90.13 E-value: 3.41e-22
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 185134993 66 FKLSDIGEGIMEVTVKEWYVKEGDKVSQFDSICEVQSDKASVTITSRYDGVIKKLYYEVDATALVGTPLVDI 137
Cdd:COG0508 5 IKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02528 |
PLN02528 |
2-oxoisovalerate dehydrogenase E2 component |
66-495 |
1.58e-170 |
|
2-oxoisovalerate dehydrogenase E2 component
Pssm-ID: 215289 [Multi-domain] Cd Length: 416 Bit Score: 486.92 E-value: 1.58e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185134993 66 FKLSDIGEGIMEVTVKEWYVKEGDKVSQFDSICEVQSDKASVTITSRYDGVIKKLYYEVDATALVGTPLVDIETEPGPEV 145
Cdd:PLN02528 1 VPLAQTGEGIAECELLRWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGKVAQINFSPGDIVKVGETLLKIMVEDSQHL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185134993 146 VHEEDVVETPAMSNDEHTHQEIKGHKT---QATPAVRRLAMENNIKLSEVVGTGRDGRILKEDILNFLAkQTGAILPPTP 222
Cdd:PLN02528 81 RSDSLLLPTDSSNIVSLAESDERGSNLsgvLSTPAVRHLAKQYGIDLNDILGTGKDGRVLKEDVLKYAA-QKGVVKDSSS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185134993 223 FHEiqppppaASAPSSASMPKMKPTPSVQLpvvsrpvftGKDSTEPLKGFHKAMVKTMTAALKIPHFGYKDEVDLTRLVQ 302
Cdd:PLN02528 160 AEE-------ATIAEQEEFSTSVSTPTEQS---------YEDKTIPLRGFQRAMVKTMTAAAKVPHFHYVEEINVDALVE 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185134993 303 LRKELKGLSEARGVKLSYMPFFIKAASLGLLHFPILNASVDEAVQNITYKASHNIGLAMDTSQGLLVPNVKNVQLLSVFE 382
Cdd:PLN02528 224 LKASFQENNTDPTVKHTFLPFLIKSLSMALSKYPLLNSCFNEETSEIRLKGSHNIGVAMATEHGLVVPNIKNVQSLSLLE 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185134993 383 IAVELNRMQTLGATGQLGTADLTGGTFTLSNIGSIGGTYAKPVILPPEVAIGALGKIQVLPRFNSRDEVVKAHVMNVSWS 462
Cdd:PLN02528 304 ITKELSRLQHLAAENKLNPEDITGGTITLSNIGAIGGKFGSPVLNLPEVAIIALGRIQKVPRFVDDGNVYPASIMTVTIG 383
|
410 420 430
....*....|....*....|....*....|...
gi 185134993 463 ADHRIIDGATMARFSNLWRDYLENPASMVLDLK 495
Cdd:PLN02528 384 ADHRVLDGATVARFCNEWKSYVEKPELLMLHMR 416
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
60-492 |
1.05e-149 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 438.49 E-value: 1.05e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185134993 60 SGPILPFKLSDIGEgIMEVTVKEWYVKEGDKVSQFDSICEVQSDKASVTITSRYDGVIKKLYYEVDATALVGTPLVDIET 139
Cdd:PRK11855 116 GGGVVEVKVPDIGE-ITEVEVIEWLVKVGDTVEEDQSLITVETDKATMEIPSPVAGVVKEIKVKVGDKVSVGSLLVVIEV 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185134993 140 EPGPEVVHEEDVVETPA-------------MSNDEHT--HQEIKGHKTQ-ATPAVRRLAMENNIKLSEVVGTGRDGRILK 203
Cdd:PRK11855 195 AAAAPAAAAAPAAAAPAaaaaaapapapaaAAAPAAAapAAAAAPGKAPhASPAVRRLARELGVDLSQVKGTGKKGRITK 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185134993 204 EDILNFL-AKQTGAILPPTPfheiqppppaasapssasmPKMKPTPSVQLPVVSRPVFT--GKDSTEPLKGFHKAMVKTM 280
Cdd:PRK11855 275 EDVQAFVkGAMSAAAAAAAA-------------------AAAAGGGGLGLLPWPKVDFSkfGEIETKPLSRIKKISAANL 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185134993 281 TAAL-KIPHFGYKDEVDLTRLVQLRKELKGLSEARGVKLSYMPFFIKAASLGLLHFPILNASVDEAVQNITYKASHNIGL 359
Cdd:PRK11855 336 HRSWvTIPHVTQFDEADITDLEALRKQLKKEAEKAGVKLTMLPFFIKAVVAALKEFPVFNASLDEDGDELTYKKYFNIGF 415
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185134993 360 AMDTSQGLLVPNVKNVQLLSVFEIAVELNRMQTLGATGQLGTADLTGGTFTLSNIGSIGGTYAKPVILPPEVAIGALGKI 439
Cdd:PRK11855 416 AVDTPNGLVVPVIKDVDKKSLLEIAREIAELAKKARDGKLKPDDMQGGCFTISSLGGIGGTAFTPIINAPEVAILGVGKS 495
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 185134993 440 QVLPrFNSRDEVVKAHVMNVSWSADHRIIDGATMARFSNLWRDYLENPASMVL 492
Cdd:PRK11855 496 QMKP-VWDGKEFVPRLMLPLSLSYDHRVIDGATAARFTNYLKQLLADPRRMLL 547
|
|
| PRK11856 |
PRK11856 |
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed |
66-493 |
8.46e-123 |
|
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
Pssm-ID: 237001 [Multi-domain] Cd Length: 411 Bit Score: 364.88 E-value: 8.46e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185134993 66 FKLSDIGEGIMEVTVKEWYVKEGDKVSQFDSICEVQSDKASVTITSRYDGVIKKLYYEVDATALVGTPLVDIETE----- 140
Cdd:PRK11856 5 FKMPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDVVPVGSVIAVIEEEgeaea 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185134993 141 ---------PGPEVVHEEDVVETPAMSNDEHTHQEIKGHKTQATPAVRRLAMENNIKLSEVVGTGRDGRILKEDILNFLA 211
Cdd:PRK11856 85 aaaaeaapeAPAPEPAPAAAAAAAAAPAAAAAPAAPAAAAAKASPAVRKLARELGVDLSTVKGSGPGGRITKEDVEAAAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185134993 212 KQTGAilpptpfheiqppppaasapssasmpkmkPTPSVQLPVVSRPVFTGKDSTEPLKGFHKAMVKTMTAA-LKIPHFG 290
Cdd:PRK11856 165 AAAPA-----------------------------AAAAAAAAAAPPAAAAEGEERVPLSGMRKAIAKRMVESkREIPHFT 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185134993 291 YKDEVDLTRLVQLRKELKglseARGVKLSYMPFFIKAASLGLLHFPILNASVDEavQNITYKASHNIGLAMDTSQGLLVP 370
Cdd:PRK11856 216 LTDEVDVTALLALRKQLK----AIGVKLTVTDFLIKAVALALKKFPELNASWDD--DAIVLKKYVNIGIAVATDGGLIVP 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185134993 371 NVKNVQLLSVFEIAVELNRMQTLGATGQLGTADLTGGTFTLSNIGSIGGTYAKPVILPPEVAIGALGKIQVLPRFNsRDE 450
Cdd:PRK11856 290 VIRDADKKSLFELAREIKDLAEKAREGKLKPEELQGGTFTISNLGMFGGDYFTPIINPPEVAILGVGAIVERPVVV-DGE 368
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 185134993 451 VVKAHVMNVSWSADHRIIDGATMARFSNLWRDYLENPASMVLD 493
Cdd:PRK11856 369 IVVRKVMPLSLSFDHRVIDGADAARFLKALKELLENPALLLLE 411
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
280-490 |
2.16e-93 |
|
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: 282.51 E-value: 2.16e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185134993 280 MTAAL-KIPHFGYKDEVDLTRLVQLRKELKGLSEARGVKLSYMPFFIKAASLGLLHFPILNASVDEAVQNITYKASHNIG 358
Cdd:pfam00198 1 MTESKqTIPHFTLTDEVDVTELLALREELKEDAADEETKLTFLPFLVKAVALALKKFPELNASWDGEEGEIVYKKYVNIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185134993 359 LAMDTSQGLLVPNVKNVQLLSVFEIAVELNRMQTLGATGQLGTADLTGGTFTLSNIGSIGGTYAKPVILPPEVAIGALGK 438
Cdd:pfam00198 81 IAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVGR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 185134993 439 IQVLPRFNsRDEVVKAHVMNVSWSADHRIIDGATMARFSNLWRDYLENPASM 490
Cdd:pfam00198 161 IRKRPVVV-DGEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELL 211
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
70-492 |
3.21e-82 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 267.25 E-value: 3.21e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185134993 70 DIGEGimEVTVKEWYVKEGDKVSQFDSICEVQSDKASVTITSRYDGVIKKLYYEVDATALVGTPLVDIETE--------- 140
Cdd:PRK11854 213 DIGGD--EVEVTEVMVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVKTGSLIMRFEVEgaapaaapa 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185134993 141 ------PGPEVVHEEDVVETPAMSNDEHTHQEIKGHKTQATPAVRRLAMENNIKLSEVVGTGRDGRILKEDILNFL---- 210
Cdd:PRK11854 291 kqeaaaPAPAAAKAEAPAAAPAAKAEGKSEFAENDAYVHATPLVRRLAREFGVNLAKVKGTGRKGRILKEDVQAYVkdav 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185134993 211 -AKQTGAILPPTPfheiqppppaasapssASMPKMKPTPSVQlpvvsrPVFTGKDSTEPLKGFHKAMVKTMTAAL-KIPH 288
Cdd:PRK11854 371 kRAEAAPAAAAAG----------------GGGPGLLPWPKVD------FSKFGEIEEVELGRIQKISGANLHRNWvMIPH 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185134993 289 FGYKDEVDLTRLVQLRKELKGLSEAR--GVKLSYMPFFIKAASLGLLHFPILNASVDEAVQNITYKASHNIGLAMDTSQG 366
Cdd:PRK11854 429 VTQFDKADITELEAFRKQQNAEAEKRklGVKITPLVFIMKAVAAALEQMPRFNSSLSEDGQRLTLKKYVNIGIAVDTPNG 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185134993 367 LLVPNVKNVQLLSVFEIAVELNRMQTLGATGQLGTADLTGGTFTLSNIGSIGGTYAKPVILPPEVAIGALGKIQVLPRFN 446
Cdd:PRK11854 509 LVVPVFKDVNKKGIIELSRELMDISKKARDGKLTAGDMQGGCFTISSIGGLGTTHFTPIVNAPEVAILGVSKSAMEPVWN 588
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 185134993 447 SrDEVVKAHVMNVSWSADHRIIDGATMARFSNLWRDYLENPASMVL 492
Cdd:PRK11854 589 G-KEFAPRLMLPLSLSYDHRVIDGADGARFITIINDRLSDIRRLVL 633
|
|
| sucB |
TIGR01347 |
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ... |
67-494 |
2.65e-71 |
|
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: 232.32 E-value: 2.65e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185134993 67 KLSDIGEGIMEVTVKEWYVKEGDKVSQFDSICEVQSDKASVTITSRYDGVIKKLYYEVDATALVGTPLVDIE--TEPGPE 144
Cdd:TIGR01347 4 KVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAILEegNDATAA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185134993 145 VVHEEDVVETPAMSNDEHTHQEIKGHKTQATPAVRRLAMENNIKLSEVVGTGRDGRILKEDILNFLAKQTGAiLPPTPFH 224
Cdd:TIGR01347 84 PPAKSGEEKEETPAASAAAAPTAAANRPSLSPAARRLAKEHGIDLSAVPGTGVTGRVTKEDIIKKTEAPASA-QPPAAAA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185134993 225 EIQPPPPAASAPSSASMPKMKPTpsvqlpvVSRPVFTGKDSTEPLKGFHkamvktmtaalkiphfgykdEVDLTRLVQLR 304
Cdd:TIGR01347 163 AAAAPAAATRPEERVKMTRLRQR-------IAERLKEAQNSTAMLTTFN--------------------EVDMSAVMELR 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185134993 305 KELKGLSEAR-GVKLSYMPFFIKAASLGLLHFPILNASVDEavQNITYKASHNIGLAMDTSQGLLVPNVKNVQLLSVFEI 383
Cdd:TIGR01347 216 KRYKEEFEKKhGVKLGFMSFFVKAVVAALKRFPEVNAEIDG--DDIVYKDYYDISVAVSTDRGLVVPVVRNADRMSFADI 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185134993 384 AVELNRMQTLGATGQLGTADLTGGTFTLSNIGSIGGTYAKPVILPPEVAIGALGKIQVLPrFNSRDEVVKAHVMNVSWSA 463
Cdd:TIGR01347 294 EKEIADLGKKARDGKLTLEDMTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHGIKERP-VAVNGQIEIRPMMYLALSY 372
|
410 420 430
....*....|....*....|....*....|.
gi 185134993 464 DHRIIDGATMARFSNLWRDYLENPASMVLDL 494
Cdd:TIGR01347 373 DHRLIDGKEAVTFLVTIKELLEDPRRLLLDL 403
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
60-492 |
6.15e-69 |
|
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: 230.15 E-value: 6.15e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185134993 60 SGPILPFKLSDIGeGIMEVTVKEWYVKEGDKVSQFDSICEVQSDKASVTITSRYDGVIKKLYYEVDATALVG-------- 131
Cdd:TIGR01348 113 SSGVQEVTVPDIG-DIEKVTVIEVLVKVGDTVSADQSLITLESDKASMEVPAPASGVVKSVKVKVGDSVPTGdliltlsv 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185134993 132 ---TPLVDIETEPGPEVVHEEDVVETPAMSNDEHTHQEIK---GHKTQ-------ATPAVRRLAMENNIKLSEVVGTGRD 198
Cdd:TIGR01348 192 agsTPATAPAPASAQPAAQSPAATQPEPAAAPAAAKAQAPapqQAGTQnpakvdhAAPAVRRLAREFGVDLSAVKGTGIK 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185134993 199 GRILKEDILNFLAKQTGailpptpfheiqpPPPAASAPSSASMPKMKPTPSVQlpvvsrpvFT--GKDSTEPLKGFHKAM 276
Cdd:TIGR01348 272 GRILREDVQRFVKEPSV-------------RAQAAAASAAGGAPGALPWPNVD--------FSkfGEVEEVDMSRIRKIS 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185134993 277 VKTMTAA-LKIPHFGYKDEVDLTRLVQLRKELKGLSEARGVKLSYMPFFIKAASLGLLHFPILNASVDEAVQNITYKASH 355
Cdd:TIGR01348 331 GANLTRNwTMIPHVTHFDKADITEMEAFRKQQNAAVEKEGVKLTVLHILMKAVAAALKKFPKFNASLDLGGEQLILKKYV 410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185134993 356 NIGLAMDTSQGLLVPNVKNVQLLSVFEIAVELNRMQTLGATGQLGTADLTGGTFTLSNIGSIGGTYAKPVILPPEVAIGA 435
Cdd:TIGR01348 411 NIGVAVDTPNGLLVPVIKDVDRKGITELALELSDLAKKARDGKLTPDEMQGACFTISSLGGIGGTAFTPIVNAPEVAILG 490
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 185134993 436 LGKIQVLPRFNSRdEVVKAHVMNVSWSADHRIIDGATMARFSNLWRDYLENPASMVL 492
Cdd:TIGR01348 491 VSKSGMEPVWNGK-EFEPRLMLPLSLSYDHRVIDGADAARFTTYICESLADIRRLLL 546
|
|
| PRK05704 |
PRK05704 |
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase; |
67-494 |
1.35e-66 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
Pssm-ID: 235571 [Multi-domain] Cd Length: 407 Bit Score: 219.71 E-value: 1.35e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185134993 67 KLSDIGEGIMEVTVKEWYVKEGDKVSQFDSICEVQSDKASVTITSRYDGVIKKLYYEVDATALVGTPLVDIET--EPGPE 144
Cdd:PRK05704 6 KVPTLPESVTEATIATWHKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGDTVTVGQVLGRIDEgaAAGAA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185134993 145 VVHEEDVVETPAMSNDEHTHQEIKGHKTQATPAVRRLAMENNIKLSEVVGTGRDGRILKEDILNFLAKQTGAILPPTPfh 224
Cdd:PRK05704 86 AAAAAAAAAAAAAPAQAQAAAAAEQSNDALSPAARKLAAENGLDASAVKGTGKGGRVTKEDVLAALAAAAAAPAAPAA-- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185134993 225 eiqppppaasapssaSMPKMKPTPSVQLPV-----------VSRPVFTGKDSTeplkgfhkAMVKTmtaalkiphFgykD 293
Cdd:PRK05704 164 ---------------AAPAAAPAPLGARPEervpmtrlrktIAERLLEAQNTT--------AMLTT---------F---N 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185134993 294 EVDLTRLVQLRKELKGLSEAR-GVKLSYMPFFIKAASLGLLHFPILNASVDEavQNITYKASHNIGLAMDTSQGLLVPNV 372
Cdd:PRK05704 209 EVDMTPVMDLRKQYKDAFEKKhGVKLGFMSFFVKAVVEALKRYPEVNASIDG--DDIVYHNYYDIGIAVGTPRGLVVPVL 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185134993 373 KNVQLLSVFEIAVELNRMQTLGATGQLGTADLTGGTFTLSNigsiGGTY----AKPVILPPEVAIgaLG--KIQVLP-RF 445
Cdd:PRK05704 287 RDADQLSFAEIEKKIAELAKKARDGKLSIEELTGGTFTITN----GGVFgslmSTPIINPPQSAI--LGmhKIKERPvAV 360
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 185134993 446 NsrDEVVKAHVMNVSWSADHRIIDGATMARFSNLWRDYLENPASMVLDL 494
Cdd:PRK05704 361 N--GQIVIRPMMYLALSYDHRIIDGKEAVGFLVTIKELLEDPERLLLDL 407
|
|
| PRK11857 |
PRK11857 |
dihydrolipoamide acetyltransferase; Reviewed |
171-487 |
1.61e-64 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237002 [Multi-domain] Cd Length: 306 Bit Score: 211.19 E-value: 1.61e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185134993 171 KTQATPAVRRLAMENNIKLSEVVGTGRDGRILKEDILNFLAKQTGAILPPTPfheiqppppaasapssASMPKMKPTPSV 250
Cdd:PRK11857 1 KILATPIARALAKKLGIDISLLKGSGRDGKILAEDVENFIKSLKSAPTPAEA----------------ASVSSAQQAAKT 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185134993 251 QLPVVSRPVFTGKdsTEPLKGFHKAMVKTMTAALK-IPHFGYKDEVDLTRLVQLRKELK-GLSEARGVKLSYMPFFIKAA 328
Cdd:PRK11857 65 AAPAAAPPKLEGK--REKVAPIRKAIARAMTNSWSnVAYVNLVNEIDMTKLWDLRKSVKdPVLKTEGVKLTFLPFIAKAI 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185134993 329 SLGLLHFPILNASVDEAVQNITYKASHNIGLAMDTSQGLLVPNVKNVQLLSVFEIAVELNRMQTLGATGQLGTADLTGGT 408
Cdd:PRK11857 143 LIALKEFPIFAAKYDEATSELVYPDTLNLGIAVDTEAGLMVPVIKNAQKLSIVEIAKEISRLAKAARERKIKPDEMKGGS 222
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 185134993 409 FTLSNIGSIGGTYAKPVILPPEVAIGALGKIQVLPRFnSRDEVVKAHVMNVSWSADHRIIDGATMARFSNLWRDYLENP 487
Cdd:PRK11857 223 FTITNYGSVGSLYGVPVINYPELAIAGVGAIIDKAIV-KNGQIVAGKVMHLTVAADHRWIDGATIGRFASRVKELLEKP 300
|
|
| SucB_Actino |
TIGR02927 |
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model ... |
60-485 |
3.01e-61 |
|
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: 210.25 E-value: 3.01e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185134993 60 SGPILPFKLSDIGEGIMEVTVKEWYVKEGDKVSQFDSICEVQSDKASVTITSRYDGVIKKLYYEVDATALVGTPLVDI-- 137
Cdd:TIGR02927 123 SGEATEVKMPELGESVTEGTVTSWLKAVGDTVEVDEPLLEVSTDKVDTEIPSPVAGTLLEIRAPEDDTVEVGTVLAIIgd 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185134993 138 -------ETEPGPEVVHEEDVVETPAMSNDEHTHQEIKGHKTQA----------------------TPAVRRLAMENNIK 188
Cdd:TIGR02927 203 anaapaePAEEEAPAPSEAGSEPAPDPAARAPHAAPDPPAPAPApaktaapaaaapvssgdsgpyvTPLVRKLAKDKGVD 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185134993 189 LSEVVGTGRDGRILKEDILNFLAKQTGAILPPTpfheiqppppaasaPSSASMPKMKPTPSVQLPVVSRPVFTGkdSTEP 268
Cdd:TIGR02927 283 LSTVKGTGVGGRIRKQDVLAAAKAAEEARAAAA--------------APAAAAAPAAPAAAAKPAEPDTAKLRG--TTQK 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185134993 269 LKGFHKAMVKTMTAALKI-PHFGYKDEVDLTRLVQLRKELKG-LSEARGVKLSYMPFFIKAASLGLLHFPILNASVDEAV 346
Cdd:TIGR02927 347 MNRIRQITADKTIESLQTsAQLTQVHEVDMTRVAALRARAKNdFLEKNGVNLTFLPFFVQAVTEALKAHPNVNASYNAET 426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185134993 347 QNITYKASHNIGLAMDTSQGLLVPNVKNVQLLSVFEIAVELNRMQTLGATGQLGTADLTGGTFTLSNIGSIGGTYAKPVI 426
Cdd:TIGR02927 427 KEVTYHDVEHVGIAVDTPRGLLVPVIHNAGDLSLPGLAKAINDLAARARDNKLKPDELSGGTFTITNIGSGGALFDTPIL 506
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 185134993 427 LPPEVAIGALGKIQVLPRF----NSRDEVVKAHVMNVSWSADHRIIDGATMARFSNLWRDYLE 485
Cdd:TIGR02927 507 NPPQAAILGTGAIVKRPRVikdeDGGESIAIRSVCYLPLTYDHRLVDGADAGRFLTTIKKRLE 569
|
|
| PTZ00144 |
PTZ00144 |
dihydrolipoamide succinyltransferase; Provisional |
49-494 |
3.09e-58 |
|
dihydrolipoamide succinyltransferase; Provisional
Pssm-ID: 240289 [Multi-domain] Cd Length: 418 Bit Score: 198.37 E-value: 3.09e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185134993 49 SSRFFHTSYvTSGPILPFKLSDIGEGIMEVTVKEWYVKEGDKVSQFDSICEVQSDKASVTITSRYDGVIKKLYYEVDATA 128
Cdd:PTZ00144 31 PACSAHFSK-SYFSIKVIKVPTMGDSISEGTVVEWKKKVGDYVKEDEVICIIETDKVSVDIRAPASGVITKIFAEEGDTV 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185134993 129 LVGTPLVDIETEPGPEVVHEEDVVETPAMSNDEH-------THQEIKGHKTQATPAVRrlamenniklsevvgtgrdgri 201
Cdd:PTZ00144 110 EVGAPLSEIDTGGAPPAAAPAAAAAAKAEKTTPEkpkaaapTPEPPAASKPTPPAAAK---------------------- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185134993 202 lkedilnflaKQTGAILPPTPFHEIQPPPPAASAPSsasMPKMKptpsvqlpvvsrpvftgKDSTEPLKGFHK--AMVKT 279
Cdd:PTZ00144 168 ----------PPEPAPAAKPPPTPVARADPRETRVP---MSRMR-----------------QRIAERLKASQNtcAMLTT 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185134993 280 MTaalkiphfgykdEVDLTRLVQLRKELK-GLSEARGVKLSYMPFFIKAASLGLLHFPILNASVDEavQNITYKASHNIG 358
Cdd:PTZ00144 218 FN------------ECDMSALMELRKEYKdDFQKKHGVKLGFMSAFVKASTIALKKMPIVNAYIDG--DEIVYRNYVDIS 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185134993 359 LAMDTSQGLLVPNVKNVQLLSVFEIAVELNRMQTLGATGQLGTADLTGGTFTLSNIGSIGGTYAKPVILPPEVAIgaLGK 438
Cdd:PTZ00144 284 VAVATPTGLVVPVIRNCENKSFAEIEKELADLAEKARNNKLTLEDMTGGTFTISNGGVFGSLMGTPIINPPQSAI--LGM 361
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 185134993 439 IQVLPRFNSR-DEVVKAHVMNVSWSADHRIIDGATMARFSNLWRDYLENPASMVLDL 494
Cdd:PTZ00144 362 HAIKKRPVVVgNEIVIRPIMYLALTYDHRLIDGRDAVTFLKKIKDLIEDPARMLLDL 418
|
|
| PDHac_trf_mito |
TIGR01349 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
76-492 |
4.60e-56 |
|
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: 193.09 E-value: 4.60e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185134993 76 MEV-TVKEWYVKEGDKVSQFDSICEVQSDKASVTITSRYDGVIKKLYYEVDATAL-VGTPLV-------DIET------- 139
Cdd:TIGR01349 11 MTTgNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEGTKDVpVNKPIAvlveekeDVADafknykl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185134993 140 -----------------EPGPEVVHEEDVVETPAMSNDEHTHQEIKGHKTQATPAVRRLAMENNIKLSEVVGTGRDGRIL 202
Cdd:TIGR01349 91 essaspapkpseiaptaPPSAPKPSPAPQKQSPEPSSPAPLSDKESGDRIFASPLAKKLAKEKGIDLSAVAGSGPNGRIV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185134993 203 KEDILNFLAKQtgailpPTPFHEIQPPPPaasapssasmPKMKPTPSvqlpvvsrPVFTGKDSTEPLKGFHKAMVKTMTA 282
Cdd:TIGR01349 171 KKDIESFVPQS------PASANQQAAATT----------PATYPAAA--------PVSTGSYEDVPLSNIRKIIAKRLLE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185134993 283 ALK-IPHFGYKDEVDLTRLVQLRKELKGLSEARgVKLSYMPFFIKAASLGLLHFPILNASVDEavQNITYKASHNIGLAM 361
Cdd:TIGR01349 227 SKQtIPHYYVSIECNVDKLLALRKELNAMASEV-YKLSVNDFIIKASALALREVPEANSSWTD--NFIRRYKNVDISVAV 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185134993 362 DTSQGLLVPNVKNVQLLSVFEIAVELNRMQTLGATGQLGTADLTGGTFTLSNIGSIGGTYAKPVILPPEVAIGALG--KI 439
Cdd:TIGR01349 304 ATPDGLITPIVRNADAKGLSTISNEIKDLAKRARNNKLKPEEFQGGTFTISNLGMFGIKDFTAIINPPQACILAVGavED 383
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 185134993 440 QVLPRFNSRDEVVKAHVMNVSWSADHRIIDGATMARFSNLWRDYLENPASMVL 492
Cdd:TIGR01349 384 VAVVDNDEEKGFAVASIMSVTLSCDHRVIDGAVGAEFLKSFKKYLENPIEMLL 436
|
|
| PLN02744 |
PLN02744 |
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex |
43-492 |
1.32e-47 |
|
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
Pssm-ID: 215397 [Multi-domain] Cd Length: 539 Bit Score: 172.73 E-value: 1.32e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185134993 43 FIPQLCSSRFFhtsyvTSGPILPfKLSDIGEGIMEVTVKE-----WYVKEGDKVSQFDSICEVQSDKASVTITSRYDGVI 117
Cdd:PLN02744 93 SSSQMQSARGF-----SSSSDLP-PHQEIGMPSLSPTMTEgniarWLKKEGDKVSPGEVLCEVETDKATVEMECMEEGYL 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185134993 118 KKLYYEVDATAL-VGTPL-VDIETE-----------PGPEVVHEEDVVETPAMSNDEHTHQ-----EIKGHKTQ------ 173
Cdd:PLN02744 167 AKIVKGDGAKEIkVGEVIaITVEEEedigkfkdykpSSSAAPAAPKAKPSPPPPKEEEVEKpasspEPKASKPSappssg 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185134993 174 ----ATPAVRRLAMENNIKLSEVVGTGRDGRILKEDILNFLAKQTGAILPPTPfheiqppppaasapssasmpkmKPTPS 249
Cdd:PLN02744 247 drifASPLARKLAEDNNVPLSSIKGTGPDGRIVKADIEDYLASGGKGATAPPS----------------------TDSKA 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185134993 250 VQLPVVSRPvftgkdsteplkgfhKAMVKTMTAAL------KIPHFGYKDEVDLTRLVQLRKELKGLSEARGVK-LSYMP 322
Cdd:PLN02744 305 PALDYTDIP---------------NTQIRKVTASRllqskqTIPHYYLTVDTRVDKLMALRSQLNSLQEASGGKkISVND 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185134993 323 FFIKAASLGLLHFPILNAS-VDEAVQNitYKaSHNIGLAMDTSQGLLVPNVKNVQLLSVFEIAVELNRMQTLGATGQLGT 401
Cdd:PLN02744 370 LVIKAAALALRKVPQCNSSwTDDYIRQ--YH-NVNINVAVQTENGLYVPVVKDADKKGLSTIAEEVKQLAQKARENSLKP 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185134993 402 ADLTGGTFTLSNIGS-IGGTYAKPVILPPEVAIGALGKIQ--VLPRfNSRDEVVKAHVMNVSWSADHRIIDGATMARFSN 478
Cdd:PLN02744 447 EDYEGGTFTVSNLGGpFGIKQFCAIINPPQSAILAVGSAEkrVIPG-SGPDQYNFASFMSVTLSCDHRVIDGAIGAEWLK 525
|
490
....*....|....
gi 185134993 479 LWRDYLENPASMVL 492
Cdd:PLN02744 526 AFKGYIENPESMLL 539
|
|
| PRK14843 |
PRK14843 |
dihydrolipoamide acetyltransferase; Provisional |
175-492 |
3.80e-35 |
|
dihydrolipoamide acetyltransferase; Provisional
Pssm-ID: 184847 [Multi-domain] Cd Length: 347 Bit Score: 134.26 E-value: 3.80e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185134993 175 TPAVRRLAMENNIKLSEVVGTGRDGRILKEDILNFLAK--QTGAILPPTPFHEIQPPPPaasapssasmpkmKPTPSVQL 252
Cdd:PRK14843 52 SPLAKRIALEHNIAWQEIQGTGHRGKIMKKDVLALLPEniENDSIKSPAQIEKVEEVPD-------------NVTPYGEI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185134993 253 PVVsrpvftgkdstePLKGFHKAMVKTMTAA-LKIPHFGYKDEVDLTRLVQLRKE-LKGLSEARGVKLSYMPFFIKAASL 330
Cdd:PRK14843 119 ERI------------PMTPMRKVIAQRMVESyLTAPTFTLNYEVDMTEMLALRKKvLEPIMEATGKKTTVTDLLSLAVVK 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185134993 331 GLLHFPILNASVDEAVQNITYKASHNIGLAMDTSQGLLVPNVKNVQLLSVFEIAVELNRMQTLGATGQLGTADLTGGTFT 410
Cdd:PRK14843 187 TLMKHPYINASLTEDGKTIITHNYVNLAMAVGMDNGLMTPVVYNAEKMSLSELVVAFKDVIGRTLDGKLAPSELQNSTFT 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185134993 411 LSNIGSIGGTYAKPVILPPEVAI-GALGKIQVLPRFNSrdEVVKAHVMNVSWSADHRIIDGATMARFSNLWRDYLENPAS 489
Cdd:PRK14843 267 ISNLGMFGVQSFGPIINQPNSAIlGVSSTIEKPVVVNG--EIVIRPIMSLGLTIDHRVVDGMAGAKFMKDLKELIETPIS 344
|
...
gi 185134993 490 MVL 492
Cdd:PRK14843 345 MLI 347
|
|
| PLN02226 |
PLN02226 |
2-oxoglutarate dehydrogenase E2 component |
60-494 |
7.85e-31 |
|
2-oxoglutarate dehydrogenase E2 component
Pssm-ID: 177871 [Multi-domain] Cd Length: 463 Bit Score: 124.48 E-value: 7.85e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185134993 60 SGPILPFKLSDIGEGIMEVTVKEWYVKEGDKVSQFDSICEVQSDKASVTITSRYDGVIKKLYYEVDATALVGTPLVDIET 139
Cdd:PLN02226 88 SGDTVEAVVPHMGESITDGTLATFLKKPGERVQADEAIAQIETDKVTIDIASPASGVIQEFLVKEGDTVEPGTKVAIISK 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185134993 140 epgpevvheedvvetpamSNDEHTHQEiKGHKTQATPAVRRLAMENNIKLSEVVGTGrdgrilkedilnfLAKQTGAILP 219
Cdd:PLN02226 168 ------------------SEDAASQVT-PSQKIPETTDPKPSPPAEDKQKPKVESAP-------------VAEKPKAPSS 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185134993 220 PTPFHEiqppppaasAPSSASMPKMKPTPSVQLPVVSRPVFTG-KDSTEPLkgfhkAMVKTMtaalkiphfgykDEVDLT 298
Cdd:PLN02226 216 PPPPKQ---------SAKEPQLPPKERERRVPMTRLRKRVATRlKDSQNTF-----ALLTTF------------NEVDMT 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185134993 299 RLVQLRKELK-GLSEARGVKLSYMPFFIKAASLGLLHFPILNASVDEavQNITYKASHNIGLAMDTSQGLLVPNVKNVQL 377
Cdd:PLN02226 270 NLMKLRSQYKdAFYEKHGVKLGLMSGFIKAAVSALQHQPVVNAVIDG--DDIIYRDYVDISIAVGTSKGLVVPVIRGADK 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185134993 378 LSVFEIAVELNRMQTLGATGQLGTADLTGGTFTLSNIGSIGGTYAKPVILPPEVAIGALGKIQVLPRFNSrDEVVKAHVM 457
Cdd:PLN02226 348 MNFAEIEKTINGLAKKANEGTISIDEMAGGSFTVSNGGVYGSLISTPIINPPQSAILGMHSIVSRPMVVG-GSVVPRPMM 426
|
410 420 430
....*....|....*....|....*....|....*..
gi 185134993 458 NVSWSADHRIIDGATMARFSNLWRDYLENPASMVLDL 494
Cdd:PLN02226 427 YVALTYDHRLIDGREAVYFLRRVKDVVEDPQRLLLDI 463
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
65-137 |
2.48e-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: 101.71 E-value: 2.48e-26
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 185134993 65 PFKLSDIGEGIMEVTVKEWYVKEGDKVSQFDSICEVQSDKASVTITSRYDGVIKKLYYEVDATALVGTPLVDI 137
Cdd:cd06849 2 EIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
66-137 |
3.41e-22 |
|
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: 90.13 E-value: 3.41e-22
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 185134993 66 FKLSDIGEGIMEVTVKEWYVKEGDKVSQFDSICEVQSDKASVTITSRYDGVIKKLYYEVDATALVGTPLVDI 137
Cdd:COG0508 5 IKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
65-137 |
2.24e-19 |
|
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue binds biotin in one group and lipoic acid in the other. Note that the HMM does not currently recognize the Glycine cleavage system H proteins.
Pssm-ID: 395290 [Multi-domain] Cd Length: 73 Bit Score: 82.26 E-value: 2.24e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 185134993 65 PFKLSDIGEGIMEVtVKEWYVKEGDKVSQFDSICEVQSDKASVTITSRYDGVIKKLYYEVDATALVGTPLVDI 137
Cdd:pfam00364 2 EIKSPMIGESVREG-VVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
|
|
| E3_binding |
pfam02817 |
e3 binding domain; This family represents a small domain of the E2 subunit of 2-oxo-acid ... |
174-207 |
9.63e-14 |
|
e3 binding domain; This family represents a small domain of the E2 subunit of 2-oxo-acid dehydrogenases responsible for the binding of the E3 subunit.
Pssm-ID: 460710 [Multi-domain] Cd Length: 36 Bit Score: 65.02 E-value: 9.63e-14
10 20 30
....*....|....*....|....*....|....
gi 185134993 174 ATPAVRRLAMENNIKLSEVVGTGRDGRILKEDIL 207
Cdd:pfam02817 3 ASPAARKLARELGIDLSDVKGTGPGGRITKEDVE 36
|
|
| kgd |
PRK12270 |
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ... |
242-476 |
3.97e-12 |
|
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;
Pssm-ID: 237030 [Multi-domain] Cd Length: 1228 Bit Score: 68.76 E-value: 3.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185134993 242 PKMKPTPSVQLPVVSRPVFTGKDSTEPLKGFHKAMVKTMTAALKIPHFGYKDEVDLTRLVQLRKELKG-LSEARGVKLSY 320
Cdd:PRK12270 93 AAAPAAPPAAAAAAAPAAAAVEDEVTPLRGAAAAVAKNMDASLEVPTATSVRAVPAKLLIDNRIVINNhLKRTRGGKVSF 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185134993 321 -------MpffIKAaslgLLHFPILNASVDE------AVQNitykASHNIGLAMDT-----SQGLLVPNVKNV------Q 376
Cdd:PRK12270 173 thligyaL---VQA----LKAFPNMNRHYAEvdgkptLVTP----AHVNLGLAIDLpkkdgSRQLVVPAIKGAetmdfaQ 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185134993 377 LLSVFEIAVELNRmqtlgaTGQLGTADLTGGTFTLSNIGSIGGTYAKPVILPPEVAIGALGKIQVLPRFNSRDEVVKAH- 455
Cdd:PRK12270 242 FWAAYEDIVRRAR------DGKLTADDFQGTTISLTNPGGIGTVHSVPRLMKGQGAIIGVGAMEYPAEFQGASEERLAEl 315
|
250 260
....*....|....*....|....*
gi 185134993 456 ----VMNVSWSADHRIIDGATMARF 476
Cdd:PRK12270 316 giskVMTLTSTYDHRIIQGAESGEF 340
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
67-143 |
3.33e-11 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 65.41 E-value: 3.33e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 185134993 67 KLSDIGEGimEVTVKEWYVKEGDKVSQFDSICEVQSDKASVTITSRYDGVIKKLYYEVDATALVGTPLVDIETEPGP 143
Cdd:PRK11854 6 KVPDIGAD--EVEVTEILVKVGDKVEAEQSLITVEGDKASMEVPSPQAGVVKEIKVKVGDKVETGALIMIFESADGA 80
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
68-137 |
1.99e-09 |
|
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases, and the H-protein of the glycine cleavage system (GCS). These domains transport CO2, acyl, or methylamine, respectively, between components of the complex/protein via a biotinyl or lipoyl group, which is covalently attached to a highly conserved lysine residue.
Pssm-ID: 133456 [Multi-domain] Cd Length: 73 Bit Score: 53.98 E-value: 1.99e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185134993 68 LSDIGEGIMEVTVKEWYVKEGDKVSQFDSICEVQSDKASVTITSRYDGVIKKLYYEVDATALVGTPLVDI 137
Cdd:cd06663 4 IPDLAQHLGDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKVEGDTPLVKI 73
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
72-219 |
3.53e-06 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 49.17 E-value: 3.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185134993 72 GEGIMEVTVKEWYVKEGDKVSQFDSICEVQSDKASVTITSRYDGVIKKLYYEVDATALVGTPLVDIETEPGPEvvheedv 151
Cdd:PRK14875 11 GLSMTEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGETLPVGALLAVVADAEVSD------- 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 185134993 152 vetpamsndehthQEIKGHktqATPAVRRLAMEnNIKLSEVVGTGRDGRILKEDIlNFLAKQTGAILP 219
Cdd:PRK14875 84 -------------AEIDAF---IAPFARRFAPE-GIDEEDAGPAPRKARIGGRTV-RYLRLGEGDGTP 133
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
79-137 |
2.22e-05 |
|
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all biotin-dependent enzymes, such as acetyl-CoA carboxylase, pyruvate carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA carboxylase, geranyl-CoA carboxylase, oxaloacetate decarboxylase, methylmalonyl-CoA decarboxylase, transcarboxylase and urea amidolyase. This domain functions in transferring CO2 from one subsite to another, allowing carboxylation, decarboxylation, or transcarboxylation. During this process, biotin is covalently attached to a specific lysine.
Pssm-ID: 133459 [Multi-domain] Cd Length: 67 Bit Score: 42.40 E-value: 2.22e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 185134993 79 TVKEWYVKEGDKVSQFDSICEVQSDKASVTITSRYDGVIKKLYYEVDATALVGTPLVDI 137
Cdd:cd06850 9 TVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
77-120 |
3.15e-03 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 39.90 E-value: 3.15e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 185134993 77 EVTVKEWYVKEGDKVSQFDSICEVQSDKASVTITSRYDGVIKKL 120
Cdd:PRK11892 16 EGTLAKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKI 59
|
|
| PRK09282 |
PRK09282 |
pyruvate carboxylase subunit B; Validated |
76-138 |
9.01e-03 |
|
pyruvate carboxylase subunit B; Validated
Pssm-ID: 236449 [Multi-domain] Cd Length: 592 Bit Score: 38.67 E-value: 9.01e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 185134993 76 MEVTVKEWYVKEGDKVSQFDSICEVQSDKASVTITSRYDGVIKKLYYEVDATALVGTPLVDIE 138
Cdd:PRK09282 529 MPGTVVKVKVKEGDKVKAGDTVLVLEAMKMENEIQAPVDGTVKEILVKEGDRVNPGDVLMEIE 591
|
|
| |
