|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00144 |
PTZ00144 |
dihydrolipoamide succinyltransferase; Provisional |
1-421 |
0e+00 |
|
dihydrolipoamide succinyltransferase; Provisional
Pssm-ID: 240289 [Multi-domain] Cd Length: 418 Bit Score: 714.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835283857 1 MTKNLVFRLNKSLLHHVKSFNRTFLNHKYNSnANIEGSLKRYFSIETIKVPRLGDSITEGTINEWKKKVGDYVKADETIT 80
Cdd:PTZ00144 1 STVNLVKRLNKPLLSSVKGMFRRFSLRKLQP-ACSAHFSKSYFSIKVIKVPTMGDSISEGTVVEWKKKVGDYVKEDEVIC 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835283857 81 IIDTDKVSVDINSKVSGGLSKIFADVGDVVLVDAPLCEIDTSVEPPEDICKTKEEVGESKNNENNytfnQLNRDIKDEAH 160
Cdd:PTZ00144 80 IIETDKVSVDIRAPASGVITKIFAEEGDTVEVGAPLSEIDTGGAPPAAAPAAAAAAKAEKTTPEK----PKAAAPTPEPP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835283857 161 IKDEVSKNEKDIFVKDPICFGNDYESINE--RTERRVRMLPIRKRIAERLKESQNTCALLTTFNECDMSKAMLLRSELND 238
Cdd:PTZ00144 156 AASKPTPPAAAKPPEPAPAAKPPPTPVARadPRETRVPMSRMRQRIAERLKASQNTCAMLTTFNECDMSALMELRKEYKD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835283857 239 IFQKKYSCKLGFVSLFMYASTLALKKMPNVNAYIENDEIVYKNYIDISVAVATPNGLTVPVIRNCQNKNLPQLELALSDL 318
Cdd:PTZ00144 236 DFQKKHGVKLGFMSAFVKASTIALKKMPIVNAYIDGDEIVYRNYVDISVAVATPTGLVVPVIRNCENKSFAEIEKELADL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835283857 319 ATKARSNKLSIDDFSGGTFTISNGGVFGSMLSTPIINMPQSAILGMHTIKNRPVVVNNEIVIRPIMYLALTYDHRLLDGR 398
Cdd:PTZ00144 316 AEKARNNKLTLEDMTGGTFTISNGGVFGSLMGTPIINPPQSAILGMHAIKKRPVVVGNEIVIRPIMYLALTYDHRLIDGR 395
|
410 420
....*....|....*....|...
gi 1835283857 399 EAVQFLCAIRDYIENPNLMLIDC 421
Cdd:PTZ00144 396 DAVTFLKKIKDLIEDPARMLLDL 418
|
|
| sucB |
TIGR01347 |
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ... |
47-420 |
4.96e-160 |
|
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: 456.89 E-value: 4.96e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835283857 47 TIKVPRLGDSITEGTINEWKKKVGDYVKADETITIIDTDKVSVDINSKVSGGLSKIFADVGDVVLVDAPLCEI----DTS 122
Cdd:TIGR01347 2 EIKVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAILeegnDAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835283857 123 VEPPEDICKTKEE-----------VGESKNN----------ENNYTFNQLNRDIKDEAHIKDEVSKNEKDIfVKDPICFG 181
Cdd:TIGR01347 82 AAPPAKSGEEKEEtpaasaaaaptAAANRPSlspaarrlakEHGIDLSAVPGTGVTGRVTKEDIIKKTEAP-ASAQPPAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835283857 182 NDYESINE---RTERRVRMLPIRKRIAERLKESQNTCALLTTFNECDMSKAMLLRSELNDIFQKKYSCKLGFVSLFMYAS 258
Cdd:TIGR01347 161 AAAAAAPAaatRPEERVKMTRLRQRIAERLKEAQNSTAMLTTFNEVDMSAVMELRKRYKEEFEKKHGVKLGFMSFFVKAV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835283857 259 TLALKKMPNVNAYIENDEIVYKNYIDISVAVATPNGLTVPVIRNCQNKNLPQLELALSDLATKARSNKLSIDDFSGGTFT 338
Cdd:TIGR01347 241 VAALKRFPEVNAEIDGDDIVYKDYYDISVAVSTDRGLVVPVVRNADRMSFADIEKEIADLGKKARDGKLTLEDMTGGTFT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835283857 339 ISNGGVFGSMLSTPIINMPQSAILGMHTIKNRPVVVNNEIVIRPIMYLALTYDHRLLDGREAVQFLCAIRDYIENPNLML 418
Cdd:TIGR01347 321 ITNGGVFGSLMSTPIINPPQSAILGMHGIKERPVAVNGQIEIRPMMYLALSYDHRLIDGKEAVTFLVTIKELLEDPRRLL 400
|
..
gi 1835283857 419 ID 420
Cdd:TIGR01347 401 LD 402
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
208-418 |
7.88e-102 |
|
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: 301.38 E-value: 7.88e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835283857 208 LKESQNTCALLTTFNECDMSKAMLLRSELNDIFQKKYScKLGFVSLFMYASTLALKKMPNVNAYI--ENDEIVYKNYIDI 285
Cdd:pfam00198 1 MTESKQTIPHFTLTDEVDVTELLALREELKEDAADEET-KLTFLPFLVKAVALALKKFPELNASWdgEEGEIVYKKYVNI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835283857 286 SVAVATPNGLTVPVIRNCQNKNLPQLELALSDLATKARSNKLSIDDFSGGTFTISNGGVFGSMLSTPIINMPQSAILGMH 365
Cdd:pfam00198 80 GIAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVG 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1835283857 366 TIKNRPVVVNNEIVIRPIMYLALTYDHRLLDGREAVQFLCAIRDYIENPNLML 418
Cdd:pfam00198 160 RIRKRPVVVDGEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELLL 212
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
44-119 |
3.27e-27 |
|
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component [Energy production and conversion]; Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component is part of the Pathway/BioSystem: Pyruvate oxidation
Pssm-ID: 440274 [Multi-domain] Cd Length: 77 Bit Score: 103.22 E-value: 3.27e-27
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1835283857 44 SIETIKVPRLGDSITEGTINEWKKKVGDYVKADETITIIDTDKVSVDINSKVSGGLSKIFADVGDVVLVDAPLCEI 119
Cdd:COG0508 1 MAIEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
47-119 |
5.45e-27 |
|
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. 2-oxo acid dehydrogenase multienzyme complexes, like pyruvate dehydrogenase (PDH), 2-oxoglutarate dehydrogenase (OGDH) and branched-chain 2-oxo acid dehydrogenase (BCDH), contain at least three different enzymes, 2-oxo acid dehydrogenase (E1), dihydrolipoyl acyltransferase (E2) and dihydrolipoamide dehydrogenase (E3) and play a key role in redox regulation. E2, the central component of the complex, catalyzes the transfer of the acyl group of CoA from E1 to E3 via reductive acetylation of a lipoyl group covalently attached to a lysine residue.
Pssm-ID: 133458 [Multi-domain] Cd Length: 74 Bit Score: 102.48 E-value: 5.45e-27
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1835283857 47 TIKVPRLGDSITEGTINEWKKKVGDYVKADETITIIDTDKVSVDINSKVSGGLSKIFADVGDVVLVDAPLCEI 119
Cdd:cd06849 2 EIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
|
|
| CAT |
smart01059 |
Chloramphenicol acetyltransferase; Chloramphenicol acetyltransferase (CAT).catalyzes the ... |
246-404 |
2.81e-03 |
|
Chloramphenicol acetyltransferase; Chloramphenicol acetyltransferase (CAT).catalyzes the acetyl-CoA dependent acetylation of chloramphenicol (Cm), an antibiotic which inhibits prokaryotic peptidyltransferase activity. Acetylation of Cm by CAT inactivates the antibiotic. A histidine residue, located in the C-terminal section of the enzyme, plays a central role in its catalytic mechanism. There is a second family of CAT. evolutionary unrelated to the main family described above. These CAT belong to the bacterial hexapeptide-repeat containing-transferases family (see ). The crystal structure of the type III enzyme from Escherichia coli with chloramphenicol bound has been determined. CAT is a trimer of identical subunits (monomer Mr 25,000) and the trimeric structure is stabilised by a number of hydrogen bonds, some of which result in the extension of a beta-sheet across the subunit interface. Chloramphenicol binds in a deep pocket located at the boundary between adjacent subunits of the trimer, such that the majority of residues forming the binding pocket belong to one subunit while the catalytically essential histidine belongs to the adjacent subunit. His195 is appropriately positioned to act as a general base catalyst in the reaction, and the required tautomeric stabilisation is provided by an unusual interaction with a main-chain carbonyl oxygen.
Pssm-ID: 215002 Cd Length: 202 Bit Score: 38.73 E-value: 2.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835283857 246 CKLGFVSLFMYASTLALKKMPNVNAYIENDEIVYKNYIDISVAVATPNGLTVPVIRNCQNKNLPQ-LELALSDLATKARS 324
Cdd:smart01059 42 NKYSFFPAYLYAVLKAVNEIPEFRMRIDDGKLVEWDSVHPSYTIFHKEDETFSFIWTPYDEDFKDfYQNALADIERYKNN 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835283857 325 NKLSID-----------------DFSGGTFTISNGGVFgsmlSTPIINMpqsailGMHTIKNRPVVvnneivirpiMYLA 387
Cdd:smart01059 122 PGLFPKeniprndlfyisaipwvSFTSITHNISNGRND----SIPIITW------GKYFKQEGKLL----------LPVS 181
|
170
....*....|....*..
gi 1835283857 388 LTYDHRLLDGREAVQFL 404
Cdd:smart01059 182 IQVHHAVVDGYHVGRFI 198
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00144 |
PTZ00144 |
dihydrolipoamide succinyltransferase; Provisional |
1-421 |
0e+00 |
|
dihydrolipoamide succinyltransferase; Provisional
Pssm-ID: 240289 [Multi-domain] Cd Length: 418 Bit Score: 714.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835283857 1 MTKNLVFRLNKSLLHHVKSFNRTFLNHKYNSnANIEGSLKRYFSIETIKVPRLGDSITEGTINEWKKKVGDYVKADETIT 80
Cdd:PTZ00144 1 STVNLVKRLNKPLLSSVKGMFRRFSLRKLQP-ACSAHFSKSYFSIKVIKVPTMGDSISEGTVVEWKKKVGDYVKEDEVIC 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835283857 81 IIDTDKVSVDINSKVSGGLSKIFADVGDVVLVDAPLCEIDTSVEPPEDICKTKEEVGESKNNENNytfnQLNRDIKDEAH 160
Cdd:PTZ00144 80 IIETDKVSVDIRAPASGVITKIFAEEGDTVEVGAPLSEIDTGGAPPAAAPAAAAAAKAEKTTPEK----PKAAAPTPEPP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835283857 161 IKDEVSKNEKDIFVKDPICFGNDYESINE--RTERRVRMLPIRKRIAERLKESQNTCALLTTFNECDMSKAMLLRSELND 238
Cdd:PTZ00144 156 AASKPTPPAAAKPPEPAPAAKPPPTPVARadPRETRVPMSRMRQRIAERLKASQNTCAMLTTFNECDMSALMELRKEYKD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835283857 239 IFQKKYSCKLGFVSLFMYASTLALKKMPNVNAYIENDEIVYKNYIDISVAVATPNGLTVPVIRNCQNKNLPQLELALSDL 318
Cdd:PTZ00144 236 DFQKKHGVKLGFMSAFVKASTIALKKMPIVNAYIDGDEIVYRNYVDISVAVATPTGLVVPVIRNCENKSFAEIEKELADL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835283857 319 ATKARSNKLSIDDFSGGTFTISNGGVFGSMLSTPIINMPQSAILGMHTIKNRPVVVNNEIVIRPIMYLALTYDHRLLDGR 398
Cdd:PTZ00144 316 AEKARNNKLTLEDMTGGTFTISNGGVFGSLMGTPIINPPQSAILGMHAIKKRPVVVGNEIVIRPIMYLALTYDHRLIDGR 395
|
410 420
....*....|....*....|...
gi 1835283857 399 EAVQFLCAIRDYIENPNLMLIDC 421
Cdd:PTZ00144 396 DAVTFLKKIKDLIEDPARMLLDL 418
|
|
| PRK05704 |
PRK05704 |
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase; |
44-420 |
3.22e-163 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
Pssm-ID: 235571 [Multi-domain] Cd Length: 407 Bit Score: 464.69 E-value: 3.22e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835283857 44 SIEtIKVPRLGDSITEGTINEWKKKVGDYVKADETITIIDTDKVSVDINSKVSGGLSKIFADVGDVVLVDAPLCEIDT-- 121
Cdd:PRK05704 2 MVE-IKVPTLPESVTEATIATWHKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGDTVTVGQVLGRIDEga 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835283857 122 ------------SVEPPEDICKTKEEVGESKNN-----------ENNYTFNQLNRDIKD--------EAHIKDEVS---- 166
Cdd:PRK05704 81 aagaaaaaaaaaAAAAAAPAQAQAAAAAEQSNDalspaarklaaENGLDASAVKGTGKGgrvtkedvLAALAAAAAapaa 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835283857 167 -KNEKDIFVKDPIcfgndyesiNERTERRVRMLPIRKRIAERLKESQNTCALLTTFNECDMSKAMLLRSELNDIFQKKYS 245
Cdd:PRK05704 161 pAAAAPAAAPAPL---------GARPEERVPMTRLRKTIAERLLEAQNTTAMLTTFNEVDMTPVMDLRKQYKDAFEKKHG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835283857 246 CKLGFVSLFMYASTLALKKMPNVNAYIENDEIVYKNYIDISVAVATPNGLTVPVIRNCQNKNLPQLELALSDLATKARSN 325
Cdd:PRK05704 232 VKLGFMSFFVKAVVEALKRYPEVNASIDGDDIVYHNYYDIGIAVGTPRGLVVPVLRDADQLSFAEIEKKIAELAKKARDG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835283857 326 KLSIDDFSGGTFTISNGGVFGSMLSTPIINMPQSAILGMHTIKNRPVVVNNEIVIRPIMYLALTYDHRLLDGREAVQFLC 405
Cdd:PRK05704 312 KLSIEELTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHKIKERPVAVNGQIVIRPMMYLALSYDHRIIDGKEAVGFLV 391
|
410
....*....|....*
gi 1835283857 406 AIRDYIENPNLMLID 420
Cdd:PRK05704 392 TIKELLEDPERLLLD 406
|
|
| sucB |
TIGR01347 |
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ... |
47-420 |
4.96e-160 |
|
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: 456.89 E-value: 4.96e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835283857 47 TIKVPRLGDSITEGTINEWKKKVGDYVKADETITIIDTDKVSVDINSKVSGGLSKIFADVGDVVLVDAPLCEI----DTS 122
Cdd:TIGR01347 2 EIKVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAILeegnDAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835283857 123 VEPPEDICKTKEE-----------VGESKNN----------ENNYTFNQLNRDIKDEAHIKDEVSKNEKDIfVKDPICFG 181
Cdd:TIGR01347 82 AAPPAKSGEEKEEtpaasaaaaptAAANRPSlspaarrlakEHGIDLSAVPGTGVTGRVTKEDIIKKTEAP-ASAQPPAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835283857 182 NDYESINE---RTERRVRMLPIRKRIAERLKESQNTCALLTTFNECDMSKAMLLRSELNDIFQKKYSCKLGFVSLFMYAS 258
Cdd:TIGR01347 161 AAAAAAPAaatRPEERVKMTRLRQRIAERLKEAQNSTAMLTTFNEVDMSAVMELRKRYKEEFEKKHGVKLGFMSFFVKAV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835283857 259 TLALKKMPNVNAYIENDEIVYKNYIDISVAVATPNGLTVPVIRNCQNKNLPQLELALSDLATKARSNKLSIDDFSGGTFT 338
Cdd:TIGR01347 241 VAALKRFPEVNAEIDGDDIVYKDYYDISVAVSTDRGLVVPVVRNADRMSFADIEKEIADLGKKARDGKLTLEDMTGGTFT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835283857 339 ISNGGVFGSMLSTPIINMPQSAILGMHTIKNRPVVVNNEIVIRPIMYLALTYDHRLLDGREAVQFLCAIRDYIENPNLML 418
Cdd:TIGR01347 321 ITNGGVFGSLMSTPIINPPQSAILGMHGIKERPVAVNGQIEIRPMMYLALSYDHRLIDGKEAVTFLVTIKELLEDPRRLL 400
|
..
gi 1835283857 419 ID 420
Cdd:TIGR01347 401 LD 402
|
|
| PRK11856 |
PRK11856 |
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed |
45-420 |
1.35e-119 |
|
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
Pssm-ID: 237001 [Multi-domain] Cd Length: 411 Bit Score: 354.10 E-value: 1.35e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835283857 45 IETIKVPRLGDSITEGTINEWKKKVGDYVKADETITIIDTDKVSVDINSKVSGGLSKIFADVGDVVLVDAPLCEIDTSVE 124
Cdd:PRK11856 2 MFEFKMPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDVVPVGSVIAVIEEEGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835283857 125 --------------PPEDICKTKEEVGESKNNENNYTFN----------------QLNRDIKD-----------EAHIKD 163
Cdd:PRK11856 82 aeaaaaaeaapeapAPEPAPAAAAAAAAAPAAAAAPAAPaaaaakaspavrklarELGVDLSTvkgsgpggritKEDVEA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835283857 164 EVSKNEKDifVKDPICFGNDYESINERTERRVRMLPIRKRIAERLKESQNTCALLTTFNECDMSKAMLLRSELNDIFQKk 243
Cdd:PRK11856 162 AAAAAAPA--AAAAAAAAAAPPAAAAEGEERVPLSGMRKAIAKRMVESKREIPHFTLTDEVDVTALLALRKQLKAIGVK- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835283857 244 ysckLGFVSLFMYASTLALKKMPNVNAYIENDEIVYKNYIDISVAVATPNGLTVPVIRNCQNKNLPQLELALSDLATKAR 323
Cdd:PRK11856 239 ----LTVTDFLIKAVALALKKFPELNASWDDDAIVLKKYVNIGIAVATDGGLIVPVIRDADKKSLFELAREIKDLAEKAR 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835283857 324 SNKLSIDDFSGGTFTISNGGVFGSMLSTPIINMPQSAILGMHTIKNRPVVVNNEIVIRPIMYLALTYDHRLLDGREAVQF 403
Cdd:PRK11856 315 EGKLKPEELQGGTFTISNLGMFGGDYFTPIINPPEVAILGVGAIVERPVVVDGEIVVRKVMPLSLSFDHRVIDGADAARF 394
|
410
....*....|....*..
gi 1835283857 404 LCAIRDYIENPNLMLID 420
Cdd:PRK11856 395 LKALKELLENPALLLLE 411
|
|
| PLN02226 |
PLN02226 |
2-oxoglutarate dehydrogenase E2 component |
15-420 |
1.88e-111 |
|
2-oxoglutarate dehydrogenase E2 component
Pssm-ID: 177871 [Multi-domain] Cd Length: 463 Bit Score: 335.19 E-value: 1.88e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835283857 15 HHVKSFNRTFL--NHKYNSNANIEGS-LKRY---FSIET-----IKVPRLGDSITEGTINEWKKKVGDYVKADETITIID 83
Cdd:PLN02226 50 NHAHSFHNLALpgNSGISRSASLVSStLQRWvrpFSSESgdtveAVVPHMGESITDGTLATFLKKPGERVQADEAIAQIE 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835283857 84 TDKVSVDINSKVSGGLSKIFADVGDVVLVDAPLCEIDTSVEPPEDICKTkEEVGESKNNENNYTFNQLNRDIKDEAHIKD 163
Cdd:PLN02226 130 TDKVTIDIASPASGVIQEFLVKEGDTVEPGTKVAIISKSEDAASQVTPS-QKIPETTDPKPSPPAEDKQKPKVESAPVAE 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835283857 164 evsKNEKDIFVKDPICFGNDYESINERTERRVRMLPIRKRIAERLKESQNTCALLTTFNECDMSKAMLLRSELNDIFQKK 243
Cdd:PLN02226 209 ---KPKAPSSPPPPKQSAKEPQLPPKERERRVPMTRLRKRVATRLKDSQNTFALLTTFNEVDMTNLMKLRSQYKDAFYEK 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835283857 244 YSCKLGFVSLFMYASTLALKKMPNVNAYIENDEIVYKNYIDISVAVATPNGLTVPVIRNCQNKNLPQLELALSDLATKAR 323
Cdd:PLN02226 286 HGVKLGLMSGFIKAAVSALQHQPVVNAVIDGDDIIYRDYVDISIAVGTSKGLVVPVIRGADKMNFAEIEKTINGLAKKAN 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835283857 324 SNKLSIDDFSGGTFTISNGGVFGSMLSTPIINMPQSAILGMHTIKNRPVVVNNEIVIRPIMYLALTYDHRLLDGREAVQF 403
Cdd:PLN02226 366 EGTISIDEMAGGSFTVSNGGVYGSLISTPIINPPQSAILGMHSIVSRPMVVGGSVVPRPMMYVALTYDHRLIDGREAVYF 445
|
410
....*....|....*..
gi 1835283857 404 LCAIRDYIENPNLMLID 420
Cdd:PLN02226 446 LRRVKDVVEDPQRLLLD 462
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
208-418 |
7.88e-102 |
|
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: 301.38 E-value: 7.88e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835283857 208 LKESQNTCALLTTFNECDMSKAMLLRSELNDIFQKKYScKLGFVSLFMYASTLALKKMPNVNAYI--ENDEIVYKNYIDI 285
Cdd:pfam00198 1 MTESKQTIPHFTLTDEVDVTELLALREELKEDAADEET-KLTFLPFLVKAVALALKKFPELNASWdgEEGEIVYKKYVNI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835283857 286 SVAVATPNGLTVPVIRNCQNKNLPQLELALSDLATKARSNKLSIDDFSGGTFTISNGGVFGSMLSTPIINMPQSAILGMH 365
Cdd:pfam00198 80 GIAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVG 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1835283857 366 TIKNRPVVVNNEIVIRPIMYLALTYDHRLLDGREAVQFLCAIRDYIENPNLML 418
Cdd:pfam00198 160 RIRKRPVVVDGEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELLL 212
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
44-418 |
2.32e-85 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 270.54 E-value: 2.32e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835283857 44 SIETIKVPRLGDsITEGTINEWKKKVGDYVKADETITIIDTDKVSVDINSKVSGGLSKIFADVGDVVLVDAPLCEIDTSV 123
Cdd:PRK11855 118 GVVEVKVPDIGE-ITEVEVIEWLVKVGDTVEEDQSLITVETDKATMEIPSPVAGVVKEIKVKVGDKVSVGSLLVVIEVAA 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835283857 124 EPPEDICK----------------------------TKEEVGESKNN-----------ENNYTFNQL------NRDIKD- 157
Cdd:PRK11855 197 AAPAAAAApaaaapaaaaaaapapapaaaaapaaaaPAAAAAPGKAPhaspavrrlarELGVDLSQVkgtgkkGRITKEd 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835283857 158 -EAHIKDEVSKNE--------------------KDIFVKdpicFGndyesinerTERRVRMLPIRKRIAERLKESQNTCA 216
Cdd:PRK11855 277 vQAFVKGAMSAAAaaaaaaaaagggglgllpwpKVDFSK----FG---------EIETKPLSRIKKISAANLHRSWVTIP 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835283857 217 LLTTFNECDMSKAMLLRSELNDIFQKKySCKLGFVSLFMYASTLALKKMPNVNAYI--ENDEIVYKNYIDISVAVATPNG 294
Cdd:PRK11855 344 HVTQFDEADITDLEALRKQLKKEAEKA-GVKLTMLPFFIKAVVAALKEFPVFNASLdeDGDELTYKKYFNIGFAVDTPNG 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835283857 295 LTVPVIRNCQNKNLPQLELALSDLATKARSNKLSIDDFSGGTFTISNGGVFGSMLSTPIINMPQSAILGMHTIKNRPVVV 374
Cdd:PRK11855 423 LVVPVIKDVDKKSLLEIAREIAELAKKARDGKLKPDDMQGGCFTISSLGGIGGTAFTPIINAPEVAILGVGKSQMKPVWD 502
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1835283857 375 NNEIVIRPIMYLALTYDHRLLDGREAVQFLCAIRDYIENPNLML 418
Cdd:PRK11855 503 GKEFVPRLMLPLSLSYDHRVIDGATAARFTNYLKQLLADPRRML 546
|
|
| SucB_Actino |
TIGR02927 |
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model ... |
48-416 |
2.86e-76 |
|
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: 247.62 E-value: 2.86e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835283857 48 IKVPRLGDSITEGTINEWKKKVGDYVKADETITIIDTDKVSVDINSKVSGGLSKIFADVGDVVLVDAPLCEI-------- 119
Cdd:TIGR02927 129 VKMPELGESVTEGTVTSWLKAVGDTVEVDEPLLEVSTDKVDTEIPSPVAGTLLEIRAPEDDTVEVGTVLAIIgdanaapa 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835283857 120 -----------------------DTSVEPPEDICKTKEEVGESK--------NNENNYTFNQLNRDIKDEAHI------- 161
Cdd:TIGR02927 209 epaeeeapapseagsepapdpaaRAPHAAPDPPAPAPAPAKTAApaaaapvsSGDSGPYVTPLVRKLAKDKGVdlstvkg 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835283857 162 --------KDEV------SKNEKDIFVKDPICFGN------------DYESINERTERRVRmlpIRKRIAERLKESQNTC 215
Cdd:TIGR02927 289 tgvggrirKQDVlaaakaAEEARAAAAAPAAAAAPaapaaaakpaepDTAKLRGTTQKMNR---IRQITADKTIESLQTS 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835283857 216 ALLTTFNECDMSKAMLLRSELNDIFQKKYSCKLGFVSLFMYASTLALKKMPNVNAYI--ENDEIVYKNYIDISVAVATPN 293
Cdd:TIGR02927 366 AQLTQVHEVDMTRVAALRARAKNDFLEKNGVNLTFLPFFVQAVTEALKAHPNVNASYnaETKEVTYHDVEHVGIAVDTPR 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835283857 294 GLTVPVIRNCQNKNLPQLELALSDLATKARSNKLSIDDFSGGTFTISNGGVFGSMLSTPIINMPQSAILGMHTIKNRPVV 373
Cdd:TIGR02927 446 GLLVPVIHNAGDLSLPGLAKAINDLAARARDNKLKPDELSGGTFTITNIGSGGALFDTPILNPPQAAILGTGAIVKRPRV 525
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1835283857 374 VNNE-----IVIRPIMYLALTYDHRLLDGREAVQFLCAIRDYIENPNL 416
Cdd:TIGR02927 526 IKDEdggesIAIRSVCYLPLTYDHRLVDGADAGRFLTTIKKRLEEGDF 573
|
|
| PDHac_trf_mito |
TIGR01349 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
48-419 |
2.39e-71 |
|
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: 230.84 E-value: 2.39e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835283857 48 IKVPRLGDSITEGTINEWKKKVGDYVKADETITIIDTDKVSVDINSKVSGGLSKIFADVG-DVVLVDAPLCEIdtsVEPP 126
Cdd:TIGR01349 2 ITMPALSPTMTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEGtKDVPVNKPIAVL---VEEK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835283857 127 EDI----------------CKTKEEVGESKNN-----------------------------------------ENNYTFN 149
Cdd:TIGR01349 79 EDVadafknyklessaspaPKPSEIAPTAPPSapkpspapqkqspepsspaplsdkesgdrifasplakklakEKGIDLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835283857 150 QLN----------RDIKDEAHIKDEVSKNE---KDIFVKDPICFGN--DYESINerterrvrMLPIRKRIAERLKESQNT 214
Cdd:TIGR01349 159 AVAgsgpngrivkKDIESFVPQSPASANQQaaaTTPATYPAAAPVStgSYEDVP--------LSNIRKIIAKRLLESKQT 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835283857 215 CALLTTFNECDMSKAMLLRSELNDIFQKKYscKLGFVSLFMYASTLALKKMPNVNAYIENDEIVYKNYIDISVAVATPNG 294
Cdd:TIGR01349 231 IPHYYVSIECNVDKLLALRKELNAMASEVY--KLSVNDFIIKASALALREVPEANSSWTDNFIRRYKNVDISVAVATPDG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835283857 295 LTVPVIRNCQNKNLPQLELALSDLATKARSNKLSIDDFSGGTFTISNGGVFGSMLSTPIINMPQSAILGMHTIKNRPVVV 374
Cdd:TIGR01349 309 LITPIVRNADAKGLSTISNEIKDLAKRARNNKLKPEEFQGGTFTISNLGMFGIKDFTAIINPPQACILAVGAVEDVAVVD 388
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1835283857 375 NNE---IVIRPIMYLALTYDHRLLDGREAVQFLCAIRDYIENPNLMLI 419
Cdd:TIGR01349 389 NDEekgFAVASIMSVTLSCDHRVIDGAVGAEFLKSFKKYLENPIEMLL 436
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
44-413 |
1.59e-70 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 233.74 E-value: 1.59e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835283857 44 SIETIKVPRLGDsiTEGTINEWKKKVGDYVKADETITIIDTDKVSVDINSKVSGGLSKIFADVGDVVLV----------- 112
Cdd:PRK11854 205 GVKDVNVPDIGG--DEVEVTEVMVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVKTgslimrfeveg 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835283857 113 ----DAPLCEIDT-------SVEPPEDICKTKEEVGESKNNENNYTF-----NQLNRD----------------IKDE-- 158
Cdd:PRK11854 283 aapaAAPAKQEAAapapaaaKAEAPAAAPAAKAEGKSEFAENDAYVHatplvRRLAREfgvnlakvkgtgrkgrILKEdv 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835283857 159 -AHIKDEVSKNEK---------------DIFVKDPICFGndyesinERTErrVRMLPIRKRIAERLKESQNTCALLTTFN 222
Cdd:PRK11854 363 qAYVKDAVKRAEAapaaaaaggggpgllPWPKVDFSKFG-------EIEE--VELGRIQKISGANLHRNWVMIPHVTQFD 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835283857 223 ECDMSKAMLLRSELNDI-FQKKYSCKLGFVSLFMYASTLALKKMPNVNAYIEND--EIVYKNYIDISVAVATPNGLTVPV 299
Cdd:PRK11854 434 KADITELEAFRKQQNAEaEKRKLGVKITPLVFIMKAVAAALEQMPRFNSSLSEDgqRLTLKKYVNIGIAVDTPNGLVVPV 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835283857 300 IRNCQNKNLPQLELALSDLATKARSNKLSIDDFSGGTFTISNGGVFGSMLSTPIINMPQSAILGMHTIKNRPVVVNNEIV 379
Cdd:PRK11854 514 FKDVNKKGIIELSRELMDISKKARDGKLTAGDMQGGCFTISSIGGLGTTHFTPIVNAPEVAILGVSKSAMEPVWNGKEFA 593
|
410 420 430
....*....|....*....|....*....|....
gi 1835283857 380 IRPIMYLALTYDHRLLDGREAVQFLCAIRDYIEN 413
Cdd:PRK11854 594 PRLMLPLSLSYDHRVIDGADGARFITIINDRLSD 627
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
44-419 |
2.21e-53 |
|
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: 186.23 E-value: 2.21e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835283857 44 SIETIKVPRLGDsITEGTINEWKKKVGDYVKADETITIIDTDKVSVDINSKVSGGLSKIFADVGDVVLV----------- 112
Cdd:TIGR01348 115 GVQEVTVPDIGD-IEKVTVIEVLVKVGDTVSADQSLITLESDKASMEVPAPASGVVKSVKVKVGDSVPTgdliltlsvag 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835283857 113 DAPLCEID-------------TSVEPPEDICKTKEE--VGESKNNENNYTFN-------QLNRDIKDEAH------IKDE 164
Cdd:TIGR01348 194 STPATAPApasaqpaaqspaaTQPEPAAAPAAAKAQapAPQQAGTQNPAKVDhaapavrRLAREFGVDLSavkgtgIKGR 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835283857 165 VSKNEKDIFVKDPICFGN-------------------DYESINERteRRVRMLPIRKRIAERLKESQNTCALLTTFNECD 225
Cdd:TIGR01348 274 ILREDVQRFVKEPSVRAQaaaasaaggapgalpwpnvDFSKFGEV--EEVDMSRIRKISGANLTRNWTMIPHVTHFDKAD 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835283857 226 MSKAMLLRSELNDIfQKKYSCKLGFVSLFMYASTLALKKMPNVNAYIEND--EIVYKNYIDISVAVATPNGLTVPVIRNC 303
Cdd:TIGR01348 352 ITEMEAFRKQQNAA-VEKEGVKLTVLHILMKAVAAALKKFPKFNASLDLGgeQLILKKYVNIGVAVDTPNGLLVPVIKDV 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835283857 304 QNKNLPQLELALSDLATKARSNKLSIDDFSGGTFTISNGGVFGSMLSTPIINMPQSAILGMHTIKNRPVVVNNEIVIRPI 383
Cdd:TIGR01348 431 DRKGITELALELSDLAKKARDGKLTPDEMQGACFTISSLGGIGGTAFTPIVNAPEVAILGVSKSGMEPVWNGKEFEPRLM 510
|
410 420 430
....*....|....*....|....*....|....*.
gi 1835283857 384 MYLALTYDHRLLDGREAVQFLCAIRDYIENPNLMLI 419
Cdd:TIGR01348 511 LPLSLSYDHRVIDGADAARFTTYICESLADIRRLLL 546
|
|
| PRK14843 |
PRK14843 |
dihydrolipoamide acetyltransferase; Provisional |
194-419 |
4.07e-50 |
|
dihydrolipoamide acetyltransferase; Provisional
Pssm-ID: 184847 [Multi-domain] Cd Length: 347 Bit Score: 172.78 E-value: 4.07e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835283857 194 RVRMLPIRKRIAERLKESQNTCALLTTFNECDMSKAMLLRSELNDIFQKKYSCKLGFVSLFMYASTLALKKMPNVNAYIE 273
Cdd:PRK14843 120 RIPMTPMRKVIAQRMVESYLTAPTFTLNYEVDMTEMLALRKKVLEPIMEATGKKTTVTDLLSLAVVKTLMKHPYINASLT 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835283857 274 ND--EIVYKNYIDISVAVATPNGLTVPVIRNCQNKNLPQLELALSDLATKARSNKLSIDDFSGGTFTISNGGVFGSMLST 351
Cdd:PRK14843 200 EDgkTIITHNYVNLAMAVGMDNGLMTPVVYNAEKMSLSELVVAFKDVIGRTLDGKLAPSELQNSTFTISNLGMFGVQSFG 279
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1835283857 352 PIINMPQSAILGMHTIKNRPVVVNNEIVIRPIMYLALTYDHRLLDGREAVQFLCAIRDYIENPNLMLI 419
Cdd:PRK14843 280 PIINQPNSAILGVSSTIEKPVVVNGEIVIRPIMSLGLTIDHRVVDGMAGAKFMKDLKELIETPISMLI 347
|
|
| PLN02744 |
PLN02744 |
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex |
48-419 |
1.40e-49 |
|
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
Pssm-ID: 215397 [Multi-domain] Cd Length: 539 Bit Score: 176.20 E-value: 1.40e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835283857 48 IKVPRLGDSITEGTINEWKKKVGDYVKADETITIIDTDKVSVDINSKVSGGLSKI-FAD------VGDVVLVdaplceid 120
Cdd:PLN02744 115 IGMPSLSPTMTEGNIARWLKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIvKGDgakeikVGEVIAI-------- 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835283857 121 tSVEPPEDICKTK----------------EEVGESKNNENNytfnQLNRDIKDEAHIKDEVSKNEKDIF----------- 173
Cdd:PLN02744 187 -TVEEEEDIGKFKdykpsssaapaapkakPSPPPPKEEEVE----KPASSPEPKASKPSAPPSSGDRIFasplarklaed 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835283857 174 -----------------VKDPIcfgNDYESINERTERRVRMLP---------------IRKRIAERLKESQNTCA--LLT 219
Cdd:PLN02744 262 nnvplssikgtgpdgriVKADI---EDYLASGGKGATAPPSTDskapaldytdipntqIRKVTASRLLQSKQTIPhyYLT 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835283857 220 TFNECDmsKAMLLRSELNDIFQKKYSCKLGFVSLFMYASTLALKKMPNVNAYIENDEIVYKNYIDISVAVATPNGLTVPV 299
Cdd:PLN02744 339 VDTRVD--KLMALRSQLNSLQEASGGKKISVNDLVIKAAALALRKVPQCNSSWTDDYIRQYHNVNINVAVQTENGLYVPV 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835283857 300 IRNCQNKNLPQLELALSDLATKARSNKLSIDDFSGGTFTISN-GGVFGSMLSTPIINMPQSAILGMHTIKNR--PVVVNN 376
Cdd:PLN02744 417 VKDADKKGLSTIAEEVKQLAQKARENSLKPEDYEGGTFTVSNlGGPFGIKQFCAIINPPQSAILAVGSAEKRviPGSGPD 496
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1835283857 377 EIVIRPIMYLALTYDHRLLDGREAVQFLCAIRDYIENPNLMLI 419
Cdd:PLN02744 497 QYNFASFMSVTLSCDHRVIDGAIGAEWLKAFKGYIENPESMLL 539
|
|
| PRK11857 |
PRK11857 |
dihydrolipoamide acetyltransferase; Reviewed |
186-417 |
7.07e-48 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237002 [Multi-domain] Cd Length: 306 Bit Score: 165.74 E-value: 7.07e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835283857 186 SINERTE-RRVRMLPIRKRIAERLKESQNTCALLTTFNECDMSKAMLLRSELNDIFQKKYSCKLGFVSLFMYASTLALKK 264
Cdd:PRK11857 69 AAPPKLEgKREKVAPIRKAIARAMTNSWSNVAYVNLVNEIDMTKLWDLRKSVKDPVLKTEGVKLTFLPFIAKAILIALKE 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835283857 265 MPNVNA-YIE-NDEIVYKNYIDISVAVATPNGLTVPVIRNCQNKNLPQLELALSDLATKARSNKLSIDDFSGGTFTISNG 342
Cdd:PRK11857 149 FPIFAAkYDEaTSELVYPDTLNLGIAVDTEAGLMVPVIKNAQKLSIVEIAKEISRLAKAARERKIKPDEMKGGSFTITNY 228
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1835283857 343 GVFGSMLSTPIINMPQSAILGMHTIKNRPVVVNNEIVIRPIMYLALTYDHRLLDGREAVQFLCAIRDYIENPNLM 417
Cdd:PRK11857 229 GSVGSLYGVPVINYPELAIAGVGAIIDKAIVKNGQIVAGKVMHLTVAADHRWIDGATIGRFASRVKELLEKPEIL 303
|
|
| PLN02528 |
PLN02528 |
2-oxoisovalerate dehydrogenase E2 component |
54-419 |
9.17e-43 |
|
2-oxoisovalerate dehydrogenase E2 component
Pssm-ID: 215289 [Multi-domain] Cd Length: 416 Bit Score: 154.88 E-value: 9.17e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835283857 54 GDSITEGTINEWKKKVGDYVKADETITIIDTDKVSVDINSKVSGGLSKIFADVGDVVLVDAPLCEIDT---------SVE 124
Cdd:PLN02528 7 GEGIAECELLRWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGKVAQINFSPGDIVKVGETLLKIMVedsqhlrsdSLL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835283857 125 PPEDICKTKEEVGESKNNENNYTF----------NQLNRDI-------KDEAHIKDEVSK-NEKDIFVKDPICFGNDYES 186
Cdd:PLN02528 87 LPTDSSNIVSLAESDERGSNLSGVlstpavrhlaKQYGIDLndilgtgKDGRVLKEDVLKyAAQKGVVKDSSSAEEATIA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835283857 187 INERTERRV----------RMLPIR--KRIaerLKESQNTCALLTTF---NECDMSKAMLLRSELNDIfQKKYSCKLGFV 251
Cdd:PLN02528 167 EQEEFSTSVstpteqsyedKTIPLRgfQRA---MVKTMTAAAKVPHFhyvEEINVDALVELKASFQEN-NTDPTVKHTFL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835283857 252 SLFMYASTLALKKMPNVNAYIEND--EIVYKNYIDISVAVATPNGLTVPVIRNCQNKNLPQLELALSDLATKARSNKLSI 329
Cdd:PLN02528 243 PFLIKSLSMALSKYPLLNSCFNEEtsEIRLKGSHNIGVAMATEHGLVVPNIKNVQSLSLLEITKELSRLQHLAAENKLNP 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835283857 330 DDFSGGTFTISNGGVFGSMLSTPIINMPQSAILGMHTIKNRPVVVN-NEIVIRPIMYLALTYDHRLLDGREAVQFLCAIR 408
Cdd:PLN02528 323 EDITGGTITLSNIGAIGGKFGSPVLNLPEVAIIALGRIQKVPRFVDdGNVYPASIMTVTIGADHRVLDGATVARFCNEWK 402
|
410
....*....|.
gi 1835283857 409 DYIENPNLMLI 419
Cdd:PLN02528 403 SYVEKPELLML 413
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
44-119 |
3.27e-27 |
|
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component [Energy production and conversion]; Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component is part of the Pathway/BioSystem: Pyruvate oxidation
Pssm-ID: 440274 [Multi-domain] Cd Length: 77 Bit Score: 103.22 E-value: 3.27e-27
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1835283857 44 SIETIKVPRLGDSITEGTINEWKKKVGDYVKADETITIIDTDKVSVDINSKVSGGLSKIFADVGDVVLVDAPLCEI 119
Cdd:COG0508 1 MAIEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
47-119 |
5.45e-27 |
|
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. 2-oxo acid dehydrogenase multienzyme complexes, like pyruvate dehydrogenase (PDH), 2-oxoglutarate dehydrogenase (OGDH) and branched-chain 2-oxo acid dehydrogenase (BCDH), contain at least three different enzymes, 2-oxo acid dehydrogenase (E1), dihydrolipoyl acyltransferase (E2) and dihydrolipoamide dehydrogenase (E3) and play a key role in redox regulation. E2, the central component of the complex, catalyzes the transfer of the acyl group of CoA from E1 to E3 via reductive acetylation of a lipoyl group covalently attached to a lysine residue.
Pssm-ID: 133458 [Multi-domain] Cd Length: 74 Bit Score: 102.48 E-value: 5.45e-27
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1835283857 47 TIKVPRLGDSITEGTINEWKKKVGDYVKADETITIIDTDKVSVDINSKVSGGLSKIFADVGDVVLVDAPLCEI 119
Cdd:cd06849 2 EIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
|
|
| kgd |
PRK12270 |
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ... |
247-404 |
7.06e-19 |
|
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;
Pssm-ID: 237030 [Multi-domain] Cd Length: 1228 Bit Score: 89.18 E-value: 7.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835283857 247 KLGFVSLFMYASTLALKKMPNVNA-YIEND---EIVYKNYIDISVA--VATPNG---LTVPVIRNCQNKNLPQLELALSD 317
Cdd:PRK12270 169 KVSFTHLIGYALVQALKAFPNMNRhYAEVDgkpTLVTPAHVNLGLAidLPKKDGsrqLVVPAIKGAETMDFAQFWAAYED 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835283857 318 LATKARSNKLSIDDFSGGTFTISNGGVFGSMLSTPIInMP-QSAILGM--------------HTIknrpvvvnNEIVIRP 382
Cdd:PRK12270 249 IVRRARDGKLTADDFQGTTISLTNPGGIGTVHSVPRL-MKgQGAIIGVgameypaefqgaseERL--------AELGISK 319
|
170 180
....*....|....*....|..
gi 1835283857 383 IMYLALTYDHRLLDGREAVQFL 404
Cdd:PRK12270 320 VMTLTSTYDHRIIQGAESGEFL 341
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
46-119 |
3.60e-17 |
|
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: 75.71 E-value: 3.60e-17
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1835283857 46 ETIKVPRLGDSITEGtINEWKKKVGDYVKADETITIIDTDKVSVDINSKVSGGLSKIFADVGDVVLVDAPLCEI 119
Cdd:pfam00364 1 TEIKSPMIGESVREG-VVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
47-119 |
6.62e-14 |
|
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: 66.31 E-value: 6.62e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1835283857 47 TIKVPRLGDSITEGTINEWKKKVGDYVKADETITIIDTDKVSVDINSKVSGGLSKIFADVGDVVLVDAPLCEI 119
Cdd:cd06663 1 TILIPDLAQHLGDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKVEGDTPLVKI 73
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
44-139 |
3.52e-13 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 71.19 E-value: 3.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835283857 44 SIEtIKVPRLGdsITEGTINEWKKKVGDYVKADETITIIDTDKVSVDINSKVSGGLSKIFADVGDVVLVDAPLCEIDTSV 123
Cdd:PRK11854 2 AIE-IKVPDIG--ADEVEVTEILVKVGDKVEAEQSLITVEGDKASMEVPSPQAGVVKEIKVKVGDKVETGALIMIFESAD 78
|
90
....*....|....*.
gi 1835283857 124 EPPEDICKTKEEVGES 139
Cdd:PRK11854 79 GAADAAPAQAEEKKEA 94
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
44-129 |
9.26e-12 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 66.12 E-value: 9.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835283857 44 SIETIKVPRLGDSITEGTINEWKKKVGDYVKADETITIIDTDKVSVDINSKVSGGLSKIFADVGDVVLVDAPLCEIDTSV 123
Cdd:PRK14875 1 SITPITMPKWGLSMTEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGETLPVGALLAVVADAE 80
|
....*.
gi 1835283857 124 EPPEDI 129
Cdd:PRK14875 81 VSDAEI 86
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
60-119 |
1.76e-06 |
|
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: 45.10 E-value: 1.76e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835283857 60 GTINEWKKKVGDYVKADETITIIDTDKVSVDINSKVSGGLSKIFADVGDVVLVDAPLCEI 119
Cdd:cd06850 8 GTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| PRK09282 |
PRK09282 |
pyruvate carboxylase subunit B; Validated |
60-119 |
4.55e-06 |
|
pyruvate carboxylase subunit B; Validated
Pssm-ID: 236449 [Multi-domain] Cd Length: 592 Bit Score: 48.69 E-value: 4.55e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835283857 60 GTINEWKKKVGDYVKADETITIIDTDKVSVDINSKVSGGLSKIFADVGDVVLVDAPLCEI 119
Cdd:PRK09282 531 GTVVKVKVKEGDKVKAGDTVLVLEAMKMENEIQAPVDGTVKEILVKEGDRVNPGDVLMEI 590
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
48-115 |
3.85e-05 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 45.68 E-value: 3.85e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1835283857 48 IKVPRLGDSITEGTINEWKKKVGDYVKADETITIIDTDKVSVDINSKVSGGLSKIFADVG-DVVLVDAP 115
Cdd:PRK11892 5 ILMPALSPTMEEGTLAKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKILVPEGtEGVKVNTP 73
|
|
| AccB |
COG0511 |
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ... |
68-120 |
1.70e-04 |
|
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440277 [Multi-domain] Cd Length: 136 Bit Score: 41.42 E-value: 1.70e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1835283857 68 KVGDYVKADETITIIDTDKVSVDINSKVSGGLSKIFADVGDVVLVDAPLCEID 120
Cdd:COG0511 84 KVGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVVEILVENGQPVEYGQPLFVIE 136
|
|
| CAT |
smart01059 |
Chloramphenicol acetyltransferase; Chloramphenicol acetyltransferase (CAT).catalyzes the ... |
246-404 |
2.81e-03 |
|
Chloramphenicol acetyltransferase; Chloramphenicol acetyltransferase (CAT).catalyzes the acetyl-CoA dependent acetylation of chloramphenicol (Cm), an antibiotic which inhibits prokaryotic peptidyltransferase activity. Acetylation of Cm by CAT inactivates the antibiotic. A histidine residue, located in the C-terminal section of the enzyme, plays a central role in its catalytic mechanism. There is a second family of CAT. evolutionary unrelated to the main family described above. These CAT belong to the bacterial hexapeptide-repeat containing-transferases family (see ). The crystal structure of the type III enzyme from Escherichia coli with chloramphenicol bound has been determined. CAT is a trimer of identical subunits (monomer Mr 25,000) and the trimeric structure is stabilised by a number of hydrogen bonds, some of which result in the extension of a beta-sheet across the subunit interface. Chloramphenicol binds in a deep pocket located at the boundary between adjacent subunits of the trimer, such that the majority of residues forming the binding pocket belong to one subunit while the catalytically essential histidine belongs to the adjacent subunit. His195 is appropriately positioned to act as a general base catalyst in the reaction, and the required tautomeric stabilisation is provided by an unusual interaction with a main-chain carbonyl oxygen.
Pssm-ID: 215002 Cd Length: 202 Bit Score: 38.73 E-value: 2.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835283857 246 CKLGFVSLFMYASTLALKKMPNVNAYIENDEIVYKNYIDISVAVATPNGLTVPVIRNCQNKNLPQ-LELALSDLATKARS 324
Cdd:smart01059 42 NKYSFFPAYLYAVLKAVNEIPEFRMRIDDGKLVEWDSVHPSYTIFHKEDETFSFIWTPYDEDFKDfYQNALADIERYKNN 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835283857 325 NKLSID-----------------DFSGGTFTISNGGVFgsmlSTPIINMpqsailGMHTIKNRPVVvnneivirpiMYLA 387
Cdd:smart01059 122 PGLFPKeniprndlfyisaipwvSFTSITHNISNGRND----SIPIITW------GKYFKQEGKLL----------LPVS 181
|
170
....*....|....*..
gi 1835283857 388 LTYDHRLLDGREAVQFL 404
Cdd:smart01059 182 IQVHHAVVDGYHVGRFI 198
|
|
| |
