|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11856 |
PRK11856 |
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed |
1-388 |
2.19e-158 |
|
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
Pssm-ID: 237001 [Multi-domain] Cd Length: 411 Bit Score: 451.55 E-value: 2.19e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2224332745 1 MPDFLLPDLGEGLTEAAILTWHVNVGDTVKVDQIVVEVETAKAAVEVPVPFAGVVSALHGTPGQLLPVGAPLLSV---GG 77
Cdd:PRK11856 2 MFEFKMPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDVVPVGSVIAVIeeeGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2224332745 78 FAEPGVTTSAGSGNVLIGYGTAPSTRRKRVRRPEAPAPKAKAPGVISPFVRKLAADNGLDLAKVTASGADGIIRRADVEA 157
Cdd:PRK11856 82 AEAAAAAEAAPEAPAPEPAPAAAAAAAAAPAAAAAPAAPAAAAAKASPAVRKLARELGVDLSTVKGSGPGGRITKEDVEA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2224332745 158 ALKKPVAK------------------GKRIPLTGVRKAVADKLTTSRREIPEATVWVDVDATGLVAARAALNAGTDRpVS 219
Cdd:PRK11856 162 AAAAAAPAaaaaaaaaaappaaaaegEERVPLSGMRKAIAKRMVESKREIPHFTLTDEVDVTALLALRKQLKAIGVK-LT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2224332745 220 LLGLIARFAVAGLRKYPELNSRVEGDEIVVLDEIHLGFAAQTDRGLVVPVVRDAGALSTRDLSAAIGDRARTARDGKLAP 299
Cdd:PRK11856 241 VTDFLIKAVALALKKFPELNASWDDDAIVLKKYVNIGIAVATDGGLIVPVIRDADKKSLFELAREIKDLAEKAREGKLKP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2224332745 300 ADLTGGTFTVNNYGVFGVDGSAAIINHPEAAILGIGRIIDRPWVVDGALAVRKVCELTLAFDHRVCDGGTAGGFLRFVAD 379
Cdd:PRK11856 321 EELQGGTFTISNLGMFGGDYFTPIINPPEVAILGVGAIVERPVVVDGEIVVRKVMPLSLSFDHRVIDGADAARFLKALKE 400
|
....*....
gi 2224332745 380 CVESPVTAL 388
Cdd:PRK11856 401 LLENPALLL 409
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
182-388 |
2.08e-85 |
|
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: 258.24 E-value: 2.08e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2224332745 182 LTTSRREIPEATVWVDVDATGLVAARAALN---AGTDRPVSLLGLIARFAVAGLRKYPELNSRVEGD--EIVVLDEIHLG 256
Cdd:pfam00198 1 MTESKQTIPHFTLTDEVDVTELLALREELKedaADEETKLTFLPFLVKAVALALKKFPELNASWDGEegEIVYKKYVNIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2224332745 257 FAAQTDRGLVVPVVRDAGALSTRDLSAAIGDRARTARDGKLAPADLTGGTFTVNNYGVFGVDGSAAIINHPEAAILGIGR 336
Cdd:pfam00198 81 IAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVGR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2224332745 337 IIDRPWVVDGALAVRKVCELTLAFDHRVCDGGTAGGFLRFVADCVESPVTAL 388
Cdd:pfam00198 161 IRKRPVVVDGEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELLL 212
|
|
| sucB |
TIGR01347 |
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ... |
2-391 |
3.66e-85 |
|
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: 264.67 E-value: 3.66e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2224332745 2 PDFLLPDLGEGLTEAAILTWHVNVGDTVKVDQIVVEVETAKAAVEVPVPFAGVVSALHGTPGQLLPVGAPLLSVGGFAEP 81
Cdd:TIGR01347 1 IEIKVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAILEEGNDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2224332745 82 GVTTSAGSGnvligygtaPSTRRKRVRRPEAPAPKAKAPGVISPFVRKLAADNGLDLAKVTASGADGIIRRADVEAALKK 161
Cdd:TIGR01347 81 TAAPPAKSG---------EEKEETPAASAAAAPTAAANRPSLSPAARRLAKEHGIDLSAVPGTGVTGRVTKEDIIKKTEA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2224332745 162 PVAKG------------------KRIPLTGVRKAVADKLTTSRREIPEATVWVDVDATGLVAARA----ALNAGTDRPVS 219
Cdd:TIGR01347 152 PASAQppaaaaaaaapaaatrpeERVKMTRLRQRIAERLKEAQNSTAMLTTFNEVDMSAVMELRKrykeEFEKKHGVKLG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2224332745 220 LLGLIARFAVAGLRKYPELNSRVEGDEIVVLDEIHLGFAAQTDRGLVVPVVRDAGALSTRDLSAAIGDRARTARDGKLAP 299
Cdd:TIGR01347 232 FMSFFVKAVVAALKRFPEVNAEIDGDDIVYKDYYDISVAVSTDRGLVVPVVRNADRMSFADIEKEIADLGKKARDGKLTL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2224332745 300 ADLTGGTFTVNNYGVFGVDGSAAIINHPEAAILGIGRIIDRPWVVDGALAVRKVCELTLAFDHRVCDGGTAGGFLRFVAD 379
Cdd:TIGR01347 312 EDMTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHGIKERPVAVNGQIEIRPMMYLALSYDHRLIDGKEAVTFLVTIKE 391
|
410
....*....|..
gi 2224332745 380 CVESPVTALGDL 391
Cdd:TIGR01347 392 LLEDPRRLLLDL 403
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
3-75 |
9.29e-25 |
|
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: 96.29 E-value: 9.29e-25
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2224332745 3 DFLLPDLGEGLTEAAILTWHVNVGDTVKVDQIVVEVETAKAAVEVPVPFAGVVSALHGTPGQLLPVGAPLLSV 75
Cdd:COG0508 4 EIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
3-72 |
5.11e-23 |
|
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: 91.31 E-value: 5.11e-23
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2224332745 3 DFLLPDLGEGLTEAAILTWHVNVGDTVKVDQIVVEVETAKAAVEVPVPFAGVVSALHGTPGQLLPVGAPL 72
Cdd:cd06849 2 EIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVI 71
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11856 |
PRK11856 |
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed |
1-388 |
2.19e-158 |
|
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
Pssm-ID: 237001 [Multi-domain] Cd Length: 411 Bit Score: 451.55 E-value: 2.19e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2224332745 1 MPDFLLPDLGEGLTEAAILTWHVNVGDTVKVDQIVVEVETAKAAVEVPVPFAGVVSALHGTPGQLLPVGAPLLSV---GG 77
Cdd:PRK11856 2 MFEFKMPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDVVPVGSVIAVIeeeGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2224332745 78 FAEPGVTTSAGSGNVLIGYGTAPSTRRKRVRRPEAPAPKAKAPGVISPFVRKLAADNGLDLAKVTASGADGIIRRADVEA 157
Cdd:PRK11856 82 AEAAAAAEAAPEAPAPEPAPAAAAAAAAAPAAAAAPAAPAAAAAKASPAVRKLARELGVDLSTVKGSGPGGRITKEDVEA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2224332745 158 ALKKPVAK------------------GKRIPLTGVRKAVADKLTTSRREIPEATVWVDVDATGLVAARAALNAGTDRpVS 219
Cdd:PRK11856 162 AAAAAAPAaaaaaaaaaappaaaaegEERVPLSGMRKAIAKRMVESKREIPHFTLTDEVDVTALLALRKQLKAIGVK-LT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2224332745 220 LLGLIARFAVAGLRKYPELNSRVEGDEIVVLDEIHLGFAAQTDRGLVVPVVRDAGALSTRDLSAAIGDRARTARDGKLAP 299
Cdd:PRK11856 241 VTDFLIKAVALALKKFPELNASWDDDAIVLKKYVNIGIAVATDGGLIVPVIRDADKKSLFELAREIKDLAEKAREGKLKP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2224332745 300 ADLTGGTFTVNNYGVFGVDGSAAIINHPEAAILGIGRIIDRPWVVDGALAVRKVCELTLAFDHRVCDGGTAGGFLRFVAD 379
Cdd:PRK11856 321 EELQGGTFTISNLGMFGGDYFTPIINPPEVAILGVGAIVERPVVVDGEIVVRKVMPLSLSFDHRVIDGADAARFLKALKE 400
|
....*....
gi 2224332745 380 CVESPVTAL 388
Cdd:PRK11856 401 LLENPALLL 409
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
3-384 |
1.25e-94 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 293.27 E-value: 1.25e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2224332745 3 DFLLPDLGEgLTEAAILTWHVNVGDTVKVDQIVVEVETAKAAVEVPVPFAGVVSALHGTPGQLLPVGAPLLSVGGFAEPG 82
Cdd:PRK11855 121 EVKVPDIGE-ITEVEVIEWLVKVGDTVEEDQSLITVETDKATMEIPSPVAGVVKEIKVKVGDKVSVGSLLVVIEVAAAAP 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2224332745 83 VTTSAGSGNVligygTAPSTRRKRVRRPEAPAPKAKAPGVI----------SPFVRKLAADNGLDLAKVTASGADGIIRR 152
Cdd:PRK11855 200 AAAAAPAAAA-----PAAAAAAAPAPAPAAAAAPAAAAPAAaaapgkaphaSPAVRRLARELGVDLSQVKGTGKKGRITK 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2224332745 153 ADVEAALKKPVAKGK-------------------------------RIPLTGVRKAVADKLTTSRREIPEATVWVDVDAT 201
Cdd:PRK11855 275 EDVQAFVKGAMSAAAaaaaaaaaagggglgllpwpkvdfskfgeieTKPLSRIKKISAANLHRSWVTIPHVTQFDEADIT 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2224332745 202 GLVAARAALNAGTDR---PVSLLGLIARFAVAGLRKYPELNSRV--EGDEIVVLDEIHLGFAAQTDRGLVVPVVRDAGAL 276
Cdd:PRK11855 355 DLEALRKQLKKEAEKagvKLTMLPFFIKAVVAALKEFPVFNASLdeDGDELTYKKYFNIGFAVDTPNGLVVPVIKDVDKK 434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2224332745 277 STRDLSAAIGDRARTARDGKLAPADLTGGTFTVNNYGVFGVDGSAAIINHPEAAILGIGRIIDRPWVVDGALAVRKVCEL 356
Cdd:PRK11855 435 SLLEIAREIAELAKKARDGKLKPDDMQGGCFTISSLGGIGGTAFTPIINAPEVAILGVGKSQMKPVWDGKEFVPRLMLPL 514
|
410 420
....*....|....*....|....*...
gi 2224332745 357 TLAFDHRVCDGGTAGGFLRFVADCVESP 384
Cdd:PRK11855 515 SLSYDHRVIDGATAARFTNYLKQLLADP 542
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
182-388 |
2.08e-85 |
|
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: 258.24 E-value: 2.08e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2224332745 182 LTTSRREIPEATVWVDVDATGLVAARAALN---AGTDRPVSLLGLIARFAVAGLRKYPELNSRVEGD--EIVVLDEIHLG 256
Cdd:pfam00198 1 MTESKQTIPHFTLTDEVDVTELLALREELKedaADEETKLTFLPFLVKAVALALKKFPELNASWDGEegEIVYKKYVNIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2224332745 257 FAAQTDRGLVVPVVRDAGALSTRDLSAAIGDRARTARDGKLAPADLTGGTFTVNNYGVFGVDGSAAIINHPEAAILGIGR 336
Cdd:pfam00198 81 IAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVGR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2224332745 337 IIDRPWVVDGALAVRKVCELTLAFDHRVCDGGTAGGFLRFVADCVESPVTAL 388
Cdd:pfam00198 161 IRKRPVVVDGEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELLL 212
|
|
| sucB |
TIGR01347 |
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ... |
2-391 |
3.66e-85 |
|
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: 264.67 E-value: 3.66e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2224332745 2 PDFLLPDLGEGLTEAAILTWHVNVGDTVKVDQIVVEVETAKAAVEVPVPFAGVVSALHGTPGQLLPVGAPLLSVGGFAEP 81
Cdd:TIGR01347 1 IEIKVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAILEEGNDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2224332745 82 GVTTSAGSGnvligygtaPSTRRKRVRRPEAPAPKAKAPGVISPFVRKLAADNGLDLAKVTASGADGIIRRADVEAALKK 161
Cdd:TIGR01347 81 TAAPPAKSG---------EEKEETPAASAAAAPTAAANRPSLSPAARRLAKEHGIDLSAVPGTGVTGRVTKEDIIKKTEA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2224332745 162 PVAKG------------------KRIPLTGVRKAVADKLTTSRREIPEATVWVDVDATGLVAARA----ALNAGTDRPVS 219
Cdd:TIGR01347 152 PASAQppaaaaaaaapaaatrpeERVKMTRLRQRIAERLKEAQNSTAMLTTFNEVDMSAVMELRKrykeEFEKKHGVKLG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2224332745 220 LLGLIARFAVAGLRKYPELNSRVEGDEIVVLDEIHLGFAAQTDRGLVVPVVRDAGALSTRDLSAAIGDRARTARDGKLAP 299
Cdd:TIGR01347 232 FMSFFVKAVVAALKRFPEVNAEIDGDDIVYKDYYDISVAVSTDRGLVVPVVRNADRMSFADIEKEIADLGKKARDGKLTL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2224332745 300 ADLTGGTFTVNNYGVFGVDGSAAIINHPEAAILGIGRIIDRPWVVDGALAVRKVCELTLAFDHRVCDGGTAGGFLRFVAD 379
Cdd:TIGR01347 312 EDMTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHGIKERPVAVNGQIEIRPMMYLALSYDHRLIDGKEAVTFLVTIKE 391
|
410
....*....|..
gi 2224332745 380 CVESPVTALGDL 391
Cdd:TIGR01347 392 LLEDPRRLLLDL 403
|
|
| PRK05704 |
PRK05704 |
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase; |
1-391 |
2.29e-84 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
Pssm-ID: 235571 [Multi-domain] Cd Length: 407 Bit Score: 262.46 E-value: 2.29e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2224332745 1 MPDFLLPDLGEGLTEAAILTWHVNVGDTVKVDQIVVEVETAKAAVEVPVPFAGVVSALHGTPGQLLPVGAPLlsvggfae 80
Cdd:PRK05704 2 MVEIKVPTLPESVTEATIATWHKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGDTVTVGQVL-------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2224332745 81 pGVTTSAGSGNVLIGYGTAPSTRRKRVRRPEAPAPKAKAPGVISPFVRKLAADNGLDLAKVTASGADGIIRRADVEAALK 160
Cdd:PRK05704 74 -GRIDEGAAAGAAAAAAAAAAAAAAAPAQAQAAAAAEQSNDALSPAARKLAAENGLDASAVKGTGKGGRVTKEDVLAALA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2224332745 161 KPVAKG--------------------KRIPLTGVRKAVADKLTTSRREIPEATVWVDVDATGLVAARAAL-NAGTDRPVS 219
Cdd:PRK05704 153 AAAAAPaapaaaapaaapaplgarpeERVPMTRLRKTIAERLLEAQNTTAMLTTFNEVDMTPVMDLRKQYkDAFEKKHGV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2224332745 220 LLGLIARF---AVAGLRKYPELNSRVEGDEIVVLDEIHLGFAAQTDRGLVVPVVRDAGALSTRDLSAAIGDRARTARDGK 296
Cdd:PRK05704 233 KLGFMSFFvkaVVEALKRYPEVNASIDGDDIVYHNYYDIGIAVGTPRGLVVPVLRDADQLSFAEIEKKIAELAKKARDGK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2224332745 297 LAPADLTGGTFTVNNYGVFGVDGSAAIINHPEAAILGIGRIIDRPWVVDGALAVRKVCELTLAFDHRVCDGGTAGGFLRF 376
Cdd:PRK05704 313 LSIEELTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHKIKERPVAVNGQIVIRPMMYLALSYDHRIIDGKEAVGFLVT 392
|
410
....*....|....*
gi 2224332745 377 VADCVESPVTALGDL 391
Cdd:PRK05704 393 IKELLEDPERLLLDL 407
|
|
| PTZ00144 |
PTZ00144 |
dihydrolipoamide succinyltransferase; Provisional |
6-391 |
1.28e-68 |
|
dihydrolipoamide succinyltransferase; Provisional
Pssm-ID: 240289 [Multi-domain] Cd Length: 418 Bit Score: 222.25 E-value: 1.28e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2224332745 6 LPDLGEGLTEAAILTWHVNVGDTVKVDQIVVEVETAKAAVEVPVPFAGVVSALHGTPGQLLPVGAPLLSVGGFAEPGVTT 85
Cdd:PTZ00144 49 VPTMGDSISEGTVVEWKKKVGDYVKEDEVICIIETDKVSVDIRAPASGVITKIFAEEGDTVEVGAPLSEIDTGGAPPAAA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2224332745 86 SAGSGNVligygTAPSTRRKRVRRPEAPAPKAKAPGVISPFVRKLAADngldlAKVTASGADGIIRRADVEaalkkpvak 165
Cdd:PTZ00144 129 PAAAAAA-----KAEKTTPEKPKAAAPTPEPPAASKPTPPAAAKPPEP-----APAAKPPPTPVARADPRE--------- 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2224332745 166 gKRIPLTGVRKAVADKLTTSRREIPEATVWVDVDATGLVAARAALNAGTDRPVSL-LGLIARF---AVAGLRKYPELNSR 241
Cdd:PTZ00144 190 -TRVPMSRMRQRIAERLKASQNTCAMLTTFNECDMSALMELRKEYKDDFQKKHGVkLGFMSAFvkaSTIALKKMPIVNAY 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2224332745 242 VEGDEIVVLDEIHLGFAAQTDRGLVVPVVRDAGALSTRDLSAAIGDRARTARDGKLAPADLTGGTFTVNNYGVFGVDGSA 321
Cdd:PTZ00144 269 IDGDEIVYRNYVDISVAVATPTGLVVPVIRNCENKSFAEIEKELADLAEKARNNKLTLEDMTGGTFTISNGGVFGSLMGT 348
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2224332745 322 AIINHPEAAILGIGRIIDRPWVVDGALAVRKVCELTLAFDHRVCDGGTAGGFLRFVADCVESPVTALGDL 391
Cdd:PTZ00144 349 PIINPPQSAILGMHAIKKRPVVVGNEIVIRPIMYLALTYDHRLIDGRDAVTFLKKIKDLIEDPARMLLDL 418
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
3-382 |
1.00e-63 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 214.87 E-value: 1.00e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2224332745 3 DFLLPDLGegLTEAAILTWHVNVGDTVKVDQIVVEVETAKAAVEVPVPFAGVVSALHGTPGQLLPVGAPLLSVGgfaepg 82
Cdd:PRK11854 208 DVNVPDIG--GDEVEVTEVMVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVKTGSLIMRFE------ 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2224332745 83 VTTSAGSGNVLIGYGTAPSTRRKRVRRPeAPAPKAKAPGV-----------ISPFVRKLAADNGLDLAKVTASGADGIIR 151
Cdd:PRK11854 280 VEGAAPAAAPAKQEAAAPAPAAAKAEAP-AAAPAAKAEGKsefaendayvhATPLVRRLAREFGVNLAKVKGTGRKGRIL 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2224332745 152 RADVEAALKKPVAKGKR------------------------------IPLTGVRKAVADKLTTSRREIPEATVWVDVDAT 201
Cdd:PRK11854 359 KEDVQAYVKDAVKRAEAapaaaaaggggpgllpwpkvdfskfgeieeVELGRIQKISGANLHRNWVMIPHVTQFDKADIT 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2224332745 202 GLVAARAALNA-----GTDRPVSLLGLIARFAVAGLRKYPELNSRV--EGDEIVVLDEIHLGFAAQTDRGLVVPVVRDAG 274
Cdd:PRK11854 439 ELEAFRKQQNAeaekrKLGVKITPLVFIMKAVAAALEQMPRFNSSLseDGQRLTLKKYVNIGIAVDTPNGLVVPVFKDVN 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2224332745 275 ALSTRDLSAAIGDRARTARDGKLAPADLTGGTFTVNNYGVFGVDGSAAIINHPEAAILGIGRIIDRPwVVDG-ALAVRKV 353
Cdd:PRK11854 519 KKGIIELSRELMDISKKARDGKLTAGDMQGGCFTISSIGGLGTTHFTPIVNAPEVAILGVSKSAMEP-VWNGkEFAPRLM 597
|
410 420
....*....|....*....|....*....
gi 2224332745 354 CELTLAFDHRVCDGGTAGGFLRFVADCVE 382
Cdd:PRK11854 598 LPLSLSYDHRVIDGADGARFITIINDRLS 626
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
6-388 |
2.34e-59 |
|
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: 201.26 E-value: 2.34e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2224332745 6 LPDLGeGLTEAAILTWHVNVGDTVKVDQIVVEVETAKAAVEVPVPFAGVVSALHGTPGQLLPVGAPL--LSVGGFAEPGV 83
Cdd:TIGR01348 121 VPDIG-DIEKVTVIEVLVKVGDTVSADQSLITLESDKASMEVPAPASGVVKSVKVKVGDSVPTGDLIltLSVAGSTPATA 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2224332745 84 TTSAGSgnvligYGTAPSTRRKRVRRPEAPA-PKAKAPGVI-------------SPFVRKLAADNGLDLAKVTASGADGI 149
Cdd:TIGR01348 200 PAPASA------QPAAQSPAATQPEPAAAPAaAKAQAPAPQqagtqnpakvdhaAPAVRRLAREFGVDLSAVKGTGIKGR 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2224332745 150 IRRADVEAALKKPVAKGK----------------------------RIPLTGVRKAVADKLTTSRREIPEATVWVDVDAT 201
Cdd:TIGR01348 274 ILREDVQRFVKEPSVRAQaaaasaaggapgalpwpnvdfskfgeveEVDMSRIRKISGANLTRNWTMIPHVTHFDKADIT 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2224332745 202 GLVAARAALNAG---TDRPVSLLGLIARFAVAGLRKYPELNSRV-EGDEIVVLDE-IHLGFAAQTDRGLVVPVVRDAGAL 276
Cdd:TIGR01348 354 EMEAFRKQQNAAvekEGVKLTVLHILMKAVAAALKKFPKFNASLdLGGEQLILKKyVNIGVAVDTPNGLLVPVIKDVDRK 433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2224332745 277 STRDLSAAIGDRARTARDGKLAPADLTGGTFTVNNYGVFGVDGSAAIINHPEAAILGIGRIIDRPwVVDG-ALAVRKVCE 355
Cdd:TIGR01348 434 GITELALELSDLAKKARDGKLTPDEMQGACFTISSLGGIGGTAFTPIVNAPEVAILGVSKSGMEP-VWNGkEFEPRLMLP 512
|
410 420 430
....*....|....*....|....*....|...
gi 2224332745 356 LTLAFDHRVCDGGTAGGFLRFVADCVESPVTAL 388
Cdd:TIGR01348 513 LSLSYDHRVIDGADAARFTTYICESLADIRRLL 545
|
|
| PLN02528 |
PLN02528 |
2-oxoisovalerate dehydrogenase E2 component |
4-384 |
6.93e-55 |
|
2-oxoisovalerate dehydrogenase E2 component
Pssm-ID: 215289 [Multi-domain] Cd Length: 416 Bit Score: 186.46 E-value: 6.93e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2224332745 4 FLLPDLGEGLTEAAILTWHVNVGDTVKVDQIVVEVETAKAAVEVPVPFAGVVSALHGTPGQLLPVGAPLLSVggfaepgv 83
Cdd:PLN02528 1 VPLAQTGEGIAECELLRWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGKVAQINFSPGDIVKVGETLLKI-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2224332745 84 ttSAGSGNVLIGYGTAPST-RRKRVRRPEAPAPKAKAPGVIS-PFVRKLAADNGLDLAKVTASGADGIIRRADVeaaLKK 161
Cdd:PLN02528 73 --MVEDSQHLRSDSLLLPTdSSNIVSLAESDERGSNLSGVLStPAVRHLAKQYGIDLNDILGTGKDGRVLKEDV---LKY 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2224332745 162 PVAKG---------------------------------KRIPLTGVRKAVAdKLTTSRREIPEaTVWVD---VDAtgLVA 205
Cdd:PLN02528 148 AAQKGvvkdsssaeeatiaeqeefstsvstpteqsyedKTIPLRGFQRAMV-KTMTAAAKVPH-FHYVEeinVDA--LVE 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2224332745 206 ARAALNAGTDRPVSLLGLIARFAVA---GLRKYPELNSRVEGD--EIVVLDEIHLGFAAQTDRGLVVPVVRDAGALSTRD 280
Cdd:PLN02528 224 LKASFQENNTDPTVKHTFLPFLIKSlsmALSKYPLLNSCFNEEtsEIRLKGSHNIGVAMATEHGLVVPNIKNVQSLSLLE 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2224332745 281 LSAAIGDRARTARDGKLAPADLTGGTFTVNNYGVFGVDGSAAIINHPEAAILGIGRIIDRPWVVD-GALAVRKVCELTLA 359
Cdd:PLN02528 304 ITKELSRLQHLAAENKLNPEDITGGTITLSNIGAIGGKFGSPVLNLPEVAIIALGRIQKVPRFVDdGNVYPASIMTVTIG 383
|
410 420
....*....|....*....|....*
gi 2224332745 360 FDHRVCDGGTAGGFLRFVADCVESP 384
Cdd:PLN02528 384 ADHRVLDGATVARFCNEWKSYVEKP 408
|
|
| PLN02744 |
PLN02744 |
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex |
6-388 |
9.99e-53 |
|
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
Pssm-ID: 215397 [Multi-domain] Cd Length: 539 Bit Score: 183.52 E-value: 9.99e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2224332745 6 LPDLGEGLTEAAILTWHVNVGDTVKVDQIVVEVETAKAAVEVPVPFAGVVSA-LHGTPGQLLPVGAPLL-------SVGG 77
Cdd:PLN02744 117 MPSLSPTMTEGNIARWLKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKiVKGDGAKEIKVGEVIAitveeeeDIGK 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2224332745 78 FAEPGVTTSAGSGNVLIGYGTAPSTR---RKRVRRPEAPAPKAKAPG------VISPFVRKLAADNGLDLAKVTASGADG 148
Cdd:PLN02744 197 FKDYKPSSSAAPAAPKAKPSPPPPKEeevEKPASSPEPKASKPSAPPssgdriFASPLARKLAEDNNVPLSSIKGTGPDG 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2224332745 149 IIRRADVEAALKKPVAKGKR---------------IPLTGVRKAVADKLTTSRREIPEATVWVDVDATGLVAARAALNAG 213
Cdd:PLN02744 277 RIVKADIEDYLASGGKGATAppstdskapaldytdIPNTQIRKVTASRLLQSKQTIPHYYLTVDTRVDKLMALRSQLNSL 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2224332745 214 TD----RPVSLLGLIARFAVAGLRKYPELNSRVEGDEIVVLDEIHLGFAAQTDRGLVVPVVRDAGALSTRDLSAAIGDRA 289
Cdd:PLN02744 357 QEasggKKISVNDLVIKAAALALRKVPQCNSSWTDDYIRQYHNVNINVAVQTENGLYVPVVKDADKKGLSTIAEEVKQLA 436
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2224332745 290 RTARDGKLAPADLTGGTFTVNNY-GVFGVDGSAAIINHPEAAILGIG----RIIdrPWVVDGALAVRKVCELTLAFDHRV 364
Cdd:PLN02744 437 QKARENSLKPEDYEGGTFTVSNLgGPFGIKQFCAIINPPQSAILAVGsaekRVI--PGSGPDQYNFASFMSVTLSCDHRV 514
|
410 420
....*....|....*....|....
gi 2224332745 365 CDGGTAGGFLRFVADCVESPVTAL 388
Cdd:PLN02744 515 IDGAIGAEWLKAFKGYIENPESML 538
|
|
| PLN02226 |
PLN02226 |
2-oxoglutarate dehydrogenase E2 component |
5-391 |
4.22e-52 |
|
2-oxoglutarate dehydrogenase E2 component
Pssm-ID: 177871 [Multi-domain] Cd Length: 463 Bit Score: 180.34 E-value: 4.22e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2224332745 5 LLPDLGEGLTEAAILTWHVNVGDTVKVDQIVVEVETAKAAVEVPVPFAGVVSALhgtpgqllpvgapLLSVGGFAEPGVT 84
Cdd:PLN02226 95 VVPHMGESITDGTLATFLKKPGERVQADEAIAQIETDKVTIDIASPASGVIQEF-------------LVKEGDTVEPGTK 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2224332745 85 TSAGSGNVLIGYGTAPSTRRkrvrrPEAPAPKAKAPgviSPFVRKLAADNGLDLAKVTASGADGIIRRADVEAALKkPVA 164
Cdd:PLN02226 162 VAIISKSEDAASQVTPSQKI-----PETTDPKPSPP---AEDKQKPKVESAPVAEKPKAPSSPPPPKQSAKEPQLP-PKE 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2224332745 165 KGKRIPLTGVRKAVADKLTTSRREIPEATVWVDVDATGLVAARAAL-NAGTDRPVSLLGLIARF---AVAGLRKYPELNS 240
Cdd:PLN02226 233 RERRVPMTRLRKRVATRLKDSQNTFALLTTFNEVDMTNLMKLRSQYkDAFYEKHGVKLGLMSGFikaAVSALQHQPVVNA 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2224332745 241 RVEGDEIVVLDEIHLGFAAQTDRGLVVPVVRDAGALSTRDLSAAIGDRARTARDGKLAPADLTGGTFTVNNYGVFGVDGS 320
Cdd:PLN02226 313 VIDGDDIIYRDYVDISIAVGTSKGLVVPVIRGADKMNFAEIEKTINGLAKKANEGTISIDEMAGGSFTVSNGGVYGSLIS 392
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2224332745 321 AAIINHPEAAILGIGRIIDRPWVVDGALAVRKVCELTLAFDHRVCDGGTAGGFLRFVADCVESPVTALGDL 391
Cdd:PLN02226 393 TPIINPPQSAILGMHSIVSRPMVVGGSVVPRPMMYVALTYDHRLIDGREAVYFLRRVKDVVEDPQRLLLDI 463
|
|
| PRK14843 |
PRK14843 |
dihydrolipoamide acetyltransferase; Provisional |
106-388 |
8.68e-50 |
|
dihydrolipoamide acetyltransferase; Provisional
Pssm-ID: 184847 [Multi-domain] Cd Length: 347 Bit Score: 171.24 E-value: 8.68e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2224332745 106 RVRRPEAPAPKAKAPGVISPFVRKLAADNGLDLAKVTASGADGIIRRADVEAALKKPV---------------------- 163
Cdd:PRK14843 34 RVHKEDVETYKDTNVVRISPLAKRIALEHNIAWQEIQGTGHRGKIMKKDVLALLPENIendsikspaqiekveevpdnvt 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2224332745 164 --AKGKRIPLTGVRKAVADKLTTSRREIPEATVWVDVDATGLVAARAAL----NAGTDRPVSLLGLIARFAVAGLRKYPE 237
Cdd:PRK14843 114 pyGEIERIPMTPMRKVIAQRMVESYLTAPTFTLNYEVDMTEMLALRKKVlepiMEATGKKTTVTDLLSLAVVKTLMKHPY 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2224332745 238 LNSRV--EGDEIVVLDEIHLGFAAQTDRGLVVPVVRDAGALSTRDLSAAIGDRARTARDGKLAPADLTGGTFTVNNYGVF 315
Cdd:PRK14843 194 INASLteDGKTIITHNYVNLAMAVGMDNGLMTPVVYNAEKMSLSELVVAFKDVIGRTLDGKLAPSELQNSTFTISNLGMF 273
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2224332745 316 GVDGSAAIINHPEAAILGIGRIIDRPWVVDGALAVRKVCELTLAFDHRVCDGGTAGGFLRFVADCVESPVTAL 388
Cdd:PRK14843 274 GVQSFGPIINQPNSAILGVSSTIEKPVVVNGEIVIRPIMSLGLTIDHRVVDGMAGAKFMKDLKELIETPISML 346
|
|
| PRK11857 |
PRK11857 |
dihydrolipoamide acetyltransferase; Reviewed |
123-384 |
1.47e-44 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237002 [Multi-domain] Cd Length: 306 Bit Score: 156.11 E-value: 1.47e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2224332745 123 ISPFVRKLAADNGLDLAKVTASGADGIIRRADVEAALKKPVA-----------------------------KGKRIPLTG 173
Cdd:PRK11857 4 ATPIARALAKKLGIDISLLKGSGRDGKILAEDVENFIKSLKSaptpaeaasvssaqqaaktaapaaappklEGKREKVAP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2224332745 174 VRKAVADKLTTSRREIPEATVWVDVDATGLVAARA----ALNAGTDRPVSLLGLIARFAVAGLRKYPELNSRVE--GDEI 247
Cdd:PRK11857 84 IRKAIARAMTNSWSNVAYVNLVNEIDMTKLWDLRKsvkdPVLKTEGVKLTFLPFIAKAILIALKEFPIFAAKYDeaTSEL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2224332745 248 VVLDEIHLGFAAQTDRGLVVPVVRDAGALSTRDLSAAIGDRARTARDGKLAPADLTGGTFTVNNYGVFGVDGSAAIINHP 327
Cdd:PRK11857 164 VYPDTLNLGIAVDTEAGLMVPVIKNAQKLSIVEIAKEISRLAKAARERKIKPDEMKGGSFTITNYGSVGSLYGVPVINYP 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 2224332745 328 EAAILGIGRIIDRPWVVDGALAVRKVCELTLAFDHRVCDGGTAGGFLRFVADCVESP 384
Cdd:PRK11857 244 ELAIAGVGAIIDKAIVKNGQIVAGKVMHLTVAADHRWIDGATIGRFASRVKELLEKP 300
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
3-75 |
9.29e-25 |
|
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: 96.29 E-value: 9.29e-25
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2224332745 3 DFLLPDLGEGLTEAAILTWHVNVGDTVKVDQIVVEVETAKAAVEVPVPFAGVVSALHGTPGQLLPVGAPLLSV 75
Cdd:COG0508 4 EIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
|
|
| kgd |
PRK12270 |
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ... |
79-377 |
4.84e-23 |
|
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;
Pssm-ID: 237030 [Multi-domain] Cd Length: 1228 Bit Score: 101.51 E-value: 4.84e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2224332745 79 AEPGVTTSAGSGNVLIGYGTAPSTRRKRVRRPEAPAPKAKAPGVISPFVRKLAAdngldlakvTASGADGIIRRADVEAA 158
Cdd:PRK12270 38 PGSTAAPTAAAAAAAAAASAPAAAPAAKAPAAPAPAPPAAAAPAAPPKPAAAAA---------AAAAPAAPPAAAAAAAP 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2224332745 159 LKKPVAKGkRIPLTGVRKAVADKLTTSRrEIPEATVWVDVDATGLVAARAALNAGTDR----PVSLLGLIARFAVAGLRK 234
Cdd:PRK12270 109 AAAAVEDE-VTPLRGAAAAVAKNMDASL-EVPTATSVRAVPAKLLIDNRIVINNHLKRtrggKVSFTHLIGYALVQALKA 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2224332745 235 YPELN---SRVEGDEIVVLDE-IHLGFA---AQTD--RGLVVPVVRDAGALSTRDLSAAIGDRARTARDGKLAPADLTGG 305
Cdd:PRK12270 187 FPNMNrhyAEVDGKPTLVTPAhVNLGLAidlPKKDgsRQLVVPAIKGAETMDFAQFWAAYEDIVRRARDGKLTADDFQGT 266
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2224332745 306 TFTVNNYGVFGVDGSAAIINHPEAAILGIGRiIDRPWVVDGA-------LAVRKVCELTLAFDHRVCDGGTAGGFLRFV 377
Cdd:PRK12270 267 TISLTNPGGIGTVHSVPRLMKGQGAIIGVGA-MEYPAEFQGAseerlaeLGISKVMTLTSTYDHRIIQGAESGEFLRTI 344
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
3-72 |
5.11e-23 |
|
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: 91.31 E-value: 5.11e-23
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2224332745 3 DFLLPDLGEGLTEAAILTWHVNVGDTVKVDQIVVEVETAKAAVEVPVPFAGVVSALHGTPGQLLPVGAPL 72
Cdd:cd06849 2 EIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVI 71
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
2-73 |
4.13e-14 |
|
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: 66.85 E-value: 4.13e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2224332745 2 PDFLLPDLGEGLTEAaILTWHVNVGDTVKVDQIVVEVETAKAAVEVPVPFAGVVSALHGTPGQLLPVGAPLL 73
Cdd:pfam00364 1 TEIKSPMIGESVREG-VVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLA 71
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
5-72 |
1.01e-10 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 62.65 E-value: 1.01e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2224332745 5 LLPDLGEGLTEAAILTWHVNVGDTVKVDQIVVEVETAKAAVEVPVPFAGVVSALHGTPGQLLPVGAPL 72
Cdd:PRK14875 6 TMPKWGLSMTEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGETLPVGALL 73
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
3-72 |
1.19e-08 |
|
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases, and the H-protein of the glycine cleavage system (GCS). These domains transport CO2, acyl, or methylamine, respectively, between components of the complex/protein via a biotinyl or lipoyl group, which is covalently attached to a highly conserved lysine residue.
Pssm-ID: 133456 [Multi-domain] Cd Length: 73 Bit Score: 51.29 E-value: 1.19e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2224332745 3 DFLLPDLGEGLTEAAILTWHVNVGDTVKVDQIVVEVETAKAAVEVPVPFAGVVSALHGTPGQLLPVGAPL 72
Cdd:cd06663 1 TILIPDLAQHLGDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKVEGDTPL 70
|
|
| E3_binding |
pfam02817 |
e3 binding domain; This family represents a small domain of the E2 subunit of 2-oxo-acid ... |
123-156 |
1.84e-08 |
|
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: 49.61 E-value: 1.84e-08
10 20 30
....*....|....*....|....*....|....
gi 2224332745 123 ISPFVRKLAADNGLDLAKVTASGADGIIRRADVE 156
Cdd:pfam02817 3 ASPAARKLARELGIDLSDVKGTGPGGRITKEDVE 36
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
18-75 |
1.07e-07 |
|
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: 48.57 E-value: 1.07e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 2224332745 18 ILTWHVNVGDTVKVDQIVVEVETAKAAVEVPVPFAGVVSALHGTPGQLLPVGAPLLSV 75
Cdd:cd06850 10 VVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| AccB |
COG0511 |
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ... |
23-76 |
8.57e-06 |
|
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440277 [Multi-domain] Cd Length: 136 Bit Score: 44.89 E-value: 8.57e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 2224332745 23 VNVGDTVKVDQIVVEVETAKAAVEVPVPFAGVVSALHGTPGQLLPVGAPLLSVG 76
Cdd:COG0511 83 VKVGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVVEILVENGQPVEYGQPLFVIE 136
|
|
| PRK06549 |
PRK06549 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
18-76 |
3.61e-04 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235826 [Multi-domain] Cd Length: 130 Bit Score: 40.18 E-value: 3.61e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 2224332745 18 ILTWHVNVGDTVKVDQIVVEVETAKAAVEVPVPFAGVVSALHGTPGQLLPVGAPLLSVG 76
Cdd:PRK06549 72 ILKVLVAVGDQVTENQPLLILEAMKMENEIVASSAGTVTAIHVTPGQVVNPGDGLITIG 130
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
1-124 |
4.18e-04 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 42.21 E-value: 4.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2224332745 1 MP-DFLLPDLGEGLTEAAILTWHVNVGDTVKVDQIVVEVETAKAAVEVPVPFAGVVSAL---HGTPGqlLPVGAP---LL 73
Cdd:PRK11892 1 MAiEILMPALSPTMEEGTLAKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKIlvpEGTEG--VKVNTPiavLL 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 2224332745 74 SVGGFAEPGVTTSAGSGNVLIGYGTAPSTRRKRVRRPEAPAPKAKAPGVIS 124
Cdd:PRK11892 79 EEGESASDAGAAPAAAAEAAAAAPAAAAAAAAKKAAPAPAAPAAPAAEVAA 129
|
|
| GcvH |
COG0509 |
Glycine cleavage system protein H (lipoate-binding) [Amino acid transport and metabolism]; ... |
25-65 |
7.61e-04 |
|
Glycine cleavage system protein H (lipoate-binding) [Amino acid transport and metabolism]; Glycine cleavage system protein H (lipoate-binding) is part of the Pathway/BioSystem: Glycine cleavage
Pssm-ID: 440275 Cd Length: 128 Bit Score: 39.34 E-value: 7.61e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 2224332745 25 VGDTVKVDQIVVEVETAKAAVEVPVPFAGVV----SALHGTPGQL 65
Cdd:COG0509 47 VGTEVEAGEPFGVVESVKAVSDLYAPVSGEVvevnEALEDDPELV 91
|
|
| PRK09282 |
PRK09282 |
pyruvate carboxylase subunit B; Validated |
23-77 |
9.64e-04 |
|
pyruvate carboxylase subunit B; Validated
Pssm-ID: 236449 [Multi-domain] Cd Length: 592 Bit Score: 41.37 E-value: 9.64e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 2224332745 23 VNVGDTVKVDQIVVEVETAKAAVEVPVPFAGVVSALHGTPGQLLPVGAPLLSVGG 77
Cdd:PRK09282 538 VKEGDKVKAGDTVLVLEAMKMENEIQAPVDGTVKEILVKEGDRVNPGDVLMEIEP 592
|
|
| PRK14042 |
PRK14042 |
pyruvate carboxylase subunit B; Provisional |
16-66 |
3.03e-03 |
|
pyruvate carboxylase subunit B; Provisional
Pssm-ID: 172536 [Multi-domain] Cd Length: 596 Bit Score: 39.70 E-value: 3.03e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 2224332745 16 AAILTWHVNVGDTVKVDQIVVEVETAKAAVEVPVPFAGVVSAL------HGTPGQLL 66
Cdd:PRK14042 534 GSIIAIHVSAGDEVKAGQAVLVIEAMKMETEIKAPANGVVAEIlcqkgdKVTPGQVL 590
|
|
| |
