|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05704 |
PRK05704 |
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase; |
112-505 |
0e+00 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
Pssm-ID: 235571 [Multi-domain] Cd Length: 407 Bit Score: 668.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550952243 112 IDAKVPVMGESVAEGQVGQWLVQPGEAVEQDQALLEIETDKVAVEVPAPAAGVLEEQLVAEGDTVTPDQVIGKIRAGASA 191
Cdd:PRK05704 3 VEIKVPTLPESVTEATIATWHKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGDTVTVGQVLGRIDEGAAA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550952243 192 SA--------APKSEDAPKAAASSSSSGGDAKAMPSANRVASENNLDLSKVEGTGKDGRVTKGDALKAVQSGGTASA--P 261
Cdd:PRK05704 83 GAaaaaaaaaAAAAAAPAQAQAAAAAEQSNDALSPAARKLAAENGLDASAVKGTGKGGRVTKEDVLAALAAAAAAPAapA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550952243 262 AAEKSSKPRDTGPR-EERVKMTRLRQTIARRLKDAQNSAAMLTTYNEADMSAIMSLRKEIQDDFVAKHGVKLGFMSFFVK 340
Cdd:PRK05704 163 AAAPAAAPAPLGARpEERVPMTRLRKTIAERLLEAQNTTAMLTTFNEVDMTPVMDLRKQYKDAFEKKHGVKLGFMSFFVK 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550952243 341 ACVAALKDVPAVNAEIDGTDIIYKNYYDMGVAVGTDRGLVVPVVRDADDLSLAGVEKSIMDLGKRARDGKLGIDDMQGAS 420
Cdd:PRK05704 243 AVVEALKRYPEVNASIDGDDIVYHNYYDIGIAVGTPRGLVVPVLRDADQLSFAEIEKKIAELAKKARDGKLSIEELTGGT 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550952243 421 FTISNGGVYGSLLSSPILNAPQSGILGMHKIQERPVAINGEVKIRPMMYLALSYDHRIVDGKEAVTFLVRVKESLENPQR 500
Cdd:PRK05704 323 FTITNGGVFGSLMSTPIINPPQSAILGMHKIKERPVAVNGQIVIRPMMYLALSYDHRIIDGKEAVGFLVTIKELLEDPER 402
|
....*
gi 550952243 501 LLLDI 505
Cdd:PRK05704 403 LLLDL 407
|
|
| sucB |
TIGR01347 |
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ... |
112-505 |
0e+00 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This model describes the TCA cycle 2-oxoglutarate system E2 component, dihydrolipoamide succinyltransferase. It is closely related to the pyruvate dehydrogenase E2 component, dihydrolipoamide acetyltransferase. The seed for this model includes mitochondrial and Gram-negative bacterial forms. Mycobacterial candidates are highly derived, differ in having and extra copy of the lipoyl-binding domain at the N-terminus. They score below the trusted cutoff, but above the noise cutoff and above all examples of dihydrolipoamide acetyltransferase. [Energy metabolism, TCA cycle]
Pssm-ID: 273565 [Multi-domain] Cd Length: 403 Bit Score: 584.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550952243 112 IDAKVPVMGESVAEGQVGQWLVQPGEAVEQDQALLEIETDKVAVEVPAPAAGVLEEQLVAEGDTVTPDQVIGKIRAGASA 191
Cdd:TIGR01347 1 IEIKVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAILEEGNDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550952243 192 SAAPKSEDAPK--------AAASSSSSGGDAKAMPSANRVASENNLDLSKVEGTGKDGRVTKGDALKAVQSGGTASAPAA 263
Cdd:TIGR01347 81 TAAPPAKSGEEkeetpaasAAAAPTAAANRPSLSPAARRLAKEHGIDLSAVPGTGVTGRVTKEDIIKKTEAPASAQPPAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550952243 264 EKSSKPRDTGPR-EERVKMTRLRQTIARRLKDAQNSAAMLTTYNEADMSAIMSLRKEIQDDFVAKHGVKLGFMSFFVKAC 342
Cdd:TIGR01347 161 AAAAAAPAAATRpEERVKMTRLRQRIAERLKEAQNSTAMLTTFNEVDMSAVMELRKRYKEEFEKKHGVKLGFMSFFVKAV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550952243 343 VAALKDVPAVNAEIDGTDIIYKNYYDMGVAVGTDRGLVVPVVRDADDLSLAGVEKSIMDLGKRARDGKLGIDDMQGASFT 422
Cdd:TIGR01347 241 VAALKRFPEVNAEIDGDDIVYKDYYDISVAVSTDRGLVVPVVRNADRMSFADIEKEIADLGKKARDGKLTLEDMTGGTFT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550952243 423 ISNGGVYGSLLSSPILNAPQSGILGMHKIQERPVAINGEVKIRPMMYLALSYDHRIVDGKEAVTFLVRVKESLENPQRLL 502
Cdd:TIGR01347 321 ITNGGVFGSLMSTPIINPPQSAILGMHGIKERPVAVNGQIEIRPMMYLALSYDHRLIDGKEAVTFLVTIKELLEDPRRLL 400
|
...
gi 550952243 503 LDI 505
Cdd:TIGR01347 401 LDL 403
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
292-502 |
3.55e-93 |
|
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to three copies of a lipoyl binding domain followed by the catalytic domain.
Pssm-ID: 425518 [Multi-domain] Cd Length: 212 Bit Score: 282.12 E-value: 3.55e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550952243 292 LKDAQNSAAMLTTYNEADMSAIMSLRKEIQDDFvAKHGVKLGFMSFFVKACVAALKDVPAVNAEIDGTD--IIYKNYYDM 369
Cdd:pfam00198 1 MTESKQTIPHFTLTDEVDVTELLALREELKEDA-ADEETKLTFLPFLVKAVALALKKFPELNASWDGEEgeIVYKKYVNI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550952243 370 GVAVGTDRGLVVPVVRDADDLSLAGVEKSIMDLGKRARDGKLGIDDMQGASFTISNGGVYGSLLSSPILNAPQSGILGMH 449
Cdd:pfam00198 80 GIAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVG 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 550952243 450 KIQERPVAINGEVKIRPMMYLALSYDHRIVDGKEAVTFLVRVKESLENPQRLL 502
Cdd:pfam00198 160 RIRKRPVVVDGEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELLL 212
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
2-75 |
4.53e-29 |
|
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: 109.03 E-value: 4.53e-29
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 550952243 2 TEITVPTLGESVTEATVGEWQVSEGDAVKKDDILVELETDKVSVEVRAEEDGVLSKIVAQEGDTVEIGATLAEL 75
Cdd:cd06849 1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
1-75 |
1.01e-28 |
|
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: 108.23 E-value: 1.01e-28
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 550952243 1 MTEITVPTLGESVTEATVGEWQVSEGDAVKKDDILVELETDKVSVEVRAEEDGVLSKIVAQEGDTVEIGATLAEL 75
Cdd:COG0508 2 AIEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
112-185 |
6.65e-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: 103.25 E-value: 6.65e-27
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 550952243 112 IDAKVPVMGESVAEGQVGQWLVQPGEAVEQDQALLEIETDKVAVEVPAPAAGVLEEQLVAEGDTVTPDQVIGKI 185
Cdd:cd06849 1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
112-185 |
8.00e-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: 8.00e-27
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 550952243 112 IDAKVPVMGESVAEGQVGQWLVQPGEAVEQDQALLEIETDKVAVEVPAPAAGVLEEQLVAEGDTVTPDQVIGKI 185
Cdd:COG0508 3 IEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
2-83 |
8.00e-19 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 88.08 E-value: 8.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550952243 2 TEITVPTLGESVTEATVGEWQVSEGDAVKKDDILVELETDKVSVEVRAEEDGVLSKIVAQEGDTVEIGATLAELGAGGGA 81
Cdd:PRK14875 3 TPITMPKWGLSMTEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGETLPVGALLAVVADAEVS 82
|
..
gi 550952243 82 SA 83
Cdd:PRK14875 83 DA 84
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
2-75 |
4.50e-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: 4.50e-17
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 550952243 2 TEITVPTLGESVTEATVgEWQVSEGDAVKKDDILVELETDKVSVEVRAEEDGVLSKIVAQEGDTVEIGATLAEL 75
Cdd:pfam00364 1 TEIKSPMIGESVREGVV-EWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05704 |
PRK05704 |
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase; |
112-505 |
0e+00 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
Pssm-ID: 235571 [Multi-domain] Cd Length: 407 Bit Score: 668.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550952243 112 IDAKVPVMGESVAEGQVGQWLVQPGEAVEQDQALLEIETDKVAVEVPAPAAGVLEEQLVAEGDTVTPDQVIGKIRAGASA 191
Cdd:PRK05704 3 VEIKVPTLPESVTEATIATWHKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGDTVTVGQVLGRIDEGAAA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550952243 192 SA--------APKSEDAPKAAASSSSSGGDAKAMPSANRVASENNLDLSKVEGTGKDGRVTKGDALKAVQSGGTASA--P 261
Cdd:PRK05704 83 GAaaaaaaaaAAAAAAPAQAQAAAAAEQSNDALSPAARKLAAENGLDASAVKGTGKGGRVTKEDVLAALAAAAAAPAapA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550952243 262 AAEKSSKPRDTGPR-EERVKMTRLRQTIARRLKDAQNSAAMLTTYNEADMSAIMSLRKEIQDDFVAKHGVKLGFMSFFVK 340
Cdd:PRK05704 163 AAAPAAAPAPLGARpEERVPMTRLRKTIAERLLEAQNTTAMLTTFNEVDMTPVMDLRKQYKDAFEKKHGVKLGFMSFFVK 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550952243 341 ACVAALKDVPAVNAEIDGTDIIYKNYYDMGVAVGTDRGLVVPVVRDADDLSLAGVEKSIMDLGKRARDGKLGIDDMQGAS 420
Cdd:PRK05704 243 AVVEALKRYPEVNASIDGDDIVYHNYYDIGIAVGTPRGLVVPVLRDADQLSFAEIEKKIAELAKKARDGKLSIEELTGGT 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550952243 421 FTISNGGVYGSLLSSPILNAPQSGILGMHKIQERPVAINGEVKIRPMMYLALSYDHRIVDGKEAVTFLVRVKESLENPQR 500
Cdd:PRK05704 323 FTITNGGVFGSLMSTPIINPPQSAILGMHKIKERPVAVNGQIVIRPMMYLALSYDHRIIDGKEAVGFLVTIKELLEDPER 402
|
....*
gi 550952243 501 LLLDI 505
Cdd:PRK05704 403 LLLDL 407
|
|
| sucB |
TIGR01347 |
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ... |
112-505 |
0e+00 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This model describes the TCA cycle 2-oxoglutarate system E2 component, dihydrolipoamide succinyltransferase. It is closely related to the pyruvate dehydrogenase E2 component, dihydrolipoamide acetyltransferase. The seed for this model includes mitochondrial and Gram-negative bacterial forms. Mycobacterial candidates are highly derived, differ in having and extra copy of the lipoyl-binding domain at the N-terminus. They score below the trusted cutoff, but above the noise cutoff and above all examples of dihydrolipoamide acetyltransferase. [Energy metabolism, TCA cycle]
Pssm-ID: 273565 [Multi-domain] Cd Length: 403 Bit Score: 584.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550952243 112 IDAKVPVMGESVAEGQVGQWLVQPGEAVEQDQALLEIETDKVAVEVPAPAAGVLEEQLVAEGDTVTPDQVIGKIRAGASA 191
Cdd:TIGR01347 1 IEIKVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAILEEGNDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550952243 192 SAAPKSEDAPK--------AAASSSSSGGDAKAMPSANRVASENNLDLSKVEGTGKDGRVTKGDALKAVQSGGTASAPAA 263
Cdd:TIGR01347 81 TAAPPAKSGEEkeetpaasAAAAPTAAANRPSLSPAARRLAKEHGIDLSAVPGTGVTGRVTKEDIIKKTEAPASAQPPAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550952243 264 EKSSKPRDTGPR-EERVKMTRLRQTIARRLKDAQNSAAMLTTYNEADMSAIMSLRKEIQDDFVAKHGVKLGFMSFFVKAC 342
Cdd:TIGR01347 161 AAAAAAPAAATRpEERVKMTRLRQRIAERLKEAQNSTAMLTTFNEVDMSAVMELRKRYKEEFEKKHGVKLGFMSFFVKAV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550952243 343 VAALKDVPAVNAEIDGTDIIYKNYYDMGVAVGTDRGLVVPVVRDADDLSLAGVEKSIMDLGKRARDGKLGIDDMQGASFT 422
Cdd:TIGR01347 241 VAALKRFPEVNAEIDGDDIVYKDYYDISVAVSTDRGLVVPVVRNADRMSFADIEKEIADLGKKARDGKLTLEDMTGGTFT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550952243 423 ISNGGVYGSLLSSPILNAPQSGILGMHKIQERPVAINGEVKIRPMMYLALSYDHRIVDGKEAVTFLVRVKESLENPQRLL 502
Cdd:TIGR01347 321 ITNGGVFGSLMSTPIINPPQSAILGMHGIKERPVAVNGQIEIRPMMYLALSYDHRLIDGKEAVTFLVTIKELLEDPRRLL 400
|
...
gi 550952243 503 LDI 505
Cdd:TIGR01347 401 LDL 403
|
|
| PTZ00144 |
PTZ00144 |
dihydrolipoamide succinyltransferase; Provisional |
115-505 |
1.07e-162 |
|
dihydrolipoamide succinyltransferase; Provisional
Pssm-ID: 240289 [Multi-domain] Cd Length: 418 Bit Score: 467.24 E-value: 1.07e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550952243 115 KVPVMGESVAEGQVGQWLVQPGEAVEQDQALLEIETDKVAVEVPAPAAGVLEEQLVAEGDTVTPDQVIGKIRAGASASAA 194
Cdd:PTZ00144 48 KVPTMGDSISEGTVVEWKKKVGDYVKEDEVICIIETDKVSVDIRAPASGVITKIFAEEGDTVEVGAPLSEIDTGGAPPAA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550952243 195 PksedapkaaasssssggdakamPSANRVASENNLDLSKVEGTGKDGRVTKGDALKAVQSGGTASAPAAEKSS-KPRD-T 272
Cdd:PTZ00144 128 A----------------------PAAAAAAKAEKTTPEKPKAAAPTPEPPAASKPTPPAAAKPPEPAPAAKPPpTPVArA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550952243 273 GPREERVKMTRLRQTIARRLKDAQNSAAMLTTYNEADMSAIMSLRKEIQDDFVAKHGVKLGFMSFFVKACVAALKDVPAV 352
Cdd:PTZ00144 186 DPRETRVPMSRMRQRIAERLKASQNTCAMLTTFNECDMSALMELRKEYKDDFQKKHGVKLGFMSAFVKASTIALKKMPIV 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550952243 353 NAEIDGTDIIYKNYYDMGVAVGTDRGLVVPVVRDADDLSLAGVEKSIMDLGKRARDGKLGIDDMQGASFTISNGGVYGSL 432
Cdd:PTZ00144 266 NAYIDGDEIVYRNYVDISVAVATPTGLVVPVIRNCENKSFAEIEKELADLAEKARNNKLTLEDMTGGTFTISNGGVFGSL 345
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 550952243 433 LSSPILNAPQSGILGMHKIQERPVAINGEVKIRPMMYLALSYDHRIVDGKEAVTFLVRVKESLENPQRLLLDI 505
Cdd:PTZ00144 346 MGTPIINPPQSAILGMHAIKKRPVVVGNEIVIRPIMYLALTYDHRLIDGRDAVTFLKKIKDLIEDPARMLLDL 418
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
1-503 |
5.88e-154 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 450.04 E-value: 5.88e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550952243 1 MTEITVPTLGEsVTEATVGEWQVSEGDAVKKDDILVELETDKVSVEVRAEEDGVLSKIVAQEGDTVEIGATLAELGAGGG 80
Cdd:PRK11855 2 AIEFKVPDIGE-VVEVEVIEWLVKEGDTVEEDQPLVTVETDKATMEIPSPAAGVVKEIKVKVGDTVSVGGLLAVIEAAGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550952243 81 ASAS--------KASDDKPAKKSEDKSDAKSGGSGGGDLIDAKVPVMGEsVAEGQVGQWLVQPGEAVEQDQALLEIETDK 152
Cdd:PRK11855 81 AAAAaapaaaaaPAAAAAAAPAPAAAAPAAAAAAAGGGVVEVKVPDIGE-ITEVEVIEWLVKVGDTVEEDQSLITVETDK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550952243 153 VAVEVPAPAAGVLEEQLVAEGDTVTPDQVIGKIRAGASASA----------------------APKSEDAPKAAASSSSS 210
Cdd:PRK11855 160 ATMEIPSPVAGVVKEIKVKVGDKVSVGSLLVVIEVAAAAPAaaaapaaaapaaaaaaapapapAAAAAPAAAAPAAAAAP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550952243 211 GGDAKAMPSANRVASENNLDLSKVEGTGKDGRVTKGDALKAVQSGGTASAPAAEKSSKPRDTGP--------------RE 276
Cdd:PRK11855 240 GKAPHASPAVRRLARELGVDLSQVKGTGKKGRITKEDVQAFVKGAMSAAAAAAAAAAAAGGGGLgllpwpkvdfskfgEI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550952243 277 ERVKMTRLRQTIARRLKDAQNSAAMLTTYNEADMSAIMSLRKEIQDDFvAKHGVKLGFMSFFVKACVAALKDVPAVNAEI 356
Cdd:PRK11855 320 ETKPLSRIKKISAANLHRSWVTIPHVTQFDEADITDLEALRKQLKKEA-EKAGVKLTMLPFFIKAVVAALKEFPVFNASL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550952243 357 D--GTDIIYKNYYDMGVAVGTDRGLVVPVVRDADDLSLAGVEKSIMDLGKRARDGKLGIDDMQGASFTISNGGVYGSLLS 434
Cdd:PRK11855 399 DedGDELTYKKYFNIGFAVDTPNGLVVPVIKDVDKKSLLEIAREIAELAKKARDGKLKPDDMQGGCFTISSLGGIGGTAF 478
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 550952243 435 SPILNAPQSGILGMHKIQERPVAINGEVKIRPMMYLALSYDHRIVDGKEAVTFLVRVKESLENPQRLLL 503
Cdd:PRK11855 479 TPIINAPEVAILGVGKSQMKPVWDGKEFVPRLMLPLSLSYDHRVIDGATAARFTNYLKQLLADPRRMLL 547
|
|
| PRK11856 |
PRK11856 |
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed |
115-504 |
2.78e-136 |
|
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
Pssm-ID: 237001 [Multi-domain] Cd Length: 411 Bit Score: 399.94 E-value: 2.78e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550952243 115 KVPVMGESVAEGQVGQWLVQPGEAVEQDQALLEIETDKVAVEVPAPAAGVLEEQLVAEGDTVTPDQVIGKIRAG------ 188
Cdd:PRK11856 6 KMPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDVVPVGSVIAVIEEEgeaeaa 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550952243 189 --------------ASASAAPKSEDAPKAAASSSSSGGDAKAMPSANRVASENNLDLSKVEGTGKDGRVTKGDALKAVQS 254
Cdd:PRK11856 86 aaaeaapeapapepAPAAAAAAAAAPAAAAAPAAPAAAAAKASPAVRKLARELGVDLSTVKGSGPGGRITKEDVEAAAAA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550952243 255 GG-TASAPAAEKSSKPRDTGPREERVKMTRLRQTIARRLKDAQNSAAMLTTYNEADMSAIMSLRKEIQddfvaKHGVKLG 333
Cdd:PRK11856 166 AApAAAAAAAAAAAPPAAAAEGEERVPLSGMRKAIAKRMVESKREIPHFTLTDEVDVTALLALRKQLK-----AIGVKLT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550952243 334 FMSFFVKACVAALKDVPAVNAEIDGTDIIYKNYYDMGVAVGTDRGLVVPVVRDADDLSLAGVEKSIMDLGKRARDGKLGI 413
Cdd:PRK11856 241 VTDFLIKAVALALKKFPELNASWDDDAIVLKKYVNIGIAVATDGGLIVPVIRDADKKSLFELAREIKDLAEKAREGKLKP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550952243 414 DDMQGASFTISNGGVYGSLLSSPILNAPQSGILGMHKIQERPVAINGEVKIRPMMYLALSYDHRIVDGKEAVTFLVRVKE 493
Cdd:PRK11856 321 EELQGGTFTISNLGMFGGDYFTPIINPPEVAILGVGAIVERPVVVDGEIVVRKVMPLSLSFDHRVIDGADAARFLKALKE 400
|
410
....*....|.
gi 550952243 494 SLENPQRLLLD 504
Cdd:PRK11856 401 LLENPALLLLE 411
|
|
| PLN02226 |
PLN02226 |
2-oxoglutarate dehydrogenase E2 component |
106-505 |
2.56e-127 |
|
2-oxoglutarate dehydrogenase E2 component
Pssm-ID: 177871 [Multi-domain] Cd Length: 463 Bit Score: 379.10 E-value: 2.56e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550952243 106 SGGGDLIDAKVPVMGESVAEGQVGQWLVQPGEAVEQDQALLEIETDKVAVEVPAPAAGVLEEQLVAEGDTVTPDQVIGKI 185
Cdd:PLN02226 86 SESGDTVEAVVPHMGESITDGTLATFLKKPGERVQADEAIAQIETDKVTIDIASPASGVIQEFLVKEGDTVEPGTKVAII 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550952243 186 RAGA-SASAAPKSEDAPKAAASSSSSGGDAKAMPsanrvasennldlsKVEGTgkdgrvTKGDALKAVQSGGTASAPAAE 264
Cdd:PLN02226 166 SKSEdAASQVTPSQKIPETTDPKPSPPAEDKQKP--------------KVESA------PVAEKPKAPSSPPPPKQSAKE 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550952243 265 KSSKPRDtgpREERVKMTRLRQTIARRLKDAQNSAAMLTTYNEADMSAIMSLRKEIQDDFVAKHGVKLGFMSFFVKACVA 344
Cdd:PLN02226 226 PQLPPKE---RERRVPMTRLRKRVATRLKDSQNTFALLTTFNEVDMTNLMKLRSQYKDAFYEKHGVKLGLMSGFIKAAVS 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550952243 345 ALKDVPAVNAEIDGTDIIYKNYYDMGVAVGTDRGLVVPVVRDADDLSLAGVEKSIMDLGKRARDGKLGIDDMQGASFTIS 424
Cdd:PLN02226 303 ALQHQPVVNAVIDGDDIIYRDYVDISIAVGTSKGLVVPVIRGADKMNFAEIEKTINGLAKKANEGTISIDEMAGGSFTVS 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550952243 425 NGGVYGSLLSSPILNAPQSGILGMHKIQERPVAINGEVKIRPMMYLALSYDHRIVDGKEAVTFLVRVKESLENPQRLLLD 504
Cdd:PLN02226 383 NGGVYGSLISTPIINPPQSAILGMHSIVSRPMVVGGSVVPRPMMYVALTYDHRLIDGREAVYFLRRVKDVVEDPQRLLLD 462
|
.
gi 550952243 505 I 505
Cdd:PLN02226 463 I 463
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
2-503 |
6.82e-121 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 368.18 E-value: 6.82e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550952243 2 TEITVPTLGesVTEATVGEWQVSEGDAVKKDDILVELETDKVSVEVRAEEDGVLSKIVAQEGDTVEIGATLAELGAGGGA 81
Cdd:PRK11854 106 KDVHVPDIG--SDEVEVTEILVKVGDTVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVSTGSLIMVFEVAGEA 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550952243 82 SASKASDDKPAKksedksdAKSGGSGGGDLIDAKVPVMGesVAEGQVGQWLVQPGEAVEQDQALLEIETDKVAVEVPAPA 161
Cdd:PRK11854 184 PAAAPAAAEAAA-------PAAAPAAAAGVKDVNVPDIG--GDEVEVTEVMVKVGDKVEAEQSLITVEGDKASMEVPAPF 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550952243 162 AGVLEEQLVAEGDTVTPDQVIGKIRAGASASAAPKSEDAPKAAASSSSSGGDAKAMPSAN-------------------- 221
Cdd:PRK11854 255 AGTVKEIKVNVGDKVKTGSLIMRFEVEGAAPAAAPAKQEAAAPAPAAAKAEAPAAAPAAKaegksefaendayvhatplv 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550952243 222 -RVASENNLDLSKVEGTGKDGRVTK-------GDALKAVQSGGTASAPAAE-------KSSKPRDTGPREErVKMTRLRQ 286
Cdd:PRK11854 335 rRLAREFGVNLAKVKGTGRKGRILKedvqayvKDAVKRAEAAPAAAAAGGGgpgllpwPKVDFSKFGEIEE-VELGRIQK 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550952243 287 TIARRLKDAQNSAAMLTTYNEADMSAIMSLRKEIQD-DFVAKHGVKLGFMSFFVKACVAALKDVPAVNAEI--DGTDIIY 363
Cdd:PRK11854 414 ISGANLHRNWVMIPHVTQFDKADITELEAFRKQQNAeAEKRKLGVKITPLVFIMKAVAAALEQMPRFNSSLseDGQRLTL 493
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550952243 364 KNYYDMGVAVGTDRGLVVPVVRDADDLSLAGVEKSIMDLGKRARDGKLGIDDMQGASFTISNGGVYGSLLSSPILNAPQS 443
Cdd:PRK11854 494 KKYVNIGIAVDTPNGLVVPVFKDVNKKGIIELSRELMDISKKARDGKLTAGDMQGGCFTISSIGGLGTTHFTPIVNAPEV 573
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 550952243 444 GILGMHKIQERPVAINGEVKIRPMMYLALSYDHRIVDGKEAVTFLVRVKESLENPQRLLL 503
Cdd:PRK11854 574 AILGVSKSAMEPVWNGKEFAPRLMLPLSLSYDHRVIDGADGARFITIINDRLSDIRRLVL 633
|
|
| SucB_Actino |
TIGR02927 |
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model ... |
4-496 |
4.39e-119 |
|
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: 361.64 E-value: 4.39e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550952243 4 ITVPTLGESVTEATVGEWQVSEGDAVKKDDILVELETDKVSVEVRAEEDGVLSKIVAQEGDTVEIGATLAELGAGGGASA 83
Cdd:TIGR02927 5 VKMPALGESVTEGTVTSWLKAVGDTVEADEPLLEVSTDKVDTEIPSPAAGVLLEIRAPEDDTVEVGGVLAIIGEPGEAGS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550952243 84 S--------------KASDDKPAKKSEDKSDAKSGGSGGGDLIDAKVPVMGESVAEGQVGQWLVQPGEAVEQDQALLEIE 149
Cdd:TIGR02927 85 EpapaapepeaapepEAPAPAPTPAAEAPAPAAPQAGGSGEATEVKMPELGESVTEGTVTSWLKAVGDTVEVDEPLLEVS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550952243 150 TDKVAVEVPAPAAGVLEEQLVAEGDTVTPDQVIGKIrAGASASAAPKSEDAPKAAA------------------------ 205
Cdd:TIGR02927 165 TDKVDTEIPSPVAGTLLEIRAPEDDTVEVGTVLAII-GDANAAPAEPAEEEAPAPSeagsepapdpaaraphaapdppap 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550952243 206 --SSSSSGGDAKAMPSAN------------RVASENNLDLSKVEGTGKDGRVTKGDALKAVQ--------------SGGT 257
Cdd:TIGR02927 244 apAPAKTAAPAAAAPVSSgdsgpyvtplvrKLAKDKGVDLSTVKGTGVGGRIRKQDVLAAAKaaeearaaaaapaaAAAP 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550952243 258 ASAPAAEKSSKPRDTGPREERVKMTRLRQTIARRLKDAQNSAAMLTTYNEADMSAIMSLRKEIQDDFVAKHGVKLGFMSF 337
Cdd:TIGR02927 324 AAPAAAAKPAEPDTAKLRGTTQKMNRIRQITADKTIESLQTSAQLTQVHEVDMTRVAALRARAKNDFLEKNGVNLTFLPF 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550952243 338 FVKACVAALKDVPAVNAEI--DGTDIIYKNYYDMGVAVGTDRGLVVPVVRDADDLSLAGVEKSIMDLGKRARDGKLGIDD 415
Cdd:TIGR02927 404 FVQAVTEALKAHPNVNASYnaETKEVTYHDVEHVGIAVDTPRGLLVPVIHNAGDLSLPGLAKAINDLAARARDNKLKPDE 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550952243 416 MQGASFTISNGGVYGSLLSSPILNAPQSGILGMHKIQERPVAINGE-----VKIRPMMYLALSYDHRIVDGKEAVTFLVR 490
Cdd:TIGR02927 484 LSGGTFTITNIGSGGALFDTPILNPPQAAILGTGAIVKRPRVIKDEdggesIAIRSVCYLPLTYDHRLVDGADAGRFLTT 563
|
....*.
gi 550952243 491 VKESLE 496
Cdd:TIGR02927 564 IKKRLE 569
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
2-503 |
9.97e-95 |
|
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: 297.94 E-value: 9.97e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550952243 2 TEITVPTLGESvTEATVGEWQVSEGDAVKKDDILVELETDKVSVEVRAEEDGVLSKIVAQEGDTVEIGATLAELGAGGGA 81
Cdd:TIGR01348 1 TEIKVPDIGDN-EEGEVIEVLVKPGDKVEAGQSLITLESDKASMEVPSSAAGIIKEIKVKVGDTLPVGGVIATLEVGAGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550952243 82 S---------ASKASDDKPAKKSEDKSDAKSGGSGGGdlIDAKVPVMGeSVAEGQVGQWLVQPGEAVEQDQALLEIETDK 152
Cdd:TIGR01348 80 QaqaeakkeaAPAPTAGAPAPAAQAQAAPAAGQSSGV--QEVTVPDIG-DIEKVTVIEVLVKVGDTVSADQSLITLESDK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550952243 153 VAVEVPAPAAGVLEEQLVAEGDTVTPDQVIGKIR---------------------------AGASASAAPKSEDAPKAAA 205
Cdd:TIGR01348 157 ASMEVPAPASGVVKSVKVKVGDSVPTGDLILTLSvagstpatapapasaqpaaqspaatqpEPAAAPAAAKAQAPAPQQA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550952243 206 SSSSSGGDAKAMPSANRVASENNLDLSKVEGTGKDGRVTKGDALKAV--QSGGTASAPAAEKSSKPRDTGPRE------- 276
Cdd:TIGR01348 237 GTQNPAKVDHAAPAVRRLAREFGVDLSAVKGTGIKGRILREDVQRFVkePSVRAQAAAASAAGGAPGALPWPNvdfskfg 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550952243 277 --ERVKMTRLRQTIARRLKDAQNSAAMLTTYNEADMSAIMSLRKEiQDDFVAKHGVKLGFMSFFVKACVAALKDVPAVNA 354
Cdd:TIGR01348 317 evEEVDMSRIRKISGANLTRNWTMIPHVTHFDKADITEMEAFRKQ-QNAAVEKEGVKLTVLHILMKAVAAALKKFPKFNA 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550952243 355 EID--GTDIIYKNYYDMGVAVGTDRGLVVPVVRDADDLSLAGVEKSIMDLGKRARDGKLGIDDMQGASFTISNGGVYGSL 432
Cdd:TIGR01348 396 SLDlgGEQLILKKYVNIGVAVDTPNGLLVPVIKDVDRKGITELALELSDLAKKARDGKLTPDEMQGACFTISSLGGIGGT 475
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 550952243 433 LSSPILNAPQSGILGMHKIQERPVAINGEVKIRPMMYLALSYDHRIVDGKEAVTFLVRVKESLENPQRLLL 503
Cdd:TIGR01348 476 AFTPIVNAPEVAILGVSKSGMEPVWNGKEFEPRLMLPLSLSYDHRVIDGADAARFTTYICESLADIRRLLL 546
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
292-502 |
3.55e-93 |
|
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to three copies of a lipoyl binding domain followed by the catalytic domain.
Pssm-ID: 425518 [Multi-domain] Cd Length: 212 Bit Score: 282.12 E-value: 3.55e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550952243 292 LKDAQNSAAMLTTYNEADMSAIMSLRKEIQDDFvAKHGVKLGFMSFFVKACVAALKDVPAVNAEIDGTD--IIYKNYYDM 369
Cdd:pfam00198 1 MTESKQTIPHFTLTDEVDVTELLALREELKEDA-ADEETKLTFLPFLVKAVALALKKFPELNASWDGEEgeIVYKKYVNI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550952243 370 GVAVGTDRGLVVPVVRDADDLSLAGVEKSIMDLGKRARDGKLGIDDMQGASFTISNGGVYGSLLSSPILNAPQSGILGMH 449
Cdd:pfam00198 80 GIAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVG 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 550952243 450 KIQERPVAINGEVKIRPMMYLALSYDHRIVDGKEAVTFLVRVKESLENPQRLL 502
Cdd:pfam00198 160 RIRKRPVVVDGEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELLL 212
|
|
| PDHac_trf_mito |
TIGR01349 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
3-503 |
2.10e-76 |
|
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: 246.63 E-value: 2.10e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550952243 3 EITVPTLGESVTEATVGEWQVSEGDAVKKDDILVELETDKVSVEVRAEEDGVLSKIVAQEG-DTVEIGATLAELgaggga 81
Cdd:TIGR01349 1 KITMPALSPTMTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEGtKDVPVNKPIAVL------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550952243 82 saskasddkpAKKSEDKSDAKSGGSGGGDLIDAKVPVMGESVAEgqvgqwlvqpgeaveqdqalleietdkvaVEVPAPA 161
Cdd:TIGR01349 75 ----------VEEKEDVADAFKNYKLESSASPAPKPSEIAPTAP-----------------------------PSAPKPS 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550952243 162 AGVLEEqlvaegdtvtpdqvigkirAGASASAAPKSedapkaaasSSSSGGDAKAMPSANRVASENNLDLSKVEGTGKDG 241
Cdd:TIGR01349 116 PAPQKQ-------------------SPEPSSPAPLS---------DKESGDRIFASPLAKKLAKEKGIDLSAVAGSGPNG 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550952243 242 RVTKGDALKAV-------QSGGTASAPAAEKSSKPRDTGPREErVKMTRLRQTIARRLKDAQNSAAMLTTYNEADMSAIM 314
Cdd:TIGR01349 168 RIVKKDIESFVpqspasaNQQAAATTPATYPAAAPVSTGSYED-VPLSNIRKIIAKRLLESKQTIPHYYVSIECNVDKLL 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550952243 315 SLRKEIQDDFVAKhgVKLGFMSFFVKACVAALKDVPAVNAEIDGTDIIYKNYYDMGVAVGTDRGLVVPVVRDADDLSLAG 394
Cdd:TIGR01349 247 ALRKELNAMASEV--YKLSVNDFIIKASALALREVPEANSSWTDNFIRRYKNVDISVAVATPDGLITPIVRNADAKGLST 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550952243 395 VEKSIMDLGKRARDGKLGIDDMQGASFTISNGGVYGSLLSSPILNAPQSGILGMHKIQERPVAINGEVK---IRPMMYLA 471
Cdd:TIGR01349 325 ISNEIKDLAKRARNNKLKPEEFQGGTFTISNLGMFGIKDFTAIINPPQACILAVGAVEDVAVVDNDEEKgfaVASIMSVT 404
|
490 500 510
....*....|....*....|....*....|..
gi 550952243 472 LSYDHRIVDGKEAVTFLVRVKESLENPQRLLL 503
Cdd:TIGR01349 405 LSCDHRVIDGAVGAEFLKSFKKYLENPIEMLL 436
|
|
| PRK11857 |
PRK11857 |
dihydrolipoamide acetyltransferase; Reviewed |
216-501 |
9.75e-62 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237002 [Multi-domain] Cd Length: 306 Bit Score: 204.26 E-value: 9.75e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550952243 216 AMPSANRVASENNLDLSKVEGTGKDGRVTKGDALKAVQSGGTASAPA----------AEKSSKPRDTGPREE--RVKMTR 283
Cdd:PRK11857 4 ATPIARALAKKLGIDISLLKGSGRDGKILAEDVENFIKSLKSAPTPAeaasvssaqqAAKTAAPAAAPPKLEgkREKVAP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550952243 284 LRQTIARRLKDAQNSAAMLTTYNEADMSAIMSLRKEIQDDFVAKHGVKLGFMSFFVKACVAALKDVPAVNAEID--GTDI 361
Cdd:PRK11857 84 IRKAIARAMTNSWSNVAYVNLVNEIDMTKLWDLRKSVKDPVLKTEGVKLTFLPFIAKAILIALKEFPIFAAKYDeaTSEL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550952243 362 IYKNYYDMGVAVGTDRGLVVPVVRDADDLSLAGVEKSIMDLGKRARDGKLGIDDMQGASFTISNGGVYGSLLSSPILNAP 441
Cdd:PRK11857 164 VYPDTLNLGIAVDTEAGLMVPVIKNAQKLSIVEIAKEISRLAKAARERKIKPDEMKGGSFTITNYGSVGSLYGVPVINYP 243
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 550952243 442 QSGILGMHKIQERPVAINGEVKIRPMMYLALSYDHRIVDGKEAVTFLVRVKESLENPQRL 501
Cdd:PRK11857 244 ELAIAGVGAIIDKAIVKNGQIVAGKVMHLTVAADHRWIDGATIGRFASRVKELLEKPEIL 303
|
|
| PRK14843 |
PRK14843 |
dihydrolipoamide acetyltransferase; Provisional |
218-503 |
8.62e-60 |
|
dihydrolipoamide acetyltransferase; Provisional
Pssm-ID: 184847 [Multi-domain] Cd Length: 347 Bit Score: 200.52 E-value: 8.62e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550952243 218 PSANRVASENNLDLSKVEGTGKDGRVTKGDAL----KAVQSGGTASAPAAEKSSKPRDTGPRE---ERVKMTRLRQTIAR 290
Cdd:PRK14843 53 PLAKRIALEHNIAWQEIQGTGHRGKIMKKDVLallpENIENDSIKSPAQIEKVEEVPDNVTPYgeiERIPMTPMRKVIAQ 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550952243 291 RLKDAQNSAAMLTTYNEADMSAIMSLRKEIQDDFVAKHGVKLGFMSFFVKACVAALKDVPAVNAEI--DGTDIIYKNYYD 368
Cdd:PRK14843 133 RMVESYLTAPTFTLNYEVDMTEMLALRKKVLEPIMEATGKKTTVTDLLSLAVVKTLMKHPYINASLteDGKTIITHNYVN 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550952243 369 MGVAVGTDRGLVVPVVRDADDLSLAGVEKSIMDLGKRARDGKLGIDDMQGASFTISNGGVYGSLLSSPILNAPQSGILGM 448
Cdd:PRK14843 213 LAMAVGMDNGLMTPVVYNAEKMSLSELVVAFKDVIGRTLDGKLAPSELQNSTFTISNLGMFGVQSFGPIINQPNSAILGV 292
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 550952243 449 HKIQERPVAINGEVKIRPMMYLALSYDHRIVDGKEAVTFLVRVKESLENPQRLLL 503
Cdd:PRK14843 293 SSTIEKPVVVNGEIVIRPIMSLGLTIDHRVVDGMAGAKFMKDLKELIETPISMLI 347
|
|
| PLN02528 |
PLN02528 |
2-oxoisovalerate dehydrogenase E2 component |
120-503 |
2.76e-53 |
|
2-oxoisovalerate dehydrogenase E2 component
Pssm-ID: 215289 [Multi-domain] Cd Length: 416 Bit Score: 185.31 E-value: 2.76e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550952243 120 GESVAEGQVGQWLVQPGEAVEQDQALLEIETDKVAVEVPAPAAGVLEEQLVAEGDTVTPDQVIGKIRAGASASAAPKSED 199
Cdd:PLN02528 7 GEGIAECELLRWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGKVAQINFSPGDIVKVGETLLKIMVEDSQHLRSDSLL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550952243 200 APKAAASSSSSGGDAK---------AMPSANRVASENNLDLSKVEGTGKDGRVTKGDALK-AVQSGGTASAPAAEkSSKP 269
Cdd:PLN02528 87 LPTDSSNIVSLAESDErgsnlsgvlSTPAVRHLAKQYGIDLNDILGTGKDGRVLKEDVLKyAAQKGVVKDSSSAE-EATI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550952243 270 RDTGPREERVKMTRLR----QTIA-----RRLKDAQNSAAMLTTY---NEADMSAIMSLRKEIQDDfVAKHGVKLGFMSF 337
Cdd:PLN02528 166 AEQEEFSTSVSTPTEQsyedKTIPlrgfqRAMVKTMTAAAKVPHFhyvEEINVDALVELKASFQEN-NTDPTVKHTFLPF 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550952243 338 FVKACVAALKDVPAVNAEIDG--TDIIYKNYYDMGVAVGTDRGLVVPVVRDADDLSLAGVEKSIMDLGKRARDGKLGIDD 415
Cdd:PLN02528 245 LIKSLSMALSKYPLLNSCFNEetSEIRLKGSHNIGVAMATEHGLVVPNIKNVQSLSLLEITKELSRLQHLAAENKLNPED 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550952243 416 MQGASFTISNGGVYGSLLSSPILNAPQSGILGMHKIQERP-VAINGEVKIRPMMYLALSYDHRIVDGKEAVTFLVRVKES 494
Cdd:PLN02528 325 ITGGTITLSNIGAIGGKFGSPVLNLPEVAIIALGRIQKVPrFVDDGNVYPASIMTVTIGADHRVLDGATVARFCNEWKSY 404
|
....*....
gi 550952243 495 LENPQRLLL 503
Cdd:PLN02528 405 VEKPELLML 413
|
|
| PLN02744 |
PLN02744 |
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex |
3-503 |
5.57e-50 |
|
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
Pssm-ID: 215397 [Multi-domain] Cd Length: 539 Bit Score: 179.28 E-value: 5.57e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550952243 3 EITVPTLGESVTEATVGEWQVSEGDAVKKDDILVELETDKVSVEVRAEEDGVLSKIVAQEGD-----------TVEIGAT 71
Cdd:PLN02744 114 EIGMPSLSPTMTEGNIARWLKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVKGDGAkeikvgeviaiTVEEEED 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550952243 72 LAELG-----AGGGASASKASDDKPAKKSEDksdaksggsgggdlidakvpvmgesvaegqvgqwlvqpgeaveqdqall 146
Cdd:PLN02744 194 IGKFKdykpsSSAAPAAPKAKPSPPPPKEEE------------------------------------------------- 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550952243 147 eietdkvaVEVPAPAagvleeqlvaegdtvtPDQVIGKiragasASAAPKSEDAPKaaasssssggdakAMPSANRVASE 226
Cdd:PLN02744 225 --------VEKPASS----------------PEPKASK------PSAPPSSGDRIF-------------ASPLARKLAED 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550952243 227 NNLDLSKVEGTGKDGRVTKGDALKAVQSGGTASAPAAEKSSKPRDTGPREerVKMTRLRQTIARRLKDAQNSAAMLTTYN 306
Cdd:PLN02744 262 NNVPLSSIKGTGPDGRIVKADIEDYLASGGKGATAPPSTDSKAPALDYTD--IPNTQIRKVTASRLLQSKQTIPHYYLTV 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550952243 307 EADMSAIMSLRKEIQDDFVAKHGVKLGFMSFFVKACVAALKDVPAVNAEidGTDIIYKNYYD--MGVAVGTDRGLVVPVV 384
Cdd:PLN02744 340 DTRVDKLMALRSQLNSLQEASGGKKISVNDLVIKAAALALRKVPQCNSS--WTDDYIRQYHNvnINVAVQTENGLYVPVV 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550952243 385 RDADDLSLAGVEKSIMDLGKRARDGKLGIDDMQGASFTISN-GGVYGSLLSSPILNAPQSGILGMHKIQER--PVAINGE 461
Cdd:PLN02744 418 KDADKKGLSTIAEEVKQLAQKARENSLKPEDYEGGTFTVSNlGGPFGIKQFCAIINPPQSAILAVGSAEKRviPGSGPDQ 497
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 550952243 462 VKIRPMMYLALSYDHRIVDGKEAVTFLVRVKESLENPQRLLL 503
Cdd:PLN02744 498 YNFASFMSVTLSCDHRVIDGAIGAEWLKAFKGYIENPESMLL 539
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
2-75 |
4.53e-29 |
|
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: 109.03 E-value: 4.53e-29
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 550952243 2 TEITVPTLGESVTEATVGEWQVSEGDAVKKDDILVELETDKVSVEVRAEEDGVLSKIVAQEGDTVEIGATLAEL 75
Cdd:cd06849 1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
1-75 |
1.01e-28 |
|
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: 108.23 E-value: 1.01e-28
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 550952243 1 MTEITVPTLGESVTEATVGEWQVSEGDAVKKDDILVELETDKVSVEVRAEEDGVLSKIVAQEGDTVEIGATLAEL 75
Cdd:COG0508 2 AIEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
112-185 |
6.65e-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: 103.25 E-value: 6.65e-27
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 550952243 112 IDAKVPVMGESVAEGQVGQWLVQPGEAVEQDQALLEIETDKVAVEVPAPAAGVLEEQLVAEGDTVTPDQVIGKI 185
Cdd:cd06849 1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
112-185 |
8.00e-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: 8.00e-27
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 550952243 112 IDAKVPVMGESVAEGQVGQWLVQPGEAVEQDQALLEIETDKVAVEVPAPAAGVLEEQLVAEGDTVTPDQVIGKI 185
Cdd:COG0508 3 IEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
2-83 |
8.00e-19 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 88.08 E-value: 8.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550952243 2 TEITVPTLGESVTEATVGEWQVSEGDAVKKDDILVELETDKVSVEVRAEEDGVLSKIVAQEGDTVEIGATLAELGAGGGA 81
Cdd:PRK14875 3 TPITMPKWGLSMTEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGETLPVGALLAVVADAEVS 82
|
..
gi 550952243 82 SA 83
Cdd:PRK14875 83 DA 84
|
|
| kgd |
PRK12270 |
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ... |
251-495 |
5.43e-18 |
|
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;
Pssm-ID: 237030 [Multi-domain] Cd Length: 1228 Bit Score: 87.64 E-value: 5.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550952243 251 AVQSGGTASAPAAEKSSKPRDTGPREERVKMTRLRqTIARRLkdAQNSAAML-----TTYNEADMSAIMSLRKEIQDDFV 325
Cdd:PRK12270 87 AAAAAAAAAPAAPPAAAAAAAPAAAAVEDEVTPLR-GAAAAV--AKNMDASLevptaTSVRAVPAKLLIDNRIVINNHLK 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550952243 326 AKHGVKLGFMSFFVKACVAALKDVPAVN---AEIDGTDIIYKN-YYDMGVAV------GTdRGLVVPVVRDADDLSLAGV 395
Cdd:PRK12270 164 RTRGGKVSFTHLIGYALVQALKAFPNMNrhyAEVDGKPTLVTPaHVNLGLAIdlpkkdGS-RQLVVPAIKGAETMDFAQF 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550952243 396 EKSIMDLGKRARDGKLGIDDMQGASFTISNGGVYGSLLSSPILNAPQSGILGMHKIqERPVAING-------EVKIRPMM 468
Cdd:PRK12270 243 WAAYEDIVRRARDGKLTADDFQGTTISLTNPGGIGTVHSVPRLMKGQGAIIGVGAM-EYPAEFQGaseerlaELGISKVM 321
|
250 260
....*....|....*....|....*..
gi 550952243 469 YLALSYDHRIVDGKEAVTFLVRVKESL 495
Cdd:PRK12270 322 TLTSTYDHRIIQGAESGEFLRTIHQLL 348
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
2-75 |
4.50e-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: 4.50e-17
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 550952243 2 TEITVPTLGESVTEATVgEWQVSEGDAVKKDDILVELETDKVSVEVRAEEDGVLSKIVAQEGDTVEIGATLAEL 75
Cdd:pfam00364 1 TEIKSPMIGESVREGVV-EWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
115-194 |
5.04e-17 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 82.68 E-value: 5.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550952243 115 KVPVMGESVAEGQVGQWLVQPGEAVEQDQALLEIETDKVAVEVPAPAAGVLEEQLVAEGDTVTPDQVIGKIRAGASASAA 194
Cdd:PRK14875 6 TMPKWGLSMTEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGETLPVGALLAVVADAEVSDAE 85
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
115-185 |
1.34e-16 |
|
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: 74.17 E-value: 1.34e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 550952243 115 KVPVMGESVAEGqVGQWLVQPGEAVEQDQALLEIETDKVAVEVPAPAAGVLEEQLVAEGDTVTPDQVIGKI 185
Cdd:pfam00364 4 KSPMIGESVREG-VVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
112-195 |
3.32e-16 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 81.59 E-value: 3.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550952243 112 IDAKVPVMGesVAEGQVGQWLVQPGEAVEQDQALLEIETDKVAVEVPAPAAGVLEEQLVAEGDTVTPDQVIGKIRAGASA 191
Cdd:PRK11854 3 IEIKVPDIG--ADEVEVTEILVKVGDKVEAEQSLITVEGDKASMEVPSPQAGVVKEIKVKVGDKVETGALIMIFESADGA 80
|
....
gi 550952243 192 SAAP 195
Cdd:PRK11854 81 ADAA 84
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
1-104 |
1.39e-14 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 75.72 E-value: 1.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550952243 1 MTEITVPTLGESVTEATVGEWQVSEGDAVKKDDILVELETDKVSVEVRAEEDGVLSKIVAQEG-DTVEIGATLAELGAGG 79
Cdd:PRK11892 2 AIEILMPALSPTMEEGTLAKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKILVPEGtEGVKVNTPIAVLLEEG 81
|
90 100
....*....|....*....|....*
gi 550952243 80 GASASKASDDKPAKKSEDKSDAKSG 104
Cdd:PRK11892 82 ESASDAGAAPAAAAEAAAAAPAAAA 106
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
116-185 |
1.26e-11 |
|
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: 60.15 E-value: 1.26e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550952243 116 VPVMGESVAEGQVGQWLVQPGEAVEQDQALLEIETDKVAVEVPAPAAGVLEEQLVAEGDTVTPDQVIGKI 185
Cdd:cd06663 4 IPDLAQHLGDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKVEGDTPLVKI 73
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
17-75 |
5.05e-11 |
|
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: 58.20 E-value: 5.05e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 550952243 17 TVGEWQVSEGDAVKKDDILVELETDKVSVEVRAEEDGVLSKIVAQEGDTVEIGATLAEL 75
Cdd:cd06850 9 TVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
3-75 |
8.07e-11 |
|
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: 57.84 E-value: 8.07e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 550952243 3 EITVPTLGESVTEATVGEWQVSEGDAVKKDDILVELETDKVSVEVRAEEDGVLSKIVAQEGDTVEIGATLAEL 75
Cdd:cd06663 1 TILIPDLAQHLGDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKVEGDTPLVKI 73
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
126-185 |
1.78e-10 |
|
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: 56.66 E-value: 1.78e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 550952243 126 GQVGQWLVQPGEAVEQDQALLEIETDKVAVEVPAPAAGVLEEQLVAEGDTVTPDQVIGKI 185
Cdd:cd06850 8 GTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| E3_binding |
pfam02817 |
e3 binding domain; This family represents a small domain of the E2 subunit of 2-oxo-acid ... |
216-249 |
6.62e-09 |
|
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: 51.15 E-value: 6.62e-09
10 20 30
....*....|....*....|....*....|....
gi 550952243 216 AMPSANRVASENNLDLSKVEGTGKDGRVTKGDAL 249
Cdd:pfam02817 3 ASPAARKLARELGIDLSDVKGTGPGGRITKEDVE 36
|
|
| PRK09282 |
PRK09282 |
pyruvate carboxylase subunit B; Validated |
132-186 |
5.50e-08 |
|
pyruvate carboxylase subunit B; Validated
Pssm-ID: 236449 [Multi-domain] Cd Length: 592 Bit Score: 55.23 E-value: 5.50e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 550952243 132 LVQPGEAVEQDQALLEIETDKVAVEVPAPAAGVLEEQLVAEGDTVTPDQVIGKIR 186
Cdd:PRK09282 537 KVKEGDKVKAGDTVLVLEAMKMENEIQAPVDGTVKEILVKEGDRVNPGDVLMEIE 591
|
|
| AccB |
COG0511 |
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ... |
23-76 |
6.43e-08 |
|
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: 51.43 E-value: 6.43e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 550952243 23 VSEGDAVKKDDILVELETDKVSVEVRAEEDGVLSKIVAQEGDTVEIGATLAELG 76
Cdd:COG0511 83 VKVGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVVEILVENGQPVEYGQPLFVIE 136
|
|
| PRK14040 |
PRK14040 |
oxaloacetate decarboxylase subunit alpha; |
5-76 |
8.42e-08 |
|
oxaloacetate decarboxylase subunit alpha;
Pssm-ID: 237592 [Multi-domain] Cd Length: 593 Bit Score: 54.94 E-value: 8.42e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 550952243 5 TVPTLGESVTEATVGE-WQ--VSEGDAVKKDDILVELETDKVSVEVRAEEDGVLSKIVAQEGDTVEIGATLAELG 76
Cdd:PRK14040 519 PAAAAGEPVTAPLAGNiFKviVTEGQTVAEGDVLLILEAMKMETEIRAAQAGTVRGIAVKEGDAVAVGDTLLTLA 593
|
|
| AccB |
COG0511 |
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ... |
132-182 |
2.62e-07 |
|
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: 49.89 E-value: 2.62e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 550952243 132 LVQPGEAVEQDQALLEIETDKVAVEVPAPAAGVLEEQLVAEGDTVTPDQVI 182
Cdd:COG0511 82 FVKVGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVVEILVENGQPVEYGQPL 132
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
112-225 |
2.83e-07 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 53.00 E-value: 2.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550952243 112 IDAKVPVMGESVAEGQVGQWLVQPGEAVEQDQALLEIETDKVAVEVPAPAAGVLEEQLVAEG-DTVTPDQVIGKIRA-GA 189
Cdd:PRK11892 3 IEILMPALSPTMEEGTLAKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKILVPEGtEGVKVNTPIAVLLEeGE 82
|
90 100 110
....*....|....*....|....*....|....*.
gi 550952243 190 SASAAPKSEDAPKAAASSSSSGGDAKAMPSANRVAS 225
Cdd:PRK11892 83 SASDAGAAPAAAAEAAAAAPAAAAAAAAKKAAPAPA 118
|
|
| PRK05641 |
PRK05641 |
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
23-76 |
1.01e-06 |
|
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235540 [Multi-domain] Cd Length: 153 Bit Score: 48.32 E-value: 1.01e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 550952243 23 VSEGDAVKKDDILVELETDKVSVEVRAEEDGVLSKIVAQEGDTVEIGATLAELG 76
Cdd:PRK05641 100 VREGQQVKVGQGLLILEAMKMENEIPAPKDGVVKKILVKEGDTVDTGQPLIELG 153
|
|
| PRK09282 |
PRK09282 |
pyruvate carboxylase subunit B; Validated |
23-75 |
1.06e-06 |
|
pyruvate carboxylase subunit B; Validated
Pssm-ID: 236449 [Multi-domain] Cd Length: 592 Bit Score: 51.38 E-value: 1.06e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 550952243 23 VSEGDAVKKDDILVELETDKVSVEVRAEEDGVLSKIVAQEGDTVEIGATLAEL 75
Cdd:PRK09282 538 VKEGDKVKAGDTVLVLEAMKMENEIQAPVDGTVKEILVKEGDRVNPGDVLMEI 590
|
|
| PRK05641 |
PRK05641 |
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
36-180 |
1.23e-06 |
|
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235540 [Multi-domain] Cd Length: 153 Bit Score: 48.32 E-value: 1.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550952243 36 VELETDKVSVEVRAEEDGVLSKIVAQEGDTVEIGATlaelGAGGGASASKASDDKPAKKSEDKSDAKSGGSGGGDLIDAK 115
Cdd:PRK05641 4 VKVIVDGVEYEVEVEELGPGKFRVSFEGKTYEVEAK----GLGIDLSAVQEQVPTPAPAPAPAVPSAPTPVAPAAPAPAP 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 550952243 116 VPVmGESVAE----GQVGQWLVQPGEAVEQDQALLEIETDKVAVEVPAPAAGVLEEQLVAEGDTVTPDQ 180
Cdd:PRK05641 80 ASA-GENVVTapmpGKILRILVREGQQVKVGQGLLILEAMKMENEIPAPKDGVVKKILVKEGDTVDTGQ 147
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
17-75 |
1.14e-05 |
|
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the Pathway/BioSystem: Urea cycle
Pssm-ID: 440660 [Multi-domain] Cd Length: 1144 Bit Score: 48.15 E-value: 1.14e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 550952243 17 TVGEWQVSEGDAVKKDDILVELETDKVSVEVRAEEDGVLSKIVAQEGDTVEIGATLAEL 75
Cdd:COG1038 1086 TVVKVLVKEGDEVKKGDPLLTIEAMKMETTITAPRDGTVKEVLVKEGDQVEAGDLLIEL 1144
|
|
| PRK14042 |
PRK14042 |
pyruvate carboxylase subunit B; Provisional |
133-185 |
4.27e-05 |
|
pyruvate carboxylase subunit B; Provisional
Pssm-ID: 172536 [Multi-domain] Cd Length: 596 Bit Score: 46.25 E-value: 4.27e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 550952243 133 VQPGEAVEQDQALLEIETDKVAVEVPAPAAGVLEEQLVAEGDTVTPDQVIGKI 185
Cdd:PRK14042 541 VSAGDEVKAGQAVLVIEAMKMETEIKAPANGVVAEILCQKGDKVTPGQVLIRV 593
|
|
| PRK08225 |
PRK08225 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
23-76 |
5.52e-05 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 181304 [Multi-domain] Cd Length: 70 Bit Score: 41.31 E-value: 5.52e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 550952243 23 VSEGDAVKKDDILVELETDKVSVEVRAEEDGVLSKIVAQEGDTVEIGATLAELG 76
Cdd:PRK08225 17 VKVGDTVEEGQDVVILESMKMEIPIVAEEAGTVKKINVQEGDFVNEGDVLLEIE 70
|
|
| PRK05889 |
PRK05889 |
biotin/lipoyl-binding carrier protein; |
16-73 |
1.01e-04 |
|
biotin/lipoyl-binding carrier protein;
Pssm-ID: 180306 [Multi-domain] Cd Length: 71 Bit Score: 40.56 E-value: 1.01e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 550952243 16 ATVGEWQVSEGDAVKKDDILVELETDKVSVEVRAEEDGVLSKIVAQEGDTVEIGATLA 73
Cdd:PRK05889 11 ASVLEVVVNEGDQIGKGDTLVLLESMKMEIPVLAEVAGTVSKVSVSVGDVIQAGDLIA 68
|
|
| PRK14040 |
PRK14040 |
oxaloacetate decarboxylase subunit alpha; |
114-182 |
1.29e-04 |
|
oxaloacetate decarboxylase subunit alpha;
Pssm-ID: 237592 [Multi-domain] Cd Length: 593 Bit Score: 44.54 E-value: 1.29e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 550952243 114 AKVPVMGESVA---EGQVGQWLVQPGEAVEQDQALLEIETDKVAVEVPAPAAGVLEEQLVAEGDTVTPDQVI 182
Cdd:PRK14040 518 APAAAAGEPVTaplAGNIFKVIVTEGQTVAEGDVLLILEAMKMETEIRAAQAGTVRGIAVKEGDAVAVGDTL 589
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
23-76 |
2.51e-04 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 43.97 E-value: 2.51e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 550952243 23 VSEGDAVKKDDILVELETDKVSVEVRAEEDGVLSKIVAQEGDTVEIGATLAELG 76
Cdd:PRK12999 1092 VKEGDEVKAGDPLAVIEAMKMETTITAPVDGTVKRVLVKAGDQVEAGDLLVELE 1145
|
|
| PRK07051 |
PRK07051 |
biotin carboxyl carrier domain-containing protein; |
23-77 |
5.38e-04 |
|
biotin carboxyl carrier domain-containing protein;
Pssm-ID: 180811 [Multi-domain] Cd Length: 80 Bit Score: 38.84 E-value: 5.38e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 550952243 23 VSEGDAVKKDDILVELETDKVSVEVRAEEDGVLSKIVAQEGDTVEIGATLAELGA 77
Cdd:PRK07051 26 VEVGDAVAAGDVVGLIEVMKQFTEVEAEAAGRVVEFLVEDGEPVEAGQVLARIEE 80
|
|
| AcrA |
COG0845 |
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ... |
44-185 |
2.17e-03 |
|
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope biogenesis, Defense mechanisms];
Pssm-ID: 440606 [Multi-domain] Cd Length: 324 Bit Score: 40.31 E-value: 2.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550952243 44 SVEVRAEEDGVLSKIVAQEGDTVEIGATLAEL------GAGGGASASKASDDKPAKKSED-----KSDAKSGGSGGGDLI 112
Cdd:COG0845 23 EVEVRARVSGRVEEVLVDEGDRVKKGQVLARLdppdlqAALAQAQAQLAAAQAQLELAKAeleryKALLKKGAVSQQELD 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 550952243 113 DAKVPVmgeSVAEGQVgqwlvqpgEAVEQDQALLEIETDKvaVEVPAPAAGVLEEQLVAEGDTVTPDQVIGKI 185
Cdd:COG0845 103 QAKAAL---DQAQAAL--------AAAQAALEQARANLAY--TTIRAPFDGVVGERNVEPGQLVSAGTPLFTI 162
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
12-185 |
6.50e-03 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 38.88 E-value: 6.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550952243 12 SVTEATVGEWQVSEGDAVKKDDILVELETDKVSVEVRAEEDGV------LSKIVAQEGDTVEIGATLAELgAGGGASASK 85
Cdd:COG1566 50 AKVSGRVTEVLVKEGDRVKKGQVLARLDPTDLQAALAQAEAQLaaaeaqLARLEAELGAEAEIAAAEAQL-AAAQAQLDL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550952243 86 ASDDKPAKKSEDKSDAKSggsgGGDLIDAKVPV----MGESVAEGQVGQWLVQPGEAVEQDQALLEIETDKVAVE----- 156
Cdd:COG1566 129 AQRELERYQALYKKGAVS----QQELDEARAALdaaqAQLEAAQAQLAQAQAGLREEEELAAAQAQVAQAEAALAqaeln 204
|
170 180 190
....*....|....*....|....*....|....
gi 550952243 157 -----VPAPAAGVLEEQLVAEGDTVTPDQVIGKI 185
Cdd:COG1566 205 larttIRAPVDGVVTNLNVEPGEVVSAGQPLLTI 238
|
|
| PRK07051 |
PRK07051 |
biotin carboxyl carrier domain-containing protein; |
133-185 |
9.53e-03 |
|
biotin carboxyl carrier domain-containing protein;
Pssm-ID: 180811 [Multi-domain] Cd Length: 80 Bit Score: 35.37 E-value: 9.53e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 550952243 133 VQPGEAVEQDQALLEIETDKVAVEVPAPAAGVLEEQLVAEGDTVTPDQVIGKI 185
Cdd:PRK07051 26 VEVGDAVAAGDVVGLIEVMKQFTEVEAEAAGRVVEFLVEDGEPVEAGQVLARI 78
|
|
| |
