| Tag | Content |
|---|
| CPLM ID | CPLM-005277 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Biotin carboxylase |
Protein Synonyms/Alias | Acetyl-CoA carboxylase subunit A; ACC |
Gene Name | accC |
Gene Synonyms/Alias | fabG; b3256; JW3224 |
Created Date | July 27, 2013 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 27 | ACKELGIKTVAVHSS | acetylation | [1] | | 106 | GFIFIGPKAETIRLM | acetylation | [1] | | 116 | TIRLMGDKVSAIAAM | acetylation | [1] | | 124 | VSAIAAMKKAGVPCV | acetylation | [1] | | 125 | SAIAAMKKAGVPCVP | acetylation | [1] | | 144 | PLGDDMDKNRAIAKR | acetylation | [1] | | 202 | NDMVYMEKYLENPRH | acetylation | [1] | | 238 | SMQRRHQKVVEEAPA | acetylation | [1] | | 324 | AGQPLSIKQEEVHVR | acetylation | [1] | | 353 | TFLPSPGKITRFHAP | acetylation | [1] | | 442 | TNIHYLEKKLGLQEK | acetylation | [1] | | 443 | NIHYLEKKLGLQEK* | acetylation | [1] |
|
Reference | [1] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli. Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C. Mol Cell. 2013 Jul 25;51(2):265-72. [ PMID: 23830618] |
Functional Description | This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. |
Sequence Annotation | DOMAIN 1 445 Biotin carboxylation.
DOMAIN 120 317 ATP-grasp.
ACT_SITE 292 292 Potential.
BINDING 116 116 ATP.
BINDING 201 201 ATP.
BINDING 236 236 ATP. |
Keyword | 3D-structure; ATP-binding; Biotin; Complete proteome; Direct protein sequencing; Fatty acid biosynthesis; Fatty acid metabolism; Ligase; Lipid biosynthesis; Lipid metabolism; Nucleotide-binding; Reference proteome. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 449 AA |
Protein Sequence | MLDKIVIANR GEIALRILRA CKELGIKTVA VHSSADRDLK HVLLADETVC IGPAPSVKSY 60
LNIPAIISAA EITGAVAIHP GYGFLSENAN FAEQVERSGF IFIGPKAETI RLMGDKVSAI 120
AAMKKAGVPC VPGSDGPLGD DMDKNRAIAK RIGYPVIIKA SGGGGGRGMR VVRGDAELAQ 180
SISMTRAEAK AAFSNDMVYM EKYLENPRHV EIQVLADGQG NAIYLAERDC SMQRRHQKVV 240
EEAPAPGITP ELRRYIGERC AKACVDIGYR GAGTFEFLFE NGEFYFIEMN TRIQVEHPVT 300
EMITGVDLIK EQLRIAAGQP LSIKQEEVHV RGHAVECRIN AEDPNTFLPS PGKITRFHAP 360
GGFGVRWESH IYAGYTVPPY YDSMIGKLIC YGENRDVAIA RMKNALQELI IDGIKTNVDL 420
QIRIMNDENF QHGGTNIHYL EKKLGLQEK 449 |
Gene Ontology | GO:0005737; C:cytoplasm; IC:EcoliWiki. GO:0003989; F:acetyl-CoA carboxylase activity; IEA:EC. GO:0005524; F:ATP binding; IEA:UniProtKB-KW. GO:0004075; F:biotin carboxylase activity; IDA:EcoliWiki. GO:0046872; F:metal ion binding; IEA:InterPro. GO:0006633; P:fatty acid biosynthetic process; IMP:EcoCyc. GO:2001295; P:malonyl-CoA biosynthetic process; IEA:UniProtKB-UniPathway. GO:0045717; P:negative regulation of fatty acid biosynthetic process; IMP:EcoliWiki. |
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Pfam | |
SMART | |
PROSITE | |
PRINTS | |