ID ACCA_ALHEH Reviewed; 318 AA. AC Q0A7K0; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 17-OCT-2006, sequence version 1. DT 16-JUN-2009, entry version 23. DE RecName: Full=Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; DE Short=Acetyl-CoA carboxylase carboxyltransferase subunit alpha; DE Short=ACCase subunit alpha; DE EC=6.4.1.2; GN Name=accA; OrderedLocusNames=Mlg_1843; OS Alkalilimnicola ehrlichei (strain MLHE-1). OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; OC Ectothiorhodospiraceae; Alkalilimnicola. OX NCBI_TaxID=187272; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Sims D., Brettin T., Bruce D., Han C., Tapia R., Gilna P., RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., RA Mikhailova N., Oremland R.S., Hoeft S.E., Switzer-Blum J., Kulp T., RA King G., Tabita R., Witte B., Santini J.M., Basu P., Hollibaugh J.T., RA Xie G., Stolz J.F., Richardson P.; RT "Complete sequence of Alkalilimnicola ehrilichei MLHE-1."; RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Component of the acetyl coenzyme A carboxylase (ACC) CC complex. First, biotin carboxylase catalyzes the carboxylation of CC biotin on its carrier protein (BCCP) and then the CO(2) group is CC transferred by the carboxyltransferase to acetyl-CoA to form CC malonyl-CoA (By similarity). CC -!- CATALYTIC ACTIVITY: ATP + acetyl-CoA + HCO(3)(-) = ADP + phosphate CC + malonyl-CoA. CC -!- PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA CC from acetyl-CoA: step 1/1. CC -!- SUBUNIT: Acetyl-CoA carboxylase is an heterohexamer composed of CC biotin carboxyl carrier protein (accB), biotin carboxylase (accC) CC and two subunits each of ACCase subunit alpha (accA) and ACCase CC subunit beta (accD) (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Belongs to the accA family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000453; ABI57187.1; -; Genomic_DNA. DR RefSeq; YP_742677.1; -. DR SMR; Q0A7K0; 4-314. DR GeneID; 4269211; -. DR GenomeReviews; CP000453_GR; Mlg_1843. DR KEGG; aeh:Mlg_1843; -. DR NMPDR; fig|187272.6.peg.1754; -. DR HOGENOM; Q0A7K0; -. DR OMA; Q0A7K0; HSVYTVA. DR GO; GO:0009317; C:acetyl-CoA carboxylase complex; IEA:InterPro. DR GO; GO:0003989; F:acetyl-CoA carboxylase activity; IEA:HAMAP. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:HAMAP. DR HAMAP; MF_00823; -; 1. DR InterPro; IPR001095; Acetyl_CoA_COase_a_su. DR InterPro; IPR011763; COA_CT_C. DR PANTHER; PTHR22855:SF3; Ac-CoA_carboxylA; 1. DR Pfam; PF03255; ACCA; 1. DR PRINTS; PR01069; ACCCTRFRASEA. DR TIGRFAMs; TIGR00513; accA; 1. DR PROSITE; PS50989; COA_CT_CTER; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Cytoplasm; Fatty acid biosynthesis; KW Ligase; Lipid synthesis; Nucleotide-binding. FT CHAIN 1 318 Acetyl-coenzyme A carboxylase carboxyl FT transferase subunit alpha. FT /FTId=PRO_1000062573. SQ SEQUENCE 318 AA; 35545 MW; 969A00E3AE8046CA CRC64; MNLNFLDFEQ PIAELEAKIE ELRHVGHDAE VNISEEIQRL QEKSHVLTEK IFANLTAWQI AQLARHPNRP YALDYIDGLF EEFEELHGDR TYADDPAIVG GVARFDGRPV MVIGHQKGRD TREKVRRNFG MPRPEGYRKA LRLMRMAERF QLPIFTFIDT PGAYPGVGAE ERGQSEAIAR NLAAMARLRT PIICTVTGEG GSGGALAIGV GDRLLMLGYS VYSVISPEGC ASILWKSAER ASDAAEAMGI TAHRLHELGL NDRVVEEPLG GAHRNPEAMM ESLRAELREQ LQALEGQSTE TLLADRYQRM MAFGQFRE //