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Database: UniProt
Entry: O52058
LinkDB: O52058
Original site: O52058 
ID   ACCC_ALLVD              Reviewed;         449 AA.
AC   O52058; D3RUH1;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-JUN-2010, sequence version 2.
DT   16-JAN-2019, entry version 105.
DE   RecName: Full=Biotin carboxylase;
DE            EC=6.3.4.14;
DE   AltName: Full=Acetyl-CoA carboxylase subunit A;
DE            Short=ACC;
DE            EC=6.4.1.2;
GN   Name=accC; OrderedLocusNames=Alvin_1906;
OS   Allochromatium vinosum (strain ATCC 17899 / DSM 180 / NBRC 103801 /
OS   NCIMB 10441 / D) (Chromatium vinosum).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales;
OC   Chromatiaceae; Allochromatium.
OX   NCBI_TaxID=572477;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB 10441 / D;
RX   PubMed=22675582; DOI=10.4056/sigs.2335270;
RA   Weissgerber T., Zigann R., Bruce D., Chang Y.J., Detter J.C., Han C.,
RA   Hauser L., Jeffries C.D., Land M., Munk A.C., Tapia R., Dahl C.;
RT   "Complete genome sequence of Allochromatium vinosum DSM 180(T).";
RL   Stand. Genomic Sci. 5:311-330(2011).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 309-449.
RX   PubMed=9560425; DOI=10.1007/s002030050594;
RA   Pattaragulwanit K., Brune D.C., Trueper H.G., Dahl C.;
RT   "Molecular genetic evidence for extracytoplasmic localization of
RT   sulfur globules in Chromatium vinosum.";
RL   Arch. Microbiol. 169:434-444(1998).
CC   -!- FUNCTION: This protein is a component of the acetyl coenzyme A
CC       carboxylase complex; first, biotin carboxylase catalyzes the
CC       carboxylation of the carrier protein and then the transcarboxylase
CC       transfers the carboxyl group to form malonyl-CoA. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein]
CC         = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505,
CC         Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144,
CC         ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) +
CC         malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384,
CC         ChEBI:CHEBI:456216; EC=6.4.1.2;
CC   -!- PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA
CC       from acetyl-CoA: step 1/1.
CC   -!- SUBUNIT: Acetyl-CoA carboxylase is a heterohexamer of biotin
CC       carboxyl carrier protein, biotin carboxylase and the two subunits
CC       of carboxyl transferase in a 2:2 complex. {ECO:0000250}.
DR   EMBL; CP001896; ADC62830.1; -; Genomic_DNA.
DR   EMBL; AF017119; AAB91545.1; -; Genomic_DNA.
DR   ProteinModelPortal; O52058; -.
DR   SMR; O52058; -.
DR   STRING; 572477.Alvin_1906; -.
DR   EnsemblBacteria; ADC62830; ADC62830; Alvin_1906.
DR   KEGG; alv:Alvin_1906; -.
DR   eggNOG; ENOG4105CER; Bacteria.
DR   eggNOG; COG0439; LUCA.
DR   HOGENOM; HOG000008988; -.
DR   KO; K01961; -.
DR   OMA; FVEICSH; -.
DR   UniPathway; UPA00655; UER00711.
DR   Proteomes; UP000001441; Chromosome.
DR   GO; GO:0003989; F:acetyl-CoA carboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004075; F:biotin carboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:2001295; P:malonyl-CoA biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.30.1490.20; -; 1.
DR   InterPro; IPR004549; Acetyl_CoA_COase_biotin_COase.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR005481; BC-like_N.
DR   InterPro; IPR011764; Biotin_carboxylation_dom.
DR   InterPro; IPR005482; Biotin_COase_C.
DR   InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR   InterPro; IPR016185; PreATP-grasp_dom_sf.
DR   InterPro; IPR011054; Rudment_hybrid_motif.
DR   Pfam; PF02785; Biotin_carb_C; 1.
DR   Pfam; PF00289; Biotin_carb_N; 1.
DR   Pfam; PF02786; CPSase_L_D2; 1.
DR   SMART; SM00878; Biotin_carb_C; 1.
DR   SUPFAM; SSF51246; SSF51246; 1.
DR   SUPFAM; SSF52440; SSF52440; 1.
DR   TIGRFAMs; TIGR00514; accC; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
DR   PROSITE; PS50979; BC; 1.
DR   PROSITE; PS00866; CPSASE_1; 1.
DR   PROSITE; PS00867; CPSASE_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Biotin; Complete proteome; Fatty acid biosynthesis;
KW   Fatty acid metabolism; Ligase; Lipid biosynthesis; Lipid metabolism;
KW   Nucleotide-binding; Reference proteome.
FT   CHAIN         1    449       Biotin carboxylase.
FT                                /FTId=PRO_0000146790.
FT   DOMAIN        4    448       Biotin carboxylation.
FT   DOMAIN      123    320       ATP-grasp. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00409}.
FT   ACT_SITE    295    295       {ECO:0000255}.
FT   CONFLICT    427    427       I -> L (in Ref. 2; AAB91545).
FT                                {ECO:0000305}.
FT   CONFLICT    437    437       Missing (in Ref. 2; AAB91545).
FT                                {ECO:0000305}.
SQ   SEQUENCE   449 AA;  49268 MW;  40510894E20C82E4 CRC64;
     MSAMIEKVLI ANRGEIALRI LRACRELGIK TVAVHSEADR DLKHVLLADE SVCIGPAPAM
     QSYLNVPAII SAAEVTDTVA IHPGYGFLSE NADFAERVEK SGFIFIGPRP ETIRLMGDKV
     SAIAAMKAAG VPCVPGSDGP IDDNKKRTLE LAREIGYPIM IKSSGGGGGR GMRVVHSEAT
     LLNAIALTRA EAAAAFNNDM VYMEKYLENP RHIEFQVLAD QMGNAIHLGE RDCSMQRRHQ
     KVVEEAPAPG ITEEQRREIG ERCAAACRSI GYRGAGTFEF LYENGQFYFI EMNTRVQVEH
     PVTEMVTGVD IVKEQILIAA GEPLRYRQSD IQMRGHAIEC RINAEHPETF MPSPGKITDF
     HAPGGPGVRI ETHIYSGYTV PCHYDSMIGK LITHGEDRES AVARMCNALR ETVIEGIHSN
     IKLQRSIMRD GAFLAGGANI HYLEKMLGL
//
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