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Database: UniProt
Entry: A1WHZ3_VEREI
LinkDB: A1WHZ3_VEREI
Original site: A1WHZ3_VEREI 
ID   A1WHZ3_VEREI            Unreviewed;       449 AA.
AC   A1WHZ3;
DT   06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2007, sequence version 1.
DT   08-MAY-2019, entry version 77.
DE   RecName: Full=Biotin carboxylase {ECO:0000256|RuleBase:RU365063};
DE            EC=6.3.4.14 {ECO:0000256|RuleBase:RU365063};
DE            EC=6.4.1.2 {ECO:0000256|RuleBase:RU365063};
GN   OrderedLocusNames=Veis_1490 {ECO:0000313|EMBL:ABM57250.1};
OS   Verminephrobacter eiseniae (strain EF01-2).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Verminephrobacter.
OX   NCBI_TaxID=391735 {ECO:0000313|EMBL:ABM57250.1, ECO:0000313|Proteomes:UP000000374};
RN   [1] {ECO:0000313|Proteomes:UP000000374}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EF01-2 {ECO:0000313|Proteomes:UP000000374};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chertkov O.,
RA   Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Stahl D.,
RA   Richardson P.;
RT   "Complete sequence of chromosome 1 of Verminephrobacter eiseniae EF01-
RT   2.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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.
CC       {ECO:0000256|RuleBase:RU365063}.
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         Evidence={ECO:0000256|RuleBase:RU365063};
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         Evidence={ECO:0000256|RuleBase:RU365063};
CC   -!- PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA
CC       from acetyl-CoA: step 1/1. {ECO:0000256|RuleBase:RU365063}.
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.
CC       {ECO:0000256|RuleBase:RU365063}.
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DR   EMBL; CP000542; ABM57250.1; -; Genomic_DNA.
DR   RefSeq; WP_011809257.1; NC_008786.1.
DR   STRING; 391735.Veis_1490; -.
DR   EnsemblBacteria; ABM57250; ABM57250; Veis_1490.
DR   KEGG; vei:Veis_1490; -.
DR   eggNOG; ENOG4105CER; Bacteria.
DR   eggNOG; COG0439; LUCA.
DR   HOGENOM; HOG000008988; -.
DR   KO; K01961; -.
DR   OMA; FVEICSH; -.
DR   OrthoDB; 361205at2; -.
DR   BioCyc; VEIS391735:GHY5-1471-MONOMER; -.
DR   UniPathway; UPA00655; UER00711.
DR   Proteomes; UP000000374; Chromosome.
DR   GO; GO:0003989; F:acetyl-CoA carboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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   4: Predicted;
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409,
KW   ECO:0000256|RuleBase:RU365063};
KW   Biotin {ECO:0000256|RuleBase:RU365063};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000374};
KW   Fatty acid biosynthesis {ECO:0000256|RuleBase:RU365063};
KW   Fatty acid metabolism {ECO:0000256|RuleBase:RU365063};
KW   Ligase {ECO:0000256|RuleBase:RU365063};
KW   Lipid biosynthesis {ECO:0000256|RuleBase:RU365063};
KW   Lipid metabolism {ECO:0000256|RuleBase:RU365063};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409,
KW   ECO:0000256|RuleBase:RU365063};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000374}.
FT   DOMAIN        1    445       Biotin carboxylation.
FT                                {ECO:0000259|PROSITE:PS50979}.
FT   DOMAIN      120    317       ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
SQ   SEQUENCE   449 AA;  49560 MW;  5EBCB6D35045C4E1 CRC64;
     MFKKILVANR GEIALRIQRA CHELGVKAVM VYSEADREAK YIKLAEEAVC IGPAPSPLSY
     LNMPAIISAA EVTDAEAIHP GYGFLSENAD FAERVEKSGF QFIGPTPESI RSMGDKVSAK
     QAMIRAGVPC VPGSEGELPD DPVQVRRIAK AVGYPVIIKA AGGGGGRGMR VVHTEAALVN
     AVQMTKAEAG AAFGNPAVYM EKFLQNPRHI EIQVLADKHR NAVYLGERDC SMQRRHQKVI
     EEAPAPGIAR KLIEKIGERC VAACKKIGYR GAGTFEFLYE NEEFYFIEMN TRVQVEHPVT
     EWITGVDIVK TQIMVAAGEK LPMTQRQVQI RGHAIECRVN AEDPYRFTPS PGRITTWHPP
     GGPGVRVDSH AYTNYVVPPN YDSMIGKIIV HGDTREQALA RMRTALSETV IEGISTNVPL
     HRELMIDAKF MAGGTNIHYL EEWLSQRQR
//
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