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Database: UniProt
Entry: N9MJL3_9GAMM
LinkDB: N9MJL3_9GAMM
Original site: N9MJL3_9GAMM 
ID   N9MJL3_9GAMM            Unreviewed;       456 AA.
AC   N9MJL3;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   13-FEB-2019, entry version 22.
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   ORFNames=F897_01980 {ECO:0000313|EMBL:ENX08829.1};
OS   Acinetobacter variabilis.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Moraxellaceae; Acinetobacter.
OX   NCBI_TaxID=70346 {ECO:0000313|EMBL:ENX08829.1, ECO:0000313|Proteomes:UP000013101};
RN   [1] {ECO:0000313|EMBL:ENX08829.1, ECO:0000313|Proteomes:UP000013101}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIPH 2171 {ECO:0000313|EMBL:ENX08829.1,
RC   ECO:0000313|Proteomes:UP000013101};
RG   The Broad Institute Genome Sequencing Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Cerqueira G., Feldgarden M., Courvalin P., Perichon B.,
RA   Grillot-Courvalin C., Clermont D., Rocha E., Yoon E.-J., Nemec A.,
RA   Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA   Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B.,
RA   Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA   Imamovic A., Larimer J., McCowan C., Murphy C., Neiman D., Pearson M.,
RA   Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S.,
RA   Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Acinetobacter sp. NIPH 2171.";
RL   Submitted (FEB-2013) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:ENX08829.1}.
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DR   EMBL; APRS01000012; ENX08829.1; -; Genomic_DNA.
DR   RefSeq; WP_005235439.1; NZ_KB850113.1.
DR   EnsemblBacteria; ENX08829; ENX08829; F897_01980.
DR   PATRIC; fig|1217693.3.peg.1908; -.
DR   UniPathway; UPA00655; UER00711.
DR   Proteomes; UP000013101; Unassembled WGS sequence.
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:UP000013101};
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}.
FT   DOMAIN        1    444       Biotin carboxylation.
FT                                {ECO:0000259|PROSITE:PS50979}.
FT   DOMAIN      120    315       ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
SQ   SEQUENCE   456 AA;  50334 MW;  BBB29019A39C0225 CRC64;
     MLQKVLIANR GEIALRIARA CKTLGIKTVG VYSDADKDLM HLRFCDEAVC IGPGASSDSY
     LNIPALITAA EITSADAIHP GYGFLSENAE FAEIVESSGF IFIGPRPEHI RLMGNKVSAI
     IAMKKAGVPT VPGCDHAVTI HNALAEAKEI GFPLIVKAAS GGGGRGMRIV ERVDTLLESV
     QAAQRDAEMW FGDDTVYMER FLQKPRHVEV QVLGDGNGHA IHLYDRDCSL QRRHQKVLEE
     APAPNLPKQA RADILEACVN ACKLMQYRGA GTFEFLFEEG EFFFIEMNTR VQVEHPVTEM
     VTGIDIIEQQ LRIAAGLGLD IQQEDVRVQG HAIECRINAE DPSNFMPSPG KIETFYAPGG
     AGIRLDSHIY PGYSIPPYYD SMIAKLIAHG KDRETAIARM KQALDEMILT GVKTNIPLHK
     DLILQDENFC EQAMDIHYLE KHLLKQLEGA EDKEKA
//
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