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Database: UniProt
Entry: F0RGR5_CELLC
LinkDB: F0RGR5_CELLC
Original site: F0RGR5_CELLC 
ID   F0RGR5_CELLC            Unreviewed;       451 AA.
AC   F0RGR5;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   08-MAY-2019, entry version 44.
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=Celly_1266 {ECO:0000313|EMBL:ADY29094.1};
OS   Cellulophaga lytica (strain ATCC 23178 / DSM 7489 / JCM 8516 / NBRC
OS   14961 / NCIMB 1423 / VKM B-1433 / Cy l20).
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Cellulophaga.
OX   NCBI_TaxID=867900 {ECO:0000313|EMBL:ADY29094.1, ECO:0000313|Proteomes:UP000007487};
RN   [1] {ECO:0000313|EMBL:ADY29094.1, ECO:0000313|Proteomes:UP000007487}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23178 / DSM 7489 / JCM 8516 / NBRC 14961 / NCIMB 1423 /
RC   VKM B-1433 / Cy l20 {ECO:0000313|Proteomes:UP000007487};
RX   PubMed=21677859; DOI=10.4056/sigs.1774329;
RA   Pati A., Abt B., Teshima H., Nolan M., Lapidus A., Lucas S.,
RA   Hammon N., Deshpande S., Cheng J.F., Tapia R., Han C., Goodwin L.,
RA   Pitluck S., Liolios K., Pagani I., Mavromatis K., Ovchinikova G.,
RA   Chen A., Palaniappan K., Land M., Hauser L., Jeffries C.D.,
RA   Detter J.C., Brambilla E.M., Kannan K.P., Rohde M., Spring S.,
RA   Goker M., Woyke T., Bristow J., Eisen J.A., Markowitz V.,
RA   Hugenholtz P., Kyrpides N.C., Klenk H.P., Ivanova N.;
RT   "Complete genome sequence of Cellulophaga lytica type strain
RT   (LIM- 21).";
RL   Stand. Genomic Sci. 4:221-232(2011).
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; CP002534; ADY29094.1; -; Genomic_DNA.
DR   RefSeq; WP_013620841.1; NC_015167.1.
DR   STRING; 867900.Celly_1266; -.
DR   EnsemblBacteria; ADY29094; ADY29094; Celly_1266.
DR   KEGG; cly:Celly_1266; -.
DR   eggNOG; ENOG4105CER; Bacteria.
DR   eggNOG; COG0439; LUCA.
DR   KO; K01961; -.
DR   OMA; ITHFHTP; -.
DR   BioCyc; CLYT867900:G1GRQ-1282-MONOMER; -.
DR   UniPathway; UPA00655; UER00711.
DR   Proteomes; UP000007487; 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   InterPro; IPR004549; Acetyl_CoA_COase_biotin_COase.
DR   InterPro; IPR011761; ATP-grasp.
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:UP000007487};
KW   Fatty acid biosynthesis {ECO:0000256|RuleBase:RU365063};
KW   Fatty acid metabolism {ECO:0000256|RuleBase:RU365063};
KW   Ligase {ECO:0000256|RuleBase:RU365063, ECO:0000313|EMBL:ADY29094.1};
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:UP000007487}.
FT   DOMAIN        1    444       Biotin carboxylation.
FT                                {ECO:0000259|PROSITE:PS50979}.
FT   DOMAIN      120    317       ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
SQ   SEQUENCE   451 AA;  50202 MW;  78762D6A862CCFED CRC64;
     MFKKILIANR GEIALRIIRT CKEMGIKTVA VYSKADEESL HVRFADEAVC IGPAPSNESY
     LKIPNIIAAA EITNADAIHP GYGFLSENSK FSKICAEHDI KFIGASGEHI DRMGDKASAR
     ETMKKAGVPT IPGSDGLLKD VAEAKKVAKK MGYPVMIKAT AGGGGKGMRA VWSEDKMEAL
     YESAVQEATA AFGNGAMYME KLIEEPRHIE IQVVGDQYGK ACHLSERDCS IQRRHQKLTE
     ETPSPFMTDK LRDDMGAAAV KAAEYIKYEG AGTIEFLVDK HRNFYFMEMN TRIQVEHPIT
     EQVVDYDLIR EQILVAGGVP ISGKNYYPKL HSIECRINAE DPRNDFRPSP GKITTLHTPG
     GHGVRLDTNV YSGYTIPPYY DSMVAKLITT AQTREEAINK MKRALDEFVI EGVKTTIPFH
     RQLMDHPDYL AGNYTTAFME DFVMEPSKDD E
//
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