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Database: UniProt
Entry: A0A0D2NAX2_GOSRA
LinkDB: A0A0D2NAX2_GOSRA
Original site: A0A0D2NAX2_GOSRA 
ID   A0A0D2NAX2_GOSRA        Unreviewed;       518 AA.
AC   A0A0D2NAX2;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   16-JAN-2019, entry version 16.
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=B456_005G116100 {ECO:0000313|EMBL:KJB29722.1};
OS   Gossypium raimondii (New World cotton).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Malvales; Malvaceae; Malvoideae;
OC   Gossypium.
OX   NCBI_TaxID=29730 {ECO:0000313|EMBL:KJB29722.1, ECO:0000313|Proteomes:UP000032304};
RN   [1] {ECO:0000313|EMBL:KJB29722.1, ECO:0000313|Proteomes:UP000032304}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23257886; DOI=10.1038/nature11798;
RA   Paterson A.H., Wendel J.F., Gundlach H., Guo H., Jenkins J., Jin D.,
RA   Llewellyn D., Showmaker K.C., Shu S., Udall J., Yoo M.J., Byers R.,
RA   Chen W., Doron-Faigenboim A., Duke M.V., Gong L., Grimwood J.,
RA   Grover C., Grupp K., Hu G., Lee T.H., Li J., Lin L., Liu T.,
RA   Marler B.S., Page J.T., Roberts A.W., Romanel E., Sanders W.S.,
RA   Szadkowski E., Tan X., Tang H., Xu C., Wang J., Wang Z., Zhang D.,
RA   Zhang L., Ashrafi H., Bedon F., Bowers J.E., Brubaker C.L., Chee P.W.,
RA   Das S., Gingle A.R., Haigler C.H., Harker D., Hoffmann L.V., Hovav R.,
RA   Jones D.C., Lemke C., Mansoor S., ur Rahman M., Rainville L.N.,
RA   Rambani A., Reddy U.K., Rong J.K., Saranga Y., Scheffler B.E.,
RA   Scheffler J.A., Stelly D.M., Triplett B.A., Van Deynze A.,
RA   Vaslin M.F., Waghmare V.N., Walford S.A., Wright R.J., Zaki E.A.,
RA   Zhang T., Dennis E.S., Mayer K.F., Peterson D.G., Rokhsar D.S.,
RA   Wang X., Schmutz J.;
RT   "Repeated polyploidization of Gossypium genomes and the evolution of
RT   spinnable cotton fibres.";
RL   Nature 492:423-427(2012).
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; CM001744; KJB29722.1; -; Genomic_DNA.
DR   EnsemblPlants; KJB29722; KJB29722; B456_005G116100.
DR   Gramene; KJB29722; KJB29722; B456_005G116100.
DR   UniPathway; UPA00655; UER00711.
DR   Proteomes; UP000032304; Chromosome 5.
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:UP000032304};
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:UP000032304}.
FT   DOMAIN       68    495       Biotin carboxylation.
FT                                {ECO:0000259|PROSITE:PS50979}.
FT   DOMAIN      169    366       ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
SQ   SEQUENCE   518 AA;  56850 MW;  CD755B41DF2F9A6D CRC64;
     MAMDASLTMC KSVTSPPGLF LGRSRVIRSS QCTFMVGSRI NFPRQKAQST QVRCKSSRCG
     GALGAKCRAE KILVANRGEI AVRVIRTAHE MGIPCVAVYS TIDKDALHVK LADESVCIGE
     APSSQSYLLI PNVLSAAISR NCTMLHPGYG FLSENAVFVE MCRDHRINFI GPNNAGVPTV
     PGSDGLLQST EEAIKLAHEI GFPVMIKATA GGGGRGMRLA KEPDEFVKLL QQAKSEAAAA
     FGNDGVYLEK YIQNPRHIEF QVLADKYGNV VHFGERDCSI QRRNQKLLEE APSPALTPEL
     RKAMGDAAVA AAASIGYIGV GTVEFLLDER GSFYFMEMNT RIQVEHPVTE MISSVDLIEE
     QIRVAMGEKL RYKQEDIVLR GHSIECRINA EDAFKGFRPR PGRITSYLPS GGPFVRMDSH
     VYSDYVVPPS YDSLLGKLIV WAPTREKAIE RMKRALDDTV ITGVPTTIEY HKLILDIEDF
     RNGKVDTAFI PKHEEELAAP QKMVVAKSPA KELTSATA
//
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