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Database: UniProt
Entry: I0Z7E6_COCSC
LinkDB: I0Z7E6_COCSC
Original site: I0Z7E6_COCSC 
ID   I0Z7E6_COCSC            Unreviewed;       554 AA.
AC   I0Z7E6;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   05-JUN-2019, entry version 30.
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=COCSUDRAFT_64553 {ECO:0000313|EMBL:EIE26565.1};
OS   Coccomyxa subellipsoidea (strain C-169) (Green microalga).
OC   Eukaryota; Viridiplantae; Chlorophyta; Trebouxiophyceae;
OC   Elliptochloris clade; Coccomyxa.
OX   NCBI_TaxID=574566 {ECO:0000313|EMBL:EIE26565.1, ECO:0000313|Proteomes:UP000007264};
RN   [1] {ECO:0000313|EMBL:EIE26565.1, ECO:0000313|Proteomes:UP000007264}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C-169 {ECO:0000313|EMBL:EIE26565.1,
RC   ECO:0000313|Proteomes:UP000007264};
RX   PubMed=22630137; DOI=10.1186/gb-2012-13-5-r39;
RA   Blanc G., Agarkova I., Grimwood J., Kuo A., Brueggeman A., Dunigan D.,
RA   Gurnon J., Ladunga I., Lindquist E., Lucas S., Pangilinan J.,
RA   Proschold T., Salamov A., Schmutz J., Weeks D., Yamada T.,
RA   Claverie J.M., Grigoriev I., Van Etten J., Lomsadze A., Borodovsky M.;
RT   "The genome of the polar eukaryotic microalga coccomyxa subellipsoidea
RT   reveals traits of cold adaptation.";
RL   Genome Biol. 13:R39-R39(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}.
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:EIE26565.1}.
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DR   EMBL; AGSI01000002; EIE26565.1; -; Genomic_DNA.
DR   RefSeq; XP_005651109.1; XM_005651052.1.
DR   STRING; 248742.XP_005651109.1; -.
DR   GeneID; 17044575; -.
DR   KEGG; csl:COCSUDRAFT_64553; -.
DR   KO; K01961; -.
DR   OrthoDB; 254436at2759; -.
DR   UniPathway; UPA00655; UER00711.
DR   Proteomes; UP000007264; 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   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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000007264};
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:UP000007264}.
FT   DOMAIN       78    522       Biotin carboxylation.
FT                                {ECO:0000259|PROSITE:PS50979}.
FT   DOMAIN      197    393       ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
FT   REGION      520    541       Disordered. {ECO:0000256|MobiDB-lite:
FT                                I0Z7E6}.
FT   COILED      382    402       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   554 AA;  60075 MW;  4421294A7EF2D982 CRC64;
     MHAPAILAHS PAVGHPIGAS RSPHTAKVNA RSLSKSVVLQ SEIFGSSCGQ FLPRQASLAA
     SPIRCTERSR RSVAPTAAFS KVLIANRGEI AVRVIRACKE LGLKTVAVYS IADVDCLHVQ
     LADEAVCIGE AASSASYLNI PNIIAAAISR GADAIHPGYG FLSENSTFVD ICSDHGIEFI
     GPKSDHIRTM GDKSTARDTM KAAGVPTVPG SDGLIKDEAE AIEVSRKMGF PVMIKATAGG
     GGRGMRLAMH EGEFVSLLQQ ATQEAEAAFG NGKVYLERYV QNPRHIEFQV LADKHGNCIH
     LGERDCSIQR RNQKLLEEAP SPALTPEVRK AMGDAAVNAA KSIGYIGVGT IEFLWEATGF
     YFMEMNTRIQ VEHPVTEMIT GIDLIQEQIR AAQGEVLRFK QEDIQIKGHA IECRINAEDP
     FKNFRPGPGR VIGYLAPGGP HVRMDSHLYP DYLVPPNYDS LLGKLIVWGE DRNQAIARMH
     RALNELVISG VPTTTIYHTM ILQIEDFVNG NVDTGFIPKH QAELSEPPPP REGSNVVEKA
     AKRAHKRAKK LALA
//
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