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Database: UniProt
Entry: A0A0L1JTI3_9RHOB
LinkDB: A0A0L1JTI3_9RHOB
Original site: A0A0L1JTI3_9RHOB 
ID   A0A0L1JTI3_9RHOB        Unreviewed;       449 AA.
AC   A0A0L1JTI3;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   16-JAN-2019, entry version 14.
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=ATO11_06460 {ECO:0000313|EMBL:KNG94997.1};
OS   Pseudaestuariivita atlantica.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Pseudaestuariivita.
OX   NCBI_TaxID=1317121 {ECO:0000313|EMBL:KNG94997.1, ECO:0000313|Proteomes:UP000036938};
RN   [1] {ECO:0000313|EMBL:KNG94997.1, ECO:0000313|Proteomes:UP000036938}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=22II-S11-z3 {ECO:0000313|EMBL:KNG94997.1,
RC   ECO:0000313|Proteomes:UP000036938};
RA   Li G., Lai Q., Du Y., Liu X., Sun F., Shao Z.;
RT   "Aestuariivita atlantica sp. nov., isolated from deep sea sediment of
RT   the Atlantic Ocean.";
RL   Int. J. Syst. Evol. Microbiol. 0:0-0(2015).
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:KNG94997.1}.
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DR   EMBL; AQQZ01000002; KNG94997.1; -; Genomic_DNA.
DR   RefSeq; WP_050529991.1; NZ_AQQZ01000002.1.
DR   EnsemblBacteria; KNG94997; KNG94997; ATO11_06460.
DR   PATRIC; fig|1317121.7.peg.1673; -.
DR   OrthoDB; 361205at2; -.
DR   UniPathway; UPA00655; UER00711.
DR   Proteomes; UP000036938; 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   Complete proteome {ECO:0000313|Proteomes:UP000036938};
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:KNG94997.1};
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:UP000036938}.
FT   DOMAIN        1    444       Biotin carboxylation.
FT                                {ECO:0000259|PROSITE:PS50979}.
FT   DOMAIN      120    316       ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
SQ   SEQUENCE   449 AA;  48583 MW;  6BD5DBC183C177A1 CRC64;
     MFDKILIANR GEIALRVIRA CREMGIASVA VHSTADADAM HVRMADEAIC IGPAPGTQSY
     LHMPAIISAC EITGAQAIHP GYGFLSENAR FVQIVQDHGL TFIGPTADHI NIMGDKITAK
     DTMKALGVPC VPGSDGGVPD LAAARAIGEE FGYPVIVKAT AGGGGRGMKV AQNAADMEIA
     FSSARSEAKA AFGNDECYIE KYLTTPRHIE IQVFGDGKGN AVHLGERDCS LQRRHQKVFE
     EAPGPAISPE ERAEIGAVCA KAVADINYAG AGTIEFLYEK GEFYFIEMNT RLQVEHPVTE
     AIFGVDLVRE QIRVAAGLPL SFSKDDLQIN GHAIEVRLNA EKLPSFTPSP GRISQYHAPG
     GLGVRMDSAI YDGYSIPPYY DSLIGKLIVH GRDRPEALAR LNRALGELII DGIDTTVPLF
     HALLEEADIH SGDYNIHWLE HWLDSWADR
//
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