GenomeNet

Database: UniProt
Entry: A0A317ZDS9_9BACT
LinkDB: A0A317ZDS9_9BACT
Original site: A0A317ZDS9_9BACT 
ID   A0A317ZDS9_9BACT        Unreviewed;       454 AA.
AC   A0A317ZDS9;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=Biotin carboxylase {ECO:0000256|ARBA:ARBA00013263, ECO:0000256|RuleBase:RU365063};
DE            EC=6.3.4.14 {ECO:0000256|ARBA:ARBA00013263, ECO:0000256|RuleBase:RU365063};
DE   AltName: Full=Acetyl-coenzyme A carboxylase biotin carboxylase subunit A {ECO:0000256|RuleBase:RU365063};
GN   Name=accC {ECO:0000313|EMBL:PXA03260.1};
GN   ORFNames=DDZ13_12605 {ECO:0000313|EMBL:PXA03260.1};
OS   Coraliomargarita sinensis.
OC   Bacteria; Verrucomicrobiota; Opitutae; Puniceicoccales;
OC   Coraliomargaritaceae; Coraliomargarita.
OX   NCBI_TaxID=2174842 {ECO:0000313|EMBL:PXA03260.1, ECO:0000313|Proteomes:UP000247099};
RN   [1] {ECO:0000313|EMBL:PXA03260.1, ECO:0000313|Proteomes:UP000247099}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WN38 {ECO:0000313|EMBL:PXA03260.1,
RC   ECO:0000313|Proteomes:UP000247099};
RA   Zhou L.Y.;
RT   "Coraliomargarita sinensis sp. nov., isolated from a marine solar
RT   saltern.";
RL   Submitted (MAY-2018) 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|ARBA:ARBA00003761, 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] + phosphate;
CC         Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145,
CC         ChEBI:CHEBI:456216; EC=6.3.4.14;
CC         Evidence={ECO:0000256|RuleBase:RU365063};
CC   -!- PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from
CC       acetyl-CoA: step 1/1. {ECO:0000256|ARBA:ARBA00004956,
CC       ECO:0000256|RuleBase:RU365063}.
CC   -!- SUBUNIT: Acetyl-CoA carboxylase is a heterohexamer of biotin carboxyl
CC       carrier protein, biotin carboxylase and the two subunits of carboxyl
CC       transferase in a 2:2 complex. {ECO:0000256|ARBA:ARBA00011750,
CC       ECO:0000256|RuleBase:RU365063}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PXA03260.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; QHJQ01000010; PXA03260.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A317ZDS9; -.
DR   InParanoid; A0A317ZDS9; -.
DR   OrthoDB; 9807469at2; -.
DR   UniPathway; UPA00655; UER00711.
DR   Proteomes; UP000247099; 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; 3.30.470.20; ATP-grasp fold, B domain; 1.
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   NCBIfam; TIGR00514; accC; 1.
DR   PANTHER; PTHR48095:SF2; BIOTIN CARBOXYLASE, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR48095; PYRUVATE CARBOXYLASE SUBUNIT A; 1.
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; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR   SUPFAM; SSF51246; Rudiment single hybrid motif; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
DR   PROSITE; PS50979; BC; 1.
DR   PROSITE; PS00867; CPSASE_2; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Biotin {ECO:0000256|RuleBase:RU365063};
KW   Fatty acid biosynthesis {ECO:0000256|RuleBase:RU365063};
KW   Fatty acid metabolism {ECO:0000256|RuleBase:RU365063};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU365063};
KW   Lipid biosynthesis {ECO:0000256|RuleBase:RU365063};
KW   Lipid metabolism {ECO:0000256|RuleBase:RU365063};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000247099}.
FT   DOMAIN          1..446
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          120..317
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
SQ   SEQUENCE   454 AA;  50299 MW;  1D28608328D9F91F CRC64;
     MIKKVLIANR GEIALRIVRA CNELGIKTLC VYSEADEQSL HVQLADEAIC IGPPPSHLSY
     LKADRIIAAA EIANVDAIHP GYGFLAENAD FAEQCENCKI KFIGPSSDAI VNFGDKARAR
     EMAVKAKVPV IPGSEGIVDN EKDALAVAKK IGFPVIIKAV AGGGGKGMRV AHNAVAFTKE
     YSSARNEAEK AFGNGAVYIE KFLEAPRHIE IQILGDQHGN VIHLGERDCS VQRRHQKVIE
     EAPSPFISAE TRKKMGRDAV KLAKSVNYEG AGTIEFLMDE KQNYYFIEMN TRIQVEHGVT
     EEITGVDLVK EQLLIASGQK LSYEQKDIKI TRHAIECRVC AEDPSRNFAP CPGEITLYYS
     PGGHGVRIDS HVYSGYTIPP HYDSMIAKVM TFGKTRELAL DRMDRALGEY LIRGIKTNIP
     FSRAIIRDPY FREGKATTKF IEEFINRVPK DIYT
//
DBGET integrated database retrieval system