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Database: UniProt
Entry: F1DSV8_9BACT
LinkDB: F1DSV8_9BACT
Original site: F1DSV8_9BACT 
ID   F1DSV8_9BACT            Unreviewed;       157 AA.
AC   F1DSV8;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   SubName: Full=Acetyl CoA-carboxylase {ECO:0000313|EMBL:ADZ16237.1};
DE   Flags: Fragment;
GN   Name=accC {ECO:0000313|EMBL:ADZ16237.1};
OS   uncultured bacterium.
OC   Bacteria; environmental samples.
OX   NCBI_TaxID=77133 {ECO:0000313|EMBL:ADZ16237.1};
RN   [1] {ECO:0000313|EMBL:ADZ16237.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=21517915; DOI=10.1111/j.1574-6941.2011.01117.x;
RA   Lliros M., Alonso-Saez L., Gich F., Plasencia A., Auguet O.,
RA   Casamayor E.O., Borrego C.M.;
RT   "Active bacteria and archaea cells fixing bicarbonate in the dark along the
RT   water column of a stratified eutrophic lagoon.";
RL   FEMS Microbiol. Ecol. 77:370-384(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|ARBA:ARBA00003761}.
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DR   EMBL; HQ901316; ADZ16237.1; -; Genomic_DNA.
DR   AlphaFoldDB; F1DSV8; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR005481; BC-like_N.
DR   InterPro; IPR011764; Biotin_carboxylation_dom.
DR   InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR   InterPro; IPR016185; PreATP-grasp_dom_sf.
DR   PANTHER; PTHR48095:SF2; BIOTIN CARBOXYLASE, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR48095; PYRUVATE CARBOXYLASE SUBUNIT A; 1.
DR   Pfam; PF00289; Biotin_carb_N; 1.
DR   Pfam; PF02786; CPSase_L_D2; 1.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
DR   PROSITE; PS50979; BC; 1.
DR   PROSITE; PS00866; CPSASE_1; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}.
FT   DOMAIN          1..157
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          37..134
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ADZ16237.1"
FT   NON_TER         157
FT                   /evidence="ECO:0000313|EMBL:ADZ16237.1"
SQ   SEQUENCE   157 AA;  16931 MW;  761F1CF67A1F7A8C CRC64;
     FLSENADFAE RVEKSGFAFI GPTAASIRLM GDKVSAKRAM IKAGVPCVPG SEGALPDNPK
     EIITTAKKVG YPVIIKAAGG GGGRGMRVVH TEAALLNGVN MTKEEAGRAF GNPEVYMEKF
     LEKPRHVEIQ ILADTHGNAI WLGERDCSMQ RRHQKVI
//
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