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Database: UniProt
Entry: B1GX65_9BACT
LinkDB: B1GX65_9BACT
Original site: B1GX65_9BACT 
ID   B1GX65_9BACT            Unreviewed;       152 AA.
AC   B1GX65;
DT   29-APR-2008, integrated into UniProtKB/TrEMBL.
DT   29-APR-2008, sequence version 1.
DT   22-FEB-2023, entry version 36.
DE   SubName: Full=Putative biotin carboxylase {ECO:0000313|EMBL:CAQ15987.1};
DE            EC=6.3.4.14 {ECO:0000313|EMBL:CAQ15987.1};
DE   Flags: Fragment;
GN   Name=accC {ECO:0000313|EMBL:CAQ15987.1};
OS   uncultured bacterium.
OC   Bacteria; environmental samples.
OX   NCBI_TaxID=77133 {ECO:0000313|EMBL:CAQ15987.1};
RN   [1] {ECO:0000313|EMBL:CAQ15987.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Auguet J.C., Borrego C.M., Baneras L., Casamayor E.O.;
RT   "Fingerprinting the genetic diversity of the biotin carboxylase gene (accC)
RT   in aquatic ecosystems as a potential marker for studies of carbon dioxide
RT   assimilation in the dark.";
RL   Environ. Microbiol. 10:2527-2536(2008).
RN   [2] {ECO:0000313|EMBL:CAQ15987.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Auguet J.;
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AM943477; CAQ15987.1; -; Genomic_DNA.
DR   AlphaFoldDB; B1GX65; -.
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   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; PTHR18866; CARBOXYLASE:PYRUVATE/ACETYL-COA/PROPIONYL-COA CARBOXYLASE; 1.
DR   PANTHER; PTHR18866:SF33; METHYLCROTONOYL-COA CARBOXYLASE SUBUNIT ALPHA, MITOCHONDRIAL-RELATED; 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};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:CAQ15987.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}.
FT   DOMAIN          1..152
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          47..136
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:CAQ15987.1"
FT   NON_TER         152
FT                   /evidence="ECO:0000313|EMBL:CAQ15987.1"
SQ   SEQUENCE   152 AA;  16307 MW;  6F19BEE52EAB9BCF CRC64;
     DAIHPGYGFL FENEQFAERC EEEGIVFIGP KHPSIAAMGD KIASKKLALE AKVNTIPGHN
     EAIATTEEAV KIAQGIGYPV MIKASAGGGG KGLRVAFNDK EAAEGFAACK TEAMNSFGDD
     RIFIEKFVEG PRHIEIPGIG RFSWQCGLPE RA
//
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