ID B1GX48_9BACT Unreviewed; 150 AA.
AC B1GX48;
DT 29-APR-2008, integrated into UniProtKB/TrEMBL.
DT 29-APR-2008, sequence version 1.
DT 22-FEB-2023, entry version 38.
DE SubName: Full=Putative biotin carboxylase {ECO:0000313|EMBL:CAQ15970.1};
DE EC=6.3.4.14 {ECO:0000313|EMBL:CAQ15970.1};
DE Flags: Fragment;
GN Name=accC {ECO:0000313|EMBL:CAQ15970.1};
OS uncultured bacterium.
OC Bacteria; environmental samples.
OX NCBI_TaxID=77133 {ECO:0000313|EMBL:CAQ15970.1};
RN [1] {ECO:0000313|EMBL:CAQ15970.1}
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:CAQ15970.1}
RP NUCLEOTIDE SEQUENCE.
RA Auguet J.;
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; AM943460; CAQ15970.1; -; Genomic_DNA.
DR AlphaFoldDB; B1GX48; -.
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:CAQ15970.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}.
FT DOMAIN 1..150
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 37..138
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:CAQ15970.1"
FT NON_TER 150
FT /evidence="ECO:0000313|EMBL:CAQ15970.1"
SQ SEQUENCE 150 AA; 16488 MW; E84269E0ECC98BF2 CRC64;
FLSENSAFAE ECEKNNIIFI GPKSKAIEMM GSKLAAKEAV MKYDIPMVPG VDHAIIDVEE
AKRTAQQVGF PILIKASAGG GGKGMRIVEK EEDFESQMER AISEATNAFG DGSVFIEKYV
TKPRHIEIQI MADNHGNVLY LLKENAVQLL
//
