ID A0A318ABJ5_9MICC Unreviewed; 681 AA.
AC A0A318ABJ5;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=biotin carboxylase {ECO:0000256|ARBA:ARBA00013263};
DE EC=6.3.4.14 {ECO:0000256|ARBA:ARBA00013263};
GN ORFNames=DCC25_10845 {ECO:0000313|EMBL:PXA78810.1};
OS Auritidibacter sp. NML120636.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Auritidibacter.
OX NCBI_TaxID=2170743 {ECO:0000313|EMBL:PXA78810.1, ECO:0000313|Proteomes:UP000247286};
RN [1] {ECO:0000313|EMBL:PXA78810.1, ECO:0000313|Proteomes:UP000247286}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NML120636 {ECO:0000313|EMBL:PXA78810.1,
RC ECO:0000313|Proteomes:UP000247286};
RA Bernard K., Pacheco A.L., Burdz T., Wiebe D., Beniac D., Booth T.,
RA Goldenberger D., Seth-Smith H., Egli A., Bernier A.-M.;
RT "Auritidibacter winnipegensis sp. nov. recovered from Human Clinical
RT Materials and Emendation of the Genus Auritidibacter (Yassin et al 2011).";
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
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:PXA78810.1}.
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DR EMBL; QHLO01000017; PXA78810.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A318ABJ5; -.
DR Proteomes; UP000247286; Unassembled WGS sequence.
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 CDD; cd06850; biotinyl_domain; 1.
DR Gene3D; 2.40.50.100; -; 1.
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; IPR001882; Biotin_BS.
DR InterPro; IPR011764; Biotin_carboxylation_dom.
DR InterPro; IPR005482; Biotin_COase_C.
DR InterPro; IPR000089; Biotin_lipoyl.
DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR InterPro; IPR011053; Single_hybrid_motif.
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; PF02785; Biotin_carb_C; 1.
DR Pfam; PF00289; Biotin_carb_N; 1.
DR Pfam; PF00364; Biotin_lipoyl; 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 SUPFAM; SSF51230; Single hybrid motif; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS50979; BC; 1.
DR PROSITE; PS00188; BIOTIN; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS00866; CPSASE_1; 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|ARBA:ARBA00023267};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000247286}.
FT DOMAIN 8..455
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 127..326
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 592..668
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 681 AA; 73211 MW; 7A667AB33F5E9A3D CRC64;
MDQPTASVFR TVMIANRGEI ACRVIRTVHQ MGMTAVAVYT TPDAQALHVR LADRAVHLPD
HQATTGYLDI DAVVAAAVET GSDAIHPGYG FLSENADFAR ACARAGITFI GPDAQALEIM
GDKITSKKHV GAAGVPLIQG ISEPGLSDEE LVDKACSMTF PVLIKPSAGG GGKGMYVAEF
LDQLPEMLAT ARRIAHASFG DDTLFIEQLI GSPRHVEVQI LADQHGNVIH LGERECSLQR
RHQKVIEEAP SVVLTDQTRA RIGQAACDTA LSVNYRGAGT VEFLVSDHDP DTFYFMEMNT
RLQVEHPVTE EITGIDLVEQ QLRIAAGEPL AYTQDEIQLR GHSVEARVYA EVPAAGFLPS
TGTILELAEP AGTGVRVDSG LRRGSVIGTN FDPMLAKVIA TGTHRDQALD RLDRALKNMV
VLGVQTNISY LRQLINDSRV RAGALDTTMI ERILPEMDFP GPGADDAQIA ATLAYHFEPA
PTTSLSSGWR CDGWRSMAES PSVRRHVSYR TASGDTEDFD VTLDPSTVVE QVGDHEYLLS
TPESMTTRVH AVVATQRAGQ SQLWCFTPNF AGLLTISDRQ AITSNEVQAQ QAGTAGLISN
PDVSSPLPGT VMSVLATSGD QVSAGDTLVI VEAMKMEHRL VAPFDGVVTI HTAETEQVKL
GQVLASITPD DDKNPENEPA N
//
