ID A0A318K269_9NOCA Unreviewed; 646 AA.
AC A0A318K269;
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};
DE EC=6.3.4.14 {ECO:0000256|ARBA:ARBA00013263};
GN ORFNames=DFR70_107246 {ECO:0000313|EMBL:PXX62378.1};
OS Nocardia tenerifensis.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Nocardia.
OX NCBI_TaxID=228006 {ECO:0000313|EMBL:PXX62378.1, ECO:0000313|Proteomes:UP000247569};
RN [1] {ECO:0000313|EMBL:PXX62378.1, ECO:0000313|Proteomes:UP000247569}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44704 {ECO:0000313|EMBL:PXX62378.1,
RC ECO:0000313|Proteomes:UP000247569};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00024172};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13502;
CC Evidence={ECO:0000256|ARBA:ARBA00024172};
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:PXX62378.1}.
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DR EMBL; QJKF01000007; PXX62378.1; -; Genomic_DNA.
DR RefSeq; WP_040733559.1; NZ_QJKF01000007.1.
DR AlphaFoldDB; A0A318K269; -.
DR OrthoDB; 4435847at2; -.
DR Proteomes; UP000247569; 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}.
FT DOMAIN 1..439
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 117..313
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 567..640
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 646 AA; 69008 MW; FDBB78697E4F9946 CRC64;
MITTLLIANR GEVAARIART CDRLGIDYVT VSVDEDRDET YHHGAVATVR LPEVGSHLDA
AALVRAATET GCDAVHPGYG FLSENAGFAR AVRSAGLVFV GPSSRVIETM ADKASARTVL
ADAGVPVLPG TRQATDDLDA LASAAEDVGY PLIVKPAGGG GGKGMSVVRS QAELRESLAS
ATRTATAAFA DGRLHLERYV EHARHIEVQV FGDEFGSAVH LFDRDCSLQR RHQKVIEEAP
APRIPETIRA RIFDAAVRGA RALNYVGAGT FEFLLVGEEF FFIEMNTRLQ VEHTVTEEIT
GIDLVDWQLR VASGEPLPAT QEQIAYSGAS VQVRMYAEDP FRAFLPCPGA LEVTQWPDVR
IERAFDHRLN VTGGFDPMIA KLVATGATRD EALAAARQAC TDLRWTGIST NLGFVGHVLG
SPIVAAVEHD TAYLDRIDPT AEFADPDLLG ALAVAAALTA PDRTTPWSAG APVGDRALLD
PADRDLGSID LSVDGRPFTI RVNGYDGDAV RVRADTTDRG VACVRTGGET ISVGSIPCVV
RRAGEAWAIQ VAGVSREVRY AEYRSFGAAE ADPEIRSPMP GTIVRLHVES GARVEKGQLL
GVVEAMKMEH ELTAPHPGIV RVTATEGAVV TADQPLFLIE ERSAAL
//
