ID A0A1U7MU45_9MICO Unreviewed; 590 AA.
AC A0A1U7MU45;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=biotin carboxylase {ECO:0000256|ARBA:ARBA00013263};
DE EC=6.3.4.14 {ECO:0000256|ARBA:ARBA00013263};
GN ORFNames=BJF81_11305 {ECO:0000313|EMBL:OLT23316.1};
OS Ornithinimicrobium sp. CNJ-824.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales;
OC Ornithinimicrobiaceae; Ornithinimicrobium.
OX NCBI_TaxID=1904966 {ECO:0000313|EMBL:OLT23316.1, ECO:0000313|Proteomes:UP000185694};
RN [1] {ECO:0000313|EMBL:OLT23316.1, ECO:0000313|Proteomes:UP000185694}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CNJ-824 {ECO:0000313|EMBL:OLT23316.1,
RC ECO:0000313|Proteomes:UP000185694};
RX PubMed=27902408; DOI=10.1099/mic.0.000386;
RA Schorn M.A., Alanjary M.M., Aguinaldo K., Korobeynikov A., Podell S.,
RA Patin N., Lincecum T., Jensen P.R., Ziemert N., Moore B.S.;
RT "Sequencing rare marine actinomycete genomes reveals high density of unique
RT natural product biosynthetic gene clusters.";
RL Microbiology 162:2075-2086(2016).
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:OLT23316.1}.
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DR EMBL; MKKA01000006; OLT23316.1; -; Genomic_DNA.
DR RefSeq; WP_075957076.1; NZ_MKKA01000006.1.
DR AlphaFoldDB; A0A1U7MU45; -.
DR STRING; 1904966.BJF81_11305; -.
DR OrthoDB; 9760256at2; -.
DR Proteomes; UP000185694; 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; 3.40.50.20; -; 1.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
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; 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:UP000185694}.
FT DOMAIN 2..445
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 121..318
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 513..589
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT REGION 493..522
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 590 AA; 62197 MW; 94DA164D2DB9488D CRC64;
MPISKVLIAN RGEIAVRIAR ACKDAGLTSV AVYADTDRDA LHVKVADEAH ALGGSTPGES
YLVQEKLLEV AARTGADAVH PGYGFLAENA SFAQAVIDAG LTWIGPGPEA IDALGDKAKA
KHIAVRADAP LAPGTKDPVA DADEVVALAE EFGLPVAIKA VYGGGGRGLK VARTMEEIPE
LFDSAVREAV TAFGRGECLV EKFLDRPRHV ETQCLADQHG NVVVVSTRDC SLQRRNQKLV
EEAPAPFLTE EQRAELVRAS KAILKEAGYV GAGTCEFLVA QDGTISFLEV NTRLQVEHPV
TEEVTGIDLV REQFRIADGE ELGYADPAPH AHSFEFRING EDAGRDFLPA PGTVSRMVVP
HGPGVRWDAG IVEGDTVAGA FDSMIAKLVV TGRTREQALE RSRRALEELV VEGMPTVLPF
HRAIVSDPAF APEGEEAFTV HTRWIETEFD NQIEPWSGPV ADAPSEDGER QRVVVEVGGQ
RLEVSLPAGL ALGGNGGAGA GRRKAPKRSR GAGGAAAASG DAVTAPMQGT IVKIAVEEGQ
QVAEGDVVVV LEAMKMEQPL KAHKGGTVSG LTASVGETVS NGAVICELKD
//
