ID A0A3A4BGB8_9ACTN Unreviewed; 584 AA.
AC A0A3A4BGB8;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-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=D5H75_12315 {ECO:0000313|EMBL:RJL33542.1};
OS Bailinhaonella thermotolerans.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Streptosporangiaceae; Bailinhaonella.
OX NCBI_TaxID=1070861 {ECO:0000313|EMBL:RJL33542.1, ECO:0000313|Proteomes:UP000265768};
RN [1] {ECO:0000313|EMBL:RJL33542.1, ECO:0000313|Proteomes:UP000265768}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YIM 75507 {ECO:0000313|EMBL:RJL33542.1,
RC ECO:0000313|Proteomes:UP000265768};
RA Tang S., Feng Y.;
RT "YIM 75507 draft genome.";
RL Submitted (SEP-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:RJL33542.1}.
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DR EMBL; QZEY01000003; RJL33542.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3A4BGB8; -.
DR OrthoDB; 5166719at2; -.
DR Proteomes; UP000265768; 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:UP000265768}.
FT DOMAIN 1..443
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 119..316
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 507..583
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT REGION 491..514
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 584 AA; 62196 MW; D0D5D2FB7A5B4A7C CRC64;
MRKVLIANRG EIAVRVARAC RDAGISSVAV YADQDRDALH VKVADEAYSL GGSTPAETYL
DIEKLLKVAE ETGADAVHPG YGFLSENADF AQAVIDAGLT WIGPPPDAIV KLGDKVQARH
IAQKVGAPLV AGTADPVAGV EEVVAFAEEH GLPIAIKAAY GGGGRGLKVA RTIEEIPHLY
ESAVREAVTA FGRGECFVER YLDRPRHVET QCLADSHGNV VVVSTRDCSL QRRHQKLVEE
APAPFLSEEQ MGLLYSSSKA ILREAGYVGA GTCEFLVGQD GTISFLEVNT RLQVEHPVTE
EVSGIDLVRE MFRIADGEEL GYDDPPLRGH SIEFRINAED AGRGFLPAPG TITRMETPSG
PGVRLDAGYE TGMTVPQAFD SLVAKLIVTG RDRTQAIERA RRALAEFEVE GMPTVIPFHR
VVLDDPAFTD EPFRVHTRWI ETEFDNRIEP YSGPVATPED EARERVTVEV GGKRLEVVLP
AGLGATAAAG AGRTAKAAPR RSGKARSQGA AVSGDSLVSP MQGTIVKVVA EDGATVAAGD
AIVVLEAMKM EQPLTAHKAG TISGLTAEVG QTVNSGAVIC EIKD
//
