ID A0A1H9FAU0_9ACTN Unreviewed; 697 AA.
AC A0A1H9FAU0;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, 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=SAMN04487983_1004223 {ECO:0000313|EMBL:SEQ35019.1};
OS Streptomyces sp. yr375.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1761906 {ECO:0000313|EMBL:SEQ35019.1, ECO:0000313|Proteomes:UP000198568};
RN [1] {ECO:0000313|EMBL:SEQ35019.1, ECO:0000313|Proteomes:UP000198568}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YR375 {ECO:0000313|EMBL:SEQ35019.1,
RC ECO:0000313|Proteomes:UP000198568};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
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DR EMBL; FOFF01000004; SEQ35019.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H9FAU0; -.
DR STRING; 1761906.SAMN04487983_1004223; -.
DR OrthoDB; 9760256at2; -.
DR Proteomes; UP000198568; 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; 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:UP000198568}.
FT DOMAIN 1..454
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 120..325
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 601..683
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 697 AA; 72714 MW; 1B5A357406A3EDD2 CRC64;
MFDTVLVANR GEIAVRVIRT LRALGVRSVA VFSDADADAR HVREADTAVR LGPAPAAESY
LSVERLLDAA ARTGAQAVHP GYGFLAENAS FARACADAGL VFIGPPADAI ALMGDKIRAK
ETVAAAGVPV VPGGRDPELA EAAHALGAPV LLKPSAGGGG KGMRLVRDLS VLEEEIAAAR
REARASFGDD TLLVERWVDR PRHIEIQVLA DGHGNVVHLG ERECSLQRRH QKVVEEAPSV
FLDEATRASM GEAAVQAARS CGYRGAGTVE FIVPGTTVPV GGTPPEPPVS SYYFMEMNAR
LQVEHPVTEL VTGLDLVEWQ VRVAAGEALP FGQRDIRLTG HAVEARICAE DPARGFLPSG
GTVLRLHEPQ GDGVRTDSGL TEGTEVGSLY DPMLSKVIAY GPDRATALRK LRAALASTVT
LGVPTNAGFL RRLLAHPAVA AGELDTGLVE RVVDELVSDT VPPEVYAAAA LLRHGALAPG
DDSGSAASSR SGWADPFAAA DGWRLGGERA WTPHHLQLPG HEPVTVRVRS TPGGGAGGSV
ELLLPGADRP LQGSGGVPPQ RETGHRFAFR LDGVSHTFAA LPDGTWIGRD GDAWQVRDHD
PVAASLSGGG RAGVDSLTAP MPGTVTVVKV AVGDEVTAGQ SLLVVEAMKM EHVISAPHDG
TVAELDVTPG TTVAMDQVLA VIAPVVPVVT PAEEEKE
//
