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Database: UniProt
Entry: A0A3Q8VFZ2_9ACTN
LinkDB: A0A3Q8VFZ2_9ACTN
Original site: A0A3Q8VFZ2_9ACTN 
ID   A0A3Q8VFZ2_9ACTN        Unreviewed;       668 AA.
AC   A0A3Q8VFZ2;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=biotin carboxylase {ECO:0000256|ARBA:ARBA00013263};
DE            EC=6.3.4.14 {ECO:0000256|ARBA:ARBA00013263};
GN   ORFNames=DLM49_23765 {ECO:0000313|EMBL:AZM62147.1};
OS   Streptomyces sp. WAC 01438.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=2203204 {ECO:0000313|EMBL:AZM62147.1, ECO:0000313|Proteomes:UP000271045};
RN   [1] {ECO:0000313|EMBL:AZM62147.1, ECO:0000313|Proteomes:UP000271045}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WAC 01438 {ECO:0000313|EMBL:AZM62147.1,
RC   ECO:0000313|Proteomes:UP000271045};
RA   Waglechner N., Wright G.D.;
RT   "Evolution of GPA BGCs.";
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};
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DR   EMBL; CP029601; AZM62147.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3Q8VFZ2; -.
DR   OrthoDB; 9760256at2; -.
DR   Proteomes; UP000271045; Chromosome.
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; 3.30.700.40; -; 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:UP000271045}.
FT   DOMAIN          1..448
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          120..319
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          579..661
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
SQ   SEQUENCE   668 AA;  69661 MW;  513D71543AF3F159 CRC64;
     MFETVLVANR GEIAVRVIRT LRSLGVRSVA VYSDADAGAR HVREADTAVR IGPAPAAESY
     LSVERLLEAA RRTGAQAVHP GYGFLAENAG FARACADAGL VFIGPPADAI ALMGDKIRAK
     ETVRAAGVPV VPGSSGSGLT DAQLTEAARE IGVPVLLKPS AGGGGKGMRL VRDASALADE
     IAAARREARA SFGDDTLLVE RWIDRPRHIE IQVLADGHGG VVHLGERECS LQRRHQKIIE
     EAPSVLLDEE TRAAMGEAAV QAARSCGYRG AGTVEFIVPG SDPSSYYFME MNTRLQVEHP
     VTELVTGLDL VEWQLRVAAG EPLPFGQDAI RLTGHAVEAR VCAEDPARGF LPSGGTVLAL
     HEPQGDGVRT DSGLSEGTEV GSLYDPMLSK VIAYGPDRAT ALRRLRAALA ETVTLGVRTN
     AGFLRRLLAH PAVAAGDLDT GLVEREADDL VADDVPAATY AAAALLRQAA LAPAGGPGWA
     DPFAAADGWR LGGERAWTAH PLRVPGHDPV TVRVRSTPDG GTEVLLPGAG APVRGSVGPR
     EGHRCTFALD GVTHTFAAAP DGTWLGRDGD AWHVRDHDPV EASLTRAAQA GADSLTAPMP
     GTVTVVKVAV GDEVSAGQSL LVVEAMKMEH VISAPHAGTV TELDVSPGTA VAMDQVLAVI
     APVEEETA
//
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