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
//