ID A0A117S0V3_9ACTN Unreviewed; 683 AA.
AC A0A117S0V3;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=biotin carboxylase {ECO:0000256|ARBA:ARBA00013263};
DE EC=6.3.4.14 {ECO:0000256|ARBA:ARBA00013263};
GN ORFNames=AQJ91_15450 {ECO:0000313|EMBL:KUO20180.1};
OS Streptomyces dysideae.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=909626 {ECO:0000313|EMBL:KUO20180.1, ECO:0000313|Proteomes:UP000053260};
RN [1] {ECO:0000313|EMBL:KUO20180.1, ECO:0000313|Proteomes:UP000053260}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RV15 {ECO:0000313|EMBL:KUO20180.1,
RC ECO:0000313|Proteomes:UP000053260};
RA Ruckert C., Abdelmohsen U.R., Winkler A., Hentschel U., Kalinowski J.,
RA Kampfer P., Glaeser S.;
RT "Draft genome sequence of Streptomyces sp. RV15, isolated from a marine
RT sponge.";
RL Submitted (OCT-2015) 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:KUO20180.1}.
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DR EMBL; LMXB01000041; KUO20180.1; -; Genomic_DNA.
DR RefSeq; WP_067021326.1; NZ_KQ949082.1.
DR AlphaFoldDB; A0A117S0V3; -.
DR STRING; 909626.AQJ91_15450; -.
DR OrthoDB; 9760256at2; -.
DR Proteomes; UP000053260; 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; 3.30.700.40; -; 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:UP000053260}.
FT DOMAIN 1..459
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 120..330
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 602..676
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 683 AA; 71623 MW; BE2DE5828E205A11 CRC64;
MFDTVLVANR GEIAVRVIRT LRSLGIRSVA VFSDADADAR HVRVADTAVR LGPAPAAESY
LSADRILEAA ARTGAQAVHP GYGFLAENAD FARACAEAGQ AFIGPPADAI SLMGDKIRAK
ETVRAAGVPV VPGSSGSGLS DAELADAARE IGVPVLLKPS AGGGGKGMRL VRDLAHLADE
IAAARREARA SFGDDTLLVE RWIDRPRHIE IQVLADGHGN VLHLGERECS LQRRHQKIIE
EAPSVLLDAD TRASMGEAAV QAARSCGYRG AGTVEFIVPG DTVPIGGTPP EPPVSSYYFM
EMNARLQVEH PVTELITGLD LVEWQVRVAA GERLSFGQPD VQLTGHAIEA RVCAEDPTRG
FLPSGGTVLS LYEPQGDGVR TDSGLSEGTE VGSLYDPMLS KVIAYGPDRA TALRKLRSAL
AETVTLGVPT NAGFLRRLLA HPAVVAGELD TGLVEREVDG LVADAVPAEL YAAAALLRQA
ALAPAEGDGW ADPFAAADGW RLGGEPAWTP HHLRVPGHEP VTVRVRRTPD GRTELLLPGM
DKPLRGSGGV PPRPGAEQRF TFLLDGVAHT FAALPDGTWL GRDGDAWHVR DHDPVAAALT
GAAHAGAESL TAPMPGTVTV VKVAVGDEVT AGQSLLVVEA MKMEHVISAP HAGTVAELDV
TPGTTVAMDQ VLAVIAPHEE VTE
//
