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Database: UniProt
Entry: A0A170UFF1_9ACTN
LinkDB: A0A170UFF1_9ACTN
Original site: A0A170UFF1_9ACTN 
ID   A0A170UFF1_9ACTN        Unreviewed;       650 AA.
AC   A0A170UFF1;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-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=STXM2123_264 {ECO:0000313|EMBL:GAT79563.1};
OS   Streptomyces sp. F-3.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1840095 {ECO:0000313|EMBL:GAT79563.1, ECO:0000313|Proteomes:UP000078145};
RN   [1] {ECO:0000313|EMBL:GAT79563.1, ECO:0000313|Proteomes:UP000078145}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Wang L.S., Gao P.J., Liu L., Zhang H.Q., Cheng Z., Sun X.M.;
RT   "Streptomyces sp. F-3 geneom sequencing.";
RL   Submitted (MAY-2016) 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:GAT79563.1}.
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DR   EMBL; BDDR01000001; GAT79563.1; -; Genomic_DNA.
DR   RefSeq; WP_067388382.1; NZ_BDDR01000001.1.
DR   AlphaFoldDB; A0A170UFF1; -.
DR   STRING; 1840095.STXM2123_264; -.
DR   OrthoDB; 9760256at2; -.
DR   Proteomes; UP000078145; 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:UP000078145}.
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          556..638
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
SQ   SEQUENCE   650 AA;  69134 MW;  F6E678427AF6E52C CRC64;
     MFETVLVANR GEIAVRVIRT LRALGVRSVA VFSDADADAR HVREADTAVR IGPAPAAESY
     LCADRLLEAA ARTGAQAVHP GYGFLAENAG FARACEEAGL VFIGPPADAI SLMGDKIRAK
     ETVAAAEVPV VPGSSGFGLT DDRLAEAARR IGLPVLLKPS AGGGGKGMRL VRDADRLAEE
     IAAARREARA SFGDDTLLVE RWIDRPRHIE IQVLADGHGN VVHLGERECS LQRRHQKIVE
     EAPSVLLDEE TRAAMGEAAV RAARSCGYRG AGTVEFIVPG GDPTTYYFME MNTRLQVEHP
     VTEMITGIDL VEWQLRVAAG EPLPFTQKDV RLTGHAIEAR LCAEDPARGF LPSGGTVLRL
     REPHGEGVRT DSGLSEGTEV GSLYDPMLSK VIAHGPDRET ALRRLRAALA RTVVLGVQTN
     TGFLRRLLAH PAVVAGELDT GLVERVAGEL AVTEVPEEVY EAAAAVRLEA LRPKGGGWID
     PFSVPNGWRL GGEPKPVAFP LRVPGHDPVT HPVRGTHAVT DDTVAVTLDG VRHTFHRAGD
     WLGRDGDAWH VRDHDPVAAS LTRAAHFGAD SLTAPMPGTV TVVKVAVGDK VTAGQSLLVV
     EAMKMEHVIS APHAGTVTEL DVTPGTTVAM DQVLAVIAPD DEDGAKEETA
//
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