ID A0A1B1M9W0_STRLN Unreviewed; 638 AA.
AC A0A1B1M9W0;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=biotin carboxylase {ECO:0000256|ARBA:ARBA00013263};
DE EC=6.3.4.14 {ECO:0000256|ARBA:ARBA00013263};
GN ORFNames=GJU35_16850 {ECO:0000313|EMBL:QMV07180.1}, SLCG_5217
GN {ECO:0000313|EMBL:AXG56372.1}, SLINC_3196
GN {ECO:0000313|EMBL:ANS65420.1};
OS Streptomyces lincolnensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1915 {ECO:0000313|EMBL:ANS65420.1, ECO:0000313|Proteomes:UP000092598};
RN [1] {ECO:0000313|EMBL:ANS65420.1, ECO:0000313|Proteomes:UP000092598}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 2936 {ECO:0000313|EMBL:ANS65420.1,
RC ECO:0000313|Proteomes:UP000092598};
RA Meng S.C.;
RT "Enhancement of antibiotic productionsby engineered nitrateutilization in
RT actinobacteria.";
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AXG56372.1, ECO:0000313|Proteomes:UP000253884}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LC-G {ECO:0000313|EMBL:AXG56372.1,
RC ECO:0000313|Proteomes:UP000253884};
RX PubMed=29574602; DOI=10.1007/s10295-018-2029-1;
RA Xu Y., Tan G., Ke M., Li J., Tang Y., Meng S., Niu J., Wang Y., Liu R.,
RA Wu H., Bai L., Zhang L., Zhang B.;
RT "Enhanced lincomycin production by co-overexpression of metK1 and metK2 in
RT Streptomyces lincolnensis.";
RL J. Ind. Microbiol. Biotechnol. 45:345-355(2018).
RN [3] {ECO:0000313|EMBL:QMV07180.1, ECO:0000313|Proteomes:UP000515335}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B48 {ECO:0000313|EMBL:QMV07180.1,
RC ECO:0000313|Proteomes:UP000515335};
RX PubMed=32322696;
RA Wang R., Kong F., Wu H., Hou B., Kang Y., Cao Y., Duan S., Ye J., Zhang H.;
RT "Complete genome sequence of high-yield strain S. lincolnensis B48 and
RT identification of crucial mutations contributing to lincomycin
RT overproduction.";
RL Synth Syst Biotechnol 5:37-48(2020).
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
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DR EMBL; CP016438; ANS65420.1; -; Genomic_DNA.
DR EMBL; CP022744; AXG56372.1; -; Genomic_DNA.
DR EMBL; CP046024; QMV07180.1; -; Genomic_DNA.
DR RefSeq; WP_067433161.1; NZ_CP046024.1.
DR AlphaFoldDB; A0A1B1M9W0; -.
DR STRING; 1915.SLINC_3196; -.
DR KEGG; sls:SLINC_3196; -.
DR PATRIC; fig|1915.4.peg.3514; -.
DR OMA; FVEICSH; -.
DR OrthoDB; 9760256at2; -.
DR Proteomes; UP000092598; Chromosome.
DR Proteomes; UP000253884; Chromosome.
DR Proteomes; UP000515335; 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; 3.30.470.20; 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:UP000092598}.
FT DOMAIN 1..443
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 120..314
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 549..631
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 638 AA; 67779 MW; 372A7B9F1DD1BF95 CRC64;
MFDTVLVANR GEIAVRVIRT LRALGVRSVA VFSDADADAR HVREADTAVR LGPAPAAESY
LSVERLLEAA ARTGAQAVHP GYGFLAENAG FARACEDAGL VFIGPSAEAI SLMGDKIRAK
ETVKAAGVPV VPGGRDPELA EAARELGAPV LLKPSAGGGG KGMRLVRDLT VLEEEIAAAR
REARASFGDD TLLVERWVDR PRHIEIQVLA DGHGKVIHLG ERECSLQRRH QKIVEEAPSV
LLDEETRAAM GEAAVQAARS CGYRGAGTVE FIVPGNDPSS YYFMEMNTRL QVEHPVTELV
TGLDLVEWQL RVAAGEHLPH AQDDITLTGH AIEARVCAED PSRGFLPSGG TVLRLHEPQG
DGVRTDSGLS EGTEVGSLYD PMLSKVIAYG PDRETALRRL RAALAETVTL GVPTNAGFLR
RLLAHPAVVA GELDTGLVER VVDDLVPAEV PQEVYEAAAA VRLDALRPRG TGWTDPFSVP
SGWRLGGLTQ PVGFHLRVQD PVQYVPRGTH TVTGTRVSVT LDGVRHTFHR AADWIGRDGD
AWHVRDHDPV AASLTGAAHA GADSLTAPMP GTVTVVKVAV GDEVAAGQSL VVVEAMKMEH
VISAPHAGTV AELDVTPGTT VAMDQVLAVI TPHEEETA
//