ID A0A0D0BR60_9AGAM Unreviewed; 861 AA.
AC A0A0D0BR60;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 13-SEP-2023, entry version 32.
DE RecName: Full=Biotin carboxylase {ECO:0008006|Google:ProtNLM};
GN ORFNames=CY34DRAFT_10370 {ECO:0000313|EMBL:KIK45498.1};
OS Suillus luteus UH-Slu-Lm8-n1.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Boletales; Suillineae; Suillaceae; Suillus.
OX NCBI_TaxID=930992 {ECO:0000313|EMBL:KIK45498.1, ECO:0000313|Proteomes:UP000054485};
RN [1] {ECO:0000313|EMBL:KIK45498.1, ECO:0000313|Proteomes:UP000054485}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UH-Slu-Lm8-n1 {ECO:0000313|EMBL:KIK45498.1,
RC ECO:0000313|Proteomes:UP000054485};
RG DOE Joint Genome Institute;
RA Kuo A., Ruytinx J., Rineau F., Colpaert J., Kohler A., Nagy L.G.,
RA Floudas D., Copeland A., Barry K.W., Cichocki N., Veneault-Fourrey C.,
RA LaButti K., Lindquist E.A., Lipzen A., Lundell T., Morin E., Murat C.,
RA Sun H., Tunlid A., Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.,
RA Nordberg H.P., Cantor M.N., Hua S.X.;
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000054485}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UH-Slu-Lm8-n1 {ECO:0000313|Proteomes:UP000054485};
RG DOE Joint Genome Institute;
RG Mycorrhizal Genomics Consortium;
RA Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL Submitted (JAN-2015) 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; KN835172; KIK45498.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D0BR60; -.
DR STRING; 930992.A0A0D0BR60; -.
DR HOGENOM; CLU_000395_3_3_1; -.
DR InParanoid; A0A0D0BR60; -.
DR OrthoDB; 1459320at2759; -.
DR Proteomes; UP000054485; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
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; 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; 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:UP000054485}.
FT DOMAIN 140..620
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 259..457
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 780..858
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 861 AA; 93331 MW; 82F4F2149083E13B CRC64;
MTRWNRDGHF TRDRFAEGPS IEVLGPRLLI IDPLLFIVSP SIEVAFKIQE VAQVTRGMIP
TNRAAASSLL RSSTHVYSIP RTLLTTDASS STKYARSLQT KASVTGAMMC QPRILVQPAV
SQRRFATAVQ NTLTSERRPH FDKILIANRG EIACRVIRTA KKLGIKTVAV YSEVDANSLH
VLEADEAYCI GPAPSADSYL RMDKIIDVCR RSGAQAVHPG YGFLSENAKF AERLAEEGIV
FIGPPSSAIV SMGSKSESKN IMSAAGVPCV PGYHGANQDA ELLFAEAEKI GYPVLIKAIH
GGGGKGMRVV SSASQFKDAL ASAQRESLKS FGDADVLVEK YIERPRHIEV QVFADTLGNA
VSLWERDCSV QRRNQKIIEE APAPGLSPEL RADLSAKAVA AAKAVNYVGA GTVEFIFDND
TEKFYFMEMN TRLQVEHPVT EMITGLDLVE WQLEVAAGNL LPLLQPQIPL VGHAFEARIY
AENPRNDFLP DSGPLLYLDT PKPTHVFAPL IPSLPHNASC SELDSVKRSP DTSTHVAPSM
RLEQGFTQGA QIGVFYDPMI AKLVVHGRDR TSALRALRRA LEEYKVVGVS TNVEFLRMLA
GNGAFINGEV ETGFIKKHYE DLFPAVESPS AELLAQAALF VALREHPIQP TSLSTPWTTL
ASRRFGGDIY ERTISIQSDD ASADPTRVSL RSISPGHFDV VVHSASPKTF TGVSARLVSP
TRLSTTLNGA STGITIVSQR PPPSHPASRV TNTMERLHVF SASGTKTTLA IPPPAYLLSL
GQDVLTSSKG ALRAPMPSLV VEVKVSIGDR VEKGQPVVVL ESMKTETVLR AEVAGVVNAV
GCAKGEMVEE GRELVDIKED E
//
