ID M7UPD6_BOTF1 Unreviewed; 704 AA.
AC M7UPD6;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 22-FEB-2023, entry version 37.
DE SubName: Full=Putative 3-methylcrotonyl-carboxylase subunit alpha protein {ECO:0000313|EMBL:EMR85587.1};
GN ORFNames=BcDW1_5827 {ECO:0000313|EMBL:EMR85587.1};
OS Botryotinia fuckeliana (strain BcDW1) (Noble rot fungus) (Botrytis
OS cinerea).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Botrytis.
OX NCBI_TaxID=1290391 {ECO:0000313|EMBL:EMR85587.1, ECO:0000313|Proteomes:UP000012045};
RN [1] {ECO:0000313|Proteomes:UP000012045}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BcDW1 {ECO:0000313|Proteomes:UP000012045};
RX PubMed=23704180; DOI=10.1128/genomea.00252-13;
RA Blanco-Ulate B., Allen G., Powell A.L., Cantu D.;
RT "Draft genome sequence of Botrytis cinerea BcDW1, inoculum for noble rot of
RT grape berries.";
RL Genome Announc. 1:E0025213-E0025213(2013).
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
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DR EMBL; KB707895; EMR85587.1; -; Genomic_DNA.
DR AlphaFoldDB; M7UPD6; -.
DR STRING; 1290391.M7UPD6; -.
DR HOGENOM; CLU_000395_3_3_1; -.
DR Proteomes; UP000012045; 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}.
FT DOMAIN 30..478
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 146..344
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 623..701
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 704 AA; 77598 MW; 7444FC6538536645 CRC64;
MHSAARSRVL ARALLPSYSR RYATTPAITP ITSVLIANRG EIALRVGRTA SDLGVRCTTI
YTDPDANSQH ALSSPFAVNL GAANAYLDGE RIISVAKEQG CEALHPGYGF LSENSAFAKR
CVEEGLVFIG PPWKAIEAMG NKSRSKDIMI NAGVPCIPGY HGENQEPEHL LNEAKKIGFP
VMVKAVKGGG GKGMRIAQTE REFLEKLESA KSEGRNSFGD DVMLVEKYIA TPRHIEVQVF
ADKHGNAVAL GERDCSLQRR HQKILEEAPA PNLAENIRQD LWEKARAAAL AVGYEGAGTV
EFIFDNDTNE FFFMEMNTRL QVEHPVTEEI TGEDLVSWQF KVAAGEPLPL DQDTIAQRIS
ERGWALEARI YAENPDQNFM PDSGKLVHLR TPKLSESVRI DAGFVQGDTV SSNYDGMIAK
LIVSGPTREV AIRKLHAALQ DYEVVGLSTN IEFLKKICKS PAFIRGDVET GYIQKHHDEL
FINETIEPEA FAQAALGILS QELSAANSKS IQGPHGEAIG FNSHVQREFS FTKPIVQPSS
EKPEIYHVTI DQSDRNLYNI TVKGPNVEKS YANIVSEPKS PTISTFFPHT RIESTLIRQD
DKITLFQQGK QIQLQLATPG WYEKALGLKD VRNSVVAPMP CKVLRNEVGE GEEVEEGQAL
VVIESMKMET VIRSPQKGVV AKLVHKEGDI CKAGTVLVLF EEPE
//
