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Database: UniProt
Entry: A0A3D8REJ5_9EURO
LinkDB: A0A3D8REJ5_9EURO
Original site: A0A3D8REJ5_9EURO 
ID   A0A3D8REJ5_9EURO        Unreviewed;       712 AA.
AC   A0A3D8REJ5;
DT   16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT   16-JAN-2019, sequence version 1.
DT   13-SEP-2023, entry version 12.
DE   RecName: Full=3-methylcrotonyl-CoA carboxylase subunit alpha {ECO:0008006|Google:ProtNLM};
GN   ORFNames=DSM5745_07641 {ECO:0000313|EMBL:RDW72469.1};
OS   Aspergillus mulundensis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1810919 {ECO:0000313|EMBL:RDW72469.1, ECO:0000313|Proteomes:UP000256690};
RN   [1] {ECO:0000313|EMBL:RDW72469.1, ECO:0000313|Proteomes:UP000256690}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 5745 {ECO:0000313|EMBL:RDW72469.1,
RC   ECO:0000313|Proteomes:UP000256690};
RX   PubMed=30018880; DOI=10.5598/imafungus.2018.09.01.13;
RA   Wingfield B.D., Bills G.F., Dong Y., Huang W., Nel W.J.,
RA   Swalarsk-Parry B.S., Vaghefi N., Wilken P.M., An Z., de Beer Z.W.,
RA   De Vos L., Chen L., Duong T.A., Gao Y., Hammerbacher A., Kikkert J.R.,
RA   Li Y., Li H., Li K., Li Q., Liu X., Ma X., Naidoo K., Pethybridge S.J.,
RA   Sun J., Steenkamp E.T., van der Nest M.A., van Wyk S., Wingfield M.J.,
RA   Xiong C., Yue Q., Zhang X.;
RT   "IMA Genome-F 9: Draft genome sequence of Annulohypoxylon stygium,
RT   Aspergillus mulundensis, Berkeleyomyces basicola (syn. Thielaviopsis
RT   basicola), Ceratocystis smalleyi, two Cercospora beticola strains,
RT   Coleophoma cylindrospora, Fusarium fracticaudum, Phialophora cf. hyalina,
RT   and Morchella septimelata.";
RL   IMA Fungus 9:199-223(2018).
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:RDW72469.1}.
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DR   EMBL; PVWQ01000009; RDW72469.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3D8REJ5; -.
DR   STRING; 1810919.A0A3D8REJ5; -.
DR   OrthoDB; 1459320at2759; -.
DR   Proteomes; UP000256690; 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:UP000256690}.
FT   DOMAIN          40..488
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          156..354
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          627..705
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
SQ   SEQUENCE   712 AA;  78361 MW;  E9A10A53C348EE48 CRC64;
     MPLTSLLRTS SMRLGLTVVA RRSRRTASTI TSNSSNSPRS LDSILIANRG EIALRVGQTA
     AQHGIRVTTL YTDPDRRAQH ALSTPFAFNI GSVSAYLDGD RIIEIARAQG CQGIHPGYGF
     LSENSEFARK CTEAGLIFIG PPWKAIEDMG DKSQSKKIMT AAGVPCVPGY HGENQDPHFL
     EAEADKIRYP VLIKAIKGGG GKGMRIAHSK DEFQAQLQSA KSEAMNSFGD DHVLVEKYIT
     TPRHVEVQVF ADKHGNCVAL GERDCSIQRR HQKILEESPA PHLPDATRKD VWAKARSAAL
     AVGYEGAGTV EFIFDNDTGE FFFMEMNTRL QVEHPVTEMV TGQDLVHWQL KVAEGAVLPL
     SQEEVEANIA KHGHAIEARI YAENPAQGFI PDSGTLLHVR TPAISEDVRI DAGFVQGDEV
     SAHYDPMIAK LIVRGANRQE AIRKLAAALE EYEVAGPVTN IEFLKTICRS ADFISGEVET
     GYIEKHKDEL FSKKTIQPEV LAQVALACLR DDSRLIAQKT ANFQGTAVGF GSGFQEHHIS
     FTDSASANSE TFQVQVQQTG ENLFNVKVGE QYFEQVTSHL NTDSRIITSF FPHTRLDTTV
     IRDGDSVVAF QRGMQYRLSI PRAKWMEKAL GMKDVTNSVL APMPCKILRV EVQAGDIVEK
     DQPLVVIESM KMETVIRSPQ KGKIAKVVHQ KGDQCKSGTP LVEFAGEDEV PR
//
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