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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//