ID A0A395GTW5_9EURO Unreviewed; 710 AA.
AC A0A395GTW5;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 11.
DE SubName: Full=3-methylcrotonyl-CoA carboxylase subunit alpha {ECO:0000313|EMBL:RAK98869.1};
GN ORFNames=BO80DRAFT_147895 {ECO:0000313|EMBL:RAK98869.1};
OS Aspergillus ibericus CBS 121593.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1448316 {ECO:0000313|EMBL:RAK98869.1, ECO:0000313|Proteomes:UP000249402};
RN [1] {ECO:0000313|EMBL:RAK98869.1, ECO:0000313|Proteomes:UP000249402}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 121593 {ECO:0000313|EMBL:RAK98869.1,
RC ECO:0000313|Proteomes:UP000249402};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (FEB-2018) 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; KZ824450; RAK98869.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A395GTW5; -.
DR STRING; 1448316.A0A395GTW5; -.
DR VEuPathDB; FungiDB:BO80DRAFT_147895; -.
DR OrthoDB; 1459320at2759; -.
DR Proteomes; UP000249402; 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:UP000249402}.
FT DOMAIN 38..486
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 154..352
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 710 AA; 77515 MW; 35BA3C7E59899967 CRC64;
MPLSSLLRTS SRLGPPVARR FRRAASTVSS TAPKSPKSLD SILIANRGEI ALRVGRTAAQ
HGIRVTTLYT DPDSKAQHAL SSPFAFNLGS VSAYLDGDRI IEIAKKEGCQ GIHPGYGFLS
ENAAFARKCT EAGLVFIGPP WKAIEDMGDK SQSKKIMTAA GVPCVPGYHG DNQDVNFLEA
EADKIKYPVL IKAIKGGGGK GMRIAHTKAE FQAQLQSAKS EALNSFGDDQ VLVEKYITTP
RHIEVQVFAD KHGNAVALGE RDCSIQRRHQ KILEESPAPH LPDATRKDIW AKARSAALAV
GYEGAGTVEF IFDNDTGEFF FMEMNTRLQV EHPVTEMVTG QDLVHWQLKI AEGAPLPLLQ
EDVEAFMASR GHAIEARIYA ENPDQGFIPD SGTLLHVRTP ATTDDVRIDA GFVAGDDVSA
HYDPMIAKLI VRGNTREDAI RKLATALEEY EIAGPITNIE FLKTICRSPD FISGDVETGY
IEKHREELFT REAIAPEVLA QVALACLHHD SAPVSGTQAS FEGSAVGFGS GYQARQISLA
ELSPGTKNVT RFDIRVQQTG DNTFDIDVGG HSFEQVVSQR DPASRVVASF FPHTRLDTTV
IRDGDTIIAF QRGTQYRLTI PRAKWMEKAL GMKDVTNSVL APMPCKVLRV EVQAGDVVEK
DQPLVVIESM KMETVIRSPQ RGTIAKVVHQ QGDQCKSGTP LVEFEEESGE
//
