ID A0A0W0FX72_9AGAR Unreviewed; 1031 AA.
AC A0A0W0FX72;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=Putative 3-methylcrotonyl-CoA carboxylase {ECO:0000313|EMBL:KTB40946.1};
GN ORFNames=WG66_6480 {ECO:0000313|EMBL:KTB40946.1};
OS Moniliophthora roreri.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Marasmiaceae; Moniliophthora.
OX NCBI_TaxID=221103 {ECO:0000313|EMBL:KTB40946.1, ECO:0000313|Proteomes:UP000054988};
RN [1] {ECO:0000313|EMBL:KTB40946.1, ECO:0000313|Proteomes:UP000054988}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 2952 {ECO:0000313|EMBL:KTB40946.1,
RC ECO:0000313|Proteomes:UP000054988};
RA Aime M.C., Diaz-Valderrama J.R., Kijpornyongpan T., Phillips-Mora W.;
RT "Draft genome sequence of Moniliophthora roreri, the causal agent of frosty
RT pod rot of cacao.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
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:KTB40946.1}.
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; LATX01001532; KTB40946.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0W0FX72; -.
DR eggNOG; KOG0238; Eukaryota.
DR Proteomes; UP000054988; 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 GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd06850; biotinyl_domain; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 3.30.700.40; -; 1.
DR Gene3D; 3.40.50.20; -; 1.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR Gene3D; 3.60.130.10; Clavaminate synthase-like; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
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 InterPro; IPR042098; TauD-like_sf.
DR InterPro; IPR003819; TauD/TfdA-like.
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 Pfam; PF02668; TauD; 1.
DR SMART; SM00878; Biotin_carb_C; 1.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 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.
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}; Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000054988}.
FT DOMAIN 312..781
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 431..631
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 956..1025
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 1031 AA; 112937 MW; 3B5C196BB0D7D7A5 CRC64;
MGIEFHPLVL PDSADKSKLG DFGREVRGVH PAHVTEEHFA LIEEALYKYN ALLFRNVDLS
PEEQYAFVKA FDPEATGVYA HGTKKMQEHK NSVLSSYLNT IPRVPQVQLI GHGTVYNHEG
IPEVTLRHGH HASIHKTCVS KEDEERGVTR FFRWHMDAAL YEYDPPKVTG LYAVKVPQGP
RQVARYDDGS GDELPVPLGT TAFESGKNMF DILPPELKSL AVRARAKRLE KQLDELSAWE
EKDVKTYAFC WKNPVTGDLH LMVHPLCLME VIIDPVSQEG RKQNALYPDG AHLTNLKEIR
ELLHKMQRPG IIPSLVYPHD WGEIACRVIR TAKKLGIKCV AVYSEVDKDS MHVQMSDEAY
CIGPAPSSES YLRIERIIEI CRRSGAQAVH PGYGFLSENA KFAERLAEEG IVFIGPPASA
IVSMGSKSES KNIMLAAGVP CVPGYHGENQ DPSFLFEQAK QIGFPVLIKA VHGGGGKGMR
IVTEPTAEAF HEALTSAKRE SVKSFGNDTV LVEKYIQRPR HVEVQVFADS LGGVVSLWER
DCSVQRRNQK IIEEAPAPGL SMELRADLSS RAVAAAKAVN YVGAGTVENT RLQVEHPVTE
MVTGLDLVEW QLDVAAGNPL SLDQSSIPLV GHAFEARIYA ENPRNNFLPD SGPLLYLSTP
SPTLTFASSY ANSPSIITES HPPEAFVPAL ASHSAEVTPS VRLEQGFGQG SQIGVFYDPM
IAKLIVHGKD RTEALRMLRK ALDDYHIVGV STNIEFLRTL AGHSAFVDGE VETGFISKHF
DQLFPAIEVP DLEVLAQAAL FIALRDHPNP AAISSDAQSP WTSLVSRRFG GDNYERVVLL
QDDTVTANEP ISVSIKSTTH GIFDIEVKTP TRIAHFHSVP AQLTSPQKLS TTLNDKLCNV
TVVSQPPPPS LPASASHHSM ERLHIFNEGH KTTLVLPTPN WLLSLGGDVL NAAQAKGVLK
APMPSLVVEV KVRVGDKVEK GQSVVVLESM KTETVLRAGA SGVVKAVGCK NGEMVEEGKE
LVDIEIEGEG V
//
