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Database: UniProt
Entry: A0A0D2K3B9_9EURO
LinkDB: A0A0D2K3B9_9EURO
Original site: A0A0D2K3B9_9EURO 
ID   A0A0D2K3B9_9EURO        Unreviewed;       671 AA.
AC   A0A0D2K3B9;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   RecName: Full=Pyruvate carboxylase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=Z520_04003 {ECO:0000313|EMBL:KIY00318.1};
OS   Fonsecaea multimorphosa CBS 102226.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Fonsecaea.
OX   NCBI_TaxID=1442371 {ECO:0000313|EMBL:KIY00318.1, ECO:0000313|Proteomes:UP000053411};
RN   [1] {ECO:0000313|EMBL:KIY00318.1, ECO:0000313|Proteomes:UP000053411}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 102226 {ECO:0000313|EMBL:KIY00318.1,
RC   ECO:0000313|Proteomes:UP000053411};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Fonsecaea multimorphosa CBS 102226.";
RL   Submitted (JAN-2015) 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; KN848067; KIY00318.1; -; Genomic_DNA.
DR   RefSeq; XP_016634440.1; XM_016774513.1.
DR   AlphaFoldDB; A0A0D2K3B9; -.
DR   STRING; 1442371.A0A0D2K3B9; -.
DR   GeneID; 27709749; -.
DR   VEuPathDB; FungiDB:Z520_04003; -.
DR   OrthoDB; 2785982at2759; -.
DR   Proteomes; UP000053411; 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; PTHR45007; CARBOXYLASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_5G07570)-RELATED; 1.
DR   PANTHER; PTHR45007:SF1; CARBOXYLASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_5G07570)-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:UP000053411}.
FT   DOMAIN          7..455
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          128..323
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          574..656
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
SQ   SEQUENCE   671 AA;  72912 MW;  9BA8D14052191144 CRC64;
     MPPPQRPISR ILVANRGEIA IRILQSCHEL APQPPTTFAI YTDNDSTHIS LGRPHHAIKA
     AFGPASYMNI DYLIGVVKEH KIDAVHPGYG FLSESAEFSR RMWEEAGCVV VGPGWEVLER
     TGDKLMAKAL ASECGVPVLK AMERPTGSVE DVRRFAASVG YPLMIKAVDG GGGRGIRLVK
     SEDALDNAVQ RCVAESPSRL VFAEQAAVEG YKHIEVQIVG DGKGGVTHLW ERDCSVQRRF
     QKIVELAPAP VQNRKVIAQV IDSAVRMATQ LKYLGLGTWE YLVNVQQEKF FFLEINPRLQ
     VEHTITECIT GVDLVKQQLL LAQGLQTRLG GSHDANKAPP SASIQLRLCA EDPTAGFSLS
     IGKVSDVQFP SGNGVRVDSH LSRGGVVGSD FDNMMAKVIV TASTWEECVG KARRALEETK
     IVGVKSNLNL LKAILTHERF AAGDADTSWL ERNLDQLVAL GEQLGSITEI RESSLPALSL
     SSSNTPGSAV GGAGASTLFR KGDAWTLVLE NSGEKSSSSV KPPAHHLSIS RVTRNEFPAA
     LIADISYTIP GARTHSYKMT LNSTTSSADA AASTHRRGDP SKKTHIVLPM SGKLVEVLVD
     EGDEVRENEV IAFVKQMKME LEVRSPRAGK VKWVIEMENE EEGDDVAEGV LLVELEDEED
     SAKKPEVRSR L
//
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