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Database: UniProt
Entry: A0A1E3ILL5_9TREE
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ID   A0A1E3ILL5_9TREE        Unreviewed;       317 AA.
AC   A0A1E3ILL5;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   SubName: Full=Citrate lyase subunit beta-like protein {ECO:0000313|EMBL:ODN89494.1};
GN   ORFNames=L203_02204 {ECO:0000313|EMBL:ODN89494.1};
OS   Cryptococcus depauperatus CBS 7841.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus.
OX   NCBI_TaxID=1295531 {ECO:0000313|EMBL:ODN89494.1, ECO:0000313|Proteomes:UP000094043};
RN   [1] {ECO:0000313|EMBL:ODN89494.1, ECO:0000313|Proteomes:UP000094043}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 7841 {ECO:0000313|EMBL:ODN89494.1,
RC   ECO:0000313|Proteomes:UP000094043};
RA   Cuomo C., Litvintseva A., Heitman J., Chen Y., Sun S., Springer D.,
RA   Dromer F., Young S., Zeng Q., Chapman S., Gujja S., Saif S., Birren B.;
RT   "Evolution of pathogenesis and genome organization in the Tremellales.";
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
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:ODN89494.1}.
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DR   EMBL; AWGK01000008; ODN89494.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1E3ILL5; -.
DR   STRING; 1295531.A0A1E3ILL5; -.
DR   VEuPathDB; FungiDB:L203_02204; -.
DR   OrthoDB; 2874421at2759; -.
DR   Proteomes; UP000094043; Unassembled WGS sequence.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
DR   InterPro; IPR005000; Aldolase/citrate-lyase_domain.
DR   InterPro; IPR011206; Citrate_lyase_beta/mcl1/mcl2.
DR   InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR   InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR   PANTHER; PTHR32308:SF0; HPCH_HPAI DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR32308; LYASE BETA SUBUNIT, PUTATIVE (AFU_ORTHOLOGUE AFUA_4G13030)-RELATED; 1.
DR   Pfam; PF03328; HpcH_HpaI; 1.
DR   PIRSF; PIRSF015582; Cit_lyase_B; 1.
DR   SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
PE   4: Predicted;
KW   Lyase {ECO:0000313|EMBL:ODN89494.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR015582-2};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR015582-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000094043}.
FT   DOMAIN          23..242
FT                   /note="HpcH/HpaI aldolase/citrate lyase"
FT                   /evidence="ECO:0000259|Pfam:PF03328"
FT   BINDING         84
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT   BINDING         150
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
FT   BINDING         150
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
SQ   SEQUENCE   317 AA;  34973 MW;  1489A0B1831EF809 CRC64;
     MAFFLPRYRS LSTAAACSPV SRRAILYVPG SNPRMLEKSL LSPADSIAYD LEDSVSVGKK
     TDARRLVAEL LDSERRPKGE VVARINAIGT NYEQDDLDEL LRTRHLQTIA LPKTNSADHI
     EYIISRINRL APEYKRSGKP GAIRIIGMIE TAKAMVDIKT IAASGKGHLD ALLANCADLG
     LTRTPTKDEL LYPRSKLVTT AKAYGLQAID LVCVDYKDRD ALRNECEQGR ILGFDGKATI
     HPDQVDTIHR SFAPSSRDIL KAARVKFSFE YNDRLGKGAY TLDESMIDAP VYKQAIKILA
     KAEAAGLEVP LITLEDI
//
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