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Database: UniProt
Entry: J9VIR7_CRYNH
LinkDB: J9VIR7_CRYNH
Original site: J9VIR7_CRYNH 
ID   J9VIR7_CRYNH            Unreviewed;       269 AA.
AC   J9VIR7;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   SubName: Full=2,4-dihydroxyhept-2-ene-1,7-dioic acid aldolase {ECO:0000313|EMBL:AFR94093.1};
GN   ORFNames=CNAG_02599 {ECO:0000313|EMBL:AFR94093.1};
OS   Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 /
OS   CBS 10515 / FGSC 9487) (Filobasidiella neoformans var. grubii).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus;
OC   Cryptococcus neoformans species complex.
OX   NCBI_TaxID=235443 {ECO:0000313|EMBL:AFR94093.1, ECO:0000313|Proteomes:UP000010091};
RN   [1] {ECO:0000313|EMBL:AFR94093.1, ECO:0000313|Proteomes:UP000010091}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H99 / ATCC 208821 / CBS 10515 / FGSC 9487
RC   {ECO:0000313|Proteomes:UP000010091};
RX   PubMed=24743168; DOI=10.1371/journal.pgen.1004261;
RA   Janbon G., Ormerod K.L., Paulet D., Byrnes E.J.III., Yadav V.,
RA   Chatterjee G., Mullapudi N., Hon C.C., Billmyre R.B., Brunel F., Bahn Y.S.,
RA   Chen W., Chen Y., Chow E.W., Coppee J.Y., Floyd-Averette A., Gaillardin C.,
RA   Gerik K.J., Goldberg J., Gonzalez-Hilarion S., Gujja S., Hamlin J.L.,
RA   Hsueh Y.P., Ianiri G., Jones S., Kodira C.D., Kozubowski L., Lam W.,
RA   Marra M., Mesner L.D., Mieczkowski P.A., Moyrand F., Nielsen K., Proux C.,
RA   Rossignol T., Schein J.E., Sun S., Wollschlaeger C., Wood I.A., Zeng Q.,
RA   Neuveglise C., Newlon C.S., Perfect J.R., Lodge J.K., Idnurm A.,
RA   Stajich J.E., Kronstad J.W., Sanyal K., Heitman J., Fraser J.A.,
RA   Cuomo C.A., Dietrich F.S.;
RT   "Analysis of the genome and transcriptome of Cryptococcus neoformans var.
RT   grubii reveals complex RNA expression and microevolution leading to
RT   virulence attenuation.";
RL   PLoS Genet. 10:E1004261-E1004261(2014).
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DR   EMBL; CP003822; AFR94093.1; -; Genomic_DNA.
DR   RefSeq; XP_012048043.1; XM_012192653.1.
DR   AlphaFoldDB; J9VIR7; -.
DR   GeneID; 23886210; -.
DR   KEGG; cng:CNAG_02599; -.
DR   VEuPathDB; FungiDB:CNAG_02599; -.
DR   HOGENOM; CLU_059964_3_1_1; -.
DR   OrthoDB; 2785075at2759; -.
DR   Proteomes; UP000010091; Chromosome 3.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
DR   InterPro; IPR005000; Aldolase/citrate-lyase_domain.
DR   InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR   InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR   PANTHER; PTHR30502; 2-KETO-3-DEOXY-L-RHAMNONATE ALDOLASE; 1.
DR   PANTHER; PTHR30502:SF9; HPCH_HPAI ALDOLASE_CITRATE LYASE DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF03328; HpcH_HpaI; 1.
DR   SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
PE   4: Predicted;
FT   DOMAIN          33..225
FT                   /note="HpcH/HpaI aldolase/citrate lyase"
FT                   /evidence="ECO:0000259|Pfam:PF03328"
SQ   SEQUENCE   269 AA;  28806 MW;  E1D08D099CB52219 CRC64;
     MTLTNVATAH TTTVQNPRLR LLNNLRSKTP ALMTFIAIPS VRHAQIIALT GLDGVIIDCE
     HGHIGDDQMH NSVSAISALG VSPIIRVRGP QPDILKRALD TGAHGLMVPM INTAKEAAAV
     VTYSKFPPYG LRGQGSAFPA IGHGLTTPEY MKTANETILT IVQIETKQGV ENVEEIAAVP
     GIDYLFIGPN DLAQSLLGYT PARGDEPVFV EAIDKIVAAA RKHGKWVGRL VNDGPLAVEA
     LKTFDSVAIT GDTKAITNWY TAQIDCVRN
//
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