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Database: UniProt
Entry: A0A1B9G4U0_9TREE
LinkDB: A0A1B9G4U0_9TREE
Original site: A0A1B9G4U0_9TREE 
ID   A0A1B9G4U0_9TREE        Unreviewed;       289 AA.
AC   A0A1B9G4U0;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   RecName: Full=HpcH/HpaI aldolase/citrate lyase domain-containing protein {ECO:0000259|Pfam:PF03328};
GN   ORFNames=I302_03699 {ECO:0000313|EMBL:OCF26022.1};
OS   Kwoniella bestiolae CBS 10118.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Kwoniella.
OX   NCBI_TaxID=1296100 {ECO:0000313|EMBL:OCF26022.1, ECO:0000313|Proteomes:UP000092730};
RN   [1] {ECO:0000313|EMBL:OCF26022.1, ECO:0000313|Proteomes:UP000092730}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 10118 {ECO:0000313|EMBL:OCF26022.1,
RC   ECO:0000313|Proteomes:UP000092730};
RG   The Broad Institute Genome Sequencing Platform;
RA   Cuomo C., Litvintseva A., Chen Y., Heitman J., Sun S., Springer D.,
RA   Dromer F., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A.,
RA   Alvarado L., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA   Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA   Murphy C., Pearson M., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA   Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Cryptococcus bestiolae CBS10118.";
RL   Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000092730}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 10118 {ECO:0000313|Proteomes:UP000092730};
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 (DEC-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the HpcH/HpaI aldolase family.
CC       {ECO:0000256|ARBA:ARBA00005568}.
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DR   EMBL; KI894020; OCF26022.1; -; Genomic_DNA.
DR   RefSeq; XP_019047092.1; XM_019190344.1.
DR   AlphaFoldDB; A0A1B9G4U0; -.
DR   STRING; 1296100.A0A1B9G4U0; -.
DR   GeneID; 30208098; -.
DR   VEuPathDB; FungiDB:I302_03699; -.
DR   OrthoDB; 1822991at2759; -.
DR   Proteomes; UP000092730; Unassembled WGS sequence.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
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:SF0; PHOSPHOENOLPYRUVATE CARBOXYLASE FAMILY PROTEIN; 1.
DR   Pfam; PF03328; HpcH_HpaI; 1.
DR   SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Reference proteome {ECO:0000313|Proteomes:UP000092730}.
FT   DOMAIN          51..234
FT                   /note="HpcH/HpaI aldolase/citrate lyase"
FT                   /evidence="ECO:0000259|Pfam:PF03328"
SQ   SEQUENCE   289 AA;  31459 MW;  4778FA28CF614628 CRC64;
     MTAANGTNGD SSKFAEDPLY QQTMSFIRPN WLKEKMEEGG LGFSFGMSMT FSPDVAQLAK
     VAGYTAVLIN MEHCRAGIQT ACDIACACLN IGISPICVVP SLQSDWISRL LDNGVQGIIV
     PRTGTAAMAK ELVKYSKFRP LGERPLTFTP QMQYQLPHAE YAKIAQNNTT LTMPMIETVE
     GLENCEEIAA VEGVDAIFVG AWDLADDMGI GGQRDSPVLY EALSKICRAA MKYGKFVGLG
     GLEPRPDIIA RLRKEYDCVR YVMAGRDTSV FQAGMAAQVK TIKEIEASS
//
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