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Database: UniProt
Entry: A0A0D2AKL2_9PEZI
LinkDB: A0A0D2AKL2_9PEZI
Original site: A0A0D2AKL2_9PEZI 
ID   A0A0D2AKL2_9PEZI        Unreviewed;       327 AA.
AC   A0A0D2AKL2;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=HpcH/HpaI aldolase/citrate lyase domain-containing protein {ECO:0000259|Pfam:PF03328};
GN   ORFNames=PV09_08827 {ECO:0000313|EMBL:KIV99523.1};
OS   Verruconis gallopava.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Venturiales; Sympoventuriaceae; Verruconis.
OX   NCBI_TaxID=253628 {ECO:0000313|EMBL:KIV99523.1, ECO:0000313|Proteomes:UP000053259};
RN   [1] {ECO:0000313|EMBL:KIV99523.1, ECO:0000313|Proteomes:UP000053259}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 43764 {ECO:0000313|EMBL:KIV99523.1,
RC   ECO:0000313|Proteomes:UP000053259};
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 Ochroconis gallopava CBS43764.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
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DR   EMBL; KN847576; KIV99523.1; -; Genomic_DNA.
DR   RefSeq; XP_016209393.1; XM_016362785.1.
DR   AlphaFoldDB; A0A0D2AKL2; -.
DR   STRING; 253628.A0A0D2AKL2; -.
DR   GeneID; 27316800; -.
DR   VEuPathDB; FungiDB:PV09_08827; -.
DR   InParanoid; A0A0D2AKL2; -.
DR   OrthoDB; 2874421at2759; -.
DR   Proteomes; UP000053259; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
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   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR015582-2};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR015582-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053259}.
FT   DOMAIN          22..247
FT                   /note="HpcH/HpaI aldolase/citrate lyase"
FT                   /evidence="ECO:0000259|Pfam:PF03328"
FT   BINDING         79
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT   BINDING         148
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
FT   BINDING         148
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT   BINDING         175
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
SQ   SEQUENCE   327 AA;  36161 MW;  B397380334717F3C CRC64;
     MVRSDPLLFS LLTTRTLKHN LVPGSSRKFL DKSRNLKVDN VTYDLEDSVT PGKKAEARKT
     LRDFLHQDRA EGITEQAVRI NAVETGMALD DLSEVLKAPN LDAIVVPKVD RPSDLHFVTD
     VIRHVLPERH PSTLDASSNP IKLIALIESA KSLSNLNDIC KASPYLSGLV FAAEDFAKDM
     SLTRTPSLTE FLYARSAIAT AARAHDLPST IDLVCTAFRG EEGLRTLQEE CEGGKRLGFN
     GKQCIHPTQV EIAQRIFSPS EKEVEWAVRV VIADEKADAQ GRGAWTLDGA MIDVPVVRKA
     KNIVKKAELC GINVEEVRAK WKDQEPE
//
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