ID A0A010SKT4_9PEZI Unreviewed; 298 AA.
AC A0A010SKT4;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=HpcH/HpaI aldolase/citrate lyase family protein {ECO:0000313|EMBL:EXF85463.1};
GN ORFNames=CFIO01_13587 {ECO:0000313|EMBL:EXF85463.1};
OS Colletotrichum fioriniae PJ7.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum acutatum species complex.
OX NCBI_TaxID=1445577 {ECO:0000313|EMBL:EXF85463.1, ECO:0000313|Proteomes:UP000020467};
RN [1] {ECO:0000313|EMBL:EXF85463.1, ECO:0000313|Proteomes:UP000020467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PJ7 {ECO:0000313|EMBL:EXF85463.1,
RC ECO:0000313|Proteomes:UP000020467};
RA Baroncelli R., Thon M.R.;
RT "The genome sequence of Colletotrichum fioriniae PJ7.";
RL Submitted (FEB-2014) 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:EXF85463.1}.
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DR EMBL; JARH01000098; EXF85463.1; -; Genomic_DNA.
DR RefSeq; XP_007590894.1; XM_007590832.1.
DR AlphaFoldDB; A0A010SKT4; -.
DR STRING; 1445577.A0A010SKT4; -.
DR KEGG; cfj:CFIO01_13587; -.
DR eggNOG; ENOG502QQPK; Eukaryota.
DR HOGENOM; CLU_044864_0_0_1; -.
DR OrthoDB; 2874421at2759; -.
DR Proteomes; UP000020467; 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:EXF85463.1};
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:UP000020467}.
FT DOMAIN 1..218
FT /note="HpcH/HpaI aldolase/citrate lyase"
FT /evidence="ECO:0000259|Pfam:PF03328"
FT BINDING 53
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT BINDING 119
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
FT BINDING 119
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT BINDING 146
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
SQ SEQUENCE 298 AA; 32142 MW; ADBB068F28A4BE7E CRC64;
MLTKSLGLKS DNVTYDLEDS VTPSLKSEAR GQLRAFLSKH KSRPSAIAEL AVRINAVETK
FALDDLTSLG SLPNIDAVVV PKVNSAADLT YVTDVLRHVA PERHTATSQN PIKIIALIES
ARSVMNLSEI CKASPYLSGL VFAAEDFALD LSLTRTPSLT EFLYARSAIV TAAKAAGLPS
AIDLVCTSYK GEEGLKRLEE ESTGGKSMGF NGKQCIHPNQ VELVQKLFAP GEKEVEWAVR
VTIADEKASK AGRGAWTLDG MMIDAPVTGK AQAIIAKAER CDIDVASLRT KWKDQQPE
//
