ID   A0A1L7WCH6_9HELO        Unreviewed;       356 AA.
AC   A0A1L7WCH6;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   SubName: Full=Related to citrate lyase beta subunit {ECO:0000313|EMBL:CZR50495.1};
GN   ORFNames=PAC_00368 {ECO:0000313|EMBL:CZR50495.1};
OS   Phialocephala subalpina.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Mollisiaceae; Phialocephala;
OC   Phialocephala fortinii species complex.
OX   NCBI_TaxID=576137 {ECO:0000313|EMBL:CZR50495.1, ECO:0000313|Proteomes:UP000184330};
RN   [1] {ECO:0000313|EMBL:CZR50495.1, ECO:0000313|Proteomes:UP000184330}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAMH 11012 {ECO:0000313|EMBL:CZR50495.1,
RC   ECO:0000313|Proteomes:UP000184330};
RA   Ploux O.;
RL   Submitted (MAR-2016) 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; FJOG01000001; CZR50495.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1L7WCH6; -.
DR   STRING; 576137.A0A1L7WCH6; -.
DR   OrthoDB; 2874421at2759; -.
DR   Proteomes; UP000184330; 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:CZR50495.1};
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:UP000184330}.
FT   DOMAIN          45..276
FT                   /note="HpcH/HpaI aldolase/citrate lyase"
FT                   /evidence="ECO:0000259|Pfam:PF03328"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..19
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         111
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT   BINDING         177
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
FT   BINDING         177
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT   BINDING         204
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
SQ   SEQUENCE   356 AA;  39196 MW;  313B4313E1E94133 CRC64;
     MRGLNVPNQH QQCNHQNPPF DDRQLRLPFT FTAKMSIKAA STLRRALLYV PSSSPKFLQK
     SLTLPFPLDT ISYDLEDSVA PHLKSPARKS LLEHLSSARP SPSKIREISV RINDVSSGLA
     LDDLTTILQA KNLDALVIPK VNKASDLHFV TDVLRHQLPE RHGGGEGESV KIIALIESAE
     AIMNLNEICK ASPYLDGLIF AAEDFALDLS LTRTPSLSEF LYARSAIVTA ARAHNLGSTI
     DLVCTAFRGE NGLRTLEEES QGGKGLGFNG KQCIHPSQVE IVQRTFAPGE KEVEWAMRVV
     IGDEKAEKGG RGAWTLEGKM IDKPVVGKAR AVVRRAELCG FDVEGVREKW KDQEPE
//