ID A0A074W6F5_9PEZI Unreviewed; 316 AA.
AC A0A074W6F5;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Beta subunit of citrate lyase {ECO:0000313|EMBL:KEQ67144.1};
GN ORFNames=M437DRAFT_61578 {ECO:0000313|EMBL:KEQ67144.1};
OS Aureobasidium melanogenum CBS 110374.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Dothideales; Saccotheciaceae; Aureobasidium.
OX NCBI_TaxID=1043003 {ECO:0000313|EMBL:KEQ67144.1, ECO:0000313|Proteomes:UP000030672};
RN [1] {ECO:0000313|EMBL:KEQ67144.1, ECO:0000313|Proteomes:UP000030672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 110374 {ECO:0000313|EMBL:KEQ67144.1,
RC ECO:0000313|Proteomes:UP000030672};
RX PubMed=24984952;
RA Gostin Ar C., Ohm R.A., Kogej T., Sonjak S., Turk M., Zajc J., Zalar P.,
RA Grube M., Sun H., Han J., Sharma A., Chiniquy J., Ngan C.Y., Lipzen A.,
RA Barry K., Grigoriev I.V., Gunde-Cimerman N.;
RT "Genome sequencing of four Aureobasidium pullulans varieties:
RT biotechnological potential, stress tolerance, and description of new
RT species.";
RL BMC Genomics 15:549-549(2014).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
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DR EMBL; KL584824; KEQ67144.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A074W6F5; -.
DR STRING; 1043003.A0A074W6F5; -.
DR HOGENOM; CLU_044864_1_1_1; -.
DR OrthoDB; 2874421at2759; -.
DR Proteomes; UP000030672; 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:KEQ67144.1};
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:UP000030672}.
FT DOMAIN 9..236
FT /note="HpcH/HpaI aldolase/citrate lyase"
FT /evidence="ECO:0000259|Pfam:PF03328"
FT BINDING 71
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT BINDING 137
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
FT BINDING 137
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT BINDING 164
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
SQ SEQUENCE 316 AA; 34356 MW; D57E9F3E92E20459 CRC64;
MAASPIVRRA LLYVPGSSMR FLEKSRGVAV DTICYDLEDS VTPGKKAEAR SNLQSILSRE
RVSGIKEQAV RINSVDSGYA LDDLTQVLKG QNLDALVIPK VNSASDLHFV TDVIRHALPE
RHGPDAKSPL RLIALIESAR AVMDLSAICK ASPYLSGLIF AAEDFALDLS ITRTPDLKEF
LYARSAIATA ARAFNLPSTI DLVTTAFRGE QGQQVLKEES EGGKRMGYNG KQCIHPSQVE
LVQNIFSPSQ EEVDYAVRVV IADEKADAQG RGAWTLDGKM IDVPVVGKAK ATVKKAEVCG
IDVASVREKF KDQEPE
//
