ID A0A1C1CSE5_9EURO Unreviewed; 316 AA.
AC A0A1C1CSE5;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Citrate lyase subunit beta-like protein, mitochondrial {ECO:0000313|EMBL:OCT51411.1};
GN Name=CLYBL {ECO:0000313|EMBL:OCT51411.1};
GN ORFNames=CLCR_08827 {ECO:0000313|EMBL:OCT51411.1};
OS Cladophialophora carrionii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC Cladophialophora.
OX NCBI_TaxID=86049 {ECO:0000313|EMBL:OCT51411.1, ECO:0000313|Proteomes:UP000094526};
RN [1] {ECO:0000313|Proteomes:UP000094526}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KSF {ECO:0000313|Proteomes:UP000094526};
RA Teixeira M.M., Souza R.C., Almeida L.G., Vicente V.A., de Hoog S.,
RA Bocca A.L., de Almeida S.R., Vasconcelos A.T., Felipe M.S.;
RL Submitted (JUL-2015) 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:OCT51411.1}.
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DR EMBL; LGRB01000009; OCT51411.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1C1CSE5; -.
DR STRING; 86049.A0A1C1CSE5; -.
DR VEuPathDB; FungiDB:CLCR_08827; -.
DR VEuPathDB; FungiDB:G647_06671; -.
DR eggNOG; ENOG502QQPK; Eukaryota.
DR Proteomes; UP000094526; 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:OCT51411.1};
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:UP000094526}.
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 136
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
FT BINDING 136
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; 34631 MW; 97B44E970FE394B1 CRC64;
MAAKNVLRRA MLYVPGSSQR FLDKSRSLTA DCIAYDLEDS VTPGKKAEAR HAVRKALDTE
IPSGIKERAV RINSVGSGLA LGDLEEVVKS PNLTTLVVPK VESASDLTFI SDVLAHSRSK
DFLQEKGQIS ILALIESAKS LMNLNEICKA APHLLQGLVF AAEDFALDMS ITRTPSLTEM
LFARQSIATA ARAHNLPSTI DLVATAYKGE GDDSLLQREC EEGKRMGYNG KQCIHPSQVA
TVQKIYSPSQ EEVEWAVRIV IAQMRAEELG KGAWSMDGKM IDAPVEGKAR RIVQKAEVIG
FDVESLRQKH KDQQPE
//
