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Database: UniProt
Entry: A0A010S8G0_9PEZI
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ID   A0A010S8G0_9PEZI        Unreviewed;       409 AA.
AC   A0A010S8G0;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=Oxalate decarboxylase {ECO:0000313|EMBL:EXF80953.1};
GN   ORFNames=CFIO01_12103 {ECO:0000313|EMBL:EXF80953.1};
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:EXF80953.1, ECO:0000313|Proteomes:UP000020467};
RN   [1] {ECO:0000313|EMBL:EXF80953.1, ECO:0000313|Proteomes:UP000020467}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PJ7 {ECO:0000313|EMBL:EXF80953.1,
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=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|PIRSR:PIRSR617774-2};
CC       Note=Binds 2 manganese ions per subunit.
CC       {ECO:0000256|PIRSR:PIRSR617774-2};
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:EXF80953.1}.
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DR   EMBL; JARH01000412; EXF80953.1; -; Genomic_DNA.
DR   RefSeq; XP_007595408.1; XM_007595346.1.
DR   AlphaFoldDB; A0A010S8G0; -.
DR   STRING; 1445577.A0A010S8G0; -.
DR   KEGG; cfj:CFIO01_12103; -.
DR   eggNOG; ENOG502RJG4; Eukaryota.
DR   HOGENOM; CLU_030515_2_1_1; -.
DR   OrthoDB; 2358302at2759; -.
DR   Proteomes; UP000020467; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0033609; P:oxalate metabolic process; IEA:InterPro.
DR   CDD; cd20305; cupin_OxDC_C; 1.
DR   Gene3D; 2.60.120.10; Jelly Rolls; 2.
DR   InterPro; IPR017774; Bicupin_oxalate_deCO2ase/Oxase.
DR   InterPro; IPR006045; Cupin_1.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   InterPro; IPR011051; RmlC_Cupin_sf.
DR   NCBIfam; TIGR03404; bicupin_oxalic; 1.
DR   PANTHER; PTHR31238:SF32; CUPIN TYPE-1 DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR   PANTHER; PTHR31238; GERMIN-LIKE PROTEIN SUBFAMILY 3 MEMBER 3; 1.
DR   Pfam; PF00190; Cupin_1; 2.
DR   SMART; SM00835; Cupin_1; 2.
DR   SUPFAM; SSF51182; RmlC-like cupins; 1.
PE   4: Predicted;
KW   Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|PIRSR:PIRSR617774-2};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR617774-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000020467};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..409
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001456457"
FT   DOMAIN          87..220
FT                   /note="Cupin type-1"
FT                   /evidence="ECO:0000259|SMART:SM00835"
FT   DOMAIN          256..399
FT                   /note="Cupin type-1"
FT                   /evidence="ECO:0000259|SMART:SM00835"
FT   ACT_SITE        363
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617774-1"
FT   BINDING         122
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617774-2"
FT   BINDING         124
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617774-2"
FT   BINDING         128
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617774-2"
FT   BINDING         167
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617774-2"
FT   BINDING         302
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617774-2"
FT   BINDING         304
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617774-2"
FT   BINDING         309
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617774-2"
FT   BINDING         348
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617774-2"
SQ   SEQUENCE   409 AA;  45039 MW;  AC324F9633A91EB4 CRC64;
     MRLLQNSVAG LIGLVAVASA SPQVAKRDAQ FNIGQPIDAN GKGAPILGGT NNAIDRENPD
     NLGRQSTDSG VVPNLKWRFS DSKTRIFNGG WVREQVIQDL PQSHDIAAAQ QHIKRGAVRE
     LHWHKVAEWG FVYSGSIIIG AVGEDGKSQV EQLNYGDIWY FPKGAAHYVQ GVAEESEFLL
     AFDEADFDKI GTTFNIVDWL AHTPRDILAR NFGVNASVFD KLPATNPYIL NGTVATTNVT
     VPPGQYLSGN SSFVYRTFEH PPEKVPGNGG EFRKIDSTNF PIAKTIAATF VTLKPGGLRE
     LHWHPNAEEW LYFHKGKGKA TVFIGSAASR TFDLEAGDTA AFPDNSGHYI ENTSDTEDLV
     WIELYKSDRV VDISLTQWLA LTPPEVVAQT LKVPLEFVKN LKQEKQILI
//
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