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Database: UniProt
Entry: A0A135SWA4_9PEZI
LinkDB: A0A135SWA4_9PEZI
Original site: A0A135SWA4_9PEZI 
ID   A0A135SWA4_9PEZI        Unreviewed;       465 AA.
AC   A0A135SWA4;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=Oxalate decarboxylase family bicupin {ECO:0000313|EMBL:KXH40209.1};
GN   ORFNames=CSIM01_06387 {ECO:0000313|EMBL:KXH40209.1};
OS   Colletotrichum simmondsii.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum acutatum species complex.
OX   NCBI_TaxID=703756 {ECO:0000313|EMBL:KXH40209.1, ECO:0000313|Proteomes:UP000070328};
RN   [1] {ECO:0000313|EMBL:KXH40209.1, ECO:0000313|Proteomes:UP000070328}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS122122 {ECO:0000313|EMBL:KXH40209.1,
RC   ECO:0000313|Proteomes:UP000070328};
RA   Baroncelli R., Thon M.R.;
RT   "The genome sequence of Colletotrichum simmondsii CBS122122.";
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:KXH40209.1}.
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DR   EMBL; JFBX01000374; KXH40209.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A135SWA4; -.
DR   OrthoDB; 2358302at2759; -.
DR   Proteomes; UP000070328; 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   CDD; cd20304; cupin_OxDC_N; 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; PTHR35848:SF6; CUPIN_2 DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR35848; OXALATE-BINDING PROTEIN; 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|PIRSR:PIRSR617774-2};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR617774-2}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..465
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5007802783"
FT   DOMAIN          112..254
FT                   /note="Cupin type-1"
FT                   /evidence="ECO:0000259|SMART:SM00835"
FT   DOMAIN          291..432
FT                   /note="Cupin type-1"
FT                   /evidence="ECO:0000259|SMART:SM00835"
FT   REGION          27..62
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          443..465
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        396
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617774-1"
FT   BINDING         156
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617774-2"
FT   BINDING         158
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617774-2"
FT   BINDING         162
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617774-2"
FT   BINDING         201
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617774-2"
FT   BINDING         336
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617774-2"
FT   BINDING         338
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617774-2"
FT   BINDING         343
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617774-2"
FT   BINDING         382
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617774-2"
SQ   SEQUENCE   465 AA;  51932 MW;  0B34F1363AE98D6B CRC64;
     MHLPLLLSGA VLSFIAPTLA VPVQDSPRQR LLDGKGLPTK YRSGSPPYTP GHKDKYDSPI
     DSVGDELDPL PYRNGLGASV LGPWNEARSR QNPDLVRPPG TDHGNLANMR WSFADSHIRI
     EEGGWTRQTT IRELPTSIEL AGVNMRLDEG VVRELHWHKE AEWAYVLDGS CRITAIDYEG
     GNFIDDVQKG DLWYFPSGVP HSLQGLGENG TEFLLIFDDG HFSEESTFIL TDWLAHTPKS
     VISKNFKLAP EVFANIPEGE KYIFQGTTPG SISHEAPDGK GVKKSKHQFT HKMLAQEPKK
     TSGGEVRVTD SKNFPISKTI AAAHAIIEPG ALREMHWHPN ADEWSFFIKG RARVTIFASE
     GNARTFDYVP GDVGIVPKNM GHFVENIGDE PLEMLEIFRA DEFRDFSLFQ WMGETPKKLV
     VDHLFANDPD AGEKFWDKVK SAEKDEITKD TSVDAEDVQT ETEEL
//
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