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Database: UniProt
Entry: A0A0G2FDL3_9PEZI
LinkDB: A0A0G2FDL3_9PEZI
Original site: A0A0G2FDL3_9PEZI 
ID   A0A0G2FDL3_9PEZI        Unreviewed;       534 AA.
AC   A0A0G2FDL3;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Putative oxalate decarboxylase family bicupin {ECO:0000313|EMBL:KKY32687.1};
GN   ORFNames=UCDDA912_g07393 {ECO:0000313|EMBL:KKY32687.1};
OS   Diaporthe ampelina.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Diaporthales; Diaporthaceae; Diaporthe.
OX   NCBI_TaxID=1214573 {ECO:0000313|EMBL:KKY32687.1, ECO:0000313|Proteomes:UP000034680};
RN   [1] {ECO:0000313|EMBL:KKY32687.1, ECO:0000313|Proteomes:UP000034680}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DA912 {ECO:0000313|EMBL:KKY32687.1};
RA   Lawrence D.P., Travadon R., Rolshausen P.E., Baumgartner K.;
RT   "Distinctive expansion of gene families associated with plant cell wall
RT   degradation and secondary metabolism in the genomes of grapevine trunk
RT   pathogens.";
RL   Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KKY32687.1, ECO:0000313|Proteomes:UP000034680}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DA912 {ECO:0000313|EMBL:KKY32687.1};
RA   Morales-Cruz A., Amrine K.C., Cantu D.;
RL   Submitted (MAY-2015) 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:KKY32687.1}.
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DR   EMBL; LCUC01000292; KKY32687.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G2FDL3; -.
DR   STRING; 1214573.A0A0G2FDL3; -.
DR   OrthoDB; 2358302at2759; -.
DR   Proteomes; UP000034680; 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 CONSERVED BARREL 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000034680};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..534
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002543913"
FT   DOMAIN          148..291
FT                   /note="Cupin type-1"
FT                   /evidence="ECO:0000259|SMART:SM00835"
FT   DOMAIN          332..473
FT                   /note="Cupin type-1"
FT                   /evidence="ECO:0000259|SMART:SM00835"
FT   ACT_SITE        437
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617774-1"
FT   BINDING         194
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617774-2"
FT   BINDING         196
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617774-2"
FT   BINDING         200
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617774-2"
FT   BINDING         239
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617774-2"
FT   BINDING         377
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617774-2"
FT   BINDING         379
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617774-2"
FT   BINDING         384
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617774-2"
FT   BINDING         423
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617774-2"
SQ   SEQUENCE   534 AA;  57723 MW;  8ACECB6C8BCDDF5F CRC64;
     MYSRGYVLTV GLLQALPFSH AIPAPQMGDY GENSGPVGGV DPPIPTVTAP AGSLYGSEDL
     LGGNAALPDV ESESAVVENP EYVNGQSADR KLGLYLDFNS VNAPQPERGG YGATDPGPRT
     YYYERINPDV YAVPGTDSGD VAQAMWPMGL SHNRAGSEPG AGWARQQNQD VLPSATAMAG
     VDMRLGPNAY RELHWHTANE WSLMLKGCVR ISTVNEDGAT DVDDVCAGDV WFFPSGVPHS
     IQAFDEGCEF LLVFDDGAFS EDETFLLSEM MLRTPVSVLS KNFKADPSAF KNIPQDELYI
     FNGTPQPKEI DETQNLTSSA GSLDGTANSY TYHWSEQKPY ETPGGSVKIL DPTTFPIASN
     FAAALVVVQP GAMREIHWHT TSPEWNYFLQ GSARITVFQA PEAARTFDFT AGGVGYIPQA
     SSHYVENTGT EDVIFLEVLQ ATKFSDVSAA QWLALTPKQV VQDHLDLPEG FWENLPKEKE
     YIKQGPKNMT ALATASLDDG DAPAATTSAT ASAVERSIKA GSVEENRREV TFFA
//
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