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Database: UniProt
Entry: A0A2H3EEC6_ARMGA
LinkDB: A0A2H3EEC6_ARMGA
Original site: A0A2H3EEC6_ARMGA 
ID   A0A2H3EEC6_ARMGA        Unreviewed;       453 AA.
AC   A0A2H3EEC6;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Oxalate decarboxylase {ECO:0000313|EMBL:PBL04375.1};
GN   ORFNames=ARMGADRAFT_1070833 {ECO:0000313|EMBL:PBL04375.1};
OS   Armillaria gallica (Bulbous honey fungus) (Armillaria bulbosa).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Marasmiineae; Physalacriaceae; Armillaria.
OX   NCBI_TaxID=47427 {ECO:0000313|EMBL:PBL04375.1, ECO:0000313|Proteomes:UP000217790};
RN   [1] {ECO:0000313|Proteomes:UP000217790}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ar21-2 {ECO:0000313|Proteomes:UP000217790};
RX   PubMed=29085064; DOI=10.1038/s41559-017-0347-8;
RA   Sipos G., Prasanna A.N., Walter M.C., O'Connor E., Balint B., Krizsan K.,
RA   Kiss B., Hess J., Varga T., Slot J., Riley R., Boka B., Rigling D.,
RA   Barry K., Lee J., Mihaltcheva S., LaButti K., Lipzen A., Waldron R.,
RA   Moloney N.M., Sperisen C., Kredics L., Vagvoelgyi C., Patrignani A.,
RA   Fitzpatrick D., Nagy I., Doyle S., Anderson J.B., Grigoriev I.V.,
RA   Gueldener U., Muensterkoetter M., Nagy L.G.;
RT   "Genome expansion and lineage-specific genetic innovations in the forest
RT   pathogenic fungi Armillaria.";
RL   Nat. Ecol. Evol. 1:1931-1941(2017).
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};
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DR   EMBL; KZ293644; PBL04375.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2H3EEC6; -.
DR   STRING; 47427.A0A2H3EEC6; -.
DR   InParanoid; A0A2H3EEC6; -.
DR   OMA; TISNAKW; -.
DR   OrthoDB; 2358302at2759; -.
DR   Proteomes; UP000217790; 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:UP000217790};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..453
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5013863949"
FT   DOMAIN          119..262
FT                   /note="Cupin type-1"
FT                   /evidence="ECO:0000259|SMART:SM00835"
FT   DOMAIN          297..438
FT                   /note="Cupin type-1"
FT                   /evidence="ECO:0000259|SMART:SM00835"
FT   REGION          24..47
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        402
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617774-1"
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         164
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617774-2"
FT   BINDING         168
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617774-2"
FT   BINDING         207
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617774-2"
FT   BINDING         342
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617774-2"
FT   BINDING         344
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617774-2"
FT   BINDING         349
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617774-2"
FT   BINDING         388
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617774-2"
SQ   SEQUENCE   453 AA;  48449 MW;  B946FD94D91565D2 CRC64;
     MFQVSSLLGI ILLARLATGA PAASESASSS TTVSASESGT VSSTDTAASS TATVPFASLD
     PNLPLWDDQS DPSVVSPVRG QLGASILGPD NIPIDLQNPD LLAPPTTDAG TISNAKWPFS
     FSHNRLQTGG WARQENIGVM PIATQMASVN MRLEAGAIRE LHWHKTSEWA YVLKGSTQIS
     AVDAQGRNFL ATVGPGDLWY FPPGIPHSLQ ATADDEGGSE FILVFDDGAF SEDSTFLLTD
     WLAHVPAEVI QRNFQVDPQA FAHIPAKELY IFPSAPPPDD ATAPESPQGT IPDPFSFALS
     QVNATQLSGG SVKIVDSTTF KVSTTIAVAE VTVNPGAIRE LHWHPTQDEW SLFLEGEGRV
     TIFASQGTAR TFNYQPGDIG YVPAAMGHYV ENTGNTTMKF LEIFNTDRFE DISLNQWLAL
     TPPDVVKAHL DLDDATIAQL SKTKPVVMGP QSS
//
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