ID E4V2E9_ARTGP Unreviewed; 404 AA.
AC E4V2E9;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE SubName: Full=Oxalate decarboxylase oxdD {ECO:0000313|EMBL:EFR04214.1};
GN ORFNames=MGYG_07221 {ECO:0000313|EMBL:EFR04214.1};
OS Arthroderma gypseum (strain ATCC MYA-4604 / CBS 118893) (Microsporum
OS gypseum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Nannizzia.
OX NCBI_TaxID=535722 {ECO:0000313|Proteomes:UP000002669};
RN [1] {ECO:0000313|Proteomes:UP000002669}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4604 / CBS 118893 {ECO:0000313|Proteomes:UP000002669};
RX PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT "Comparative genome analysis of Trichophyton rubrum and related
RT dermatophytes reveals candidate genes involved in infection.";
RL MBio 3:E259-E259(2012).
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; DS989827; EFR04214.1; -; Genomic_DNA.
DR RefSeq; XP_003171222.1; XM_003171174.1.
DR AlphaFoldDB; E4V2E9; -.
DR STRING; 535722.E4V2E9; -.
DR GeneID; 10026472; -.
DR VEuPathDB; FungiDB:MGYG_07221; -.
DR eggNOG; ENOG502RJG4; Eukaryota.
DR HOGENOM; CLU_030515_2_1_1; -.
DR InParanoid; E4V2E9; -.
DR OMA; WVREQTI; -.
DR OrthoDB; 2358302at2759; -.
DR Proteomes; UP000002669; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
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:UP000002669};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..404
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003190944"
FT DOMAIN 73..214
FT /note="Cupin type-1"
FT /evidence="ECO:0000259|SMART:SM00835"
FT DOMAIN 249..393
FT /note="Cupin type-1"
FT /evidence="ECO:0000259|SMART:SM00835"
FT REGION 30..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..61
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 357
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR617774-1"
FT BINDING 116
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR617774-2"
FT BINDING 118
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR617774-2"
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 161
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR617774-2"
FT BINDING 296
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR617774-2"
FT BINDING 298
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR617774-2"
FT BINDING 303
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
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"
SQ SEQUENCE 404 AA; 43939 MW; DF3BE66AC0DD6A8B CRC64;
MKFGSTLVAA IAAVAGTAAK DYGGVPGQPI QESGKGGVFS GGTNPELDLQ NPSNINGQPA
TDNGLVPNLK WSFSLSKTRM FHGGWIREQV IQDLPASHDI AGAQVHLIKG GIRQMHWHRV
AEWGYVYAGA ILVSAVSEDG QYQIDKLTPG DMYYFPKGAA HSFQGLEDEN EVLVAFDDGD
FDKHGTTFQI ADWMSHTPRD VVAKNFNTSV GAFEKLRKTE LEIINSTISN PNVTGGPNGP
LMGKSSYTFH IRDAPEIQVP GGGGTIQIVD SKNFPISKTV ACAVVRLKPG ALRELHWHPT
AEEWLYFHSG NARATVYVSG GLSRTFDFTA GDTGVFPDNS GHYIENTSED EDLVYLELYK
ADRVADISLS QWLALTPHDI AAAAINVPIE VIEQIKKEKQ FIVQ
//
