OXDD_ARTBC
ID OXDD_ARTBC Reviewed; 404 AA.
AC D4AKL6;
DT 09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 03-AUG-2022, entry version 51.
DE RecName: Full=Probable oxalate decarboxylase ARB_04859 {ECO:0000305};
DE EC=4.1.1.2 {ECO:0000250|UniProtKB:O34714};
DE Flags: Precursor;
GN ORFNames=ARB_04859;
OS Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton
OS mentagrophytes).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=663331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], IDENTIFICATION BY MASS
RP SPECTROMETRY, SUBCELLULAR LOCATION, AND INDUCTION.
RC STRAIN=ATCC MYA-4681 / CBS 112371;
RX PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT "Comparative and functional genomics provide insights into the
RT pathogenicity of dermatophytic fungi.";
RL Genome Biol. 12:R7.1-R7.16(2011).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=21919205; DOI=10.1002/pmic.201100234;
RA Sriranganadane D., Waridel P., Salamin K., Feuermann M., Mignon B.,
RA Staib P., Neuhaus J.M., Quadroni M., Monod M.;
RT "Identification of novel secreted proteases during extracellular
RT proteolysis by dermatophytes at acidic pH.";
RL Proteomics 11:4422-4433(2011).
CC -!- FUNCTION: Converts oxalate to formate and CO(2) in an O(2)-dependent
CC reaction. Can also catalyze minor side reactions: oxalate oxidation to
CC produce H(2)O(2), and oxalate-dependent, H(2)O(2)-independent dye
CC oxidations. {ECO:0000250|UniProtKB:O34714}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + oxalate = CO2 + formate; Xref=Rhea:RHEA:16509,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15740, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:30623; EC=4.1.1.2;
CC Evidence={ECO:0000250|UniProtKB:O34714};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:O34714};
CC Note=Binds 2 manganese ions per subunit.
CC {ECO:0000250|UniProtKB:O34714};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21247460,
CC ECO:0000269|PubMed:21919205}.
CC -!- INDUCTION: Expression is up-regulated in presence of human
CC keratinocytes. {ECO:0000269|PubMed:21247460}.
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DR EMBL; ABSU01000002; EFE35925.1; -; Genomic_DNA.
DR RefSeq; XP_003016570.1; XM_003016524.1.
DR AlphaFoldDB; D4AKL6; -.
DR SMR; D4AKL6; -.
DR STRING; 663331.D4AKL6; -.
DR EnsemblFungi; EFE35925; EFE35925; ARB_04859.
DR GeneID; 9522052; -.
DR KEGG; abe:ARB_04859; -.
DR eggNOG; ENOG502RJG4; Eukaryota.
DR HOGENOM; CLU_030515_2_1_1; -.
DR OMA; WVEIYKS; -.
DR Proteomes; UP000008866; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046564; F:oxalate decarboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0033609; P:oxalate metabolic process; IEA:InterPro.
DR Gene3D; 2.60.120.10; -; 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 Pfam; PF00190; Cupin_1; 2.
DR SMART; SM00835; Cupin_1; 2.
DR SUPFAM; SSF51182; SSF51182; 1.
DR TIGRFAMs; TIGR03404; bicupin_oxalic; 1.
PE 1: Evidence at protein level;
KW Decarboxylase; Glycoprotein; Lyase; Manganese; Metal-binding;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..404
FT /note="Probable oxalate decarboxylase ARB_04859"
FT /id="PRO_0000434916"
FT DOMAIN 74..215
FT /note="Cupin type-1 1"
FT /evidence="ECO:0000255"
FT DOMAIN 249..393
FT /note="Cupin type-1 2"
FT /evidence="ECO:0000255"
FT ACT_SITE 357
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:O34714"
FT BINDING 117
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O34714"
FT BINDING 119
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O34714"
FT BINDING 123
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O34714"
FT BINDING 162
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O34714"
FT BINDING 296
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O34714"
FT BINDING 298
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O34714"
FT BINDING 303
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O34714"
FT BINDING 342
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O34714"
FT CARBOHYD 226
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 244
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 346
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 404 AA; 43703 MW; DC51440D279A4507 CRC64;
MKYSAVLVAA LAAIADATIP IPKGGVPGQP IQESGKGAVF SGGTNNQLDL QNPSNIGGQP
ATDNGLVPNM KWSFSLSKTR MLYGGWIREQ VIQDLPTSHD IAGAQVHLIK GGIRQMHWHR
VAEWAYIYAG SFLISAVTED GQFQLDKLGV GDMYYFPKGA AHSLQGLEDE NEILLIFDDG
DFDRVGTTFM VADWISHTPK DVLAKNFGVP PSTFDKTYNP DLALINSTIS TKTVEGGNGA
LTGNSSYTFH ISNAPEIQVP GGGGTIQVVD SKNFPVSKTI ACAVVRLKPG GMRELHWHPT
AEEWLYFHSG NARATVYIGG GLARTFDFTA GDAGVFPDNS GHYIENTSET EELIYLELYK
ADRVADVSLS QWLALTPSDI AAAAINVPIE VIEQIKKEKQ YIVS
