GLOX_PHACH
ID GLOX_PHACH Reviewed; 559 AA.
AC Q01772; Q01773; Q01845; Q7LIJ2;
DT 08-JUN-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Aldehyde oxidase GLOX {ECO:0000305};
DE EC=1.2.3.15 {ECO:0000269|PubMed:3553159, ECO:0000269|PubMed:8557673};
DE AltName: Full=Glyoxal oxidase {ECO:0000303|PubMed:8346264};
DE Short=GLOX {ECO:0000303|PubMed:8346264};
DE Flags: Precursor;
GN Name=GLX {ECO:0000303|PubMed:8346264};
OS Phanerodontia chrysosporium (White-rot fungus) (Sporotrichum pruinosum).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Phanerochaetaceae; Phanerodontia.
OX NCBI_TaxID=2822231;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX PubMed=8346264; DOI=10.1073/pnas.90.15.7411;
RA Kersten P., Cullen D.;
RT "Cloning and characterization of cDNA encoding glyoxal oxidase, a H2O2-
RT producing enzyme from the lignin-degrading basidiomycete Phanerochaete
RT chrysosporium.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:7411-7413(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, AND VARIANT
RP THR-308.
RC STRAIN=ATCC 24725 / DSM 6909 / CBS 481.73 / BCRC 36200 / NRRL 6361 / VKM
RC F-1767;
RX PubMed=7592374; DOI=10.1128/jb.177.21.6106-6110.1995;
RA Kersten P.J., Witek C., vanden Wymelenberg A., Cullen D.;
RT "Phanerochaete chrysosporium glyoxal oxidase is encoded by two allelic
RT variants: structure, genomic organization, and heterologous expression of
RT glx1 and glx2.";
RL J. Bacteriol. 177:6106-6110(1995).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=3553159; DOI=10.1128/jb.169.5.2195-2201.1987;
RA Kersten P.J., Kirk T.K.;
RT "Involvement of a new enzyme, glyoxal oxidase, in extracellular H2O2
RT production by Phanerochaete chrysosporium.";
RL J. Bacteriol. 169:2195-2201(1987).
RN [4]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=8557673; DOI=10.1074/jbc.271.2.681;
RA Whittaker M.M., Kersten P.J., Nakamura N., Sanders-Loehr J.,
RA Schweizer E.S., Whittaker J.W.;
RT "Glyoxal oxidase from Phanerochaete chrysosporium is a new radical-copper
RT oxidase.";
RL J. Biol. Chem. 271:681-687(1996).
CC -!- FUNCTION: Catalyzes the oxidation of aldehydes to the corresponding
CC carboxylic acids by coupling the reaction to the reduction of dioxygen
CC to hydrogen peroxide. Substrates include, methylglyoxal,
CC glycolaldehyde, acetaldehyde, formaldehyde and glyoxal. May act as a
CC source of extracellular hydrogen peroxide required for the oxidation
CC reactions catalyzed by the lignin peroxidases (ligninases) and
CC manganese peroxidases, both involved in lignin degradation.
CC {ECO:0000269|PubMed:3553159, ECO:0000269|PubMed:8557673}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glyoxal + H2O + O2 = glyoxylate + H(+) + H2O2;
CC Xref=Rhea:RHEA:33439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:34779,
CC ChEBI:CHEBI:36655; EC=1.2.3.15; Evidence={ECO:0000269|PubMed:3553159,
CC ECO:0000269|PubMed:8557673};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33440;
CC Evidence={ECO:0000269|PubMed:3553159, ECO:0000269|PubMed:8557673};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + methylglyoxal + O2 = H(+) + H2O2 + pyruvate;
CC Xref=Rhea:RHEA:49636, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:17158; EC=1.2.3.15; Evidence={ECO:0000269|PubMed:3553159,
CC ECO:0000269|PubMed:8557673};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49637;
CC Evidence={ECO:0000269|PubMed:3553159, ECO:0000269|PubMed:8557673};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6.0. {ECO:0000269|PubMed:3553159};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:7592374}.
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DR EMBL; L18991; AAA33747.1; -; mRNA.
DR EMBL; L47286; AAA87594.1; -; Genomic_DNA.
DR EMBL; L47287; AAA87595.1; -; Genomic_DNA.
DR PIR; A48296; A48296.
DR AlphaFoldDB; Q01772; -.
DR SMR; Q01772; -.
DR CLAE; GLX5A_PHACH; -.
DR KEGG; ag:AAA33747; -.
DR VEuPathDB; FungiDB:AGR57_6705; -.
DR OMA; AWCSSGA; -.
DR BRENDA; 1.2.3.15; 1380.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0004031; F:aldehyde oxidase activity; IDA:UniProtKB.
DR GO; GO:0050665; P:hydrogen peroxide biosynthetic process; IDA:UniProtKB.
DR CDD; cd02851; E_set_GO_C; 1.
DR Gene3D; 2.130.10.80; -; 1.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR011043; Gal_Oxase/kelch_b-propeller.
DR InterPro; IPR037293; Gal_Oxidase_central_sf.
DR InterPro; IPR009880; Glyoxal_oxidase_N.
DR InterPro; IPR015202; GO-like_E_set.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR Pfam; PF09118; DUF1929; 1.
DR Pfam; PF07250; Glyoxal_oxid_N; 1.
DR SUPFAM; SSF50965; SSF50965; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Oxidoreductase; Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..559
FT /note="Aldehyde oxidase GLOX"
FT /evidence="ECO:0000255"
FT /id="PRO_5004162176"
FT CARBOHYD 33
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 46
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 100
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 231
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT VARIANT 308
FT /note="K -> T (in allele GLX-2)"
FT /evidence="ECO:0000269|PubMed:7592374"
SQ SEQUENCE 559 AA; 59168 MW; 9245FA19E19B8E65 CRC64;
MLSLLAVVSL AAATLAAPAA SDAPGWRFDL KPNLSGIVAL EAIVVNSSLV VIFDRATGDQ
PLKINGESTW GALWDLDTST VRPLSVLTDS FCASGALLSN GTMVSMGGTP GGTGGDVAAP
PGNQAIRIFE PCASPSGDGC TLFEDPATVH LLEERWYPSS VRIFDGSLMI IGGSHVLTPF
YNVDPANSFE FFPSKEQTPR PSAFLERSLP ANLFPRAFAL PDGTVFIVAN NQSIIYDIEK
NTETILPDIP NGVRVTNPID GSAILLPLSP PDFIPEVLVC GGSTADTSLP STSLSSQHPA
TSQCSRIKLT PEGIKAGWQV EHMLEARMMP ELVHVPNGQI LITNGAGTGF AALSAVADPV
GNSNADHPVL TPSLYTPDAP LGKRISNAGM PTTTIPRMYH STVTLTQQGN FFIGGNNPNM
NFTPPGTPGI KFPSELRIET LDPPFMFRSR PALLTMPEKL KFGQKVTVPI TIPSDLKASK
VQVALMDLGF SSHAFHSSAR LVFMESSISA DRKSLTFTAP PNGRVFPPGP AVVFLTIDDV
TSPGERVMMG SGNPPPTLE
