GMCH_MALSM
ID GMCH_MALSM Reviewed; 618 AA.
AC Q5GMY3;
DT 22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 2.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=GMC oxidoreductase family protein Mala s 12.0101 {ECO:0000305};
DE EC=1.-.-.- {ECO:0000305};
DE AltName: Allergen=Mala s 12.0101 {ECO:0000305};
DE Flags: Precursor;
OS Malassezia sympodialis (Atopic eczema-associated yeast).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Malasseziomycetes; Malasseziales; Malasseziaceae; Malassezia.
OX NCBI_TaxID=76777 {ECO:0000312|EMBL:CAI43283.4};
RN [1] {ECO:0000312|EMBL:CAI43283.4}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, COFACTOR, SUBUNIT, AND ALLERGEN.
RX PubMed=17313403; DOI=10.1111/j.1398-9995.2006.01291.x;
RA Zargari A., Selander C., Rasool O., Ghanem M., Gadda G., Crameri R.,
RA Scheynius A.;
RT "Mala s 12 is a major allergen in patients with atopic eczema and has
RT sequence similarities to the GMC oxidoreductase family.";
RL Allergy 62:695-703(2007).
CC -!- FUNCTION: The recombinant protein is not active with choline, glucose,
CC myo-inositol, methanol, ethanol, 1-pentanol, benzyl alcohol, 2-
CC phenylethanol, cholesterol or lauryl alcohol as substrates. Binds
CC membrane lipids including phosphatidylinositol (PtdIns)(4)-phosphate
CC (P), PtdIns(4,5)P2, phosphatidic acid (PA), and to a lower extent
CC PtdIns(3,4,5)P3, cardiolipin and 3-sulfogalactosyl ceramide
CC (sulfatide). {ECO:0000269|PubMed:17313403}.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000255|PIRSR:PIRSR000137-2,
CC ECO:0000269|PubMed:17313403};
CC Note=Binds 1 FAD per subunit. {ECO:0000269|PubMed:17313403};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:17313403}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:M5EAX2}.
CC -!- ALLERGEN: Causes an allergic reaction in human. Recombinant protein
CC binds to IgE in 62% of the 21 atopic eczema patients tested allergic to
CC M.sympodialis. {ECO:0000269|PubMed:17313403}.
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC {ECO:0000255|RuleBase:RU003968}.
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DR EMBL; AJ871960; CAI43283.4; -; mRNA.
DR AlphaFoldDB; Q5GMY3; -.
DR SMR; Q5GMY3; -.
DR Allergome; 2530; Mala s 12.
DR Allergome; 3367; Mala s 12.0101.
DR VEuPathDB; FungiDB:MSYG_3072; -.
DR OMA; DEDWIAW; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
DR Gene3D; 3.50.50.60; -; 1.
DR Gene3D; 4.10.450.10; -; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR027424; Glucose_Oxidase_domain_2.
DR InterPro; IPR012132; GMC_OxRdtase.
DR InterPro; IPR000172; GMC_OxRdtase_N.
DR InterPro; IPR007867; GMC_OxRtase_C.
DR PANTHER; PTHR11552; PTHR11552; 1.
DR Pfam; PF05199; GMC_oxred_C; 1.
DR Pfam; PF00732; GMC_oxred_N; 1.
DR PIRSF; PIRSF000137; Alcohol_oxidase; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR PROSITE; PS00623; GMC_OXRED_1; 1.
DR PROSITE; PS00624; GMC_OXRED_2; 1.
PE 1: Evidence at protein level;
KW Allergen; FAD; Flavoprotein; Lipid-binding; Oxidoreductase; Secreted;
KW Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..618
FT /note="GMC oxidoreductase family protein Mala s 12.0101"
FT /evidence="ECO:0000255"
FT /id="PRO_5004256853"
FT ACT_SITE 556
FT /note="Proton donor"
FT /evidence="ECO:0000255|PIRSR:PIRSR000137-1"
FT ACT_SITE 599
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PIRSR:PIRSR000137-1"
FT BINDING 129
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|PIRSR:PIRSR000137-2"
FT BINDING 280
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|PIRSR:PIRSR000137-2"
SQ SEQUENCE 618 AA; 66277 MW; 063AFC9322F9E324 CRC64;
MKGIVSWAVV SAALVLSATE SLAFANVSSF EKRTTTGNGW DLDGKSYDYV IVGGGTAGLV
LANRLSANQG TTVAVIEAGN SGYDDNDKFV VPDANLYNSA VNTQYDWQFH TSSQKHMNNR
RASWPRGKVL GGSSAVNGLY YVRPSETEVN VWSKLAGGSG RWSWNSLLSG MKKSEHFRGP
VKSVQNQLQI QYNAGSHGSN GPIGTTWPAV TYDPVERFIK TADSMSGAIN NDPYNGNNHG
TYVALSSIDK TNWQRSFSRN GYLDPISKRS NLHVLTGHTV TGIIFDRSGK NAQATGVHYA
ASSNEASHTV HANKEVIISG GAINSPQILQ LSGIGDKNLL NGLGIDVVVD LPGVGENLQD
HVSAGMSFKP KNKKDAGPTS VTGDAKADSY VNSAVSYTSL GKLFNNKDSI LGKIQARAKQ
IADSHNVSPA VKQGQSKAYN ALADTIFPSK VSPVEILGNV MFGSISIQAA LQHPLSRGSI
KITSKDPFAY PKINPNYFAE NLDLVLLREG FKLIREMSQQ SPLKDVIDFE TVPGDKVQTN
EDWENWIRSA AGTEYHPSST CAMLPRGDGG VVDENLKVYG TSNLRVVDAS VTPIAMSCHL
ESVVYGLAEV AADIILGN