HOX_CHOCR
ID HOX_CHOCR Reviewed; 546 AA.
AC P93762; S0F2V9;
DT 01-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2014, sequence version 2.
DT 25-MAY-2022, entry version 77.
DE RecName: Full=Hexose oxidase;
DE Short=HOx;
DE EC=1.1.3.5 {ECO:0000269|PubMed:9111074};
DE Contains:
DE RecName: Full=Hexose oxidase, 40 kDa form;
DE Contains:
DE RecName: Full=Hexose oxidase, 29 kDa form;
GN Name=HOX; ORFNames=CHC_T00009130001;
OS Chondrus crispus (Carrageen Irish moss) (Polymorpha crispa).
OC Eukaryota; Rhodophyta; Florideophyceae; Rhodymeniophycidae; Gigartinales;
OC Gigartinaceae; Chondrus.
OX NCBI_TaxID=2769;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 8-22; 92-114; 189-202;
RP 215-234; 338-342; 388-397; 434-444 AND 452-468, FUNCTION, CATALYTIC
RP ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND PROTEOLYTIC
RP PROCESSING.
RX PubMed=9111074; DOI=10.1074/jbc.272.17.11581;
RA Hansen O.C., Stougaard P.;
RT "Hexose oxidase from the red alga Chondrus crispus. Purification, molecular
RT cloning, and expression in Pichia pastoris.";
RL J. Biol. Chem. 272:11581-11587(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Stackhouse;
RX PubMed=23503846; DOI=10.1073/pnas.1221259110;
RA Collen J., Porcel B., Carre W., Ball S.G., Chaparro C., Tonon T.,
RA Barbeyron T., Michel G., Noel B., Valentin K., Elias M., Artiguenave F.,
RA Arun A., Aury J.M., Barbosa-Neto J.F., Bothwell J.H., Bouget F.Y.,
RA Brillet L., Cabello-Hurtado F., Capella-Gutierrez S., Charrier B.,
RA Cladiere L., Cock J.M., Coelho S.M., Colleoni C., Czjzek M., Da Silva C.,
RA Delage L., Denoeud F., Deschamps P., Dittami S.M., Gabaldon T.,
RA Gachon C.M., Groisillier A., Herve C., Jabbari K., Katinka M., Kloareg B.,
RA Kowalczyk N., Labadie K., Leblanc C., Lopez P.J., McLachlan D.H.,
RA Meslet-Cladiere L., Moustafa A., Nehr Z., Nyvall Collen P., Panaud O.,
RA Partensky F., Poulain J., Rensing S.A., Rousvoal S., Samson G.,
RA Symeonidi A., Weissenbach J., Zambounis A., Wincker P., Boyen C.;
RT "Genome structure and metabolic features in the red seaweed Chondrus
RT crispus shed light on evolution of the Archaeplastida.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:5247-5252(2013).
RN [3]
RP PROTEIN SEQUENCE OF 4-13 AND 338-349, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP GLYCOSYLATION.
RX PubMed=11427234; DOI=10.1016/s0141-0229(01)00351-9;
RA Savary B.J., Hicks K.B., O'Connor J.V.;
RT "Hexose oxidase from Chondrus crispus: improved purification using
RT perfusion chromatography.";
RL Enzyme Microb. Technol. 29:42-51(2001).
RN [4]
RP PROTEIN SEQUENCE OF 74-91 AND 132-157, FUNCTION, COFACTOR, FAD-BINDING, AND
RP MUTAGENESIS OF HIS-79.
RX PubMed=16817897; DOI=10.1111/j.1742-4658.2006.05285.x;
RA Rand T., Qvist K.B., Walter C.P., Poulsen C.H.;
RT "Characterization of the flavin association in hexose oxidase from Chondrus
RT crispus.";
RL FEBS J. 273:2693-2703(2006).
RN [5]
RP IDENTIFICATION.
RX PubMed=4708670; DOI=10.1016/0005-2744(73)90312-4;
RA Sullivan J.D. Jr., Ikawa M.;
RT "Purification and characterization of hexose oxidase from the red alga
RT Chondrus crispus.";
RL Biochim. Biophys. Acta 309:11-22(1973).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP GLYCOSYLATION.
RX PubMed=9108257; DOI=10.1111/j.1432-1033.1997.00858.x;
RA Groen B.W., De Vries S., Duine J.A.;
RT "Characterization of hexose oxidase from the red seaweed Chondrus
RT crispus.";
RL Eur. J. Biochem. 244:858-861(1997).
RN [7]
RP COFACTOR, AND POST-TRANSLATIONAL MODIFICATION.
RX PubMed=11437594; DOI=10.1006/prep.2001.1439;
RA Wolff A.M., Hansen O.C., Poulsen U., Madrid S., Stougaard P.;
RT "Optimization of the production of Chondrus crispus hexose oxidase in
RT Pichia pastoris.";
RL Protein Expr. Purif. 22:189-199(2001).
RN [8]
RP IDENTIFICATION.
RX PubMed=24826896; DOI=10.1371/journal.pone.0097250;
RA Shearer A.G., Altman T., Rhee C.D.;
RT "Finding sequences for over 270 orphan enzymes.";
RL PLoS ONE 9:E97250-E97250(2014).
CC -!- FUNCTION: Catalyzes the selective oxidation of C1 hydroxyl moieties on
CC mono- and disaccharides with concomitant reduction of molecular oxygen
CC to hydrogen peroxide. This results in the formation of the
CC corresponding lactones, which typically undergo spontaneous hydrolysis.
CC Hexose oxidase is able to oxidize a variety of substrates including D-
CC glucose, D-galactose, maltose, cellobiose, and lactose.
CC {ECO:0000269|PubMed:16817897, ECO:0000269|PubMed:9111074}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-D-glucose + O2 = D-glucono-1,5-lactone + H2O2;
CC Xref=Rhea:RHEA:11428, ChEBI:CHEBI:15379, ChEBI:CHEBI:15903,
CC ChEBI:CHEBI:16217, ChEBI:CHEBI:16240; EC=1.1.3.5;
CC Evidence={ECO:0000269|PubMed:9111074};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-galactose + O2 = D-galactono-1,5-lactone + H2O2;
CC Xref=Rhea:RHEA:59312, ChEBI:CHEBI:4139, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:15945, ChEBI:CHEBI:16240; EC=1.1.3.5;
CC Evidence={ECO:0000269|PubMed:9111074};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-maltose + O2 = D-maltobiono-1,5-lactone + H2O2;
CC Xref=Rhea:RHEA:59344, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:17306, ChEBI:CHEBI:143029; EC=1.1.3.5;
CC Evidence={ECO:0000269|PubMed:9111074};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-cellobiose + O2 = D-cellobiono-1,5-lactone + H2O2;
CC Xref=Rhea:RHEA:59316, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:17057, ChEBI:CHEBI:17863; EC=1.1.3.5;
CC Evidence={ECO:0000269|PubMed:9111074};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-lactose + O2 = H2O2 + lactobiono-1,5-lactone;
CC Xref=Rhea:RHEA:59352, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:36218, ChEBI:CHEBI:143068; EC=1.1.3.5;
CC Evidence={ECO:0000269|PubMed:9111074};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:11437594, ECO:0000269|PubMed:16817897};
CC Note=Binds 1 FAD per subunit in a bicovalent manner.
CC {ECO:0000269|PubMed:16817897};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.3 mM for oxygen (at pH 5.8 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:9108257};
CC KM=2.7 mM for D-glucose (at pH 6.3 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:9111074};
CC KM=3.8 mM for D-galactose (at pH 6.3 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:9111074};
CC KM=8.5 mM for glucose (at pH 5.8 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:9108257};
CC KM=1.7 mM for lactose (at pH 5.8 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:9108257};
CC KM=20 mM for galactose (at pH 5.8 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:9108257};
CC KM=12.5 mM for cellobiose (at pH 5.8 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:9108257};
CC KM=28 mM for maltose (at pH 5.8 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:9108257};
CC KM=2.5 mM for glucose (at pH 6 and 26 degrees Celsius)
CC {ECO:0000269|PubMed:11427234};
CC KM=97 mM for lactose (at pH 6 and 26 degrees Celsius)
CC {ECO:0000269|PubMed:11427234};
CC KM=3.2 mM for galactose (at pH 6 and 26 degrees Celsius)
CC {ECO:0000269|PubMed:11427234};
CC KM=27 mM for cellobiose (at pH 6 and 26 degrees Celsius)
CC {ECO:0000269|PubMed:11427234};
CC KM=50 mM for maltose (at pH 6 and 26 degrees Celsius)
CC {ECO:0000269|PubMed:11427234};
CC pH dependence:
CC Optimum pH is 6 (PubMed:9108257, PubMed:11427234). A second pH
CC optimum was found at pH 10 (PubMed:9108257, PubMed:11427234).
CC {ECO:0000269|PubMed:11427234, ECO:0000269|PubMed:9108257};
CC -!- SUBUNIT: Homodimer. {ECO:0000305|PubMed:9111074}.
CC -!- PTM: Cleaved into 40 kDa and 29 kDa cleavage products, but the 2
CC polypeptide chains do not separate and seem to be physically linked
CC together. {ECO:0000269|PubMed:11437594, ECO:0000269|PubMed:9111074}.
CC -!- PTM: The FAD cofactor is bound via a bicovalent 6-S-cysteinyl, 8alpha-
CC N1-histidyl FAD linkage. {ECO:0000250|UniProtKB:Q6PW77}.
CC -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC family. {ECO:0000305}.
CC -!- CAUTION: Was initially reported to use Cu(2+) as a cofactor
CC (PubMed:4708670). However, cofactor composition could not be confirmed
CC later (PubMed:9108257), and the discrepancies in the reported
CC characteristics of the enzyme were suggested to originate from the
CC characterization of a contaminating protein in PubMed:4708670.
CC {ECO:0000305|PubMed:4708670, ECO:0000305|PubMed:9108257}.
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DR EMBL; U89770; AAB49376.1; -; mRNA.
DR EMBL; HG001523; CDF77476.1; -; Genomic_DNA.
DR RefSeq; XP_005712350.1; XM_005712293.1.
DR AlphaFoldDB; P93762; -.
DR SMR; P93762; -.
DR STRING; 2769.P93762; -.
DR EnsemblPlants; CDF77476; CDF77476; CHC_T00009130001.
DR GeneID; 17320065; -.
DR Gramene; CDF77476; CDF77476; CHC_T00009130001.
DR KEGG; ccp:CHC_T00009130001; -.
DR OMA; YSYWFEN; -.
DR OrthoDB; 1049549at2759; -.
DR Proteomes; UP000012073; Unassembled WGS sequence.
DR GO; GO:0005507; F:copper ion binding; IDA:UniProtKB.
DR GO; GO:0071949; F:FAD binding; IDA:UniProtKB.
DR GO; GO:0046562; F:glucose oxidase activity; IEA:RHEA.
DR GO; GO:0047979; F:hexose oxidase activity; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR Gene3D; 3.30.465.10; -; 1.
DR InterPro; IPR012951; BBE.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR Pfam; PF08031; BBE; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR SUPFAM; SSF56176; SSF56176; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; FAD; Flavoprotein; Glycoprotein; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..546
FT /note="Hexose oxidase"
FT /id="PRO_0000430460"
FT CHAIN 4..337
FT /note="Hexose oxidase, 40 kDa form"
FT /evidence="ECO:0000305|PubMed:11427234"
FT /id="PRO_0000430461"
FT CHAIN 338..546
FT /note="Hexose oxidase, 29 kDa form"
FT /evidence="ECO:0000305|PubMed:11427234,
FT ECO:0000305|PubMed:9111074"
FT /id="PRO_0000430462"
FT DOMAIN 40..222
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT CARBOHYD 95
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 358
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CROSSLNK 79..138
FT /note="6-(S-cysteinyl)-8alpha-(pros-histidyl)-FAD (His-
FT Cys)"
FT /evidence="ECO:0000305|PubMed:16817897"
FT MUTAGEN 79
FT /note="H->K: Loss of activity due to the absence of FAD
FT cofactor."
FT /evidence="ECO:0000269|PubMed:16817897"
FT CONFLICT 4
FT /note="L -> K (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 12..13
FT /note="IV -> AI (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 193
FT /note="D -> N (in Ref. 1; AAB49376/AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 196
FT /note="D -> E (in Ref. 1; AAB49376/AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 339..340
FT /note="Missing (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 341
FT /note="I -> M (in Ref. 1; AAB49376/AA sequence and 3; AA
FT sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 345
FT /note="T -> R (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 380
FT /note="L -> F (in Ref. 1; AAB49376)"
FT /evidence="ECO:0000305"
FT CONFLICT 417
FT /note="N -> K (in Ref. 1; AAB49376)"
FT /evidence="ECO:0000305"
FT CONFLICT 419
FT /note="A -> V (in Ref. 1; AAB49376)"
FT /evidence="ECO:0000305"
FT CONFLICT 429
FT /note="K -> E (in Ref. 1; AAB49376)"
FT /evidence="ECO:0000305"
FT CONFLICT 520
FT /note="K -> W (in Ref. 1; AAB49376)"
FT /evidence="ECO:0000305"
FT CONFLICT 538
FT /note="S -> P (in Ref. 1; AAB49376)"
FT /evidence="ECO:0000305"
FT CONFLICT 542
FT /note="Y -> P (in Ref. 1; AAB49376)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 546 AA; 61789 MW; 60091F260819853A CRC64;
MATLPQKDPG YIVIDVNAGT PDKPDPRLPS MKQGFNRRWI GTNIDFVYVV YTPQGACTAL
DRAMEKCSPG TVRIVSGGHC YEDFVFDECV KAIINVTGLV ESGYDDDRGY FVSSGDTNWG
SFKTLFRDHG RVLPGGSCYS VGLGGHIVGG GDGILARLHG LPVDWLSGVE VVVKPVLTED
SVLKYVHKDS EGDDGDLFWA HTGGGGGNFG IITKYYFKDL PMSPRGVIAS NLHFSWDGFT
RDALQDLLTK YFKLARCDWK NTVGKFQIFH QAAEEFVMYL YTSYSNDAER EVAQDRHYHL
EADIEQIYKT CEPTKALGGH AGWAPFPVRP RKRHTSKTSY IHDETMDYPF YALTETINGS
GPNQRGKYKS AYMIKDFPDL QIDVIWKYLT EVPDGLTSAE MKDALLQVDM FGGEIHNVAW
DATAVAQRKY IIKLQYQTYW QEEDKDAVNL KWIRDFYEEM YEPYGGVPDP NTQVESGKGV
FEGCYFNYPD VDLNNWKNGK YGALELYFLG NLNRLIKAKK LWDPNEIFTN KQSIPTKSLK
EYKQTK
