HEXNO_RALSU
ID HEXNO_RALSU Reviewed; 508 AA.
AC A3RXB7;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 1.
DT 03-AUG-2022, entry version 45.
DE RecName: Full=N-acetyl-D-hexosamine oxidase {ECO:0000303|PubMed:34709726};
DE Short=HexNAcO {ECO:0000303|PubMed:34709726};
DE EC=1.1.3.29 {ECO:0000269|PubMed:34709726};
GN ORFNames=RRSL_02030 {ECO:0000312|EMBL:EAP71857.1};
OS Ralstonia solanacearum (strain UW551).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Ralstonia.
OX NCBI_TaxID=342110;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UW551;
RX PubMed=16404955; DOI=10.1094/mpmi-19-0069;
RA Gabriel D.W., Allen C., Schell M., Denny T.P., Greenberg J.T., Duan Y.P.,
RA Flores-Cruz Z., Huang Q., Clifford J.M., Presting G., Gonzalez E.T.,
RA Reddy J., Elphinstone J., Swanson J., Yao J., Mulholland V., Liu L.,
RA Farmerie W., Patnaikuni M., Balogh B., Norman D., Alvarez A.,
RA Castillo J.A., Jones J., Saddler G., Walunas T., Zhukov A., Mikhailova N.;
RT "Identification of open reading frames unique to a select agent: Ralstonia
RT solanacearum race 3 biovar 2.";
RL Mol. Plant Microbe Interact. 19:69-79(2006).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR,
RP SUBSTRATE SPECIFICITY, AND 3D-STRUCTURE MODELING.
RX PubMed=34709726; DOI=10.1002/cbic.202100510;
RA Rembeza E., Boverio A., Fraaije M.W., Engqvist M.;
RT "Discovery of two novel oxidases using a high-throughput activity screen.";
RL ChemBioChem 0:0-0(2021).
CC -!- FUNCTION: Catalyzes the oxidation of a range of monosaccharides in
CC vitro, displaying the highest activity with N-acetylglucosamine
CC (GlcNAc) and N-acetylgalactosamine (GalNAc), with a reduction of O2 to
CC H2O2. Acts upon the C1 carbon of the GlcNAc or GalNAc molecule,
CC producing the corresponding lactone, which can spontaneously hydrolyze.
CC Its biological function is unclear, but its main function might be
CC connected to extracellular production of hydrogen peroxide to compete
CC with other organisms through oxidative stress, or support the action of
CC peroxidases and peroxygenases. {ECO:0000269|PubMed:34709726}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-acetyl-D-glucosamine + O2 = H(+) + H2O2 + N-acetyl-D-
CC glucosaminate; Xref=Rhea:RHEA:13029, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:38439, ChEBI:CHEBI:506227; EC=1.1.3.29;
CC Evidence={ECO:0000269|PubMed:34709726};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-acetyl-D-galactosamine + O2 = H(+) + H2O2 + N-acetyl-
CC D-galactosaminate; Xref=Rhea:RHEA:69512, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:28037, ChEBI:CHEBI:28655; EC=1.1.3.29;
CC Evidence={ECO:0000269|PubMed:34709726};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N-acetyl-D-glucosamine + O2 = H2O2 + N-acetyl-D-glucosamino-
CC 1,5-lactone; Xref=Rhea:RHEA:69504, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:42870, ChEBI:CHEBI:506227;
CC Evidence={ECO:0000269|PubMed:34709726};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N-acetyl-D-galactosamine + O2 = H2O2 + N-acetyl-D-
CC galactosamino-1,5-lactone; Xref=Rhea:RHEA:69516, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:28037, ChEBI:CHEBI:184299;
CC Evidence={ECO:0000269|PubMed:34709726};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:34709726};
CC Note=Binds 1 FAD per subunit in a bicovalent manner.
CC {ECO:0000250|UniProtKB:P93762};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.26 mM for N-acetyl-D-glucosamine {ECO:0000269|PubMed:34709726};
CC KM=0.32 mM for N-acetyl-D-galactosamine
CC {ECO:0000269|PubMed:34709726};
CC KM=182 mM for N-acetyl-D-mannosamine {ECO:0000269|PubMed:34709726};
CC KM=18.70 mM for diacetylchitobiose {ECO:0000269|PubMed:34709726};
CC KM=4.54 mM for D-glucosamine {ECO:0000269|PubMed:34709726};
CC KM=1.35 mM for D-galactosamine {ECO:0000269|PubMed:34709726};
CC KM=65.70 mM for D-mannosamine {ECO:0000269|PubMed:34709726};
CC KM=216 mM for D-glucose {ECO:0000269|PubMed:34709726};
CC KM=102 mM for D-galactose {ECO:0000269|PubMed:34709726};
CC KM=118 mM for D-mannose {ECO:0000269|PubMed:34709726};
CC Note=kcat is 5.67 sec(-1) with N-acetyl-D-glucosamine as substrate.
CC kcat is 4.46 sec(-1) with N-acetyl-D-glucosamine as substrate. kcat
CC is 2.23 sec(-1) with N-acetyl-D-mannosamine as substrate. kcat is
CC 0.84 sec(-1) with diacetylchitobiose as substrate. kcat is 0.35 sec(-
CC 1) with D-glucosamine as substrate. kcat is 0.62 sec(-1) with D-
CC galactosamine as substrate. kcat is 0.011 sec(-1) with D-mannosamine
CC as substrate. kcat is 0.16 sec(-1) with D-glucose as substrate. kcat
CC is 0.19 sec(-1) with D-galactose as substrate. kcat is 0.14 sec(-1)
CC with D-mannose as substrate. {ECO:0000269|PubMed:34709726};
CC pH dependence:
CC Optimum pH is 7.5. {ECO:0000269|PubMed:34709726};
CC -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC family. {ECO:0000305}.
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DR EMBL; AAKL01000041; EAP71857.1; -; Genomic_DNA.
DR RefSeq; WP_003264718.1; NZ_AAKL01000041.1.
DR EnsemblBacteria; EAP71857; EAP71857; RRSL_02030.
DR PATRIC; fig|342110.8.peg.2091; -.
DR Proteomes; UP000005933; Unassembled WGS sequence.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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 FAD; Flavoprotein; Oxidoreductase; Thioether bond.
FT CHAIN 1..508
FT /note="N-acetyl-D-hexosamine oxidase"
FT /id="PRO_0000455049"
FT DOMAIN 26..203
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT CROSSLNK 64..123
FT /note="6-(S-cysteinyl)-8alpha-(pros-histidyl)-FAD (His-
FT Cys)"
FT /evidence="ECO:0000250|UniProtKB:P93762"
SQ SEQUENCE 508 AA; 56364 MW; 64D76AAEA6E57F57 CRC64;
MTLDVSRQDP RYNTLKHGFN LRWPSTDAQA AGRIALCEKA DDVAPALQHI IDTGMRPTVR
SGGHCYEDFV SNNPDGAIVD LSLLNAPEVR ADGTVRIPAG TQNWNGYLEL YKRHNLTLPG
GSCYSVGAGG HICGGGYGLL SRLQGLTVDW LSAVDIVTVD RQGRAAPRTV DATRDPELFR
ACRGAGGGNF GIITAYTFAR LPEAPREVAL ATVAFDWAAM TPERFAELLR LYGEYWETRG
KDPDTWGMFS LLKLTHRSAG QIVMLTQFCN PDGTCRDLSV LNDFLARFRA CAPVPLKGRP
PGYGPAHRQG VGQLLCSKPH TVVRYDWLTA TQTVNGSGPN QRGKYKSAYM KRGFTAREAQ
RIYTHLTRTV PGIDLSQSLL QVDSYGGAVN KTERIADTAV PQRASVMKLQ YQTYWTSAAD
DAGHLRWIGD FYRDVYGTPD VSAPHAGTPY PGDRYEGCYI NYPDVDMLAY PFWPQLYYGD
GDLYAFLQRV KRRYDPNNIF HHAMSVRP
