GenomeNet

Database: UniProt
Entry: I4EXQ4_9ACTN
LinkDB: I4EXQ4_9ACTN
Original site: I4EXQ4_9ACTN 
ID   I4EXQ4_9ACTN            Unreviewed;       529 AA.
AC   I4EXQ4;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   SubName: Full=Pyranose oxidase {ECO:0000313|EMBL:CCH88167.1};
DE            EC=1.1.3.10 {ECO:0000313|EMBL:CCH88167.1};
GN   OrderedLocusNames=MODMU_2738 {ECO:0000313|EMBL:CCH88167.1};
OS   Modestobacter marinus.
OC   Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC   Geodermatophilaceae; Modestobacter.
OX   NCBI_TaxID=477641 {ECO:0000313|EMBL:CCH88167.1, ECO:0000313|Proteomes:UP000006461};
RN   [1] {ECO:0000313|EMBL:CCH88167.1, ECO:0000313|Proteomes:UP000006461}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BC501 {ECO:0000313|EMBL:CCH88167.1,
RC   ECO:0000313|Proteomes:UP000006461};
RX   PubMed=22887672; DOI=10.1128/JB.01029-12;
RA   Normand P., Gury J., Pujic P., Chouaia B., Crotti E., Brusetti L.,
RA   Daffonchio D., Vacherie B., Barbe V., Medigue C., Calteau A.,
RA   Ghodhbane-Gtari F., Essoussi I., Nouioui I., Abbassi-Ghozzi I., Gtari M.;
RT   "Genome Sequence of Radiation-Resistant Modestobacter marinus Strain BC501,
RT   a Representative Actinobacterium That Thrives on Calcareous Stone
RT   Surfaces.";
RL   J. Bacteriol. 194:4773-4774(2012).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC       {ECO:0000256|ARBA:ARBA00010790}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; FO203431; CCH88167.1; -; Genomic_DNA.
DR   AlphaFoldDB; I4EXQ4; -.
DR   STRING; 477641.MODMU_2738; -.
DR   KEGG; mmar:MODMU_2738; -.
DR   PATRIC; fig|477641.3.peg.2595; -.
DR   eggNOG; COG2303; Bacteria.
DR   HOGENOM; CLU_023699_0_0_11; -.
DR   OrthoDB; 9798604at2; -.
DR   Proteomes; UP000006461; Chromosome.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0050233; F:pyranose oxidase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR000172; GMC_OxRdtase_N.
DR   InterPro; IPR007867; GMC_OxRtase_C.
DR   PANTHER; PTHR42784; PYRANOSE 2-OXIDASE; 1.
DR   PANTHER; PTHR42784:SF1; PYRANOSE 2-OXIDASE; 1.
DR   Pfam; PF05199; GMC_oxred_C; 1.
DR   Pfam; PF00732; GMC_oxred_N; 1.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000313|EMBL:CCH88167.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006461}.
FT   DOMAIN          223..300
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00732"
FT   DOMAIN          385..500
FT                   /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05199"
SQ   SEQUENCE   529 AA;  56239 MW;  1F30F5E8756BAD5C CRC64;
     MRGSEMSRSF PPAVDVAIVG SGPNGAAYAR VLSERAPGAT IAVFEVGPAL TDPPGLHVKN
     IADLDERLVA QRRSEGLRPH TATKEEAAYT DPTKRVVRAG THLLPDGFQQ PGEDGIPALA
     MSSNVGGMGA HWTCACPRPG DAERPDFLPD LDELLDDAER LLGVSRDPFG SAPYSDVVRE
     RLGAEFDPGR RAERRVRSMP LAVHVRDDGA LVWSGADVVF GEETRANPAA TLFPEAQVRR
     VLVEDGRAVG VVVHDRRDGS DHEVRARFVV VAADALRTPQ LLFASGVRPP ALGRYLNDQP
     QMVFAVRLRD VARTPEAEHD PRGDTAIVQQ SGVSWVPYTD EDPFHGQVMQ LDASPVPIVG
     DDVPAPGTVV GLGWFCGKDL QASDRVEFDD TATDDYGMPK PRIHYTLTGQ DRETFARARD
     SIRRAAAALG DPLGDEPFVL PSGASLHYQG TTRMGAVDDG TSVCGPTSEV WGVAGLYVAG
     NNVIPTPMAC NPTLTSVALA IGGARDIADR LTADPSAVSA ESGGHAVPA
//
DBGET integrated database retrieval system