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Database: UniProt
Entry: A0A2N0Z7X4_9BACI
LinkDB: A0A2N0Z7X4_9BACI
Original site: A0A2N0Z7X4_9BACI 
ID   A0A2N0Z7X4_9BACI        Unreviewed;       567 AA.
AC   A0A2N0Z7X4;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=GMC family oxidoreductase {ECO:0000313|EMBL:PKG25607.1};
GN   ORFNames=CWS01_01825 {ECO:0000313|EMBL:PKG25607.1};
OS   Niallia nealsonii.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Niallia.
OX   NCBI_TaxID=115979 {ECO:0000313|EMBL:PKG25607.1, ECO:0000313|Proteomes:UP000233375};
RN   [1] {ECO:0000313|EMBL:PKG25607.1, ECO:0000313|Proteomes:UP000233375}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FO-92 {ECO:0000313|EMBL:PKG25607.1,
RC   ECO:0000313|Proteomes:UP000233375};
RX   PubMed=12656168; DOI=10.1099/ijs.0.02311-0;
RA   Venkateswaran K., Kempf M., Chen F., Satomi M., Nicholson W., Kern R.;
RT   "Bacillus nealsonii sp. nov., isolated from a spacecraft-assembly facility,
RT   whose spores are gamma-radiation resistant.";
RL   Int. J. Syst. Evol. Microbiol. 53:165-172(2003).
CC   -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC       {ECO:0000256|ARBA:ARBA00010790}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PKG25607.1}.
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DR   EMBL; PISE01000003; PKG25607.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2N0Z7X4; -.
DR   OrthoDB; 9787779at2; -.
DR   Proteomes; UP000233375; Unassembled WGS sequence.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
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; PTHR46056; LONG-CHAIN-ALCOHOL OXIDASE; 1.
DR   PANTHER; PTHR46056:SF4; LONG-CHAIN-ALCOHOL OXIDASE; 1.
DR   Pfam; PF05199; GMC_oxred_C; 1.
DR   Pfam; PF00732; GMC_oxred_N; 1.
DR   PRINTS; PR00420; RNGMNOXGNASE.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000233375}.
FT   DOMAIN          220..334
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00732"
FT   DOMAIN          443..556
FT                   /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05199"
SQ   SEQUENCE   567 AA;  62854 MW;  86E73D3CB003B9D2 CRC64;
     MENQDVIVIG AGGGGAVIAK ELGEKGLKVL VLEAGPWYGN KKWPIPNGEP GDQFSSSTAD
     LDINLYKQLL NKYEMNMNDL VSGRFRWGPA DRSRAQWFRN IKQKAMIWQC AGVGGTTQIY
     TANCPRAYPM AINDRWPLSY RELIPYYEKV EATLPVNFAA VTAKEELFYY GAKKMGWPMI
     PTLDVIVPGY RSQPNAILPP NENITNPNIS DEQLSWMEGC TLAGHCINGC PHGPSMDKVA
     KRSTNVSYVP LALKTGNVSI HPNAFAVKIL TEKSSSNKLR ANGVKIRNTW TGEQEVIRAK
     IVVMACGSIE SPRLWLNSDL PENPWVGRGL VNHYMDWLTG IFDEKDLISI LGTTDINPFV
     GNTCGARLDY PGLGALQSVG MSPGLTASFH GLSESGYSFL YPPKQNVPWN IEGRSFGYEL
     KELMDSYRKS LSILVTTDDE VDQRNGVTLD PLISDENGFV PVISYTPTKQ SIKKRSELVK
     IAADLLRKAG AKKIIRSNWS PGMMIHIEST MRIGHVVDEN CEAFQVKRLY IADNSVHFNS
     LGGVNPTLTT QALAVRTAEK LFENYFC
//
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