ID   A0A261V2H9_9BORD        Unreviewed;       593 AA.
AC   A0A261V2H9;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 13.
DE   SubName: Full=GMC family oxidoreductase {ECO:0000313|EMBL:OZI67812.1};
GN   ORFNames=CAL20_01885 {ECO:0000313|EMBL:OZI67812.1};
OS   Bordetella genomosp. 4.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=463044 {ECO:0000313|EMBL:OZI67812.1, ECO:0000313|Proteomes:UP000216885};
RN   [1] {ECO:0000313|EMBL:OZI67812.1, ECO:0000313|Proteomes:UP000216885}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AU9919 {ECO:0000313|EMBL:OZI67812.1,
RC   ECO:0000313|Proteomes:UP000216885};
RA   Spilker T., LiPuma J.;
RT   "Complete and WGS of Bordetella genogroups.";
RL   Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
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:OZI67812.1}.
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; NEVQ01000001; OZI67812.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A261V2H9; -.
DR   OrthoDB; 9787779at2; -.
DR   Proteomes; UP000216885; 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   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000216885}.
FT   DOMAIN          234..348
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00732"
FT   DOMAIN          445..572
FT                   /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05199"
SQ   SEQUENCE   593 AA;  65385 MW;  17664CA36C778AC0 CRC64;
     MASIKKEKVD VVLVGFGWTG AIMGQELTND GLKVLALERG PMQDTPNDAE YPKVLDELAY
     SVRGKLFQDL SKETVTIRHS LGETAVPYRQ HGSFLLGNGV GGAGFHWNGM HYRNLPEELV
     LRTRTEERYG KDFIPKDMTL QDHGVTYEDL EPHYDFFEKV CGTSGKAGNI NGKIQESGNP
     LEGPRTDEFP LPPLQQTYAQ SLFEKAARDV GYHPFAAPAS NASGPYTNPY GVRLGPCNFC
     GFCENYGCFM YSKASPQTTI LPVLLKKPNF ELRTNAYVTK VNVDKSGKMA TGVTYVDAQG
     REVEQPADLV ILCAFQTHNT RLMLLSGIGT PYDPATGEGV VGKNLAYQMN GGIRIIMPKG
     NYFNPFEGAG ASAWAFDDLN ADQFDHAPLG FIGGAVVRQA TTGGRPIKQA SPMPGSPTWG
     SGWKAGMADA YQRSFNIGMS GSVMPYRDAY MSLDPTYKDS HGLPLLRMTF DWHDNEYKML
     DYVGSQVEKV AKAMNPEKYV VNVRKPGSHW DTRVYQSTHL TGGTIMGTSP QDSVLNRYLQ
     SWDVPNLFVM GASTFPYNMG YNPTGLVGAL AYWSVKAIRE QYMKNQGRPL VQA
//