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Database: UniProt
Entry: A0A0F0H298_9ACTN
LinkDB: A0A0F0H298_9ACTN
Original site: A0A0F0H298_9ACTN 
ID   A0A0F0H298_9ACTN        Unreviewed;       529 AA.
AC   A0A0F0H298;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Dehydrogenase {ECO:0000313|EMBL:KJK48976.1};
GN   ORFNames=UK14_17025 {ECO:0000313|EMBL:KJK48976.1};
OS   Streptomyces sp. NRRL F-4428.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1609137 {ECO:0000313|EMBL:KJK48976.1, ECO:0000313|Proteomes:UP000033569};
RN   [1] {ECO:0000313|EMBL:KJK48976.1, ECO:0000313|Proteomes:UP000033569}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL F-4428 {ECO:0000313|EMBL:KJK48976.1,
RC   ECO:0000313|Proteomes:UP000033569};
RA   Ju K.-S., Doroghazi J.R., Metcalf W.;
RL   Submitted (FEB-2015) 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:KJK48976.1}.
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DR   EMBL; JYJI01000133; KJK48976.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F0H298; -.
DR   PATRIC; fig|1609137.3.peg.3838; -.
DR   OrthoDB; 9798604at2; -.
DR   Proteomes; UP000033569; 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; PR00411; PNDRDTASEI.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000033569}.
FT   DOMAIN          210..309
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00732"
FT   DOMAIN          462..519
FT                   /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05199"
SQ   SEQUENCE   529 AA;  57899 MW;  A113267A067EA81A CRC64;
     MVDVGGTPHY DVIIIGTGAG GGTLAHRLAP SGKRVLLLER GGYLPRERDN WESTAVFVKG
     KYRAPEFWLD RHGNEFPPEV NYYVGGNTKF YGAALFRLRP EDFGEIRHHG GVSPAWPLRY
     EELEPYYTQA EHLYRVHGRH GEDPGEGPAS AQYAYPPVEH EPRIQQLSDD LEKRGLHPFH
     LPIGVDLVQD ADGRAAPSSV CIRCDRVDGF PCLVRGKSDA QVVCVEPALE HPNVEMVTHA
     HVVRLETDAA GRTVTAAVVR LADGSETRFS ADVVVVSCGA VNSAALLLAS ANDRHPRGLA
     NTSDVVGRHY MRHNNLALMA VSKEPNPTRF QKTLALHDWY LGSDDWDFPL GGVQMLGKSD
     AEQIHGEAPR WAGTVTPDMP FEVLAHHAVD FWLCGEDLPL PDSRVTLEAG GAIRLTLDEK
     NNIEGLKRLR HKLQGMLGHL GMHEHHLLPH SIYLHKGMPI GATAHQAGTV RFGTDPAASA
     LDVNCKAHDL DNLYVVDTSF FPSIGAVNPS LTAIANALRV GDHLVSRLG
//
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