ID Q88CQ8_PSEPK Unreviewed; 532 AA.
AC Q88CQ8;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 112.
DE SubName: Full=Oxidoreductase, GMC family {ECO:0000313|EMBL:AAN70687.1};
GN OrderedLocusNames=PP_5122 {ECO:0000313|EMBL:AAN70687.1};
OS Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950
OS / KT2440).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=160488 {ECO:0000313|EMBL:AAN70687.1, ECO:0000313|Proteomes:UP000000556};
RN [1] {ECO:0000313|EMBL:AAN70687.1, ECO:0000313|Proteomes:UP000000556}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440
RC {ECO:0000313|Proteomes:UP000000556};
RX PubMed=12534463; DOI=10.1046/j.1462-2920.2002.00366.x;
RA Nelson K.E., Weinel C., Paulsen I.T., Dodson R.J., Hilbert H.,
RA Martins dos Santos V.A., Fouts D.E., Gill S.R., Pop M., Holmes M.,
RA Brinkac L., Beanan M., DeBoy R.T., Daugherty S., Kolonay J., Madupu R.,
RA Nelson W., White O., Peterson J., Khouri H., Hance I., Chris Lee P.,
RA Holtzapple E., Scanlan D., Tran K., Moazzez A., Utterback T., Rizzo M.,
RA Lee K., Kosack D., Moestl D., Wedler H., Lauber J., Stjepandic D.,
RA Hoheisel J., Straetz M., Heim S., Kiewitz C., Eisen J.A., Timmis K.N.,
RA Dusterhoft A., Tummler B., Fraser C.M.;
RT "Complete genome sequence and comparative analysis of the metabolically
RT versatile Pseudomonas putida KT2440.";
RL Environ. Microbiol. 4:799-808(2002).
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00010790}.
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DR EMBL; AE015451; AAN70687.1; -; Genomic_DNA.
DR RefSeq; NP_747223.1; NC_002947.4.
DR RefSeq; WP_010955659.1; NC_002947.4.
DR AlphaFoldDB; Q88CQ8; -.
DR STRING; 160488.PP_5122; -.
DR PaxDb; 160488-PP_5122; -.
DR GeneID; 83682857; -.
DR KEGG; ppu:PP_5122; -.
DR PATRIC; fig|160488.4.peg.5467; -.
DR eggNOG; COG2303; Bacteria.
DR HOGENOM; CLU_008878_3_0_6; -.
DR OrthoDB; 9787779at2; -.
DR PhylomeDB; Q88CQ8; -.
DR BioCyc; PPUT160488:G1G01-5466-MONOMER; -.
DR Proteomes; UP000000556; Chromosome.
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; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000000556}.
FT DOMAIN 78..297
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00732"
FT DOMAIN 381..519
FT /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05199"
SQ SEQUENCE 532 AA; 57666 MW; 7309740EFAA4D9FB CRC64;
MPVPDPFRQG LERGWITHDA SRLEHDLFLE ADIAVIGSGA GGATSAQMLS AAGFKVLLIE
EGPLKTSSDF HLLESEAYAS LYQEGLGRMS KDGAITILQG RAVGGTTLVN WTSSFRTPPQ
TLAHWASVHG VNGLGEDELR PWFERMEQEL GISPWALPPN ANNDVLRRGC EQLGYRWGVI
PRNVRGCWNL GYCGMGCPVN AKQSMLVTRI PATLEQGGEL LYLARAERFA HNGERIQSLT
CQALDAQGIH PTGRQVSVQA RHYLLAGGGI NSPALLLRSA APDPHGRLGK RTFLHLVNFS
AARFSERIDP YYGAPQSIYS DHFQWQDGAD GPVGYKLEVP PLHPALASTL LGGQGHENAQ
RMAELPHTHV MLALLRDGFH PESQGGSVEL RGDGSPVLDY PVTDYLRDGL RRAYRSMAHV
QFAAGATHVT PVHSDASAAS SLEQALTMID KLRLEPFRTR LGSAHVMGGC ALGEDPRHAV
CDSLGRHHQL ENLSIHDGSL FPTSIGANPQ LSVYAISARL SEALVSRLAH SA
//
