ID I4MZI4_9PSED Unreviewed; 589 AA.
AC I4MZI4;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Gluconate 2-dehydrogenase {ECO:0000313|EMBL:EIK94624.1};
GN ORFNames=PMM47T1_21093 {ECO:0000313|EMBL:EIK94624.1};
OS Pseudomonas sp. M47T1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1179778 {ECO:0000313|EMBL:EIK94624.1, ECO:0000313|Proteomes:UP000004339};
RN [1] {ECO:0000313|EMBL:EIK94624.1, ECO:0000313|Proteomes:UP000004339}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M47T1 {ECO:0000313|EMBL:EIK94624.1,
RC ECO:0000313|Proteomes:UP000004339};
RX PubMed=22887683; DOI=10.1128/JB.01116-12;
RA Proenca D.N., Espirito Santo C., Grass G., Morais P.V.;
RT "Draft Genome Sequence of Pseudomonas sp. Strain M47T1, Carried by
RT Bursaphelenchus xylophilus Isolated from Pinus pinaster.";
RL J. Bacteriol. 194:4789-4790(2012).
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:EIK94624.1}.
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DR EMBL; AJWX01000022; EIK94624.1; -; Genomic_DNA.
DR RefSeq; WP_008372745.1; NZ_AJWX01000022.1.
DR AlphaFoldDB; I4MZI4; -.
DR STRING; 1179778.PMM47T1_21093; -.
DR PATRIC; fig|1179778.3.peg.4213; -.
DR eggNOG; COG2303; Bacteria.
DR OrthoDB; 9787779at2; -.
DR Proteomes; UP000004339; 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:UP000004339}.
FT DOMAIN 233..343
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00732"
FT DOMAIN 447..568
FT /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05199"
SQ SEQUENCE 589 AA; 64307 MW; 38CCAD0A09EA43AA CRC64;
MATITNDEVD VIVVGMGWAG SLMSIELAQA GLKVRALERG EDRTNADFGY PKPADEYAYG
VRNKIMVTPK DGALTVRHSI HDTALPTRQW GAFVPGTGVG GSGLHWTGVL IRPTPTDIKL
KTYADQAYKP GQLGEGMQVQ DFPFTWEEIE PYLDRFDKIC GLSGNTGNLR GTLIPGGDPF
EGPRSFPHPL PPMEDTLNNT MFADAARKLG YHPFPNPSAN VSRAWTNPYG NQIAPCNYCG
YCSKYPCLNF SKASPQTAVL DSLKRMENFS YRTNANVLRV DLHPDGKTAR GVTYADGQGN
EVFQPAKIVV LAAFQFVNVR LMLLSKIGTP YDPVSGKGTV GRNYAFLSNG GTTLFFKDKH
FNPFATAGAT GQLFNDVSPG NFDGPGLGFL GGAKIQSAQA TGTPIGTSLP SGTPEWGQGW
KDGMVDWYGH SMKIGITTSC MSYRDHYVDL DPTYKDPWGQ PLLRITFDWK QNELKLQQHL
RKIVLGITQE LAPDSYSESY LAMDSHWDIT KYVSTHNVGG AVMGDSPETS ALNRYLQSWD
VHNVFVPGGN AFPQNFQANP TSMIGALTLF AAQAIKDLYL KNPGPLVSA
//
