ID A0A148KN10_9ALTE Unreviewed; 363 AA.
AC A0A148KN10;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=Glucose-fructose oxidoreductase {ECO:0000313|EMBL:KXI27639.1};
GN ORFNames=AX660_18955 {ECO:0000313|EMBL:KXI27639.1};
OS Paraglaciecola hydrolytica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Paraglaciecola.
OX NCBI_TaxID=1799789 {ECO:0000313|EMBL:KXI27639.1, ECO:0000313|Proteomes:UP000070299};
RN [1] {ECO:0000313|EMBL:KXI27639.1, ECO:0000313|Proteomes:UP000070299}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S66 {ECO:0000313|EMBL:KXI27639.1,
RC ECO:0000313|Proteomes:UP000070299};
RA Wen L., He K., Yang H.;
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the Gfo/Idh/MocA family.
CC {ECO:0000256|ARBA:ARBA00010928}.
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:KXI27639.1}.
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DR EMBL; LSNE01000009; KXI27639.1; -; Genomic_DNA.
DR RefSeq; WP_068378847.1; NZ_LSNE01000009.1.
DR AlphaFoldDB; A0A148KN10; -.
DR STRING; 1799789.AX660_18955; -.
DR OrthoDB; 9774191at2; -.
DR Proteomes; UP000070299; Unassembled WGS sequence.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR004104; Gfo/Idh/MocA-like_OxRdtase_C.
DR InterPro; IPR000683; Gfo/Idh/MocA-like_OxRdtase_N.
DR InterPro; IPR008354; Glc-Fru_OxRdtase_bac.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR006311; TAT_signal.
DR PANTHER; PTHR22604; OXIDOREDUCTASES; 1.
DR PANTHER; PTHR22604:SF105; TRANS-1,2-DIHYDROBENZENE-1,2-DIOL DEHYDROGENASE; 1.
DR Pfam; PF01408; GFO_IDH_MocA; 1.
DR Pfam; PF02894; GFO_IDH_MocA_C; 1.
DR PRINTS; PR01775; GLFROXRDTASE.
DR SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000070299};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..363
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007550265"
FT DOMAIN 37..160
FT /note="Gfo/Idh/MocA-like oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01408"
FT DOMAIN 199..361
FT /note="Gfo/Idh/MocA-like oxidoreductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02894"
SQ SEQUENCE 363 AA; 40412 MW; 768011F7D0728E32 CRC64;
MNNLNRRRFM QMAAGLGLAS AISNQQAMAK SNSTKIGVAL LGLGGYSRGL LAPALELTQH
CELRGIITGS PEKIPEWQQR YGIQDKNVYS YQNMHELANN PDIDVVYVVV PTSLHLQYCE
IAANAGKHVW CEKPMAMSTA QCQRIIDVCQ QNKVKLSIGY RMQHEPNTQR FMQYRTTQPY
GKIQHIIAQA GYGGNGLPAS NWRMQKAMGG GAMYDMGVYP LNGVRYMTGL EPIAVTARHD
KSHPDIFKEV DETTYFDLEF ANGLIAECGT SMVKSFSQLT MQCEKGWYQL RPMSNYTGVT
GYTSDKQEFA AIKQIQQAIQ MDNDALALQG QGQLLVPGEE GLKDIHVVQA IFESAAKNKR
ILL
//