ID GFO_ZYMMO Reviewed; 433 AA.
AC Q07982; P75002; Q5NPP7;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 2.
DT 27-MAR-2024, entry version 152.
DE RecName: Full=Glucose--fructose oxidoreductase;
DE Short=GFOR;
DE EC=1.1.99.28;
DE Flags: Precursor;
GN Name=gfo; OrderedLocusNames=ZMO0689;
OS Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Zymomonadaceae; Zymomonas.
OX NCBI_TaxID=264203;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 53-87.
RC STRAIN=ATCC 29191 / DSM 3580 / JCM 10190 / CECT 560 / NBRC 13756 / NCIMB
RC 11199 / NRRL B-4490 / ZM6;
RX PubMed=1537789; DOI=10.1128/jb.174.5.1439-1447.1992;
RA Kanagasundaram V., Scopes R.K.;
RT "Cloning, sequence analysis, and expression of the structural gene encoding
RT glucose-fructose oxidoreductase from Zymomonas mobilis.";
RL J. Bacteriol. 174:1439-1447(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 29191 / DSM 3580 / JCM 10190 / CECT 560 / NBRC 13756 / NCIMB
RC 11199 / NRRL B-4490 / ZM6;
RX PubMed=8661942; DOI=10.1007/s002030050352;
RA Wiegert T., Sahm H., Sprenger G.A.;
RT "Export of the periplasmic NADP-containing glucose-fructose oxidoreductase
RT of Zymomonas mobilis.";
RL Arch. Microbiol. 166:32-41(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31821 / ZM4 / CP4;
RX PubMed=15592456; DOI=10.1038/nbt1045;
RA Seo J.-S., Chong H., Park H.S., Yoon K.-O., Jung C., Kim J.J., Hong J.H.,
RA Kim H., Kim J.-H., Kil J.-I., Park C.J., Oh H.-M., Lee J.-S., Jin S.-J.,
RA Um H.-W., Lee H.-J., Oh S.-J., Kim J.Y., Kang H.L., Lee S.Y., Lee K.J.,
RA Kang H.S.;
RT "The genome sequence of the ethanologenic bacterium Zymomonas mobilis
RT ZM4.";
RL Nat. Biotechnol. 23:63-68(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-71, PROTEIN SEQUENCE OF 2-16
RP (PRECURSOR PROTEIN), AND PROTEIN SEQUENCE OF 53-71.
RC STRAIN=ATCC 29191 / DSM 3580 / JCM 10190 / CECT 560 / NBRC 13756 / NCIMB
RC 11199 / NRRL B-4490 / ZM6, and ATCC 31821 / ZM4 / CP4;
RX PubMed=8472911; DOI=10.1111/j.1574-6968.1993.tb06045.x;
RA Loos H., Sahm H., Sprenger G.A.;
RT "Glucose-fructose oxidoreductase, a periplasmic enzyme of Zymomonas
RT mobilis, is active in its precursor form.";
RL FEMS Microbiol. Lett. 107:293-298(1993).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
RX PubMed=8994968; DOI=10.1016/s0969-2126(96)00149-9;
RA Kingston R.L., Scopes R.K., Baker E.N.;
RT "The structure of glucose-fructose oxidoreductase from Zymomonas mobilis:
RT an osmoprotective periplasmic enzyme containing non-dissociable NADP.";
RL Structure 4:1413-1428(1996).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-fructose + D-glucose = D-glucono-1,5-lactone + D-sorbitol;
CC Xref=Rhea:RHEA:20637, ChEBI:CHEBI:4167, ChEBI:CHEBI:16217,
CC ChEBI:CHEBI:17924, ChEBI:CHEBI:37721; EC=1.1.99.28;
CC -!- COFACTOR:
CC Name=NADP(+); Xref=ChEBI:CHEBI:58349;
CC Note=Binds 1 NADP(+) per subunit. The NADP(+) cannot dissociate.;
CC -!- PATHWAY: Carbohydrate metabolism; D-sorbitol biosynthesis; D-sorbitol
CC from D-fructose and D-glucose: step 1/1.
CC -!- SUBUNIT: Homotetramer.
CC -!- SUBCELLULAR LOCATION: Periplasm.
CC -!- PTM: Predicted to be exported by the Tat system. The position of the
CC signal peptide cleavage has been experimentally proven.
CC -!- SIMILARITY: Belongs to the Gfo/Idh/MocA family. {ECO:0000305}.
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DR EMBL; M97379; AAA27690.1; -; Genomic_DNA.
DR EMBL; Z80356; CAB02496.1; -; Genomic_DNA.
DR EMBL; AE008692; AAV89313.1; -; Genomic_DNA.
DR EMBL; X73088; CAA51534.1; -; Genomic_DNA.
DR PIR; A42289; A42289.
DR RefSeq; WP_011240581.1; NZ_CP035711.1.
DR PDB; 1EVJ; X-ray; 2.70 A; A/B/C/D=82-433.
DR PDB; 1H6A; X-ray; 2.50 A; A/B=1-433.
DR PDB; 1H6B; X-ray; 2.60 A; A/B=1-433.
DR PDB; 1H6C; X-ray; 2.20 A; A/B=1-433.
DR PDB; 1H6D; X-ray; 2.05 A; A/B/C/D/E/F/G/H/I/J/K/L=1-433.
DR PDB; 1OFG; X-ray; 2.70 A; A/B/C/D/E/F=53-433.
DR PDB; 1RYD; X-ray; 2.20 A; A/B=53-433.
DR PDB; 1RYE; X-ray; 2.30 A; A/B/C/D=53-433.
DR PDBsum; 1EVJ; -.
DR PDBsum; 1H6A; -.
DR PDBsum; 1H6B; -.
DR PDBsum; 1H6C; -.
DR PDBsum; 1H6D; -.
DR PDBsum; 1OFG; -.
DR PDBsum; 1RYD; -.
DR PDBsum; 1RYE; -.
DR AlphaFoldDB; Q07982; -.
DR SMR; Q07982; -.
DR STRING; 264203.ZMO0689; -.
DR DrugBank; DB02379; Beta-D-Glucose.
DR DrugBank; DB03345; Mercaptoethanol.
DR DrugBank; DB02338; NADPH.
DR KEGG; ag:AAA27690; -.
DR KEGG; zmo:ZMO0689; -.
DR eggNOG; COG0673; Bacteria.
DR HOGENOM; CLU_023194_5_1_5; -.
DR BioCyc; MetaCyc:MONOMER-13277; -.
DR BRENDA; 1.1.99.28; 6765.
DR UniPathway; UPA00815; UER00784.
DR EvolutionaryTrace; Q07982; -.
DR Proteomes; UP000001173; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0047061; F:glucose-fructose oxidoreductase activity; IEA:UniProtKB-EC.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0006061; P:sorbitol biosynthetic process; IEA:UniProtKB-UniPathway.
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; PTHR43818; BCDNA.GH03377; 1.
DR PANTHER; PTHR43818:SF11; BCDNA.GH03377; 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 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; NADP; Oxidoreductase; Periplasm;
KW Reference proteome; Signal.
FT SIGNAL 1..52
FT /note="Tat-type signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00648,
FT ECO:0000269|PubMed:1537789, ECO:0000269|PubMed:8472911"
FT CHAIN 53..433
FT /note="Glucose--fructose oxidoreductase"
FT /id="PRO_0000010851"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 29
FT /note="T -> N (in Ref. 1 and 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 43
FT /note="A -> R (in Ref. 1 and 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 61
FT /note="Q -> L (in Ref. 1; AAA27690 and 4; CAA51534)"
FT /evidence="ECO:0000305"
FT CONFLICT 111..119
FT /note="IEALVSGNA -> MKLWSAVT (in Ref. 1; AAA27690)"
FT /evidence="ECO:0000305"
FT CONFLICT 170
FT /note="A -> S (in Ref. 1; AAA27690)"
FT /evidence="ECO:0000305"
FT CONFLICT 247..258
FT /note="PAQQWRLRRELA -> LHSSGVCVVNS (in Ref. 1; AAA27690)"
FT /evidence="ECO:0000305"
FT CONFLICT 420
FT /note="P -> A (in Ref. 1; AAA27690)"
FT /evidence="ECO:0000305"
FT CONFLICT 431..433
FT /note="GGY -> VVIDSDLTYLG (in Ref. 1; AAA27690)"
FT /evidence="ECO:0000305"
FT HELIX 57..60
FT /evidence="ECO:0007829|PDB:1H6D"
FT STRAND 64..66
FT /evidence="ECO:0007829|PDB:1H6D"
FT STRAND 84..89
FT /evidence="ECO:0007829|PDB:1H6D"
FT HELIX 93..97
FT /evidence="ECO:0007829|PDB:1H6D"
FT HELIX 99..102
FT /evidence="ECO:0007829|PDB:1H6D"
FT TURN 103..105
FT /evidence="ECO:0007829|PDB:1H6D"
FT STRAND 107..115
FT /evidence="ECO:0007829|PDB:1H6D"
FT HELIX 119..128
FT /evidence="ECO:0007829|PDB:1H6D"
FT HELIX 133..135
FT /evidence="ECO:0007829|PDB:1H6D"
FT STRAND 139..141
FT /evidence="ECO:0007829|PDB:1H6D"
FT HELIX 142..147
FT /evidence="ECO:0007829|PDB:1H6D"
FT STRAND 153..156
FT /evidence="ECO:0007829|PDB:1H6D"
FT HELIX 160..162
FT /evidence="ECO:0007829|PDB:1H6D"
FT HELIX 163..172
FT /evidence="ECO:0007829|PDB:1H6D"
FT STRAND 176..179
FT /evidence="ECO:0007829|PDB:1H6D"
FT STRAND 181..183
FT /evidence="ECO:0007829|PDB:1EVJ"
FT HELIX 187..200
FT /evidence="ECO:0007829|PDB:1H6D"
FT STRAND 204..206
FT /evidence="ECO:0007829|PDB:1H6D"
FT HELIX 209..212
FT /evidence="ECO:0007829|PDB:1H6D"
FT HELIX 214..224
FT /evidence="ECO:0007829|PDB:1H6D"
FT TURN 225..228
FT /evidence="ECO:0007829|PDB:1RYD"
FT STRAND 230..239
FT /evidence="ECO:0007829|PDB:1H6D"
FT HELIX 247..250
FT /evidence="ECO:0007829|PDB:1H6D"
FT HELIX 251..253
FT /evidence="ECO:0007829|PDB:1H6D"
FT HELIX 255..258
FT /evidence="ECO:0007829|PDB:1H6D"
FT STRAND 259..261
FT /evidence="ECO:0007829|PDB:1H6D"
FT HELIX 262..265
FT /evidence="ECO:0007829|PDB:1H6D"
FT HELIX 267..278
FT /evidence="ECO:0007829|PDB:1H6D"
FT STRAND 282..290
FT /evidence="ECO:0007829|PDB:1H6D"
FT HELIX 296..298
FT /evidence="ECO:0007829|PDB:1H6D"
FT STRAND 299..301
FT /evidence="ECO:0007829|PDB:1H6D"
FT STRAND 303..311
FT /evidence="ECO:0007829|PDB:1H6D"
FT STRAND 316..325
FT /evidence="ECO:0007829|PDB:1H6D"
FT STRAND 328..337
FT /evidence="ECO:0007829|PDB:1H6D"
FT STRAND 339..346
FT /evidence="ECO:0007829|PDB:1H6D"
FT STRAND 353..357
FT /evidence="ECO:0007829|PDB:1H6D"
FT STRAND 360..364
FT /evidence="ECO:0007829|PDB:1H6D"
FT HELIX 376..389
FT /evidence="ECO:0007829|PDB:1H6D"
FT STRAND 395..397
FT /evidence="ECO:0007829|PDB:1H6D"
FT HELIX 398..417
FT /evidence="ECO:0007829|PDB:1H6D"
SQ SEQUENCE 433 AA; 47190 MW; 13CFADE84794E736 CRC64;
MTNKISSSDN LSNAVSATDD NASRTPNLTR RALVGGGVGL AAAGALASGL QAATLPAGAS
QVPTTPAGRP MPYAIRPMPE DRRFGYAIVG LGKYALNQIL PGFAGCQHSR IEALVSGNAE
KAKIVAAEYG VDPRKIYDYS NFDKIAKDPK IDAVYIILPN SLHAEFAIRA FKAGKHVMCE
KPMATSVADC QRMIDAAKAA NKKLMIGYRC HYDPMNRAAV KLIRENQLGK LGMVTTDNSD
VMDQNDPAQQ WRLRRELAGG GSLMDIGIYG LNGTRYLLGE EPIEVRAYTY SDPNDERFVE
VEDRIIWQMR FRSGALSHGA SSYSTTTTSR FSVQGDKAVL LMDPATGYYQ NLISVQTPGH
ANQSMMPQFI MPANNQFSAQ LDHLAEAVIN NKPVRSPGEE GMQDVRLIQA IYEAARTGRP
VNTDWGYVRQ GGY
//
