Q07982 (GFO_ZYMMO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Glucose--fructose oxidoreductase
Short name=GFOR
EC=1.1.99.28

Gene names

Name:	gfo
Ordered Locus Names:	ZMO0689

Organism

Zymomonas mobilis [Complete proteome] [HAMAP]

Taxonomic identifier

542 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Sphingomonadales › Sphingomonadaceae › Zymomonas

Protein attributes

Sequence length	433 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	D-glucose + D-fructose = D-gluconolactone + D-glucitol.
Cofactor	Binds 1 NADP+ per subunit. The NADP cannot dissociate.
Pathway	Carbohydrate metabolism; D-sorbitol biosynthesis; D-sorbitol from D-fructose and D-glucose: step 1/1.
Subunit structure	Homotetramer.
Subcellular location	Periplasm.
Post-translational modification	Predicted to be exported by the Tat system. The position of the signal peptide cleavage has been experimentally proven.
Sequence similarities	Belongs to the gfo/idh/mocA family.

Ontologies

Keywords
Cellular component	Periplasm
Domain	Signal
Ligand	NADP
Molecular function	Oxidoreductase
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Cellular component	periplasmic space Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	glucose-fructose oxidoreductase activity Inferred from electronic annotation. Source: EC nucleotide binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 52

52

Tat-type signal Ref.1

Chain

53 – 433

381

Glucose--fructose oxidoreductase

PRO_0000010851

Experimental info

Sequence conflict

29

1

T → N Ref.1

Sequence conflict

29

1

T → N Ref.4

Sequence conflict

43

1

A → R Ref.1

Sequence conflict

43

1

A → R Ref.4

Sequence conflict

61

1

Q → L in AAA27690. Ref.1

Sequence conflict

61

1

Q → L in CAA51534. Ref.4

Sequence conflict

111 – 119

9

IEALVSGNA → MKLWSAVT in AAA27690. Ref.1

Sequence conflict

170

1

A → S in AAA27690. Ref.1

Sequence conflict

247 – 258

12

PAQQW…RRELA → LHSSGVCVVNS in AAA27690. Ref.1

Sequence conflict

420

1

P → A in AAA27690. Ref.1

Sequence conflict

431 – 433

3

GGY → VVIDSDLTYLG in AAA27690. Ref.1

Secondary structure

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433

Helix Strand Turn

Details...

Helix

57 – 60

4

Beta strand

64 – 66

3

Beta strand

84 – 89

6

Helix

93 – 97

5

Helix

99 – 102

4

Turn

103 – 105

3

Beta strand

107 – 115

9

Helix

119 – 128

10

Helix

133 – 135

3

Beta strand

139 – 141

3

Helix

142 – 147

6

Beta strand

153 – 156

4

Helix

160 – 162

3

Helix

163 – 172

10

Beta strand

176 – 179

4

Helix

187 – 200

14

Beta strand

204 – 206

3

Helix

209 – 211

3

Helix

214 – 224

11

Beta strand

230 – 239

10

Helix

247 – 250

4

Helix

251 – 253

3

Helix

255 – 258

4

Beta strand

259 – 261

3

Helix

262 – 265

4

Helix

267 – 278

12

Beta strand

282 – 290

9

Helix

296 – 298

3

Beta strand

299 – 301

3

Beta strand

303 – 311

9

Beta strand

316 – 325

10

Beta strand

328 – 337

10

Beta strand

339 – 346

8

Beta strand

353 – 357

5

Beta strand

360 – 364

5

Helix

376 – 389

14

Beta strand

395 – 397

3

Helix

398 – 417

20

Sequences

	Sequence		Length	Mass (Da)
	Q07982 [UniParc]. Last modified February 15, 2005. Version 2. Checksum: 13CFADE84794E736	FASTA	433	47,190
	10 20 30 40 50 60 MTNKISSSDN LSNAVSATDD NASRTPNLTR RALVGGGVGL AAAGALASGL QAATLPAGAS 70 80 90 100 110 120 QVPTTPAGRP MPYAIRPMPE DRRFGYAIVG LGKYALNQIL PGFAGCQHSR IEALVSGNAE 130 140 150 160 170 180 KAKIVAAEYG VDPRKIYDYS NFDKIAKDPK IDAVYIILPN SLHAEFAIRA FKAGKHVMCE 190 200 210 220 230 240 KPMATSVADC QRMIDAAKAA NKKLMIGYRC HYDPMNRAAV KLIRENQLGK LGMVTTDNSD 250 260 270 280 290 300 VMDQNDPAQQ WRLRRELAGG GSLMDIGIYG LNGTRYLLGE EPIEVRAYTY SDPNDERFVE 310 320 330 340 350 360 VEDRIIWQMR FRSGALSHGA SSYSTTTTSR FSVQGDKAVL LMDPATGYYQ NLISVQTPGH 370 380 390 400 410 420 ANQSMMPQFI MPANNQFSAQ LDHLAEAVIN NKPVRSPGEE GMQDVRLIQA IYEAARTGRP 430 VNTDWGYVRQ GGY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning, sequence analysis, and expression of the structural gene encoding glucose-fructose oxidoreductase from Zymomonas mobilis." Kanagasundaram V., Scopes R.K. J. Bacteriol. 174:1439-1447(1992) [PubMed: 1537789] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 53-87. Strain: ATCC 29191 / DSM 3580 / NBRC 13756 / NCIMB 11199 / NRRL B-4490 / ZM6.
[2]	"Export of the periplasmic NADP-containing glucose-fructose oxidoreductase of Zymomonas mobilis." Wiegert T., Sahm H., Sprenger G.A. Arch. Microbiol. 166:32-41(1996) [PubMed: 8661942] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 29191 / DSM 3580 / NBRC 13756 / NCIMB 11199 / NRRL B-4490 / ZM6.
[3]	"The genome sequence of the ethanologenic bacterium Zymomonas mobilis ZM4." Seo J.-S., Chong H., Park H.S., Yoon K.-O., Jung C., Kim J.J., Hong J.H., Kim H., Kim J.-H., Kil J.-I., Park C.J., Oh H.-M., Lee J.-S., Jin S.-J., Um H.-W., Lee H.-J., Oh S.-J., Kim J.Y. , Kang H.L., Lee S.Y., Lee K.J., Kang H.S. Nat. Biotechnol. 23:63-68(2005) [PubMed: 15592456] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 31821 / ZM4 / CP4.
[4]	"Glucose-fructose oxidoreductase, a periplasmic enzyme of Zymomonas mobilis, is active in its precursor form." Loos H., Sahm H., Sprenger G.A. FEMS Microbiol. Lett. 107:293-298(1993) [PubMed: 8472911] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-71, PROTEIN SEQUENCE OF 2-16 AND 53-71. Strain: ATCC 29191 / DSM 3580 / NBRC 13756 / NCIMB 11199 / NRRL B-4490 / ZM6 and ATCC 31821 / ZM4 / CP4.
[5]	"The structure of glucose-fructose oxidoreductase from Zymomonas mobilis: an osmoprotective periplasmic enzyme containing non-dissociable NADP." Kingston R.L., Scopes R.K., Baker E.N. Structure 4:1413-1428(1996) [PubMed: 8994968] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M97379 Genomic DNA. Translation: AAA27690.1.
Z80356 Genomic DNA. Translation: CAB02496.1.
AE008692 Genomic DNA. Translation: AAV89313.1.
X73088 Genomic DNA. Translation: CAA51534.1.

PIR

A42289.

RefSeq

YP_162424.1. NC_006526.2.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1EVJ	X-ray	2.70	A/B/C/D	82-433	[»]
1H6A	X-ray	2.50	A/B	1-433	[»]
1H6B	X-ray	2.60	A/B	1-433	[»]
1H6C	X-ray	2.20	A/B	1-433	[»]
1H6D	X-ray	2.05	A/B/C/D/E/F/G/H/I/J/K/L	1-433	[»]
1OFG	X-ray	2.70	A/B/C/D/E/F	53-433	[»]
1RYD	X-ray	2.20	A/B	53-433	[»]
1RYE	X-ray	2.30	A/B/C/D	53-433	[»]

ProteinModelPortal

Q07982.

SMR

Q07982. Positions 51-433.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

3187982.

GenomeReviews

Gene locus ZMO0689 in contig AE008692_GR.

KEGG

zmo:ZMO0689.

NMPDR

fig|264203.3.peg.1185.

PATRIC

32566692. VBIZymMob102260_0654.

Organism-specific databases

CMR

Search...

Phylogenomic databases

HOGENOM

HBG407231.

OMA

LRIRNGH.

ProtClustDB

CLSK2524643.

Enzyme and pathway databases

BioCyc

MetaCyc:MONOMER-13277.
ZMOB264203:ZMO0689-MONOMER.

Family and domain databases

InterPro

IPR008354. Glc-Fru_OxRdtase_bac.
IPR016040. NAD(P)-bd_dom.
IPR000683. Oxidoreductase_N.
IPR004104. OxRdtase_C.
IPR006311. TAT_signal.
[Graphical view]

Gene3D

G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.

KO

K00118.

Pfam

PF01408. GFO_IDH_MocA. 1 hit.
PF02894. GFO_IDH_MocA_C. 1 hit.
[Graphical view]

PRINTS

PR01775. GLFROXRDTASE.

PROSITE

PS51318. TAT. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

GFO_ZYMMO

Accession

Primary (citable) accession number: Q07982
Secondary accession number(s): P75002, Q5NPP7

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	February 15, 2005
Last modified:	January 25, 2012
This is version 89 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program