Glucose--fructose oxidoreductase

Details

Name
Glucose--fructose oxidoreductase
Synonyms
  • 1.1.99.28
  • GFOR
Gene Name
gfo
Organism
Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
Amino acid sequence
>lcl|BSEQ0019142|Glucose--fructose oxidoreductase
MTNKISSSDNLSNAVSATDDNASRTPNLTRRALVGGGVGLAAAGALASGLQAATLPAGAS
QVPTTPAGRPMPYAIRPMPEDRRFGYAIVGLGKYALNQILPGFAGCQHSRIEALVSGNAE
KAKIVAAEYGVDPRKIYDYSNFDKIAKDPKIDAVYIILPNSLHAEFAIRAFKAGKHVMCE
KPMATSVADCQRMIDAAKAANKKLMIGYRCHYDPMNRAAVKLIRENQLGKLGMVTTDNSD
VMDQNDPAQQWRLRRELAGGGSLMDIGIYGLNGTRYLLGEEPIEVRAYTYSDPNDERFVE
VEDRIIWQMRFRSGALSHGASSYSTTTTSRFSVQGDKAVLLMDPATGYYQNLISVQTPGH
ANQSMMPQFIMPANNQFSAQLDHLAEAVINNKPVRSPGEEGMQDVRLIQAIYEAARTGRP
VNTDWGYVRQGGY
Number of residues
433
Molecular Weight
47189.15
Theoretical pI
8.73
GO Classification
Functions
glucose-fructose oxidoreductase activity
Processes
sorbitol biosynthetic process
Components
periplasmic space
General Function
Glucose-fructose oxidoreductase activity
Specific Function
Not Available
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Periplasm
Gene sequence
>lcl|BSEQ0019143|Glucose--fructose oxidoreductase (gfo)
ATGACGAACAAAATCTCGTCTTCAGATAATCTTTCCAATGCTGTTTCAGCAACGGATGAC
AACGCTTCCCGTACGCCAAATCTGACCCGTCGCGCTCTCGTTGGTGGTGGTGTTGGACTG
GCCGCAGCTGGCGCCTTAGCCAGTGGTCTTCAGGCAGCGACGCTTCCTGCTGGTGCCAGC
CAGGTTCCGACCACGCCTGCAGGTCGCCCGATGCCTTACGCGATCCGCCCGATGCCGGAA
GATCGTCGTTTCGGTTATGCTATCGTCGGTCTGGGTAAATATGCCCTTAACCAGATTTTA
CCGGGTTTTGCCGGATGCCAGCATTCCCGCATCGAAGCTTTGGTCAGCGGTAACGCTGAA
AAAGCTAAAATCGTTGCCGCTGAATATGGCGTCGATCCCCGTAAAATTTATGATTACAGC
AACTTCGACAAGATCGCTAAAGATCCAAAAATCGACGCTGTTTACATCATTTTGCCAAAC
TCTTTGCATGCTGAATTTGCTATCCGTGCTTTCAAAGCCGGCAAGCATGTTATGTGTGAA
AAGCCGATGGCAACCTCTGTTGCTGATTGTCAGCGGATGATCGATGCAGCCAAGGCTGCT
AATAAAAAGCTGATGATCGGTTACCGTTGCCACTATGATCCAATGAACCGTGCAGCGGTA
AAATTGATCCGTGAAAACCAGTTGGGTAAACTGGGCATGGTTACCACCGACAACTCAGAC
GTTATGGATCAGAACGATCCTGCACAGCAGTGGCGTCTGCGTCGTGAACTCGCCGGTGGC
GGTTCTTTGATGGATATCGGTATTTATGGCTTGAACGGTACCCGTTACTTGCTGGGTGAA
GAACCGATCGAAGTCCGTGCTTACACCTACAGCGATCCGAATGATGAACGTTTCGTTGAA
GTCGAAGATCGTATTATTTGGCAGATGCGCTTCAGAAGCGGTGCTCTGTCTCATGGTGCA
TCTTCTTATTCGACCACGACGACTTCACGTTTCTCGGTGCAGGGCGACAAAGCTGTTCTG
TTGATGGATCCGGCTACCGGATATTATCAGAATTTGATTTCTGTCCAGACCCCAGGCCAT
GCTAACCAGTCGATGATGCCACAGTTCATCATGCCAGCGAACAACCAGTTCTCTGCACAG
TTGGATCATCTGGCTGAAGCCGTCATCAATAACAAACCAGTTCGTAGCCCGGGTGAAGAA
GGTATGCAGGATGTGCGCCTGATTCAGGCCATTTATGAAGCAGCTCGTACCGGTCGCCCC
GTCAACACGGATTGGGGTTATGTCCGTCAGGGTGGTTATTGA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDQ07982
UniProtKB Entry NameGFO_ZYMMO
GenBank Protein ID155588
GenBank Gene IDM97379
General References
  1. Kanagasundaram V, Scopes RK: Cloning, sequence analysis, and expression of the structural gene encoding glucose-fructose oxidoreductase from Zymomonas mobilis. J Bacteriol. 1992 Mar;174(5):1439-47. [Article]
  2. Wiegert T, Sahm H, Sprenger GA: Export of the periplasmic NADP-containing glucose-fructose oxidoreductase of Zymomonas mobilis. Arch Microbiol. 1996 Jul;166(1):32-41. [Article]
  3. Seo JS, Chong H, Park HS, Yoon KO, Jung C, Kim JJ, Hong JH, Kim H, Kim JH, Kil JI, Park CJ, Oh HM, Lee JS, Jin SJ, Um HW, Lee HJ, Oh SJ, Kim JY, Kang HL, Lee SY, Lee KJ, Kang HS: The genome sequence of the ethanologenic bacterium Zymomonas mobilis ZM4. Nat Biotechnol. 2005 Jan;23(1):63-8. Epub 2004 Dec 12. [Article]
  4. Loos H, Sahm H, Sprenger GA: Glucose-fructose oxidoreductase, a periplasmic enzyme of Zymomonas mobilis, is active in its precursor form. FEMS Microbiol Lett. 1993 Mar 1;107(2-3):293-8. [Article]
  5. Kingston RL, Scopes RK, Baker EN: The structure of glucose-fructose oxidoreductase from Zymomonas mobilis: an osmoprotective periplasmic enzyme containing non-dissociable NADP. Structure. 1996 Dec 15;4(12):1413-28. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB02338NADPHexperimentalunknownDetails
DB03345MercaptoethanolexperimentalunknownDetails
DB02379Beta-D-GlucoseexperimentalunknownDetails