Glucose--fructose oxidoreductase


NameGlucose--fructose oxidoreductase
Synonyms
  • 1.1.99.28
  • GFOR
Gene Namegfo
OrganismZymomonas 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 residuesNone
Molecular Weight47189.15
Theoretical pI8.73
GO Classification
Functions
  • glucose-fructose oxidoreductase activity
Processes
  • sorbitol biosynthetic process
Components
  • periplasmic space
General FunctionGlucose-fructose oxidoreductase activity
Specific FunctionNone
Transmembrane Regions
GenBank Protein ID
UniProtKB IDQ07982
UniProtKB Entry Name
Cellular LocationPeriplasm
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
GenBank Gene ID
GeneCard IDNone
GenAtlas ID
HGNC ID
Chromosome LocationNone
LocusNone
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. [1537789 ]
  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. [8661942 ]
  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. [15592456 ]
  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. [8472911 ]
  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. [8994968 ]

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