Xylose isomerase

NameXylose isomerase
Synonyms
  • 5.3.1.5
  • XI
Gene NamexylA
OrganismActinoplanes missouriensis (strain ATCC 14538 / DSM 43046 / CBS 188.64 / JCM 3121 / NCIMB 12654 / NBRC 102363 / 431)
Amino acid sequence
>lcl|BSEQ0010844|Xylose isomerase
MSVQATREDKFSFGLWTVGWQARDAFGDATRTALDPVEAVHKLAEIGAYGITFHDDDLVP
FGSDAQTRDGIIAGFKKALDETGLIVPMVTTNLFTHPVFKDGGFTSNDRSVRRYAIRKVL
RQMDLGAELGAKTLVLWGGREGAEYDSAKDVSAALDRYREALNLLAQYSEDRGYGLRFAI
EPKPNEPRGDILLPTAGHAIAFVQELERPELFGINPETGHEQMSNLNFTQGIAQALWHKK
LFHIDLNGQHGPKFDQDLVFGHGDLLNAFSLVDLLENGPDGAPAYDGPRHFDYKPSRTED
YDGVWESAKANIRMYLLLKERAKAFRADPEVQEALAASKVAELKTPTLNPGEGYAELLAD
RSAFEDYDADAVGAKGFGFVKLNQLAIEHLLGAR
Number of residues394
Molecular Weight43498.425
Theoretical pI4.93
GO Classification
Functions
  • xylose isomerase activity
  • magnesium ion binding
Processes
  • D-xylose metabolic process
  • pentose-phosphate shunt
Components
  • cytoplasm
General FunctionXylose isomerase activity
Specific FunctionNot Available
Pfam Domain Function
Transmembrane RegionsNot Available
GenBank Protein ID580713
UniProtKB IDP12851
UniProtKB Entry NameXYLA_ACTM4
Cellular LocationCytoplasm
Gene sequence
>lcl|BSEQ0010845|Xylose isomerase (xylA)
GTGTCTGTCCAGGCCACACGCGAAGACAAGTTCTCCTTCGGTCTCTGGACCGTTGGATGG
CAGGCTCGTGACGCGTTCGGTGACGCCACGCGTACGGCACTCGACCCGGTCGAGGCCGTG
CACAAGCTCGCTGAGATCGGCGCCTACGGCATCACGTTCCACGACGACGACCTGGTGCCC
TTCGGCTCGGACGCCCAGACCCGCGACGGCATCATCGCGGGCTTCAAGAAGGCGCTCGAC
GAGACCGGCCTGATCGTCCCGATGGTGACCACCAACCTCTTCACCCACCCGGTGTTCAAG
GACGGCGGCTTCACCAGCAACGACCGTTCCGTGCGGCGCTACGCGATCCGCAAGGTGCTG
CGCCAGATGGACCTCGGCGCCGAGCTGGGCGCGAAGACGCTCGTCCTCTGGGGCGGCCGC
GAGGGCGCCGAGTACGACTCGGCCAAGGACGTCAGCGCCGCCCTCGACCGCTACCGCGAG
GCGCTCAACCTGCTCGCGCAGTACTCCGAGGACCGCGGTTACGGCCTGCGCTTCGCCATC
GAGCCGAAGCCGAACGAGCCCCGCGGCGACATCCTGCTCCCGACCGCCGGCCACGCCATC
GCGTTCGTGCAGGAGCTGGAGCGTCCCGAGCTCTTCGGCATCAACCCGGAGACCGGGCAC
GAGCAGATGTCGAACCTCAACTTCACCCAGGGCATCGCCCAGGCGCTGTGGCACAAGAAG
CTGTTCCACATCGACCTGAACGGTCAGCACGGCCCGAAGTTCGACCAGGACCTGGTCTTC
GGCCACGGTGACCTGCTCAACGCGTTCTCGCTGGTCGACCTCCTGGAGAACGGCCCGGAC
GGCGCCCCGGCGTACGACGGACCCCGTCACTTCGACTACAAGCCGTCCCGTACCGAGGAC
TACGACGGCGTCTGGGAGTCGGCGAAGGCCAACATCCGGATGTACCTGCTGCTCAAGGAG
CGGGCCAAGGCGTTCCGCGCCGACCCCGAGGTGCAGGAGGCGCTCGCCGCCAGCAAGGTC
GCGGAGCTGAAGACCCCGACCCTGAACCCGGGCGAGGGATACGCCGAGCTGCTCGCCGAC
CGCAGCGCGTTCGAGGACTACGACGCCGACGCCGTGGGCGCCAAGGGCTTCGGCTTCGTC
AAGCTGAACCAGCTCGCGATCGAGCACCTGCTCGGAGCCCGCTGA
GenBank Gene IDX16042
GeneCard IDNot Available
GenAtlas IDNot Available
HGNC IDNot Available
Chromosome LocationNot Available
LocusNot Available
References
  1. Amore R, Hollenberg CP: Xylose isomerase from Actinoplanes missouriensis: primary structure of the gene and the protein. Nucleic Acids Res. 1989 Sep 25;17(18):7515. 2798103
  2. Rey F, Jenkins J, Janin J, Lasters I, Alard P, Claessens M, Matthyssens G, Wodak S: Structural analysis of the 2.8 A model of Xylose isomerase from Actinoplanes missouriensis. Proteins. 1988;4(3):165-72. 3237716
  3. Jenkins J, Janin J, Rey F, Chiadmi M, van Tilbeurgh H, Lasters I, De Maeyer M, Van Belle D, Wodak SJ, Lauwereys M, et al.: Protein engineering of xylose (glucose) isomerase from Actinoplanes missouriensis. 1. Crystallography and site-directed mutagenesis of metal binding sites. Biochemistry. 1992 Jun 23;31(24):5449-58. 1610791
  4. Ramin M, Shepard W, Fourme R, Kahn R: Multiwavelength anomalous solvent contrast (MASC): derivation of envelope structure-factor amplitudes and comparison with model values. Acta Crystallogr D Biol Crystallogr. 1999 Jan;55(Pt 1):157-67. Epub 1999 Jan 1. 10089406
  5. Lambeir AM, Lauwereys M, Stanssens P, Mrabet NT, Snauwaert J, van Tilbeurgh H, Matthyssens G, Lasters I, De Maeyer M, Wodak SJ, et al.: Protein engineering of xylose (glucose) isomerase from Actinoplanes missouriensis. 2. Site-directed mutagenesis of the xylose binding site. Biochemistry. 1992 Jun 23;31(24):5459-66. 1610792
  6. van Tilbeurgh H, Jenkins J, Chiadmi M, Janin J, Wodak SJ, Mrabet NT, Lambeir AM: Protein engineering of xylose (glucose) isomerase from Actinoplanes missouriensis. 3. Changing metal specificity and the pH profile by site-directed mutagenesis. Biochemistry. 1992 Jun 23;31(24):5467-71. 1610793