Xylose isomerase
Details
- Name
- Xylose isomerase
- Synonyms
- 5.3.1.5
- XI
- Gene Name
- xylA
- Organism
- Actinoplanes 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 residues
- 394
- Molecular Weight
- 43498.425
- Theoretical pI
- 4.93
- GO Classification
- Functionsmagnesium ion binding / xylose isomerase activityProcessesD-xylose metabolic process / pentose-phosphate shuntComponentscytoplasm
- General Function
- Xylose isomerase activity
- Specific Function
- Not Available
- Pfam Domain Function
- AP_endonuc_2 (PF01261)
- Transmembrane Regions
- Not Available
- Cellular Location
- Cytoplasm
- 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
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P12851 UniProtKB Entry Name XYLA_ACTM4 GenBank Protein ID 580713 GenBank Gene ID X16042 - General References
- 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. [Article]
- 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. [Article]
- 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. [Article]
- 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. [Article]
- 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. [Article]
- 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. [Article]