Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Xylose isomerase

Gene

xylA

Organism
Streptomyces rubiginosus
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in D-xylose catabolism.

Catalytic activityi

D-xylopyranose = D-xylulose.

Cofactori

Mg2+By similarityNote: Binds 2 magnesium ions per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei54 – 541
Active sitei57 – 571By similarity
Metal bindingi181 – 1811Magnesium 1
Metal bindingi217 – 2171Magnesium 1
Metal bindingi217 – 2171Magnesium 2
Metal bindingi220 – 2201Magnesium 2
Metal bindingi245 – 2451Magnesium 1
Metal bindingi255 – 2551Magnesium 2
Metal bindingi257 – 2571Magnesium 2
Metal bindingi287 – 2871Magnesium 1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Carbohydrate metabolism, Pentose shunt, Xylose metabolism

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BRENDAi5.3.1.5. 6089.

Names & Taxonomyi

Protein namesi
Recommended name:
Xylose isomerase (EC:5.3.1.5)
Gene namesi
Name:xylA
OrganismiStreptomyces rubiginosus
Taxonomic identifieri1929 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaStreptomycetalesStreptomycetaceaeStreptomyces

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Chemistry

DrugBankiDB00126. Vitamin C.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed
Chaini2 – 388387Xylose isomerasePRO_0000195805Add
BLAST

Interactioni

Subunit structurei

Homotetramer.

Protein-protein interaction databases

DIPiDIP-58982N.

Structurei

Secondary structure

1
388
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi7 – 93Combined sources
Beta strandi11 – 144Combined sources
Helixi15 – 184Combined sources
Helixi36 – 4510Combined sources
Beta strandi50 – 545Combined sources
Helixi55 – 584Combined sources
Helixi65 – 8218Combined sources
Beta strandi88 – 903Combined sources
Beta strandi94 – 963Combined sources
Helixi97 – 993Combined sources
Beta strandi103 – 1053Combined sources
Helixi109 – 12820Combined sources
Beta strandi132 – 1365Combined sources
Beta strandi142 – 1454Combined sources
Helixi146 – 1483Combined sources
Helixi151 – 17222Combined sources
Beta strandi177 – 1804Combined sources
Beta strandi184 – 19310Combined sources
Helixi196 – 2038Combined sources
Beta strandi206 – 2083Combined sources
Helixi209 – 2113Combined sources
Beta strandi212 – 2143Combined sources
Helixi218 – 2225Combined sources
Turni223 – 2253Combined sources
Helixi228 – 23710Combined sources
Beta strandi244 – 2463Combined sources
Beta strandi251 – 2544Combined sources
Helixi265 – 27814Combined sources
Beta strandi284 – 2863Combined sources
Helixi296 – 32227Combined sources
Helixi324 – 3329Combined sources
Helixi335 – 3384Combined sources
Helixi347 – 3526Combined sources
Helixi354 – 3563Combined sources
Turni357 – 3593Combined sources
Helixi362 – 3676Combined sources
Helixi372 – 38413Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GW9X-ray1.55A1-387[»]
1MNZX-ray0.99A1-388[»]
1O1HX-ray1.40A/B2-388[»]
1OADX-ray1.50A/B2-388[»]
1XIBX-ray1.60A1-388[»]
1XICX-ray1.60A1-388[»]
1XIDX-ray1.70A1-388[»]
1XIEX-ray1.70A1-388[»]
1XIFX-ray1.60A1-388[»]
1XIGX-ray1.70A1-388[»]
1XIHX-ray1.70A1-388[»]
1XIIX-ray1.70A1-388[»]
1XIJX-ray1.70A1-388[»]
1XISX-ray1.60A2-388[»]
2G4JX-ray1.85A2-388[»]
2GLKX-ray0.94A1-388[»]
2GUBX-ray1.80A1-388[»]
2GVEneutron diffraction2.20A1-388[»]
2XISX-ray1.71A2-388[»]
3CWHneutron diffraction2.20A1-388[»]
3GNXX-ray2.00A/E2-388[»]
3KBJX-ray2.00A1-388[»]
3KBMX-ray2.00A1-388[»]
3KBNX-ray1.53A1-388[»]
3KBSX-ray1.80A1-388[»]
3KBVX-ray1.80A1-388[»]
3KBWX-ray1.60A1-388[»]
3KCJOther1.80A1-388[»]
3KCLOther2.00A1-388[»]
3KCOOther1.80A1-388[»]
3N4AX-ray1.94A2-388[»]
3QYSX-ray1.85A1-388[»]
3QZAOther2.00A1-388[»]
3U3HX-ray0.97A1-388[»]
3XISX-ray1.60A2-388[»]
4A8IX-ray0.95A1-388[»]
4A8LX-ray1.35A1-388[»]
4A8NX-ray1.20A1-388[»]
4A8RX-ray1.42A1-388[»]
4DUOX-ray2.00A1-388[»]
4DVOOther2.00A1-388[»]
4E3VX-ray1.50A1-388[»]
4J4KX-ray1.90A1-388[»]
4LNCOther2.19A1-388[»]
4QDPOther2.00A1-388[»]
4QDWOther1.80A1-388[»]
4QE1X-ray1.55A1-388[»]
4QE4X-ray1.70A1-388[»]
4QE5X-ray1.56A1-388[»]
4QEEX-ray1.60A1-388[»]
4QEHX-ray1.55A1-388[»]
4US6X-ray1.20A/B1-388[»]
4W4QX-ray2.00A1-388[»]
4XISX-ray1.60A2-388[»]
8XIAX-ray1.90A1-388[»]
9XIAX-ray1.90A1-388[»]
ProteinModelPortaliP24300.
SMRiP24300. Positions 1-388.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP24300.

Family & Domainsi

Sequence similaritiesi

Belongs to the xylose isomerase family.Curated

Family and domain databases

Gene3Di3.20.20.150. 1 hit.
HAMAPiMF_00455. Xylose_isom_A.
InterProiIPR013022. Xyl_isomerase-like_TIM-brl.
IPR013453. XylA_actinobac.
IPR001998. Xylose_isomerase.
[Graphical view]
PfamiPF01261. AP_endonuc_2. 1 hit.
[Graphical view]
PRINTSiPR00688. XYLOSISMRASE.
SUPFAMiSSF51658. SSF51658. 1 hit.
TIGRFAMsiTIGR02631. xylA_Arthro. 1 hit.
PROSITEiPS51415. XYLOSE_ISOMERASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P24300-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNYQPTPEDR FTFGLWTVGW QGRDPFGDAT RRALDPVESV RRLAELGAHG
60 70 80 90 100
VTFHDDDLIP FGSSDSEREE HVKRFRQALD DTGMKVPMAT TNLFTHPVFK
110 120 130 140 150
DGGFTANDRD VRRYALRKTI RNIDLAVELG AETYVAWGGR EGAESGGAKD
160 170 180 190 200
VRDALDRMKE AFDLLGEYVT SQGYDIRFAI EPKPNEPRGD ILLPTVGHAL
210 220 230 240 250
AFIERLERPE LYGVNPEVGH EQMAGLNFPH GIAQALWAGK LFHIDLNGQN
260 270 280 290 300
GIKYDQDLRF GAGDLRAAFW LVDLLESAGY SGPRHFDFKP PRTEDFDGVW
310 320 330 340 350
ASAAGCMRNY LILKERAAAF RADPEVQEAL RASRLDELAR PTAADGLQAL
360 370 380
LDDRSAFEEF DVDAAAARGM AFERLDQLAM DHLLGARG
Length:388
Mass (Da):43,227
Last modified:January 23, 2007 - v4
Checksum:i4C675184B62C97FB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M73789 Genomic DNA. Translation: AAA26838.1.
PIRiB41339.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M73789 Genomic DNA. Translation: AAA26838.1.
PIRiB41339.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GW9X-ray1.55A1-387[»]
1MNZX-ray0.99A1-388[»]
1O1HX-ray1.40A/B2-388[»]
1OADX-ray1.50A/B2-388[»]
1XIBX-ray1.60A1-388[»]
1XICX-ray1.60A1-388[»]
1XIDX-ray1.70A1-388[»]
1XIEX-ray1.70A1-388[»]
1XIFX-ray1.60A1-388[»]
1XIGX-ray1.70A1-388[»]
1XIHX-ray1.70A1-388[»]
1XIIX-ray1.70A1-388[»]
1XIJX-ray1.70A1-388[»]
1XISX-ray1.60A2-388[»]
2G4JX-ray1.85A2-388[»]
2GLKX-ray0.94A1-388[»]
2GUBX-ray1.80A1-388[»]
2GVEneutron diffraction2.20A1-388[»]
2XISX-ray1.71A2-388[»]
3CWHneutron diffraction2.20A1-388[»]
3GNXX-ray2.00A/E2-388[»]
3KBJX-ray2.00A1-388[»]
3KBMX-ray2.00A1-388[»]
3KBNX-ray1.53A1-388[»]
3KBSX-ray1.80A1-388[»]
3KBVX-ray1.80A1-388[»]
3KBWX-ray1.60A1-388[»]
3KCJOther1.80A1-388[»]
3KCLOther2.00A1-388[»]
3KCOOther1.80A1-388[»]
3N4AX-ray1.94A2-388[»]
3QYSX-ray1.85A1-388[»]
3QZAOther2.00A1-388[»]
3U3HX-ray0.97A1-388[»]
3XISX-ray1.60A2-388[»]
4A8IX-ray0.95A1-388[»]
4A8LX-ray1.35A1-388[»]
4A8NX-ray1.20A1-388[»]
4A8RX-ray1.42A1-388[»]
4DUOX-ray2.00A1-388[»]
4DVOOther2.00A1-388[»]
4E3VX-ray1.50A1-388[»]
4J4KX-ray1.90A1-388[»]
4LNCOther2.19A1-388[»]
4QDPOther2.00A1-388[»]
4QDWOther1.80A1-388[»]
4QE1X-ray1.55A1-388[»]
4QE4X-ray1.70A1-388[»]
4QE5X-ray1.56A1-388[»]
4QEEX-ray1.60A1-388[»]
4QEHX-ray1.55A1-388[»]
4US6X-ray1.20A/B1-388[»]
4W4QX-ray2.00A1-388[»]
4XISX-ray1.60A2-388[»]
8XIAX-ray1.90A1-388[»]
9XIAX-ray1.90A1-388[»]
ProteinModelPortaliP24300.
SMRiP24300. Positions 1-388.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-58982N.

Chemistry

DrugBankiDB00126. Vitamin C.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi5.3.1.5. 6089.

Miscellaneous databases

EvolutionaryTraceiP24300.

Family and domain databases

Gene3Di3.20.20.150. 1 hit.
HAMAPiMF_00455. Xylose_isom_A.
InterProiIPR013022. Xyl_isomerase-like_TIM-brl.
IPR013453. XylA_actinobac.
IPR001998. Xylose_isomerase.
[Graphical view]
PfamiPF01261. AP_endonuc_2. 1 hit.
[Graphical view]
PRINTSiPR00688. XYLOSISMRASE.
SUPFAMiSSF51658. SSF51658. 1 hit.
TIGRFAMsiTIGR02631. xylA_Arthro. 1 hit.
PROSITEiPS51415. XYLOSE_ISOMERASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Genetic organization and regulation of the xylose degradation genes in Streptomyces rubiginosus."
    Wong H.C., Ting Y., Lin H.C., Reichert F., Myambo K., Watt K.W., Toy P.L., Drummond R.J.
    J. Bacteriol. 173:6849-6858(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "X-ray analysis of D-xylose isomerase at 1.9 A: native enzyme in complex with substrate and with a mechanism-designed inactivator."
    Carrell H.L., Glusker J.P., Burger V., Manfre F., Tritsch D., Biellmann J.-F.
    Proc. Natl. Acad. Sci. U.S.A. 86:4440-4444(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
  3. "A metal-mediated hydride shift mechanism for xylose isomerase based on the 1.6 A Streptomyces rubiginosus structures with xylitol and D-xylose."
    Whitlow M., Howard A.J., Finzel B.C., Poulos T.L., Winborne E., Gilliland G.L.
    Proteins 9:153-173(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).

Entry informationi

Entry nameiXYLA_STRRU
AccessioniPrimary (citable) accession number: P24300
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: January 23, 2007
Last modified: June 24, 2015
This is version 114 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Caution

According to the crystallographic study residue 40 could be Gln.Curated

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.