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P24300

- XYLA_STRRU

UniProt

P24300 - XYLA_STRRU

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Protein

Xylose isomerase

Gene

xylA

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

Functioni

Involved in D-xylose catabolism.

Catalytic activityi

D-xylopyranose = D-xylulose.

Cofactori

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

  1. magnesium ion binding Source: UniProtKB-HAMAP
  2. xylose isomerase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. D-xylose metabolic process Source: UniProtKB-HAMAP
  2. pentose-phosphate shunt Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Carbohydrate metabolism, Pentose shunt, Xylose metabolism

Keywords - Ligandi

Magnesium, Metal-binding

Names & Taxonomyi

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

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

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 – 93
Beta strandi11 – 144
Helixi15 – 184
Helixi36 – 4510
Beta strandi50 – 545
Helixi55 – 584
Helixi65 – 8218
Beta strandi88 – 903
Beta strandi94 – 963
Helixi97 – 993
Beta strandi103 – 1053
Helixi109 – 12820
Beta strandi132 – 1365
Beta strandi142 – 1454
Helixi146 – 1483
Helixi151 – 17222
Beta strandi177 – 1804
Beta strandi184 – 19310
Helixi196 – 2038
Beta strandi206 – 2083
Helixi209 – 2113
Beta strandi212 – 2143
Helixi218 – 2225
Turni223 – 2253
Helixi228 – 23710
Beta strandi244 – 2463
Beta strandi251 – 2544
Helixi265 – 27814
Beta strandi284 – 2863
Helixi296 – 32227
Helixi324 – 3329
Helixi335 – 3384
Helixi347 – 3526
Helixi354 – 3563
Turni357 – 3593
Helixi362 – 3676
Helixi372 – 38413

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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[»]
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:
EMBL
GenBank
DDBJ
Links Updated
M73789 Genomic DNA. Translation: AAA26838.1.
PIRiB41339.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M73789 Genomic DNA. Translation: AAA26838.1 .
PIRi B41339.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1GW9 X-ray 1.55 A 1-387 [» ]
1MNZ X-ray 0.99 A 1-388 [» ]
1O1H X-ray 1.40 A/B 2-388 [» ]
1OAD X-ray 1.50 A/B 2-388 [» ]
1XIB X-ray 1.60 A 1-388 [» ]
1XIC X-ray 1.60 A 1-388 [» ]
1XID X-ray 1.70 A 1-388 [» ]
1XIE X-ray 1.70 A 1-388 [» ]
1XIF X-ray 1.60 A 1-388 [» ]
1XIG X-ray 1.70 A 1-388 [» ]
1XIH X-ray 1.70 A 1-388 [» ]
1XII X-ray 1.70 A 1-388 [» ]
1XIJ X-ray 1.70 A 1-388 [» ]
1XIS X-ray 1.60 A 2-388 [» ]
2G4J X-ray 1.85 A 2-388 [» ]
2GLK X-ray 0.94 A 1-388 [» ]
2GUB X-ray 1.80 A 1-388 [» ]
2GVE neutron diffraction 2.20 A 1-388 [» ]
2XIS X-ray 1.71 A 2-388 [» ]
3CWH neutron diffraction 2.20 A 1-388 [» ]
3GNX X-ray 2.00 A/E 2-388 [» ]
3KBJ X-ray 2.00 A 1-388 [» ]
3KBM X-ray 2.00 A 1-388 [» ]
3KBN X-ray 1.53 A 1-388 [» ]
3KBS X-ray 1.80 A 1-388 [» ]
3KBV X-ray 1.80 A 1-388 [» ]
3KBW X-ray 1.60 A 1-388 [» ]
3KCJ Other 1.80 A 1-388 [» ]
3KCL Other 2.00 A 1-388 [» ]
3KCO Other 1.80 A 1-388 [» ]
3N4A X-ray 1.94 A 2-388 [» ]
3QYS X-ray 1.85 A 1-388 [» ]
3QZA Other 2.00 A 1-388 [» ]
3U3H X-ray 0.97 A 1-388 [» ]
3XIS X-ray 1.60 A 2-388 [» ]
4A8I X-ray 0.95 A 1-388 [» ]
4A8L X-ray 1.35 A 1-388 [» ]
4A8N X-ray 1.20 A 1-388 [» ]
4A8R X-ray 1.42 A 1-388 [» ]
4DUO X-ray 2.00 A 1-388 [» ]
4DVO Other 2.00 A 1-388 [» ]
4E3V X-ray 1.50 A 1-388 [» ]
4J4K X-ray 1.90 A 1-388 [» ]
4LNC Other 2.19 A 1-388 [» ]
4QDP Other 2.00 A 1-388 [» ]
4QDW Other 1.80 A 1-388 [» ]
4QE1 X-ray 1.55 A 1-388 [» ]
4QE4 X-ray 1.70 A 1-388 [» ]
4QE5 X-ray 1.56 A 1-388 [» ]
4QEE X-ray 1.60 A 1-388 [» ]
4QEH X-ray 1.55 A 1-388 [» ]
4XIS X-ray 1.60 A 2-388 [» ]
8XIA X-ray 1.90 A 1-388 [» ]
9XIA X-ray 1.90 A 1-388 [» ]
ProteinModelPortali P24300.
SMRi P24300. Positions 1-388.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-58982N.

Chemistry

DrugBanki DB00126. Vitamin C.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P24300.

Family and domain databases

Gene3Di 3.20.20.150. 1 hit.
HAMAPi MF_00455. Xylose_isom_A.
InterProi IPR013022. Xyl_isomerase-like_TIM-brl.
IPR013453. XylA_actinobac.
IPR001998. Xylose_isomerase.
[Graphical view ]
Pfami PF01261. AP_endonuc_2. 1 hit.
[Graphical view ]
PRINTSi PR00688. XYLOSISMRASE.
SUPFAMi SSF51658. SSF51658. 1 hit.
TIGRFAMsi TIGR02631. xylA_Arthro. 1 hit.
PROSITEi PS51415. XYLOSE_ISOMERASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: October 29, 2014
This is version 110 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