Skip Header

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

P56681

- XYLA_THECA

UniProt

P56681 - XYLA_THECA

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Xylose isomerase

Gene

xylA

Organism
Thermus caldophilus
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli

Functioni

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 sitei53 – 531By similarity
Active sitei56 – 561By similarity
Metal bindingi180 – 1801Magnesium 1By similarity
Metal bindingi216 – 2161Magnesium 1By similarity
Metal bindingi216 – 2161Magnesium 2By similarity
Metal bindingi219 – 2191Magnesium 2By similarity
Metal bindingi244 – 2441Magnesium 1By similarity
Metal bindingi254 – 2541Magnesium 2By similarity
Metal bindingi256 – 2561Magnesium 2By similarity
Metal bindingi286 – 2861Magnesium 1By similarity

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
OrganismiThermus caldophilus
Taxonomic identifieri272 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 387387Xylose isomerasePRO_0000195811Add
BLAST

Interactioni

Subunit structurei

Homotetramer.

Structurei

Secondary structure

1
387
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi6 – 83Combined sources
Beta strandi10 – 134Combined sources
Helixi14 – 174Combined sources
Helixi35 – 4511Combined sources
Beta strandi48 – 536Combined sources
Helixi54 – 574Combined sources
Helixi64 – 8118Combined sources
Beta strandi87 – 893Combined sources
Beta strandi93 – 953Combined sources
Helixi96 – 983Combined sources
Helixi108 – 12720Combined sources
Beta strandi132 – 1354Combined sources
Beta strandi141 – 1433Combined sources
Helixi145 – 1473Combined sources
Helixi149 – 1513Combined sources
Helixi153 – 17119Combined sources
Beta strandi176 – 1794Combined sources
Beta strandi183 – 19210Combined sources
Helixi195 – 2028Combined sources
Beta strandi205 – 2073Combined sources
Helixi208 – 2103Combined sources
Beta strandi211 – 2133Combined sources
Helixi217 – 2215Combined sources
Turni222 – 2243Combined sources
Helixi227 – 23711Combined sources
Beta strandi243 – 2453Combined sources
Beta strandi250 – 2534Combined sources
Helixi264 – 27613Combined sources
Beta strandi283 – 2853Combined sources
Helixi295 – 32127Combined sources
Helixi323 – 33210Combined sources
Turni337 – 3393Combined sources
Helixi340 – 3423Combined sources
Beta strandi343 – 3453Combined sources
Helixi348 – 3569Combined sources
Helixi361 – 3655Combined sources
Helixi371 – 38212Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BXCX-ray2.30A/B/C/D1-387[»]
ProteinModelPortaliP56681.
SMRiP56681. Positions 1-387.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP56681.

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.

P56681-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MYEPKPEHRF TFGLWTVGNV GRDPFGDAVR ERLDPVYVGH KLAELGVHGV
60 70 80 90 100
NLHDEDLIPR GTPPAERDQI VRRFKRALDE TGLKVPMVTG NLFSDPGFKD
110 120 130 140 150
GGFTSRDPWV RAYAFRKSLE TMDLGAELGA EIYVVWPGRE GAEVEATGKA
160 170 180 190 200
RKVWDWVREP LNFMAAYAED QGYGYRFALE PKPNEPRGDI YFATVGSMLA
210 220 230 240 250
LIHTLERPER FGLNPEFAHE TMAGLNFVHA VAQALDAGKL LHIDLNGQRM
260 270 280 290 300
NRFDQDLRFG SENLKAAFLL VDLLESSGYQ GPRHFDAHAL RTEDEEGVWA
310 320 330 340 350
FARGCMRTYL ILKERAEAFR EDPEVKELLA AYYQEDPAAL PLMDPYSHEK
360 370 380
AEALKRAELP LEAKRHRGYA LERLDQLAVE YLLGVRG
Length:387
Mass (Da):43,860
Last modified:July 15, 1999 - v1
Checksum:i28FB6568BA758065
GO

Cross-referencesi

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1BXC X-ray 2.30 A/B/C/D 1-387 [» ]
ProteinModelPortali P56681.
SMRi P56681. Positions 1-387.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P56681.

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. "A thermostable xylose isomerase from Thermus caldophilus: biochemical characterization, crystallization and preliminary X-ray analysis."
    Chang C., Song H.K., Park B.C., Lee D.-S., Suh S.W.
    Acta Crystallogr. D 55:294-296(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: CRYSTALLIZATION, CHARACTERIZATION.
    Strain: GK24.
  2. "Crystal structures of thermostable xylose isomerases from Thermus caldophilus and Thermus thermophilus: possible structural determinants of thermostability."
    Chang C., Park B.C., Lee D.-S., Suh S.W.
    J. Mol. Biol. 288:623-634(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
    Strain: GK24.

Entry informationi

Entry nameiXYLA_THECA
AccessioniPrimary (citable) accession number: P56681
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: July 15, 1999
Last modified: November 26, 2014
This is version 78 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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