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
Thermotoga neapolitana
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

D-xylopyranose = D-xylulose.

Cofactori

Co2+Note: Binds 2 cobalt ions per subunit.

pH dependencei

Optimum pH is 7.1.

Temperature dependencei

Optimum temperature is above 95 degrees Celsius. Extremely thermostable.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei101 – 1011
Active sitei104 – 1041By similarity
Metal bindingi232 – 2321Cobalt 1
Metal bindingi268 – 2681Cobalt 1
Metal bindingi268 – 2681Cobalt 2
Metal bindingi271 – 2711Cobalt 2
Metal bindingi296 – 2961Cobalt 1
Metal bindingi307 – 3071Cobalt 2
Metal bindingi309 – 3091Cobalt 2
Metal bindingi339 – 3391Cobalt 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

Cobalt, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Xylose isomerase (EC:5.3.1.5)
Gene namesi
Name:xylA
OrganismiThermotoga neapolitana
Taxonomic identifieri2337 [NCBI]
Taxonomic lineageiBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 444444Xylose isomerasePRO_0000195814Add
BLAST

Interactioni

Subunit structurei

Homotetramer.

Protein-protein interaction databases

STRINGi309803.CTN_0720.

Structurei

Secondary structure

1
444
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi23 – 264Combined sources
Helixi38 – 425Combined sources
Beta strandi45 – 473Combined sources
Helixi48 – 514Combined sources
Helixi68 – 703Combined sources
Helixi75 – 9319Combined sources
Beta strandi97 – 1015Combined sources
Helixi102 – 1054Combined sources
Helixi112 – 13221Combined sources
Beta strandi136 – 1416Combined sources
Beta strandi145 – 1473Combined sources
Helixi148 – 1503Combined sources
Helixi160 – 17920Combined sources
Beta strandi183 – 1875Combined sources
Beta strandi192 – 1954Combined sources
Helixi202 – 22221Combined sources
Beta strandi227 – 2315Combined sources
Beta strandi237 – 2448Combined sources
Helixi247 – 25610Combined sources
Helixi260 – 2623Combined sources
Beta strandi263 – 2686Combined sources
Helixi269 – 2746Combined sources
Helixi279 – 28810Combined sources
Beta strandi292 – 2965Combined sources
Beta strandi304 – 3063Combined sources
Helixi315 – 32814Combined sources
Beta strandi336 – 3383Combined sources
Helixi349 – 37628Combined sources
Helixi378 – 3869Combined sources
Helixi388 – 3903Combined sources
Helixi393 – 4008Combined sources
Helixi405 – 4128Combined sources
Helixi425 – 44117Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1A0EX-ray2.70A/D2-444[»]
ProteinModelPortaliP45687.
SMRiP45687. Positions 2-444.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP45687.

Family & Domainsi

Sequence similaritiesi

Belongs to the xylose isomerase family.Curated

Phylogenomic databases

eggNOGiENOG4105C93. Bacteria.
COG2115. LUCA.

Family and domain databases

Gene3Di3.20.20.150. 1 hit.
HAMAPiMF_00455. Xylose_isom_A.
InterProiIPR013022. Xyl_isomerase-like_TIM-brl.
IPR013452. Xylose_isom_bac.
IPR001998. Xylose_isomerase.
[Graphical view]
PfamiPF01261. AP_endonuc_2. 1 hit.
[Graphical view]
PRINTSiPR00688. XYLOSISMRASE.
SUPFAMiSSF51658. SSF51658. 1 hit.
TIGRFAMsiTIGR02630. xylose_isom_A. 1 hit.
PROSITEiPS51415. XYLOSE_ISOMERASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P45687-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAEFFPEIPK VQFEGKESTN PLAFKFYDPE EIIDGKPLKD HLKFSVAFWH
60 70 80 90 100
TFVNEGRDPF GDPTADRPWN RYTDPMDKAF ARVDALFEFC EKLNIEYFCF
110 120 130 140 150
HDRDIAPEGK TLRETNKILD KVVERIKERM KDSNVKLLWG TANLFSHPRY
160 170 180 190 200
MHGAATTCSA DVFAYAAAQV KKALEITKEL GGEGYVFWGG REGYETLLNT
210 220 230 240 250
DLGFELENLA RFLRMAVDYA KRIGFTGQFL IEPKPKEPTK HQYDFDVATA
260 270 280 290 300
YAFLKSHGLD EYFKFNIEAN HATLAGHTFQ HELRMARILG KLGSIDANQG
310 320 330 340 350
DLLLGWDTDQ FPTNVYDTTL AMYEVIKAGG FTKGGLNFDA KVRRASYKVE
360 370 380 390 400
DLFIGHIAGM DTFALGFKVA YKLVKDGVLD KFIEEKYRSF REGIGRDIVE
410 420 430 440
GKVDFEKLEE YIIDKETIEL PSGKQEYLES LINSYIVKTI LELR
Length:444
Mass (Da):50,893
Last modified:November 1, 1995 - v1
Checksum:i21F606C4D5F68D0B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L38994 Genomic DNA. Translation: AAB06798.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L38994 Genomic DNA. Translation: AAB06798.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1A0EX-ray2.70A/D2-444[»]
ProteinModelPortaliP45687.
SMRiP45687. Positions 2-444.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi309803.CTN_0720.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4105C93. Bacteria.
COG2115. LUCA.

Miscellaneous databases

EvolutionaryTraceiP45687.

Family and domain databases

Gene3Di3.20.20.150. 1 hit.
HAMAPiMF_00455. Xylose_isom_A.
InterProiIPR013022. Xyl_isomerase-like_TIM-brl.
IPR013452. Xylose_isom_bac.
IPR001998. Xylose_isomerase.
[Graphical view]
PfamiPF01261. AP_endonuc_2. 1 hit.
[Graphical view]
PRINTSiPR00688. XYLOSISMRASE.
SUPFAMiSSF51658. SSF51658. 1 hit.
TIGRFAMsiTIGR02630. xylose_isom_A. 1 hit.
PROSITEiPS51415. XYLOSE_ISOMERASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "xylA cloning and sequencing and biochemical characterization of xylose isomerase from Thermotoga neapolitana."
    Vieille C., Hess J.M.J., Kelly R.M., Zeikus J.G.J.
    Appl. Environ. Microbiol. 61:1867-1875(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: DSM 5068.
  2. Gallay O., Chopra R., Conti E., Brick P., Jackson R., Hartley B., Vieille C., Zeikus J.G., Blow D.
    Submitted (NOV-1997) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
    Strain: DSM 5068.

Entry informationi

Entry nameiXYLA_THENE
AccessioniPrimary (citable) accession number: P45687
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: November 11, 2015
This is version 98 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

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 one 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.