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P19148

- XYLA_THETU

UniProt

P19148 - XYLA_THETU

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Protein

Xylose isomerase

Gene

xylA

Organism
Thermoanaerobacterium thermosulfurigenes (Clostridium thermosulfurogenes)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

Catalytic activityi

D-xylopyranose = D-xylulose.

Cofactori

Binds 2 cobalt ions per subunit.

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

  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

Cobalt, Metal-binding

Enzyme and pathway databases

SABIO-RKP19148.

Names & Taxonomyi

Protein namesi
Recommended name:
Xylose isomerase (EC:5.3.1.5)
Gene namesi
Name:xylA
OrganismiThermoanaerobacterium thermosulfurigenes (Clostridium thermosulfurogenes)
Taxonomic identifieri33950 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaThermoanaerobacteralesThermoanaerobacterales Family III. Incertae SedisThermoanaerobacterium

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi101 – 1011H → F: Abolishes activity.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 439439Xylose isomerasePRO_0000195817Add
BLAST

Interactioni

Subunit structurei

Homotetramer.

Structurei

Secondary structure

1
439
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi21 – 266
Helixi38 – 425
Beta strandi44 – 474
Helixi48 – 525
Helixi68 – 714
Helixi75 – 9319
Beta strandi96 – 1016
Helixi102 – 1054
Helixi112 – 13019
Beta strandi136 – 1416
Beta strandi145 – 1473
Helixi148 – 1503
Helixi160 – 17920
Beta strandi183 – 1875
Beta strandi192 – 1954
Helixi197 – 1993
Helixi202 – 22221
Beta strandi227 – 2315
Beta strandi237 – 2448
Helixi247 – 25610
Turni260 – 2623
Beta strandi263 – 2686
Helixi269 – 2746
Helixi279 – 28810
Beta strandi292 – 2965
Beta strandi304 – 3063
Helixi315 – 32713
Beta strandi336 – 3383
Helixi350 – 37526
Helixi378 – 3869
Helixi388 – 3903
Helixi393 – 3997
Helixi405 – 41410
Helixi425 – 43612

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1A0CX-ray2.50A/B/C/D2-439[»]
ProteinModelPortaliP19148.
SMRiP19148. Positions 2-438.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP19148.

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.
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.

P19148-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MNKYFENVSK IKYEGPKSNN PYSFKFYNPE EVIDGKTMEE HLRFSIAYWH
60 70 80 90 100
TFTADGTDQF GKATMQRPWN HYTDPMDIAK ARVEAAFEFF DKINAPYFCF
110 120 130 140 150
HDRDIAPEGD TLRETNKNLD TIVAMIKDYL KTSKTKVLWG TANLFSNPRF
160 170 180 190 200
VHGASTSCNA DVFAYSAAQV KKALEITKEL GGENYVFWGG REGYETLLNT
210 220 230 240 250
DMEFELDNFA RFLHMAVDYA KEIGFEGQFL IEPKPKEPTK HQYDFDVANV
260 270 280 290 300
LAFLRKYDLD KYFKVNIEAN HATLAFHDFQ HELRYARING VLGSIDANTG
310 320 330 340 350
DMLLGWDTDQ FPTDIRMTTL AMYEVIKMGG FDKGGLNFDA KVRRASFEPE
360 370 380 390 400
DLFLGHIAGM DAFAKGFKVA YKLVKDRVFD KFIEERYASY KDGIGADIVS
410 420 430
GKADFRSLEK YALERSQIVN KSGRQELLES ILNQYLFAE
Length:439
Mass (Da):50,475
Last modified:November 1, 1990 - v1
Checksum:i55A227DBDD0EECB9
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J05650 Genomic DNA. Translation: AAA23285.1.
PIRiA36598. ISCLXM.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J05650 Genomic DNA. Translation: AAA23285.1 .
PIRi A36598. ISCLXM.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1A0C X-ray 2.50 A/B/C/D 2-439 [» ]
ProteinModelPortali P19148.
SMRi P19148. Positions 2-438.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

SABIO-RK P19148.

Miscellaneous databases

EvolutionaryTracei P19148.

Family and domain databases

Gene3Di 3.20.20.150. 1 hit.
HAMAPi MF_00455. Xylose_isom_A.
InterProi IPR013022. Xyl_isomerase-like_TIM-brl.
IPR013452. Xylose_isom_bac.
IPR001998. Xylose_isomerase.
[Graphical view ]
Pfami PF01261. AP_endonuc_2. 1 hit.
[Graphical view ]
PRINTSi PR00688. XYLOSISMRASE.
SUPFAMi SSF51658. SSF51658. 1 hit.
TIGRFAMsi TIGR02630. xylose_isom_A. 1 hit.
PROSITEi PS51415. XYLOSE_ISOMERASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Catalytic mechanism of xylose (glucose) isomerase from Clostridium thermosulfurogenes. Characterization of the structural gene and function of active site histidine."
    Lee C.Y., Bagdasarian M., Meng M.H., Zeikus J.G.
    J. Biol. Chem. 265:19082-19090(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 33743 / DSM 2229 / 4B.
  2. "Purification and characterization of thermostable glucose isomerase from Clostridium thermosulfurogenes and Thermoanaerobacter strain B6A."
    Lee C.Y., Zeikus J.G.
    Biochem. J. 273:565-571(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-7.
  3. 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 (2.5 ANGSTROMS).
    Strain: ATCC 33743 / DSM 2229 / 4B.

Entry informationi

Entry nameiXYLA_THETU
AccessioniPrimary (citable) accession number: P19148
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1990
Last modified: October 29, 2014
This is version 94 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, Direct protein sequencing

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