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P12070

- XYLA_ARTS7

UniProt

P12070 - XYLA_ARTS7

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Protein
Xylose isomerase
Gene
xylA
Organism
Arthrobacter sp. (strain NRRL B3728)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

D-xylopyranose = D-xylulose.UniRule annotation

Cofactori

Binds 2 magnesium ions per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei54 – 5411 Publication
Active sitei57 – 5711 Publication
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 bindingi293 – 2931Magnesium 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

Enzyme and pathway databases

SABIO-RKP12070.

Names & Taxonomyi

Protein namesi
Recommended name:
Xylose isomerase (EC:5.3.1.5)
Gene namesi
Name:xylA
OrganismiArthrobacter sp. (strain NRRL B3728)
Taxonomic identifieri1669 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesMicrococcineaeMicrococcaceaeArthrobacter

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 395394Xylose isomeraseUniRule annotation
PRO_0000195760Add
BLAST

Interactioni

Subunit structurei

Homotetramer.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi7 – 93
Beta strandi11 – 144
Helixi15 – 184
Helixi36 – 4611
Beta strandi50 – 545
Helixi55 – 584
Helixi65 – 8218
Beta strandi88 – 903
Beta strandi94 – 963
Helixi97 – 993
Helixi109 – 12820
Beta strandi132 – 1365
Beta strandi142 – 1454
Helixi146 – 1483
Helixi151 – 17222
Beta strandi177 – 1804
Beta strandi184 – 19310
Helixi196 – 2038
Helixi209 – 2113
Beta strandi212 – 2143
Helixi218 – 2225
Turni223 – 2253
Helixi228 – 23710
Beta strandi251 – 2544
Helixi265 – 27713
Beta strandi290 – 2923
Helixi302 – 32827
Helixi330 – 3389
Turni339 – 3424
Helixi343 – 3453
Helixi355 – 3606
Turni362 – 3676
Helixi370 – 3734
Helixi380 – 39112

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DIDX-ray2.50A/B2-395[»]
1DIEX-ray2.50A/B2-395[»]
1XLAX-ray2.30A/B2-395[»]
1XLBX-ray2.50A/B2-395[»]
1XLCX-ray2.50A/B2-395[»]
1XLDX-ray2.50A/B2-395[»]
1XLEX-ray2.50A/B2-395[»]
1XLFX-ray2.50A/B2-395[»]
1XLGX-ray2.50A/B2-395[»]
1XLHX-ray2.50A/B2-395[»]
1XLIX-ray2.50A/B2-395[»]
1XLJX-ray2.50A/B2-395[»]
1XLKX-ray2.50A/B2-395[»]
1XLLX-ray2.50A/B2-395[»]
1XLMX-ray2.40A/B2-395[»]
4XIAX-ray2.30A/B3-395[»]
5XIAX-ray2.50A/B3-395[»]
ProteinModelPortaliP12070.
SMRiP12070. Positions 3-395.

Miscellaneous databases

EvolutionaryTraceiP12070.

Family & Domainsi

Sequence similaritiesi

Belongs to the xylose isomerase family.

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.

P12070-1 [UniParc]FASTAAdd to Basket

« Hide

MSVQPTPADH FTFGLWTVGW TGADPFGVAT RKNLDPVEAV HKLAELGAYG    50
ITFHDNDLIP FDATEAEREK ILGDFNQALK DTGLKVPMVT TNLFSHPVFK 100
DGGFTSNDRS IRRFALAKVL HNIDLAAEMG AETFVMWGGR EGSEYDGSKD 150
LAAALDRMRE GVDTAAGYIK DKGYNLRIAL EPKPNEPRGD IFLPTVGHGL 200
AFIEQLEHGD IVGLNPETGH EQMAGLNFTH GIAQALWAEK LFHIDLNGQR 250
GIKYDQDLVF GHGDLTSAFF TVDLLENGFP NGGPKYTGPR HFDYKPSRTD 300
GYDGVWDSAK ANMSMYLLLK ERALAFRADP EVQEAMKTSG VFELGETTLN 350
AGESAADLMN DSASFAGFDA EAAAERNFAF IRLNQLAIEH LLGSR 395
Length:395
Mass (Da):43,292
Last modified:January 23, 2007 - v3
Checksum:iEA7A21FC47726369
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X59466 Genomic DNA. Translation: CAA42073.1.
PIRiS16214.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X59466 Genomic DNA. Translation: CAA42073.1 .
PIRi S16214.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1DID X-ray 2.50 A/B 2-395 [» ]
1DIE X-ray 2.50 A/B 2-395 [» ]
1XLA X-ray 2.30 A/B 2-395 [» ]
1XLB X-ray 2.50 A/B 2-395 [» ]
1XLC X-ray 2.50 A/B 2-395 [» ]
1XLD X-ray 2.50 A/B 2-395 [» ]
1XLE X-ray 2.50 A/B 2-395 [» ]
1XLF X-ray 2.50 A/B 2-395 [» ]
1XLG X-ray 2.50 A/B 2-395 [» ]
1XLH X-ray 2.50 A/B 2-395 [» ]
1XLI X-ray 2.50 A/B 2-395 [» ]
1XLJ X-ray 2.50 A/B 2-395 [» ]
1XLK X-ray 2.50 A/B 2-395 [» ]
1XLL X-ray 2.50 A/B 2-395 [» ]
1XLM X-ray 2.40 A/B 2-395 [» ]
4XIA X-ray 2.30 A/B 3-395 [» ]
5XIA X-ray 2.50 A/B 3-395 [» ]
ProteinModelPortali P12070.
SMRi P12070. Positions 3-395.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

SABIO-RK P12070.

Miscellaneous databases

EvolutionaryTracei P12070.

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. "D-xylose (D-glucose) isomerase from Arthrobacter strain N.R.R.L. B3728. Gene cloning, sequence and expression."
    Loviny-Anderton T., Shaw P.C., Shin M.K., Hartley B.S.
    Biochem. J. 277:263-271(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "D-xylose (D-glucose) isomerase from Arthrobacter strain N.R.R.L. B3728. Purification and properties."
    Smith C.A., Rangarajan M., Hartley B.S.
    Biochem. J. 277:255-261(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-21, CHARACTERIZATION.
  3. "Mechanism for aldose-ketose interconversion by D-xylose isomerase involving ring opening followed by a 1,2-hydride shift."
    Collyer C.A., Henrick K., Blow D.M.
    J. Mol. Biol. 212:211-235(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACTIVE SITES HIS-54 AND ASP-57.
  4. "Structures of D-xylose isomerase from Arthrobacter strain B3728 containing the inhibitors xylitol and D-sorbitol at 2.5-A and 2.3-A resolution, respectively."
    Henrick K., Collyer C.A., Blow D.M.
    J. Mol. Biol. 208:129-157(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
  5. "Comparison of backbone structures of glucose isomerase from Streptomyces and Arthrobacter."
    Henrick K., Blow D.M., Carell H.L., Glusker J.P.
    Protein Eng. 1:467-469(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: COMPARISON OF X-RAY STRUCTURES.

Entry informationi

Entry nameiXYLA_ARTS7
AccessioniPrimary (citable) accession number: P12070
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 101 of the entry and version 3 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

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