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
Escherichia coli (strain B / BL21-DE3)
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

Catalytic activityi

D-xylopyranose = D-xylulose.UniRule annotationSAAS annotation

Cofactori

Mg2+UniRule annotationNote: Binds 2 magnesium ions per subunit.UniRule annotation

Sites

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

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

IsomeraseUniRule annotation

Keywords - Biological processi

Carbohydrate metabolism, Pentose shuntUniRule annotation, Xylose metabolismUniRule annotation

Keywords - Ligandi

MagnesiumUniRule annotationSAAS annotation, Metal-bindingUniRule annotation

Names & Taxonomyi

Protein namesi
Recommended name:
Xylose isomeraseUniRule annotation (EC:5.3.1.5UniRule annotation)
Gene namesi
Name:xylAUniRule annotationImported
Ordered Locus Names:B21_03368Imported, ECBD_0169Imported, ECD_03417Imported
OrganismiEscherichia coli (strain B / BL21-DE3)Imported
Taxonomic identifieri469008 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000001509: Chromosome, UP000002032: Chromosome, UP000009074: Chromosome

Subcellular locationi

Cytoplasm UniRule annotationSAAS annotation

GO - Cellular componenti

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

Keywords - Cellular componenti

CytoplasmUniRule annotationSAAS annotation

Interactioni

Subunit structurei

Homotetramer.UniRule annotationSAAS annotation

Protein-protein interaction databases

STRINGi469008.ECBD_0169.

Structurei

3D structure databases

ProteinModelPortaliC6EEB3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the xylose isomerase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG2115.
HOGENOMiHOG000252293.
KOiK01805.
OMAiHTFQHEL.

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.

C6EEB3-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MQAYFDQLDR VRYEGSKSSN PLAFRHYNPD ELVLGKRMEE HLRFAACYWH
60 70 80 90 100
TFCWNGADMF GVGAFNRPWQ QPGEALALAK RKADVAFEFF HKLHVPFYCF
110 120 130 140 150
HDVDVSPEGA SLKEYINNFA QMVDVLAGKQ EESGVKLLWG TANCFTNPRY
160 170 180 190 200
GAGAATNPDP EVFSWAATQV VTAMEATHKL GGENYVLWGG REGYETLLNT
210 220 230 240 250
DLRQEREQLG RFMQMVVEHK HKIGFQGTLL IEPKPQEPTK HQYDYDAATV
260 270 280 290 300
YGFLKQFGLE KEIKLNIEAN HATLAGHSFH HEIATAIALG LFGSVDANRG
310 320 330 340 350
DAQLGWDTDQ FPNSVEENAL VMYEILKAGG FTTGGLNFDA KVRRQSTDKY
360 370 380 390 400
DLFYGHIGAM DTMALALKIA ARMIEDGELD KRIAQRYSGW NSELGQQILK
410 420 430 440
GQMSLADLAK YAQEHNLSPV HQSGRQEQLE NLVNHYLFDK
Length:440
Mass (Da):49,719
Last modified:September 1, 2009 - v1
Checksum:i6E21039B6EC0561F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001665 Genomic DNA. Translation: ACT27245.1.
CP001509 Genomic DNA. Translation: ACT45217.1.
AM946981 Genomic DNA. Translation: CAQ33885.1.
RefSeqiYP_003001115.1. NC_012892.2.
YP_003034430.1. NC_012947.1.
YP_003055988.1. NC_012971.2.

Genome annotation databases

EnsemblBacteriaiACT27245; ACT27245; ECBD_0169.
ACT45217; ACT45217; ECD_03417.
CAQ33885; CAQ33885; B21_03368.
GeneIDi8114364.
8157021.
8180956.
KEGGiebd:ECBD_0169.
ebe:B21_03368.
ebl:ECD_03417.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001665 Genomic DNA. Translation: ACT27245.1.
CP001509 Genomic DNA. Translation: ACT45217.1.
AM946981 Genomic DNA. Translation: CAQ33885.1.
RefSeqiYP_003001115.1. NC_012892.2.
YP_003034430.1. NC_012947.1.
YP_003055988.1. NC_012971.2.

3D structure databases

ProteinModelPortaliC6EEB3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi469008.ECBD_0169.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACT27245; ACT27245; ECBD_0169.
ACT45217; ACT45217; ECD_03417.
CAQ33885; CAQ33885; B21_03368.
GeneIDi8114364.
8157021.
8180956.
KEGGiebd:ECBD_0169.
ebe:B21_03368.
ebl:ECD_03417.

Phylogenomic databases

eggNOGiCOG2115.
HOGENOMiHOG000252293.
KOiK01805.
OMAiHTFQHEL.

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

« Hide 'large scale' publications
  1. "Sequencing and gene expression analysis of Escherichia coli BL21(DE3)."
    Krempl P.M., Mairhofer J., Eisenkolb M., Specht T., Leparc G.G., Kreil D.P., Bayer K., Striedner G.
    Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: BL21Imported.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: B / BL21-DE3 [Korea]Imported and BL21Imported.
  3. "Sequencing and gene expression analysis of Escherichia coli BL21."
    Leparc G., Striedner G., Bayer K., Kreil D., Krempl P.M.
    Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: B / BL21-DE3 [Austria]Imported.
  4. "Complete sequence of Escherichia coli 'BL21-Gold(DE3)pLysS AG'."
    US DOE Joint Genome Institute
    Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., LaButti K.M., Clum A., Larimer F., Land M., Hauser L., Kyrpides N., Anderson I., Sorek R., Rubin E.
    Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: BL21-GoldImported.
  5. "Complete sequence of Escherichia coli BL21(DE3)."
    Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., LaButti K.M., Clum A., Larimer F., Land M., Hauser L., Kyrpides N., Anderson I., Sorek R., Rubin E.
    Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: B / BL21-DE3 [JGI]Imported.
  6. Jeong H., Shim J.-H., Studier F.W., Oh T.K., Kim J.F.
    Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: BL21.

Entry informationi

Entry nameiC6EEB3_ECOBD
AccessioniPrimary (citable) accession number: C6EEB3
Secondary accession number(s): C5WAD8
Entry historyi
Integrated into UniProtKB/TrEMBL: September 1, 2009
Last sequence update: September 1, 2009
Last modified: February 4, 2015
This is version 44 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteomeImported

External Data

Dasty 3

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 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.