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P12851 (XYLA_ACTM4) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 107. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein attributes

Sequence length394 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

D-xylopyranose = D-xylulose. HAMAP-Rule MF_00455

Cofactor

Binds 2 magnesium ions per subunit.

Subunit structure

Homotetramer.

Subcellular location

Cytoplasm HAMAP-Rule MF_00455.

Sequence similarities

Belongs to the xylose isomerase family.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Pentose shunt
Xylose metabolism
   Cellular componentCytoplasm
   LigandMagnesium
Metal-binding
   Molecular functionIsomerase
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological_processD-xylose metabolic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

pentose-phosphate shunt

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionmagnesium ion binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

xylose isomerase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed HAMAP-Rule MF_00455
Chain2 – 394393Xylose isomerase HAMAP-Rule MF_00455
PRO_0000195757

Sites

Active site541
Active site571 By similarity
Metal binding1811Magnesium 1
Metal binding2171Magnesium 1
Metal binding2171Magnesium 2
Metal binding2201Magnesium 2
Metal binding2451Magnesium 1
Metal binding2551Magnesium 2
Metal binding2571Magnesium 2
Metal binding2921Magnesium 1

Secondary structure

..................................................................... 394
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P12851 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 764B1FC35AE7A780

FASTA39443,499
        10         20         30         40         50         60 
MSVQATREDK FSFGLWTVGW QARDAFGDAT RTALDPVEAV HKLAEIGAYG ITFHDDDLVP 

        70         80         90        100        110        120 
FGSDAQTRDG IIAGFKKALD ETGLIVPMVT TNLFTHPVFK DGGFTSNDRS VRRYAIRKVL 

       130        140        150        160        170        180 
RQMDLGAELG AKTLVLWGGR EGAEYDSAKD VSAALDRYRE ALNLLAQYSE DRGYGLRFAI 

       190        200        210        220        230        240 
EPKPNEPRGD ILLPTAGHAI AFVQELERPE LFGINPETGH EQMSNLNFTQ GIAQALWHKK 

       250        260        270        280        290        300 
LFHIDLNGQH GPKFDQDLVF GHGDLLNAFS LVDLLENGPD GAPAYDGPRH FDYKPSRTED 

       310        320        330        340        350        360 
YDGVWESAKA NIRMYLLLKE RAKAFRADPE VQEALAASKV AELKTPTLNP GEGYAELLAD 

       370        380        390 
RSAFEDYDAD AVGAKGFGFV KLNQLAIEHL LGAR 

« Hide

References

« Hide 'large scale' references
[1]"Xylose isomerase from Actinoplanes missouriensis: primary structure of the gene and the protein."
Amore R., Hollenberg C.P.
Nucleic Acids Res. 17:7515-7515(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 14538 / DSM 43046 / CBS 188.64 / JCM 3121 / NCIMB 12654 / NBRC 102363 / 431.
[2]"Complete genome sequence of Actinoplanes missouriensis 431 (= NBRC 102363)."
Ohnishi Y., Ishikawa J., Sekine M., Hosoyama A., Harada T., Narita H., Hata T., Konno Y., Tutikane K., Fujita N., Horinouchi S., Hayakawa M.
Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 14538 / DSM 43046 / CBS 188.64 / JCM 3121 / NCIMB 12654 / NBRC 102363 / 431.
[3]"Structural analysis of the 2.8 A model of Xylose isomerase from Actinoplanes missouriensis."
Rey F., Jenkins J., Janin J., Lasters I., Alard P., Claessens M., Matthyssens G., Wodak S.J.
Proteins 4:165-172(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
[4]"Protein engineering of xylose (glucose) isomerase from Actinoplanes missouriensis. 1. Crystallography and site-directed mutagenesis of metal binding sites."
Jenkins J., Janin J., Rey F., Chiadmi M., van Tilbeurgh H., Lasters I., de Maeyer M., van Belle D., Wodak S.J., Lauwereys M., Stanssens P., Mrabet N.T., Snauwaert J., Matthyssens G., Lambeir A.-M.
Biochemistry 31:5449-5458(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
[5]"Multiwavelength anomalous solvent contrast (MASC): derivation of envelope structure-factor amplitudes and comparison with model values."
Ramin M., Shepard W., Fourme R., Kahn R.
Acta Crystallogr. D 55:157-167(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (4.1 ANGSTROMS).
[6]"Protein engineering of xylose (glucose) isomerase from Actinoplanes missouriensis. 2. Site-directed mutagenesis of the xylose binding site."
Lambeir A.-M., Lauwereys M., Stanssens P., Mrabet N.T., Snauwaert J., van Tilbeurgh H., Matthyssens G., Lasters I., de Maeyer M., Wodak S.J., Jenkins J., Chiadmi M., Janin J.
Biochemistry 31:5459-5466(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS.
[7]"Protein engineering of xylose (glucose) isomerase from Actinoplanes missouriensis. 3. Changing metal specificity and the pH profile by site-directed mutagenesis."
van Tilbeurgh H., Jenkins J., Chiadmi M., Janin J., Wodak S.J., Mrabet N.T., Lambeir A.-M.
Biochemistry 31:5467-5472(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X16042 Genomic DNA. Translation: CAA34164.1.
AP012319 Genomic DNA. Translation: BAL86255.1.
PIRISMAXM. S05998.
RefSeqYP_005460771.1. NC_017093.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BHWX-ray4.10A/B/C/D2-394[»]
1XIMX-ray2.20A/B/C/D2-394[»]
1XINX-ray2.40A/B/C/D2-394[»]
2XIMX-ray2.30A/B/C/D2-394[»]
2XINX-ray2.30A/B/C/D2-394[»]
3XIMX-ray2.30A/B/C/D2-394[»]
3XINX-ray2.30A/B/C/D2-394[»]
4XIMX-ray2.30A/B/C/D2-394[»]
5XIMX-ray2.60A/B/C/D2-394[»]
5XINX-ray2.30A/B/C/D2-394[»]
6XIMX-ray2.50A/B/C/D2-394[»]
7XIMX-ray2.40A/B/C/D2-394[»]
8XIMX-ray2.40A/B/C/D2-394[»]
9XIMX-ray2.40A/B/C/D2-394[»]
ProteinModelPortalP12851.
SMRP12851. Positions 3-394.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAL86255; BAL86255; AMIS_10350.
GeneID12051265.
KEGGams:AMIS_10350.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK01805.
OMADLIPIDA.

Enzyme and pathway databases

BioCycAMIS512565:GL7J-1062-MONOMER.
SABIO-RKP12851.

Family and domain databases

Gene3D3.20.20.150. 1 hit.
HAMAPMF_00455. Xylose_isom_A.
InterProIPR013022. Xyl_isomerase-like_TIM-brl.
IPR013453. XylA_actinobac.
IPR001998. Xylose_isomerase.
[Graphical view]
PfamPF01261. AP_endonuc_2. 1 hit.
[Graphical view]
PRINTSPR00688. XYLOSISMRASE.
SUPFAMSSF51658. SSF51658. 1 hit.
TIGRFAMsTIGR02631. xylA_Arthro. 1 hit.
PROSITEPS51415. XYLOSE_ISOMERASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP12851.

Entry information

Entry nameXYLA_ACTM4
AccessionPrimary (citable) accession number: P12851
Secondary accession number(s): I0GZR8
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 107 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references