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Protein

Xylose isomerase

Gene

xylA

Organism
Streptomyces rubiginosus
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in D-xylose catabolism.

Catalytic activityi

D-xylopyranose = D-xylulose.

Cofactori

Mg2+By similarityNote: Binds 2 magnesium ions per subunit.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei541
Active sitei57By similarity1
Metal bindingi181Magnesium 11
Metal bindingi217Magnesium 11
Metal bindingi217Magnesium 21
Metal bindingi220Magnesium 21
Metal bindingi245Magnesium 11
Metal bindingi255Magnesium 21
Metal bindingi257Magnesium 21
Metal bindingi287Magnesium 11

GO - Molecular functioni

GO - Biological processi

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

BRENDAi5.3.1.5. 6089.

Names & Taxonomyi

Protein namesi
Recommended name:
Xylose isomerase (EC:5.3.1.5)
Gene namesi
Name:xylA
OrganismiStreptomyces rubiginosus
Taxonomic identifieri1929 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaStreptomycetalesStreptomycetaceaeStreptomyces

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Chemistry databases

DrugBankiDB01638. D-Sorbitol.
DB00126. Vitamin C.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved
ChainiPRO_00001958052 – 388Xylose isomeraseAdd BLAST387

Interactioni

Subunit structurei

Homotetramer.

Protein-protein interaction databases

DIPiDIP-58982N.

Structurei

Secondary structure

1388
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi7 – 9Combined sources3
Beta strandi11 – 14Combined sources4
Helixi15 – 18Combined sources4
Helixi36 – 45Combined sources10
Beta strandi50 – 54Combined sources5
Helixi55 – 58Combined sources4
Helixi65 – 82Combined sources18
Beta strandi85 – 90Combined sources6
Beta strandi94 – 96Combined sources3
Helixi97 – 99Combined sources3
Beta strandi103 – 105Combined sources3
Helixi109 – 128Combined sources20
Beta strandi132 – 136Combined sources5
Beta strandi142 – 146Combined sources5
Helixi151 – 172Combined sources22
Beta strandi177 – 180Combined sources4
Beta strandi184 – 193Combined sources10
Helixi196 – 203Combined sources8
Beta strandi206 – 208Combined sources3
Helixi209 – 211Combined sources3
Beta strandi212 – 214Combined sources3
Helixi218 – 222Combined sources5
Turni223 – 225Combined sources3
Helixi228 – 237Combined sources10
Beta strandi244 – 246Combined sources3
Beta strandi251 – 254Combined sources4
Beta strandi262 – 264Combined sources3
Helixi265 – 277Combined sources13
Beta strandi284 – 286Combined sources3
Helixi296 – 322Combined sources27
Helixi324 – 332Combined sources9
Helixi335 – 338Combined sources4
Helixi347 – 352Combined sources6
Helixi354 – 356Combined sources3
Turni357 – 359Combined sources3
Helixi362 – 367Combined sources6
Helixi372 – 384Combined sources13

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1GW9X-ray1.55A1-387[»]
1MNZX-ray0.99A1-388[»]
1O1HX-ray1.40A/B2-388[»]
1OADX-ray1.50A/B2-388[»]
1XIBX-ray1.60A1-388[»]
1XICX-ray1.60A1-388[»]
1XIDX-ray1.70A1-388[»]
1XIEX-ray1.70A1-388[»]
1XIFX-ray1.60A1-388[»]
1XIGX-ray1.70A1-388[»]
1XIHX-ray1.70A1-388[»]
1XIIX-ray1.70A1-388[»]
1XIJX-ray1.70A1-388[»]
1XISX-ray1.60A2-388[»]
2G4JX-ray1.85A2-388[»]
2GLKX-ray0.94A1-388[»]
2GUBX-ray1.80A1-388[»]
2GVEneutron diffraction2.20A1-388[»]
2XISX-ray1.71A2-388[»]
3CWHneutron diffraction2.20A1-388[»]
3GNXX-ray2.00A/E2-388[»]
3KBJX-ray2.00A1-388[»]
3KBMX-ray2.00A1-388[»]
3KBNX-ray1.53A1-388[»]
3KBSX-ray1.80A1-388[»]
3KBVX-ray1.80A1-388[»]
3KBWX-ray1.60A1-388[»]
3KCJOther1.80A1-388[»]
3KCLOther2.00A1-388[»]
3KCOOther1.80A1-388[»]
3N4AX-ray1.94A2-388[»]
3QYSX-ray1.85A1-388[»]
3QZAOther2.00A1-388[»]
3U3HX-ray0.97A1-388[»]
3XISX-ray1.60A2-388[»]
4A8IX-ray0.95A1-388[»]
4A8LX-ray1.35A1-388[»]
4A8NX-ray1.20A1-388[»]
4A8RX-ray1.42A1-388[»]
4DUOX-ray2.00A1-388[»]
4DVOOther2.00A1-388[»]
4E3VX-ray1.50A1-388[»]
4J4KX-ray1.90A1-388[»]
4LNCOther2.19A1-388[»]
4QDPOther2.00A1-388[»]
4QDWOther1.80A1-388[»]
4QE1X-ray1.55A1-388[»]
4QE4X-ray1.70A1-388[»]
4QE5X-ray1.56A1-388[»]
4QEEX-ray1.60A1-388[»]
4QEHX-ray1.55A1-388[»]
4US6X-ray1.20A/B1-388[»]
4W4QX-ray2.00A1-388[»]
4XISX-ray1.60A2-388[»]
4ZB0X-ray2.00A/B2-388[»]
4ZB2X-ray2.00A1-388[»]
4ZB5X-ray2.00A1-387[»]
4ZBCX-ray2.00A/B1-387[»]
5AVHX-ray0.90A2-387[»]
5AVNX-ray1.03A/B2-388[»]
5I7GX-ray1.21A1-388[»]
8XIAX-ray1.90A1-388[»]
9XIAX-ray1.90A1-388[»]
ProteinModelPortaliP24300.
SMRiP24300.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP24300.

Family & Domainsi

Sequence similaritiesi

Belongs to the xylose isomerase family.Curated

Phylogenomic databases

KOiK01805.

Family and domain databases

Gene3Di3.20.20.150. 1 hit.
HAMAPiMF_00455. Xylose_isom_A. 1 hit.
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.

P24300-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNYQPTPEDR FTFGLWTVGW QGRDPFGDAT RRALDPVESV RRLAELGAHG
60 70 80 90 100
VTFHDDDLIP FGSSDSEREE HVKRFRQALD DTGMKVPMAT TNLFTHPVFK
110 120 130 140 150
DGGFTANDRD VRRYALRKTI RNIDLAVELG AETYVAWGGR EGAESGGAKD
160 170 180 190 200
VRDALDRMKE AFDLLGEYVT SQGYDIRFAI EPKPNEPRGD ILLPTVGHAL
210 220 230 240 250
AFIERLERPE LYGVNPEVGH EQMAGLNFPH GIAQALWAGK LFHIDLNGQN
260 270 280 290 300
GIKYDQDLRF GAGDLRAAFW LVDLLESAGY SGPRHFDFKP PRTEDFDGVW
310 320 330 340 350
ASAAGCMRNY LILKERAAAF RADPEVQEAL RASRLDELAR PTAADGLQAL
360 370 380
LDDRSAFEEF DVDAAAARGM AFERLDQLAM DHLLGARG
Length:388
Mass (Da):43,227
Last modified:January 23, 2007 - v4
Checksum:i4C675184B62C97FB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M73789 Genomic DNA. Translation: AAA26838.1.
PIRiB41339.

Genome annotation databases

KEGGiag:AAA26838.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M73789 Genomic DNA. Translation: AAA26838.1.
PIRiB41339.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1GW9X-ray1.55A1-387[»]
1MNZX-ray0.99A1-388[»]
1O1HX-ray1.40A/B2-388[»]
1OADX-ray1.50A/B2-388[»]
1XIBX-ray1.60A1-388[»]
1XICX-ray1.60A1-388[»]
1XIDX-ray1.70A1-388[»]
1XIEX-ray1.70A1-388[»]
1XIFX-ray1.60A1-388[»]
1XIGX-ray1.70A1-388[»]
1XIHX-ray1.70A1-388[»]
1XIIX-ray1.70A1-388[»]
1XIJX-ray1.70A1-388[»]
1XISX-ray1.60A2-388[»]
2G4JX-ray1.85A2-388[»]
2GLKX-ray0.94A1-388[»]
2GUBX-ray1.80A1-388[»]
2GVEneutron diffraction2.20A1-388[»]
2XISX-ray1.71A2-388[»]
3CWHneutron diffraction2.20A1-388[»]
3GNXX-ray2.00A/E2-388[»]
3KBJX-ray2.00A1-388[»]
3KBMX-ray2.00A1-388[»]
3KBNX-ray1.53A1-388[»]
3KBSX-ray1.80A1-388[»]
3KBVX-ray1.80A1-388[»]
3KBWX-ray1.60A1-388[»]
3KCJOther1.80A1-388[»]
3KCLOther2.00A1-388[»]
3KCOOther1.80A1-388[»]
3N4AX-ray1.94A2-388[»]
3QYSX-ray1.85A1-388[»]
3QZAOther2.00A1-388[»]
3U3HX-ray0.97A1-388[»]
3XISX-ray1.60A2-388[»]
4A8IX-ray0.95A1-388[»]
4A8LX-ray1.35A1-388[»]
4A8NX-ray1.20A1-388[»]
4A8RX-ray1.42A1-388[»]
4DUOX-ray2.00A1-388[»]
4DVOOther2.00A1-388[»]
4E3VX-ray1.50A1-388[»]
4J4KX-ray1.90A1-388[»]
4LNCOther2.19A1-388[»]
4QDPOther2.00A1-388[»]
4QDWOther1.80A1-388[»]
4QE1X-ray1.55A1-388[»]
4QE4X-ray1.70A1-388[»]
4QE5X-ray1.56A1-388[»]
4QEEX-ray1.60A1-388[»]
4QEHX-ray1.55A1-388[»]
4US6X-ray1.20A/B1-388[»]
4W4QX-ray2.00A1-388[»]
4XISX-ray1.60A2-388[»]
4ZB0X-ray2.00A/B2-388[»]
4ZB2X-ray2.00A1-388[»]
4ZB5X-ray2.00A1-387[»]
4ZBCX-ray2.00A/B1-387[»]
5AVHX-ray0.90A2-387[»]
5AVNX-ray1.03A/B2-388[»]
5I7GX-ray1.21A1-388[»]
8XIAX-ray1.90A1-388[»]
9XIAX-ray1.90A1-388[»]
ProteinModelPortaliP24300.
SMRiP24300.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-58982N.

Chemistry databases

DrugBankiDB01638. D-Sorbitol.
DB00126. Vitamin C.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGiag:AAA26838.

Phylogenomic databases

KOiK01805.

Enzyme and pathway databases

BRENDAi5.3.1.5. 6089.

Miscellaneous databases

EvolutionaryTraceiP24300.

Family and domain databases

Gene3Di3.20.20.150. 1 hit.
HAMAPiMF_00455. Xylose_isom_A. 1 hit.
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]
ProtoNetiSearch...

Entry informationi

Entry nameiXYLA_STRRU
AccessioniPrimary (citable) accession number: P24300
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 124 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Caution

According to the crystallographic study residue 40 could be Gln.Curated

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.