P15587 (XYLA_STROL) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Xylose isomerase
EC=5.3.1.5

Gene names

Name:

xylA

Organism

Streptomyces olivochromogenes

Taxonomic identifier

1963 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Streptomycineae › Streptomycetaceae › Streptomyces

Protein attributes

Sequence length	387 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Involved in D-xylose catabolism. HAMAP MF_00455
Catalytic activity	D-xylose = D-xylulose. HAMAP MF_00455
Cofactor	Binds 2 magnesium ions per subunit By similarity. HAMAP MF_00455
Subunit structure	Homotetramer.
Subcellular location	Cytoplasm HAMAP MF_00455.
Sequence similarities	Belongs to the xylose isomerase family.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Pentose shunt Xylose metabolism
Cellular component	Cytoplasm
Ligand	Magnesium Metal-binding
Molecular function	Isomerase
Technical term	3D-structure
Gene Ontology (GO)
Biological process	D-xylose metabolic process Inferred from electronic annotation. Source: UniProtKB-KW pentose-phosphate shunt Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW xylose isomerase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed HAMAP MF_00455

Chain

2 – 387

386

Xylose isomerase HAMAP MF_00455

PRO_0000195803

Sites

Active site

54

1

By similarity

Active site

57

1

By similarity

Metal binding

181

1

Magnesium 1

Metal binding

217

1

Magnesium 1

Metal binding

217

1

Magnesium 2

Metal binding

220

1

Magnesium 2

Metal binding

245

1

Magnesium 1

Metal binding

255

1

Magnesium 2

Metal binding

257

1

Magnesium 2

Metal binding

287

1

Magnesium 1

Secondary structure

1

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387

Helix Strand Turn

Details...

Helix

7 – 9

3

Beta strand

11 – 14

4

Helix

15 – 18

4

Helix

36 – 46

11

Beta strand

50 – 54

5

Helix

55 – 58

4

Helix

65 – 82

18

Beta strand

88 – 90

3

Beta strand

94 – 96

3

Helix

97 – 99

3

Helix

109 – 129

21

Beta strand

132 – 136

5

Beta strand

142 – 145

4

Helix

151 – 172

22

Beta strand

177 – 180

4

Beta strand

184 – 193

10

Helix

196 – 203

8

Beta strand

206 – 208

3

Helix

209 – 211

3

Beta strand

212 – 214

3

Helix

218 – 222

5

Turn

223 – 225

3

Helix

228 – 237

10

Beta strand

251 – 254

4

Beta strand

262 – 264

3

Helix

265 – 278

14

Beta strand

284 – 286

3

Helix

296 – 322

27

Helix

324 – 332

9

Helix

335 – 338

4

Helix

347 – 352

6

Helix

354 – 356

3

Turn

357 – 359

3

Helix

362 – 367

6

Helix

372 – 383

12

Sequences

	Sequence		Length	Mass (Da)
	P15587 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 83CCE206015B178D	FASTA	387	42,923
	10 20 30 40 50 60 MSYQPTPEDR FTFGLWTVGW QGRDPFGDAT RPALDPVETV QRLAELGAHG VTFHDDDLIP 70 80 90 100 110 120 FGSSDTERES HIKRFRQALD ATGMTVPMAT TNLFTHPVFK DGGFTANDRD VRRYALRKTI 130 140 150 160 170 180 RNIDLAVELG AKTYVAWGGR EGAESGAAKD VRVALDRMKE AFDLLGEYVT SQGYDTRFAI 190 200 210 220 230 240 EPKPNEPRGD ILLPTVGHAL AFIERLERPE LYGVNPEVGH EQMAGLNFPH GIAQALWAGK 250 260 270 280 290 300 LFHIDLNGQS GIKYDQDLRF GAGDLRAAFW LVDLLESAGY EGPRHFDFKP PRTEDIDGVW 310 320 330 340 350 360 ASAAGCMRNY LILKERAAAF RADPEVQEAL RASRLDELAQ PTAADGVQEL LADRTAFEDF 370 380 DVDAAAARGM AFERLDQLAM DHLLGAR

References

[1]	"X-ray crystallographic structures of D-xylose isomerase-substrate complexes position the substrate and provide evidence for metal movement during catalysis." Lavie A., Allen K., Petsko G.A., Ringe D. Biochemistry 33:5469-5480(1994) [PubMed: 8180169] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], X-RAY CRYSTALLOGRAPHY (1.81 ANGSTROMS).
[2]	"Crystallographic studies of the mechanism of xylose isomerase." Farber G.K., Glasfeld A., Tiraby G., Ringe D., Petsko G.A. Biochemistry 28:7289-7297(1989) [PubMed: 2510821] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
[3]	"The 3.0 A crystal structure of xylose isomerase from Streptomyces olivochromogenes." Farber G.K., Petsko G.A., Ringe D. Protein Eng. 1:459-466(1987) [PubMed: 3508293] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

PIR

S28986.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1MUW	X-ray	0.86	A	2-386	[»]
1S5M	X-ray	0.98	A	2-386	[»]
1S5N	X-ray	0.95	A	2-386	[»]
1XYA	X-ray	1.81	A/B	2-387	[»]
1XYB	X-ray	1.96	A/B	2-387	[»]
1XYC	X-ray	2.19	A/B	2-387	[»]
1XYL	X-ray	1.80	A/B	2-386	[»]
1XYM	X-ray	1.80	A/B	2-386	[»]
2GYI	X-ray	1.60	A/B	2-386	[»]

ProteinModelPortal

P15587.

SMR

P15587. Positions 2-387.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

HAMAP

MF_00455. Xylose_isom_A.
[Tree]

InterPro

IPR013022. Xyl_isomerase-like_TIM-brl.
IPR012307. Xyl_isomerase_TIM-brl.
IPR013453. XylA_actinobac.
IPR001998. Xylose_isomerase.
[Graphical view]

Gene3D

G3DSA:3.20.20.150. Xyl_isomerase-like_TIM-brl. 1 hit.

Pfam

PF01261. AP_endonuc_2. 1 hit.
[Graphical view]

PRINTS

PR00688. XYLOSISMRASE.

SUPFAM

SSF51658. Xyl_isomerase-like_TIM-brl. 1 hit.

TIGRFAMs

TIGR02631. XylA_Arthro. 1 hit.

PROSITE

PS51415. XYLOSE_ISOMERASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

XYLA_STROL

Accession

Primary (citable) accession number: P15587

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	January 23, 2007
Last modified:	May 31, 2011
This is version 88 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program