Reviewed, UniProtKB/Swiss-Prot P12070 (XYLA_ARTS7)

Names and origin

Protein names

Recommended name:
    Xylose isomerase
    EC=5.3.1.5

Gene names

Name:

xylA

Organism

Arthrobacter sp. (strain NRRL B3728)

Taxonomic identifier

1669 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Micrococcineae › Micrococcaceae › Arthrobacter

Protein attributes

Sequence length	395 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)

Catalytic activity	D-xylose = D-xylulose. HAMAP MF_00455
Cofactor	Binds 2 magnesium ions per subunit. HAMAP MF_00455
Subunit structure	Homotetramer. HAMAP MF_00455
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 Direct protein sequencing
Gene Ontology (GO)
Biological process	D-xylose metabolic process Inferred from electronic annotation. Source: HAMAP pentose-phosphate shunt Inferred from electronic annotation. Source: HAMAP
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	magnesium ion binding Inferred from electronic annotation. Source: HAMAP xylose isomerase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.2

Chain

2 – 395

394

Xylose isomerase HAMAP MF_00455

PRO_0000195760

Sites

Active site

54

1

Ref.3

Active site

57

1

Ref.3

Metal binding

181

1

Magnesium 1 HAMAP MF_00455

Metal binding

217

1

Magnesium 1 HAMAP MF_00455

Metal binding

217

1

Magnesium 2 HAMAP MF_00455

Metal binding

220

1

Magnesium 2 HAMAP MF_00455

Metal binding

245

1

Magnesium 1 HAMAP MF_00455

Metal binding

255

1

Magnesium 2 HAMAP MF_00455

Metal binding

257

1

Magnesium 2 HAMAP MF_00455

Metal binding

293

1

Magnesium 1 HAMAP MF_00455

Secondary structure

1

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395

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 – 128

20

Beta strand

132 – 136

5

Beta strand

142 – 145

4

Helix

146 – 148

3

Helix

151 – 172

22

Beta strand

177 – 180

4

Beta strand

184 – 193

10

Helix

196 – 203

8

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

Helix

265 – 277

13

Beta strand

290 – 292

3

Helix

302 – 328

27

Helix

330 – 338

9

Turn

339 – 342

4

Helix

343 – 345

3

Helix

355 – 360

6

Turn

362 – 367

6

Helix

370 – 373

4

Helix

380 – 391

12

Sequences

	Sequence		Length	Mass (Da)
	P12070-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: EA7A21FC47726369	FASTA	395	43,292
	10 20 30 40 50 60 MSVQPTPADH FTFGLWTVGW TGADPFGVAT RKNLDPVEAV HKLAELGAYG ITFHDNDLIP 70 80 90 100 110 120 FDATEAEREK ILGDFNQALK DTGLKVPMVT TNLFSHPVFK DGGFTSNDRS IRRFALAKVL 130 140 150 160 170 180 HNIDLAAEMG AETFVMWGGR EGSEYDGSKD LAAALDRMRE GVDTAAGYIK DKGYNLRIAL 190 200 210 220 230 240 EPKPNEPRGD IFLPTVGHGL AFIEQLEHGD IVGLNPETGH EQMAGLNFTH GIAQALWAEK 250 260 270 280 290 300 LFHIDLNGQR GIKYDQDLVF GHGDLTSAFF TVDLLENGFP NGGPKYTGPR HFDYKPSRTD 310 320 330 340 350 360 GYDGVWDSAK ANMSMYLLLK ERALAFRADP EVQEAMKTSG VFELGETTLN AGESAADLMN 370 380 390 DSASFAGFDA EAAAERNFAF IRLNQLAIEH LLGSR

References

[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: 1854339] [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: 1854338] [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: 2319597] [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: 2769749] [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: 3508294] [Abstract] Cited for: COMPARISON OF X-RAY STRUCTURES.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X59466 Genomic DNA. Translation: CAA42073.1.

PIR

S16214.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1DID	X-ray	2.50	A/B	2-394	[»]
1DIE	X-ray	2.50	A/B	2-394	[»]
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	2-394	[»]
4XIA	X-ray	2.30	A/B	3-395	[»]
5XIA	X-ray	2.50	A/B	3-395	[»]

ModBase

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.

TIGRFAMs

TIGR02631. xylA_Arthro. 1 hit.

PROSITE

PS51415. XYLOSE_ISOMERASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

XYLA_ARTS7

Accession

Primary (citable) accession number: P12070

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1989
Last sequence update:	January 23, 2007
Last modified:	February 9, 2010
This is version 87 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)