Reviewed, UniProtKB/Swiss-Prot P12851 (XYLA_ACTMI)

Names and origin

Protein names

Recommended name:
    Xylose isomerase
    EC=5.3.1.5

Gene names

Name:	xylA
Synonyms:	XI

Organism

Actinoplanes missouriensis

Taxonomic identifier

1866 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Micromonosporineae › Micromonosporaceae › Actinoplanes

Protein attributes

Sequence length	394 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
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 HAMAP MF_00455

Chain

2 – 394

393

Xylose isomerase HAMAP MF_00455

PRO_0000195757

Sites

Active site

54

1

HAMAP MF_00455

Active site

57

1

By similarity

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

292

1

Magnesium 1 HAMAP MF_00455

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

394

Helix Strand Turn

Details...

Helix

7 – 9

3

Beta strand

11 – 14

4

Helix

15 – 18

4

Helix

36 – 46

11

Beta strand

49 – 52

4

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

133 – 137

5

Beta strand

141 – 145

5

Helix

146 – 148

3

Helix

151 – 172

22

Beta strand

177 – 181

5

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 – 238

11

Beta strand

251 – 254

4

Beta strand

262 – 264

3

Helix

265 – 276

12

Helix

279 – 281

3

Beta strand

289 – 291

3

Helix

301 – 327

27

Helix

329 – 337

9

Helix

341 – 344

4

Helix

354 – 359

6

Helix

361 – 363

3

Turn

364 – 366

3

Helix

369 – 373

5

Helix

379 – 390

12

Sequences

	Sequence		Length	Mass (Da)
	P12851-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 764B1FC35AE7A780	FASTA	394	43,499
	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

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: 2798103] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 14538 / DSM 43046 / IFO 13243 / JCM 3121 / NCIMB 12654.
[2]	"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: 3237716] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
[3]	"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: 1610791] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
[4]	"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: 10089406] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (4.1 ANGSTROMS).
[5]	"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: 1610792] [Abstract] Cited for: MUTAGENESIS.
[6]	"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: 1610793] [Abstract] Cited for: MUTAGENESIS.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

X16042 Genomic DNA. Translation: CAA34164.1.

PIR

ISMAXM. S05998.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1BHW	X-ray	4.10	A/B/C/D	2-394	[»]
1XIM	X-ray	2.20	A/B/C/D	2-393	[»]
1XIN	X-ray	2.40	A/B/C/D	2-394	[»]
2XIM	X-ray	2.30	A/B/C/D	2-393	[»]
2XIN	X-ray	2.30	A/B/C/D	2-394	[»]
3XIM	X-ray	2.30	A/B/C/D	2-393	[»]
3XIN	X-ray	2.30	A/B/C/D	2-394	[»]
4XIM	X-ray	2.30	A/B/C/D	2-394	[»]
5XIM	X-ray	2.60	A/B/C/D	2-394	[»]
5XIN	X-ray	2.30	A/B/C/D	2-394	[»]
6XIM	X-ray	2.50	A/B/C/D	2-394	[»]
7XIM	X-ray	2.40	A/B/C/D	2-394	[»]
8XIM	X-ray	2.40	A/B/C/D	2-394	[»]
9XIM	X-ray	2.40	A/B/C/D	2-394	[»]

ModBase

Search...

Enzyme and pathway databases

BRENDA

5.3.1.5. 1587.

Family and domain databases

HAMAP

MF_00455.
[Tree]

InterPro

IPR013022. Xyl_isomerase-like_TIM-brl.
IPR012307. Xyl_isomerase_TIM-brl.
IPR013453. XylA_actinobac.
IPR001998. Xylose_isomerase.
IPR018115. Xylose_isomerase_AS.
[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_ACTMI

Accession

Primary (citable) accession number: P12851

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1989
Last sequence update:	January 23, 2007
Last modified:	September 22, 2009
This is version 82 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)