Reviewed, UniProtKB/Swiss-Prot P08202 (ARAA_ECOLI)

Names and origin

Protein names

Recommended name:
    L-arabinose isomerase
    EC=5.3.1.4

Gene names

Name:	araA
Ordered Locus Names:	b0062, JW0061

Organism

Escherichia coli (strain K12) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	500 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Catalyzes the conversion of L-arabinose to L-ribulose. HAMAP MF_00519
Catalytic activity	L-arabinose = L-ribulose. HAMAP MF_00519
Cofactor	Binds 1 manganese ion per subunit. HAMAP MF_00519
Pathway	Carbohydrate degradation; L-arabinose degradation via L-ribulose; D-xylulose 5-phosphate from L-arabinose (bacteria route): step 1/3. HAMAP MF_00519
Subunit structure	Homohexamer. Ref.6
Sequence similarities	Belongs to the arabinose isomerase family.

Ontologies

Keywords
Biological process	Arabinose catabolism Carbohydrate metabolism
Ligand	Manganese Metal-binding
Molecular function	Isomerase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	arabinose catabolic process Inferred from electronic annotation. Source: HAMAP
Molecular function	L-arabinose isomerase activity Inferred from electronic annotation. Source: HAMAP manganese ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 500

500

L-arabinose isomerase HAMAP MF_00519

PRO_0000198385

Sites

Metal binding

306

1

Manganese HAMAP MF_00519

Metal binding

333

1

Manganese HAMAP MF_00519

Metal binding

350

1

Manganese HAMAP MF_00519

Metal binding

450

1

Manganese HAMAP MF_00519

Experimental info

Sequence conflict

72

1

R → P Ref.1

Sequence conflict

72

1

R → P Ref.2

Sequence conflict

248

1

K → E Ref.1

Sequence conflict

248

1

K → E Ref.2

Sequence conflict

360

1

A → V Ref.1

Sequence conflict

360

1

A → V Ref.2

Secondary structure

1

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500

Helix Strand Turn

Details...

Helix

3 – 6

4

Beta strand

8 – 14

7

Turn

17 – 18

2

Helix

21 – 41

21

Beta strand

45 – 50

6

Helix

57 – 69

13

Turn

71 – 72

2

Beta strand

73 – 80

8

Helix

86 – 95

10

Beta strand

100 – 104

5

Beta strand

107 – 110

4

Turn

113 – 115

3

Helix

118 – 121

4

Turn

122

1

Helix

126 – 139

14

Turn

140 – 141

2

Beta strand

145 – 149

5

Turn

151 – 152

2

Helix

154 – 174

21

Turn

175

1

Beta strand

177 – 182

6

Turn

186 – 187

2

Turn

190 – 191

2

Helix

195 – 202

8

Beta strand

205 – 209

5

Helix

211 – 219

9

Turn

220

1

Helix

223 – 236

14

Beta strand

237 – 239

3

Helix

241 – 243

3

Turn

245 – 246

2

Turn

248 – 249

2

Helix

250 – 270

21

Turn

271

1

Beta strand

273 – 277

5

Turn

279 – 280

2

Turn

283 – 284

2

Helix

291 – 299

9

Turn

300

1

Beta strand

302 – 307

6

Helix

309 – 321

13

Turn

322 – 324

3

Beta strand

325 – 327

3

Beta strand

330 – 338

9

Turn

341 – 342

2

Beta strand

345 – 349

5

Helix

356 – 358

3

Beta strand

359 – 361

3

Beta strand

364 – 366

3

Turn

372 – 375

4

Beta strand

389 – 398

10

Beta strand

400 – 412

13

Turn

420 – 421

2

Beta strand

426 – 433

8

Helix

435 – 444

10

Turn

445

1

Beta strand

449 – 456

8

Helix

459 – 468

10

Turn

469 – 470

2

Beta strand

472 – 477

6

Turn

478 – 479

2

Helix

482 – 496

15

Sequences

	Sequence		Length	Mass (Da)
	P08202-1 [UniParc]. Last modified June 27, 2006. Version 3. Checksum: E427A145A3455D36	FASTA	500	56,074
	10 20 30 40 50 60 MTIFDNYEVW FVIGSQHLYG PETLRQVTQH AEHVVNALNT EAKLPCKLVL KPLGTTPDEI 70 80 90 100 110 120 TAICRDANYD DRCAGLVVWL HTFSPAKMWI NGLTMLNKPL LQFHTQFNAA LPWDSIDMDF 130 140 150 160 170 180 MNLNQTAHGG REFGFIGARM RQQHAVVTGH WQDKQAHERI GSWMRQAVSK QDTRHLKVCR 190 200 210 220 230 240 FGDNMREVAV TDGDKVAAQI KFGFSVNTWA VGDLVQVVNS ISDGDVNALV DEYESCYTMT 250 260 270 280 290 300 PATQIHGKKR QNVLEAARIE LGMKRFLEQG GFHAFTTTFE DLHGLKQLPG LAVQRLMQQG 310 320 330 340 350 360 YGFAGEGDWK TAALLRIMKV MSTGLQGGTS FMEDYTYHFE KGNDLVLGSH MLEVCPSIAA 370 380 390 400 410 420 EEKPILDVQH LGIGGKDDPA RLIFNTQTGP AIVASLIDLG DRYRLLVNCI DTVKTPHSLP 430 440 450 460 470 480 KLPVANALWK AQPDLPTASE AWILAGGAHH TVFSHALNLN DMRQFAEMHD IEITVIDNDT 490 500 RLPAFKDALR WNEVYYGFRR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The organization of the araBAD operon of Escherichia coli." Lee N., Gielow W., Martin R., Hamilton E., Fowler A. Gene 47:231-244(1986) [PubMed: 3549454] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Systematic sequencing of the Escherichia coli genome: analysis of the 0-2.4 min region." Yura T., Mori H., Nagai H., Nagata T., Ishihama A., Fujita N., Isono K., Mizobuchi K., Nakata A. Nucleic Acids Res. 20:3305-3308(1992) [PubMed: 1630901] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12.
[3]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], SEQUENCE REVISION TO 72; 248 AND 360. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]	Bachellier S., Saurin W., Perrin D., Hofnung M., Gilson E. Submitted (JUL-1993) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 458-500.
[6]	"Crystal structure of Escherichia coli L-arabinose isomerase (ECAI), the putative target of biological tagatose production." Manjasetty B.A., Chance M.R. J. Mol. Biol. 360:297-309(2006) [PubMed: 16756997] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS), SUBUNIT.
[7]	"Crystal structure of Mn2+-bound Escherichia coli L-arabinose isomerase (ECAI) and implications in protein catalytic mechanism and thermo-stability." Zhu W., Chance M.R., Manjasetty B.A. Submitted (OCT-2007) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) IN COMPLEX WITH MANGANESE IONS.

Cross-references

Sequence databases

EMBLGenBankDDBJ

M15263 Genomic DNA. Translation: AAA23463.1.
U00096 Genomic DNA. Translation: AAC73173.1.
AP009048 Genomic DNA. Translation: BAB96631.2.
X74279 Genomic DNA. Translation: CAA52340.1.

PIR

ISECAB. F64727.

RefSeq

AP_000726.1.
NP_414604.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2AJT	X-ray	2.60	A/B/C	1-500	[»]
2HXG	X-ray	2.80	A/B/C	1-500	[»]

SMR

P08202. Positions 1-498.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:9123N.

2-D gel databases

ECO2DBASE

G054.1. 6TH EDITION.

Genome annotation databases

GeneID

947511.

GenomeReviews

Gene locus JW0061 in contig AP009048_GR.
Gene locus b0062 in contig U00096_GR.

KEGG

ecj:JW0061.
eco:b0062.

Organism-specific databases

EchoBASE

EB0050.

EcoGene

EG10052. araA.

CMR

Search...

Phylogenomic databases

HOGENOM

P08202.

OMA

P08202. EVCPTIA.

Enzyme and pathway databases

BioCyc

EcoCyc:ARABISOM-MON.
MetaCyc:ARABISOM-MON.

BRENDA

5.3.1.4. 246.

Family and domain databases

HAMAP

MF_00519.
[Tree]

InterPro

IPR003762. Lara_isomerase.
[Graphical view]

Pfam

PF02610. Arabinose_Isome. 1 hit.
[Graphical view]

PIRSF

PIRSF001478. L-ara_isomerase. 1 hit.

ProDom

PD018364. Lara_isomerase. 1 hit.
[Graphical view] [Entries sharing at least one domain]

ProtoNet

Search...

Entry information

Entry name

ARAA_ECOLI

Accession

Primary (citable) accession number: P08202
Secondary accession number(s): P78040

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
Last sequence update:	June 27, 2006
Last modified:	June 16, 2009
This is version 83 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)