B7MNR9 (ARAA_ECO81) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
L-arabinose isomerase
EC=5.3.1.4

Gene names

Name:	araA
Ordered Locus Names:	ECED1_0061

Organism

Escherichia coli O81 (strain ED1a) [Complete proteome] [HAMAP]

Taxonomic identifier

585397 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	500 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the conversion of L-arabinose to L-ribulose By similarity. HAMAP MF_00519
Catalytic activity	L-arabinose = L-ribulose. HAMAP MF_00519
Cofactor	Binds 1 manganese ion per subunit By similarity. HAMAP MF_00519
Pathway	Carbohydrate degradation; L-arabinose degradation via L-ribulose; D-xylulose 5-phosphate from L-arabinose (bacterial route): step 1/3. HAMAP MF_00519
Subunit structure	Homohexamer By similarity. HAMAP MF_00519
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	Complete proteome
Gene Ontology (GO)
Biological process	arabinose catabolic process Inferred from electronic annotation. Source: UniProtKB-KW fucose metabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: InterPro
Molecular function	L-arabinose isomerase activity Inferred from electronic annotation. Source: EC L-fucose isomerase activity Inferred from electronic annotation. Source: InterPro metal 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_1000146227
Sites
	Metal binding	306	1	Manganese By similarity
	Metal binding	333	1	Manganese By similarity
	Metal binding	350	1	Manganese By similarity
	Metal binding	450	1	Manganese By similarity

Sequences

	Sequence		Length	Mass (Da)
	B7MNR9 [UniParc]. Last modified March 24, 2009. Version 1. Checksum: E1B1B9F2FACF1FBD	FASTA	500	56,103
	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 PATQIHGEKR QNVLEAARIE LGMKRFLEQG GFHAFTTTFE DLHGLKQLPG LAVQRLMQQG 310 320 330 340 350 360 YGFAGEGDWK TAALLRIMKV MSTGLQGGTS FMEDYTYHFE KGNDLVLGSH MLEVCPSIAV 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

[1]

"Organised genome dynamics in the Escherichia coli species results in highly diverse adaptive paths." Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P., Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H., Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E. , Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C., Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S., Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J., Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E. PLoS Genet. 5:E1000344-E1000344(2009) [PubMed: 19165319] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ED1a.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CU928162 Genomic DNA. Translation: CAR06284.1.
RefSeq	YP_002396150.1. NC_011745.1.
3D structure databases
ProteinModelPortal	B7MNR9.
SMR	B7MNR9. Positions 1-498.
ModBase	Search...
Protein-protein interaction databases
STRING	B7MNR9.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBESCT00000143424; EBESCP00000137042; EBESCG00000143365.
GeneID	7142599.
GenomeReviews	Gene locus ECED1_0061 in contig CU928162_GR.
PATRIC	38484043. VBIEscCol8292_0065.
Organism-specific databases
CMR	Search...
Phylogenomic databases
GeneTree	EBGT00050000011273.
OMA	EVCPTIA.
ProtClustDB	PRK02929.
Enzyme and pathway databases
BioCyc	ECOL585397:ECED1_0061-MONOMER.
Family and domain databases
HAMAP	MF_00519. Arabinose_Isome. [Tree]
InterPro	IPR024664. Ara_Isoase_C. IPR004216. Fuc/Ara_isomerase_C. IPR009015. Fucose_isomerase_N/cen. IPR003762. Lara_isomerase. [Graphical view]
Pfam	PF11762. Arabinose_Iso_C. 1 hit. 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]
SUPFAM	SSF50443. Fuc_isomerase_C. 1 hit. SSF53743. Fuc_isomerase_N. 1 hit.
ProtoNet	Search...

Entry information

Entry name

ARAA_ECO81

Accession

Primary (citable) accession number: B7MNR9

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 28, 2009
Last sequence update:	March 24, 2009
Last modified:	January 25, 2012
This is version 21 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program