Skip Header

Contribute Send feedback
Read comments (?) or add your own

B1Y1J9 (ARAA_LEPCP) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 28. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
L-arabinose isomerase
EC=5.3.1.4
Gene names
Name:araA
Ordered Locus Names:Lcho_3203
OrganismLeptothrix cholodnii (strain ATCC 51168 / LMG 8142 / SP-6) (Leptothrix discophora (strain SP-6)) [Complete proteome] [HAMAP]
Taxonomic identifier395495 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Leptothrix

Protein attributes

Sequence length497 AA.
Sequence statusComplete.
Protein existenceInferred 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

Sequence similarities

Belongs to the arabinose isomerase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 497497L-arabinose isomerase HAMAP MF_00519
PRO_1000127610

Sites

Metal binding3061Manganese By similarity
Metal binding3331Manganese By similarity
Metal binding3501Manganese By similarity
Metal binding4501Manganese By similarity

Sequences

Sequence LengthMass (Da)Tools
B1Y1J9 [UniParc].

Last modified May 20, 2008. Version 1.
Checksum: 859E54D85957018C

FASTA49754,401
        10         20         30         40         50         60 
MHAYPQLELW FVVGSQHLYG PKTLRAVAEN AQRIVDGLNA EGGLPAKLVL KPTVTESEGI 

        70         80         90        100        110        120 
LALCREANNA PQCAGLVTWM HTFSPARMWI AGLTALQKPF MQLHTQANIE VPWATMDMDF 

       130        140        150        160        170        180 
MNLTQTAHGG REYGFIAARL RKPHEVVVGH WQDPRVQAQL GAWMRVAAAV HDSRSLKVAR 

       190        200        210        220        230        240 
FGDNMREVAV TEGDKVEAQI RFGYAVNGHS LGDLAAAIEA VTPAQTQDKL AQYEADYELT 

       250        260        270        280        290        300 
AAVRAGGAKR GQLLDAARIE IGLQGFLDRG GFKAFTTNFE NLHGIPQLPG LAVQRLMQQG 

       310        320        330        340        350        360 
YGFGAEGDWK TSALLRAIKV MGNGNGGGAS FMEDYTYDFT AGQELVIGAH MLEVCPSIAA 

       370        380        390        400        410        420 
EAKPLLDVQP LSIGKKDDPA RLIFSAKPGR AIHSTLLDMG NRFRLISHEV DVITPPHDLP 

       430        440        450        460        470        480 
QLPVARAVYH PLPDLARGTA AWIHAGGAHH TVFSQGVSIH QLQTFAEMFE IEFVHIGEHT 

       490 
DIGRLKQELR WGDATWR

« Hide

References

[1]"Complete sequence of Leptothrix cholodnii SP-6."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L. expand/collapse author list , Kyrpides N., Lykidis A., Emerson D., Richardson P.
Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 51168 / LMG 8142 / SP-6.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP001013 Genomic DNA. Translation: ACB35461.1.
RefSeqYP_001792226.1. NC_010524.1.

3D structure databases

ProteinModelPortalB1Y1J9.
SMRB1Y1J9. Positions 1-497.
ModBaseSearch...

Protein-protein interaction databases

STRINGB1Y1J9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6162328.
GenomeReviewsGene locus Lcho_3203 in contig CP001013_GR.
KEGGlch:Lcho_3203.
PATRIC22396815. VBILepCho83238_3231.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG297198.
OMAEVCPTIA.
ProtClustDBPRK02929.

Enzyme and pathway databases

BioCycLCHO395495:LCHO_3203-MONOMER.

Family and domain databases

HAMAPMF_00519. Arabinose_Isome.
[Tree]
InterProIPR024664. Ara_Isoase_C.
IPR004216. Fuc/Ara_isomerase_C.
IPR009015. Fucose_isomerase_N/cen.
IPR003762. Lara_isomerase.
[Graphical view]
KOK01804.
PfamPF11762. Arabinose_Iso_C. 1 hit.
PF02610. Arabinose_Isome. 1 hit.
[Graphical view]
PIRSFPIRSF001478. L-ara_isomerase. 1 hit.
ProDomPD018364. Lara_isomerase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMSSF50443. Fuc_isomerase_C. 1 hit.
SSF53743. Fuc_isomerase_N. 1 hit.
ProtoNetSearch...

Entry information

Entry nameARAA_LEPCP
AccessionPrimary (citable) accession number: B1Y1J9
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: May 20, 2008
Last modified: January 25, 2012
This is version 28 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents