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Reviewed, UniProtKB/Swiss-Prot B3DTJ5 (ARAA_BIFLD)

Last modified April 20, 2010. Version 18. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents
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Names and originHide

Protein namesRecommended name:
L-arabinose isomerase

EC=5.3.1.4
Gene names
Name:araA
Ordered Locus Names:BLD_1018
OrganismBifidobacterium longum (strain DJO10A) [Complete proteome] [HAMAP]
Taxonomic identifier205913 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeBifidobacterialesBifidobacteriaceaeBifidobacterium
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Protein attributesHide

Sequence length505 AA.
Sequence statusComplete.
Protein existenceInferred from homology.
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General annotation (Comments)Hide

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.

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OntologiesHide

Keywords
   Biological processArabinose catabolism
Carbohydrate metabolism
   LigandManganese
Metal-binding
   Molecular functionIsomerase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processarabinose catabolic process

Inferred from electronic annotation. Source: HAMAP

   Molecular functionL-arabinose isomerase activity

Inferred from electronic annotation. Source: HAMAP

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...
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Sequence annotation (Features)Hide

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 505505L-arabinose isomerase HAMAP MF_00519
PRO_1000127597

Sites

Metal binding3081Manganese By similarity
Metal binding3351Manganese By similarity
Metal binding3521Manganese By similarity
Metal binding4531Manganese By similarity
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SequencesHide

Sequence LengthMass (Da)Tools
B3DTJ5-1 [UniParc].

Last modified July 22, 2008. Version 1.
Checksum: 7665BFB00AD37E4C

FASTA50555,868
        10         20         30         40         50         60 
MVMENPFEGK EIWFGVGSQD LYGEEALRQV AIHSAEMVDY LNNTGKIPAK IVLKPTLKSS 

        70         80         90        100        110        120 
DGVKEFMVEA SANPNVIGVI TWCHTFSPAK MWIRGLEVLT KPLLQLATQH HKEIPWETID 

       130        140        150        160        170        180 
MDFMNLNQAA HGDREFGYIV SRLGIKRKVV VGHYTDPEVA EKLGTWARAC AGWDASNNMK 

       190        200        210        220        230        240 
VMRWGDNMRN VAVTEGDKTE AERVFGASIN TWAVNELVAA YDAVKDDQVK EIIEDYKAKY 

       250        260        270        280        290        300 
DVDPALLDAK YDSLFIAAKE EAAMVNMMRA NGCTAGVDNF EDLGALPQLP GVGPQRFPSE 

       310        320        330        340        350        360 
YGWGFSAEGD WKTAVLVRIG AVMGYGLEGG ASLMEDYSYN FTEGDELDMG SHMLEVSPSI 

       370        380        390        400        410        420 
GTIAKPKLEI HPLGIGGKAD PVRLVFSGKP AKDAVVVSMS DVRERFRLLM DVVDVVEPQG 

       430        440        450        460        470        480 
SLKELPCARA VWEPKPSLKT AVECWITAGG SHHTCMTTSV GREAWEDFAR IAGVELAVID 

       490        500 
ENTTARQFEK ELELSEMYHR LNNQH 

« Hide

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ReferencesHide

[1]"Comparative genomic analysis of the gut bacterium Bifidobacterium longum reveals loci susceptible to deletion during pure culture growth."
Lee J.H., Karamychev V.N., Kozyavkin S.A., Mills D., Pavlov A.R., Pavlova N.V., Polouchine N.N., Richardson P.M., Shakhova V.V., Slesarev A.I., Weimer B., O'Sullivan D.J.
BMC Genomics 9:247-247(2008) [PubMed: 18505588] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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Cross-referencesHide

Sequence databases

EMBL
GenBank
DDBJ
CP000605 Genomic DNA. Translation: ACD98464.1.
RefSeqYP_001954962.1.

3D structure databases

SMRB3DTJ5. Positions 5-501.
ModBaseSearch...

Genome annotation databases

GeneID6362657.
GenomeReviewsGene locus BLD_1018 in contig CP000605_GR.
KEGGblj:BLD_1018.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG297198.
OMAEVCPTIA.
ProtClustDBPRK02929.

Family and domain databases

HAMAPMF_00519. Arabinose_Isome.
[Tree]
InterProIPR003762. Lara_isomerase.
[Graphical view]
PfamPF02610. 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]
ProtoNetSearch...
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Entry informationHide

Entry nameARAA_BIFLD
AccessionPrimary (citable) accession number: B3DTJ5
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: July 22, 2008
Last modified: April 20, 2010
This is version 18 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)
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Relevant documentsHide

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents