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C6EAZ3 (C6EAZ3_ECOBD) Unreviewed, UniProtKB/TrEMBL

Last modified January 25, 2012. Version 20. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
L-arabinose isomerase HAMAP MF_00519
EC=5.3.1.4 HAMAP MF_00519
Gene names
Name:araA HAMAP MF_00519 EMBL ACT41965.1
Ordered Locus Names:B21_00063, ECBD_3555, ECD_00064
OrganismEscherichia coli (strain B / BL21-DE3) [Complete proteome] [HAMAP]
Taxonomic identifier469008 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length500 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the conversion of L-arabinose to L-ribulose By similarity. SAAS SAAS003762 HAMAP MF_00519

Catalytic activity

L-arabinose = L-ribulose. SAAS SAAS003762 HAMAP MF_00519

Cofactor

Binds 1 manganese ion per subunit By similarity. SAAS SAAS003762 HAMAP MF_00519

Pathway

Carbohydrate degradation; L-arabinose degradation via L-ribulose; D-xylulose 5-phosphate from L-arabinose (bacterial route): step 1/3. SAAS SAAS003762 HAMAP MF_00519

Subunit structure

Homohexamer By similarity. HAMAP MF_00519

Sequence similarities

Belongs to the arabinose isomerase family. HAMAP MF_00519

Sequences

Sequence LengthMass (Da)Tools
C6EAZ3 [UniParc].

Last modified September 1, 2009. Version 1.
Checksum: E1B1B9F2FACF1FBD

FASTA50056,103
        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

« Hide

References

[1]"Genome sequences of Escherichia coli B strains REL606 and BL21(DE3)."
Jeong H., Barbe V., Lee C.H., Vallenet D., Yu D.S., Choi S.H., Couloux A., Lee S.W., Yoon S.H., Cattolico L., Hur C.G., Park H.S., Segurens B., Kim S.C., Oh T.K., Lenski R.E., Studier F.W., Daegelen P., Kim J.F.
J. Mol. Biol. 394:644-652(2009) [PubMed: 19786035] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: B / BL21-DE3 [Korea].
[2]"Sequencing and gene expression analysis of Escherichia coli BL21."
Leparc G., Striedner G., Bayer K., Kreil D., Krempl P.M.
Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: B / BL21-DE3 [Austria].
[3]"Complete sequence of Escherichia coli BL21(DE3)."
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., LaButti K.M., Clum A., Larimer F., Land M., Hauser L., Kyrpides N., Anderson I., Sorek R., Rubin E.
Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: B / BL21-DE3 [JGI].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP001665 Genomic DNA. Translation: ACT30554.1.
CP001509 Genomic DNA. Translation: ACT41965.1.
AM946981 Genomic DNA. Translation: CAQ30580.1.

3D structure databases

ProteinModelPortalC6EAZ3.
SMRC6EAZ3. Positions 1-498.
ModBaseSearch...

Protein-protein interaction databases

STRINGC6EAZ3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBESCT00000157189; EBESCP00000147181; EBESCG00000157303.
EBESCT00000189134; EBESCP00000177261; EBESCG00000188039.
EBESCT00000195495; EBESCP00000180398; EBESCG00000195088.
GenomeReviewsGene locus B21_00063 in contig AM946981_GR.
Gene locus ECD_00064 in contig CP001509_GR.
Gene locus ECBD_3555 in contig CP001665_GR.
KEGGebd:ECBD_3555.

Organism-specific databases

CMRSearch...

Phylogenomic databases

GeneTreeEBGT00050000011273.
OMAEVCPTIA.
ProtClustDBPRK02929.

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 nameC6EAZ3_ECOBD
AccessionPrimary (citable) accession number: C6EAZ3
Secondary accession number(s): C5W221
Entry history
Integrated into UniProtKB/TrEMBL: September 1, 2009
Last sequence update: September 1, 2009
Last modified: January 25, 2012
This is version 20 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequences·References·Cross-refs·Entry info