Skip Header

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

Q21MP3 (ARAA_SACD2) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 35. 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

Names and origin

Protein namesRecommended name:
L-arabinose isomerase

EC=5.3.1.4
Gene names
Name:araA
Ordered Locus Names:Sde_0774
OrganismSaccharophagus degradans (strain 2-40 / ATCC 43961 / DSM 17024) [Complete proteome] [HAMAP]
Taxonomic identifier203122 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesAlteromonadaceaeSaccharophagus

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. 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 – 500500L-arabinose isomerase HAMAP MF_00519
PRO_0000312616

Sites

Metal binding3061Manganese By similarity
Metal binding3331Manganese By similarity
Metal binding3491Manganese By similarity
Metal binding4481Manganese By similarity

Sequences

Sequence LengthMass (Da)Tools
Q21MP3 [UniParc].

Last modified April 18, 2006. Version 1.
Checksum: 109BB54E5E4948B9

FASTA50055,133
        10         20         30         40         50         60 
MKIYGEKKIW FVTGSQHLYG PGVLAQVAEN SQAIAAGLTA SEHVSANIES RGVVTTPKEI 

        70         80         90        100        110        120 
LDVCQAANSD ENCVGLILWM HTFSPAKMWI AGLSALNKPY MHLHTQFGAA LPWGDINMNY 

       130        140        150        160        170        180 
MNLNQSAHGD REFGYIGTRL RQERKVVVGH WQKESVQIQV DDWVRAAMGW AESQTLKVAR 

       190        200        210        220        230        240 
FGDNMRQVAV TEGDKVSAQI QFGYEVHAFG LGDLAKACEK ITAEQITAQL ELYKQDYEID 

       250        260        270        280        290        300 
ADVFTDVHSL EMLQNEARLE LGMEAFLEEG NFKAFTNCFE NLTGLSGLPG LATQRLMSKG 

       310        320        330        340        350        360 
YGYGGEGDWK TAAMCRIVKV MSLGKAAGTS FMEDYTYNFG DPDQVLGAHM LEVCPSISNE 

       370        380        390        400        410        420 
KPKVVVERHT IGIKKDIARL IFTGTPGPAI NISTIDMGTR FRIIANEVDT VKPPQDLPNL 

       430        440        450        460        470        480 
PVAKALWEPR PSLEVAAAAW IHAGGAHHSV YTQGINLDQL NDFAEMAGVE MVVIGADTNV 

       490        500 
NEFKKELRFN AVYYHLSHGI 

« Hide

References

[1]"Complete genome sequence of the complex carbohydrate-degrading marine bacterium, Saccharophagus degradans strain 2-40 T."
Weiner R.M., Taylor L.E. II, Henrissat B., Hauser L., Land M., Coutinho P.M., Rancurel C., Saunders E.H., Longmire A.G., Zhang H., Bayer E.A., Gilbert H.J., Larimer F., Zhulin I.B., Ekborg N.A., Lamed R., Richardson P.M., Borovok I., Hutcheson S.
PLoS Genet. 4:E1000087-E1000087(2008) [PubMed: 18516288] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 2-40 / ATCC 43961 / DSM 17024.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000282 Genomic DNA. Translation: ABD80036.1.
RefSeqYP_526248.1. NC_007912.1.

3D structure databases

ProteinModelPortalQ21MP3.
SMRQ21MP3. Positions 1-496.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ21MP3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3965827.
GenomeReviewsGene locus Sde_0774 in contig CP000282_GR.
KEGGsde:Sde_0774.
NMPDRfig|203122.1.peg.4280.
PATRIC23400301. VBISacDeg56404_0854.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2160.
HOGENOMHBG297198.
OMAEVCPTIA.
PhylomeDBQ21MP3.
ProtClustDBPRK02929.

Enzyme and pathway databases

BioCycSDEG203122:SDE_0774-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_SACD2
AccessionPrimary (citable) accession number: Q21MP3
Entry history
Integrated into UniProtKB/Swiss-Prot: December 4, 2007
Last sequence update: April 18, 2006
Last modified: January 25, 2012
This is version 35 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