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A8HXA9 (A8HXA9_CHLRE) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 31. 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:
Aldose 1-epimerase PIRNR PIRNR005096
EC=5.1.3.3 PIRNR PIRNR005096
Alternative name(s):
Galactose mutarotase PIRNR PIRNR005096
Gene names
Name:AEP1 EMBL EDP08289.1
ORF Names:CHLREDRAFT_187168 EMBL EDP08289.1
OrganismChlamydomonas reinhardtii (Chlamydomonas smithii) [Reference proteome]
Taxonomic identifier3055 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Chlorophyta › Chlorophyceae › Chlamydomonadales › Chlamydomonadaceae › Chlamydomonas

Protein attributes

Sequence length388 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Converts alpha-aldose to the beta-anomer. It is active on D-glucose, L-arabinose, D-xylose, D-galactose, maltose and lactose By similarity. PIRNR PIRNR005096

Catalytic activity

Alpha-D-glucose = beta-D-glucose. PIRNR PIRNR005096

Pathway

Carbohydrate metabolism; hexose metabolism. PIRNR PIRNR005096

Sequence similarities

Belongs to the aldose epimerase family. PIRNR PIRNR005096

Sequences

Sequence LengthMass (Da)Tools
A8HXA9 [UniParc].

Last modified December 4, 2007. Version 1.
Checksum: 116A075BC1CC71BC

FASTA38841,212
        10         20         30         40         50         60 
MRILAGVLIG SSVALAALAA LKVRGLRAQS SSWHASLPVF KLKNANGMEV HVSTFGAAIL 

        70         80         90        100        110        120 
KVVVPDKAGK KADVVLGYAS VDEYETANPV TYFGVVVGRV ANRIAGAKFS LGGVDYRLLA 

       130        140        150        160        170        180 
NNGPNALHGG LKGLHKRRWE GRKVHDHDGN ESVQLHYTSP EGEEGYPGTL HVQVTYTLLR 

       190        200        210        220        230        240 
HSNELHTSIV ATTDEATPVN IAQHSYFNLA GHASGSILGH TLRLVGADHY TPVGATLIPT 

       250        260        270        280        290        300 
GEIAPVAGTP FDFTAPQTIG SRIDKVPGAA PGGYDHNFVL FGMGPQAKFI TKNGMASDKP 

       310        320        330        340        350        360 
KLAASLVDPS SGRAMDVLTT APGVQFYSGN FLDGTTVGKG GVRYGKHAGL CLETQGFPNA 

       370        380 
INEPKFPSIV LQPQDTYHHE IVYRFYNV

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References

[1]"The Chlamydomonas genome reveals the evolution of key animal and plant functions."
Merchant S.S., Prochnik S.E., Vallon O., Harris E.H., Karpowicz S.J., Witman G.B., Terry A., Salamov A., Fritz-Laylin L.K., Marechal-Drouard L., Marshall W.F., Qu L.H., Nelson D.R., Sanderfoot A.A., Spalding M.H., Kapitonov V.V., Ren Q., Ferris P. expand/collapse author list , Lindquist E., Shapiro H., Lucas S.M., Grimwood J., Schmutz J., Cardol P., Cerutti H., Chanfreau G., Chen C.L., Cognat V., Croft M.T., Dent R., Dutcher S., Fernandez E., Fukuzawa H., Gonzalez-Ballester D., Gonzalez-Halphen D., Hallmann A., Hanikenne M., Hippler M., Inwood W., Jabbari K., Kalanon M., Kuras R., Lefebvre P.A., Lemaire S.D., Lobanov A.V., Lohr M., Manuell A., Meier I., Mets L., Mittag M., Mittelmeier T., Moroney J.V., Moseley J., Napoli C., Nedelcu A.M., Niyogi K., Novoselov S.V., Paulsen I.T., Pazour G.J., Purton S., Ral J.P., Riano-Pachon D.M., Riekhof W., Rymarquis L., Schroda M., Stern D., Umen J., Willows R., Wilson N., Zimmer S.L., Allmer J., Balk J., Bisova K., Chen C.J., Elias M., Gendler K., Hauser C., Lamb M.R., Ledford H., Long J.C., Minagawa J., Page M.D., Pan J., Pootakham W., Roje S., Rose A., Stahlberg E., Terauchi A.M., Yang P., Ball S., Bowler C., Dieckmann C.L., Gladyshev V.N., Green P., Jorgensen R., Mayfield S., Mueller-Roeber B., Rajamani S., Sayre R.T., Brokstein P., Dubchak I., Goodstein D., Hornick L., Huang Y.W., Jhaveri J., Luo Y., Martinez D., Ngau W.C., Otillar B., Poliakov A., Porter A., Szajkowski L., Werner G., Zhou K., Grigoriev I.V., Rokhsar D.S., Grossman A.R.
Science 318:245-250(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CC-503.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		DS496110 Genomic DNA. Translation: EDP08289.1.
RefSeqXP_001696312.1. XM_001696260.1.
UniGeneCre.5961.

3D structure databases

ProteinModelPortalA8HXA9.
ModBaseSearch...

Protein-protein interaction databases

STRING3055.JGI187168.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsEDP08289; EDP08289; CHLREDRAFT_187168.
GeneID5722017.
KEGGcre:CHLREDRAFT_187168.

Phylogenomic databases

eggNOGCOG2017.
KOK01785.
OMAYPGNLKL.
ProtClustDBCLSN2922380.

Enzyme and pathway databases

BioCycCHLAMY:CHLREDRAFT_187168-MONOMER.
UniPathwayUPA00242.

Family and domain databases

Gene3D2.70.98.10. 1 hit.
InterProIPR015443. Aldose_1-epimerase.
IPR008183. Aldose_1/G6P_1-epimerase.
IPR011013. Gal_mutarotase_SF_dom.
IPR014718. Glyco_hydro-type_carb-bd_sub.
[Graphical view]
PANTHERPTHR10091. PTHR10091. 1 hit.
PfamPF01263. Aldose_epim. 1 hit.
[Graphical view]
PIRSFPIRSF005096. GALM. 1 hit.
SUPFAMSSF74650. Gal_mut_like. 1 hit.
ProtoNetSearch...

Entry information

Entry nameA8HXA9_CHLRE
AccessionPrimary (citable) accession number: A8HXA9
Entry history
Integrated into UniProtKB/TrEMBL: December 4, 2007
Last sequence update: December 4, 2007
Last modified: May 1, 2013
This is version 31 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