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B4KV41 (B4KV41_DROMO) Unreviewed, UniProtKB/TrEMBL

Last modified November 13, 2013. Version 32. 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:Dmoj\GI11556 EMBL EDW19381.1
ORF Names:Dmoj_GI11556 EMBL EDW19381.1, GI11556 FlyBase FBgn0134316
OrganismDrosophila mojavensis (Fruit fly) [Complete proteome]
Taxonomic identifier7230 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Ecdysozoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila ›

Protein attributes

Sequence length367 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

Ontologies

Keywords
   Biological processCarbohydrate metabolism PIRNR PIRNR005096
   Molecular functionIsomerase PIRNR PIRNR005096
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processhexose metabolic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Molecular_functionaldose 1-epimerase activity

Inferred from electronic annotation. Source: UniProtKB-EC

carbohydrate binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequences

Sequence LengthMass (Da)Tools
B4KV41 [UniParc].

Last modified September 23, 2008. Version 1.
Checksum: 840DEC55BC6745D9

FASTA36740,695
        10         20         30         40         50         60 
MVRVVEDVFG IAVNPMTQKT DHVRRFTLCS EKGMSVAILT LGGIIQSIRV PDANAKLEDV 

        70         80         90        100        110        120 
CLGYDDVAGY YRNQKFYIGA IIGRVADRVA RGRFSLCSKD ISLSRNHKDH YHLNGGYVGF 

       130        140        150        160        170        180 
DSVIWDVVGI HKDGVTFQHV SPDGHEGYPG EVTVNINYSL NEAGCLGLRI EARAKETTCI 

       190        200        210        220        230        240 
NIGHHCLFNL AGHSSGRDTL YQHMIMIKAN KIVDTDLEQI PTGKLMPTRN TPYDFSTLTN 

       250        260        270        280        290        300 
LGKRLNQVNR CPISGFDNNY CVDVDPNQVK LVARAVHPCS GRFVEIHTNQ PGVHFSTANG 

       310        320        330        340        350        360 
LPQEDRGDVP HVGKGGAHYS QHSAFCLQTQ KYPDAMNNPE FPTVIINPGQ LYDHQVVYRF 


GACPKRV

« Hide

References

[1]"Evolution of genes and genomes on the Drosophila phylogeny."
Drosophila 12 Genomes Consortium
Clark A.G., Eisen M.B., Smith D.R., Bergman C.M., Oliver B., Markow T.A., Kaufman T.C., Kellis M., Gelbart W., Iyer V.N., Pollard D.A., Sackton T.B., Larracuente A.M., Singh N.D., Abad J.P., Abt D.N., Adryan B., Aguade M. expand/collapse author list , Akashi H., Anderson W.W., Aquadro C.F., Ardell D.H., Arguello R., Artieri C.G., Barbash D.A., Barker D., Barsanti P., Batterham P., Batzoglou S., Begun D., Bhutkar A., Blanco E., Bosak S.A., Bradley R.K., Brand A.D., Brent M.R., Brooks A.N., Brown R.H., Butlin R.K., Caggese C., Calvi B.R., Bernardo de Carvalho A., Caspi A., Castrezana S., Celniker S.E., Chang J.L., Chapple C., Chatterji S., Chinwalla A., Civetta A., Clifton S.W., Comeron J.M., Costello J.C., Coyne J.A., Daub J., David R.G., Delcher A.L., Delehaunty K., Do C.B., Ebling H., Edwards K., Eickbush T., Evans J.D., Filipski A., Findeiss S., Freyhult E., Fulton L., Fulton R., Garcia A.C., Gardiner A., Garfield D.A., Garvin B.E., Gibson G., Gilbert D., Gnerre S., Godfrey J., Good R., Gotea V., Gravely B., Greenberg A.J., Griffiths-Jones S., Gross S., Guigo R., Gustafson E.A., Haerty W., Hahn M.W., Halligan D.L., Halpern A.L., Halter G.M., Han M.V., Heger A., Hillier L., Hinrichs A.S., Holmes I., Hoskins R.A., Hubisz M.J., Hultmark D., Huntley M.A., Jaffe D.B., Jagadeeshan S., Jeck W.R., Johnson J., Jones C.D., Jordan W.C., Karpen G.H., Kataoka E., Keightley P.D., Kheradpour P., Kirkness E.F., Koerich L.B., Kristiansen K., Kudrna D., Kulathinal R.J., Kumar S., Kwok R., Lander E., Langley C.H., Lapoint R., Lazzaro B.P., Lee S.J., Levesque L., Li R., Lin C.F., Lin M.F., Lindblad-Toh K., Llopart A., Long M., Low L., Lozovsky E., Lu J., Luo M., Machado C.A., Makalowski W., Marzo M., Matsuda M., Matzkin L., McAllister B., McBride C.S., McKernan B., McKernan K., Mendez-Lago M., Minx P., Mollenhauer M.U., Montooth K., Mount S.M., Mu X., Myers E., Negre B., Newfeld S., Nielsen R., Noor M.A., O'Grady P., Pachter L., Papaceit M., Parisi M.J., Parisi M., Parts L., Pedersen J.S., Pesole G., Phillippy A.M., Ponting C.P., Pop M., Porcelli D., Powell J.R., Prohaska S., Pruitt K., Puig M., Quesneville H., Ram K.R., Rand D., Rasmussen M.D., Reed L.K., Reenan R., Reily A., Remington K.A., Rieger T.T., Ritchie M.G., Robin C., Rogers Y.H., Rohde C., Rozas J., Rubenfield M.J., Ruiz A., Russo S., Salzberg S.L., Sanchez-Gracia A., Saranga D.J., Sato H., Schaeffer S.W., Schatz M.C., Schlenke T., Schwartz R., Segarra C., Singh R.S., Sirot L., Sirota M., Sisneros N.B., Smith C.D., Smith T.F., Spieth J., Stage D.E., Stark A., Stephan W., Strausberg R.L., Strempel S., Sturgill D., Sutton G., Sutton G.G., Tao W., Teichmann S., Tobari Y.N., Tomimura Y., Tsolas J.M., Valente V.L., Venter E., Venter J.C., Vicario S., Vieira F.G., Vilella A.J., Villasante A., Walenz B., Wang J., Wasserman M., Watts T., Wilson D., Wilson R.K., Wing R.A., Wolfner M.F., Wong A., Wong G.K., Wu C.I., Wu G., Yamamoto D., Yang H.P., Yang S.P., Yorke J.A., Yoshida K., Zdobnov E., Zhang P., Zhang Y., Zimin A.V., Baldwin J., Abdouelleil A., Abdulkadir J., Abebe A., Abera B., Abreu J., Acer S.C., Aftuck L., Alexander A., An P., Anderson E., Anderson S., Arachi H., Azer M., Bachantsang P., Barry A., Bayul T., Berlin A., Bessette D., Bloom T., Blye J., Boguslavskiy L., Bonnet C., Boukhgalter B., Bourzgui I., Brown A., Cahill P., Channer S., Cheshatsang Y., Chuda L., Citroen M., Collymore A., Cooke P., Costello M., D'Aco K., Daza R., De Haan G., DeGray S., DeMaso C., Dhargay N., Dooley K., Dooley E., Doricent M., Dorje P., Dorjee K., Dupes A., Elong R., Falk J., Farina A., Faro S., Ferguson D., Fisher S., Foley C.D., Franke A., Friedrich D., Gadbois L., Gearin G., Gearin C.R., Giannoukos G., Goode T., Graham J., Grandbois E., Grewal S., Gyaltsen K., Hafez N., Hagos B., Hall J., Henson C., Hollinger A., Honan T., Huard M.D., Hughes L., Hurhula B., Husby M.E., Kamat A., Kanga B., Kashin S., Khazanovich D., Kisner P., Lance K., Lara M., Lee W., Lennon N., Letendre F., LeVine R., Lipovsky A., Liu X., Liu J., Liu S., Lokyitsang T., Lokyitsang Y., Lubonja R., Lui A., MacDonald P., Magnisalis V., Maru K., Matthews C., McCusker W., McDonough S., Mehta T., Meldrim J., Meneus L., Mihai O., Mihalev A., Mihova T., Mittelman R., Mlenga V., Montmayeur A., Mulrain L., Navidi A., Naylor J., Negash T., Nguyen T., Nguyen N., Nicol R., Norbu C., Norbu N., Novod N., O'Neill B., Osman S., Markiewicz E., Oyono O.L., Patti C., Phunkhang P., Pierre F., Priest M., Raghuraman S., Rege F., Reyes R., Rise C., Rogov P., Ross K., Ryan E., Settipalli S., Shea T., Sherpa N., Shi L., Shih D., Sparrow T., Spaulding J., Stalker J., Stange-Thomann N., Stavropoulos S., Stone C., Strader C., Tesfaye S., Thomson T., Thoulutsang Y., Thoulutsang D., Topham K., Topping I., Tsamla T., Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M., Wilkinson J., Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D., Zimmer A., Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J., Chin C., Gnerre S., Grabherr M., Kleber M., Mauceli E., MacCallum I.
Nature 450:203-218(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Tucson 15081-1352.22.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CH933809 Genomic DNA. Translation: EDW19381.1.
RefSeqXP_002008905.1. XM_002008869.1.

3D structure databases

ProteinModelPortalB4KV41.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0162281; FBpp0160773; FBgn0134316.
GeneID6583232.
KEGGdmo:Dmoj_GI11556.

Organism-specific databases

FlyBaseFBgn0134316. Dmoj\GI11556.

Phylogenomic databases

InParanoidB4KV41.
KOK01785.
OrthoDBEOG7V7666.

Enzyme and pathway databases

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. SSF74650. 1 hit.
ProtoNetSearch...

Entry information

Entry nameB4KV41_DROMO
AccessionPrimary (citable) accession number: B4KV41
Entry history
Integrated into UniProtKB/TrEMBL: September 23, 2008
Last sequence update: September 23, 2008
Last modified: November 13, 2013
This is version 32 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