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Q9VKX2 (Q9VKX2_DROME) Unreviewed, UniProtKB/TrEMBL

Last modified January 25, 2012. Version 93. 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:
Malate dehydrogenase RuleBase RU003405

EC=1.1.1.37 RuleBase RU003405
Gene names
Name:Mdh1 FlyBase FBgn0262782
Synonyms:CG5362-RA EMBL AEK87152.1
ORF Names:CG5362 FlyBase FBgn0032237, Dmel_CG5362 EMBL AAF52935.2
OrganismDrosophila melanogaster (Fruit fly)
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length337 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Catalytic activity

(S)-malate + NAD+ = oxaloacetate + NADH. RuleBase RU003405

Sequence similarities

Belongs to the LDH/MDH superfamily. MDH type 2 family. RuleBase RU000421

Sequences

Sequence LengthMass (Da)Tools
Q9VKX2 [UniParc].

Last modified October 1, 2002. Version 2.
Checksum: 56E6D4E708B04A89

FASTA33736,059
        10         20         30         40         50         60 
MAEPIRVVVT GAAGQIAYSL LYMIARGEVF GKDQPIVLHL LDIPPMVGVL EGVVMELADC 

        70         80         90        100        110        120 
ALPLLVEVVP TTDPAVGFKD VSAAFLVGAM PRKEGMERKD LLSANVKIFR TQGQALDKFA 

       130        140        150        160        170        180 
KKDVKVLVVG NPANTNALVC SSYAPSIPRE NFSAMTRLDQ NRATSQIAAK LGVPISAVKN 

       190        200        210        220        230        240 
IIIWGNHSST QYPDAGQAKV TANGTVKSVV DAINDNGYLQ GSFVETVQKR GAAVIAARKM 

       250        260        270        280        290        300 
SSAMSAAKAA CDHMHDWWNG TAPGQFVSMG VFSDGSYDSP KDVIFSFPVE IKNKQWKIVS 

       310        320        330 
GLTLSDFAKT KLSVTGKELQ EEKDEALSVL DSNVSNL 

« Hide

References

« Hide 'large scale' references
[1]"The genome sequence of Drosophila melanogaster."
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. expand/collapse author list , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.H., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Gabor G.L., Abril J.F., Agbayani A., An H.J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., WoodageT, Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
Science 287:2185-2195(2000) [PubMed: 10731132] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[2]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Strain: Berkeley.
[3]Carlson J., Booth B., Frise E., Sandler J., Wan K., Yu C., Celniker S.
Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE014134 Genomic DNA. Translation: AAF52935.2.
BT128780 mRNA. Translation: AEK87152.1.
RefSeqNP_609394.1. NM_135550.1.
UniGeneDm.11601.

3D structure databases

HSSPHSSP built from PDB template 4MDH based on UniProtKB P11708.
ProteinModelPortalQ9VKX2.
SMRQ9VKX2. Positions 2-332.
ModBaseSearch...

Protein-protein interaction databases

IntActQ9VKX2. 2 interactions.
MINTMINT-1559678.
STRINGQ9VKX2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0080050; FBpp0079640; FBgn0262782.
GeneID34414.
KEGGdme:Dmel_CG5362.
NMPDRfig|7227.3.peg.1814.
UCSCCG5362-RA. d. melanogaster.

Organism-specific databases

FlyBaseFBgn0262782. Mdh1.

Phylogenomic databases

GeneTreeEMGT00050000006654.
InParanoidQ9VKX2.
OMANFSAMTR.
PhylomeDBQ9VKX2.

Gene expression databases

ArrayExpressQ9VKX2.
BgeeQ9VKX2.

Family and domain databases

HAMAPMF_01517. Malate_dehydrog_2.
[Tree]
InterProIPR001557. L-lactate/malate_DH.
IPR022383. Lactate/malate_DH_C.
IPR001236. Lactate/malate_DH_N.
IPR015955. Lactate_DH/Glyco_Ohase_4_C.
IPR001252. Malate_DH_AS.
IPR011274. Malate_DH_NAD-dep_euk.
IPR010945. Malate_DH_type2.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
Gene3DG3DSA:3.90.110.10. lact_mal_DH. 1 hit.
G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
KOK00025.
PANTHERPTHR23382. MDH_SF1. 1 hit.
PfamPF02866. Ldh_1_C. 1 hit.
PF00056. Ldh_1_N. 1 hit.
[Graphical view]
PIRSFPIRSF000102. Lac_mal_DH. 1 hit.
SUPFAMSSF56327. Lactate_DH/Glyco_hydro_4_C. 1 hit.
TIGRFAMsTIGR01759. MalateDH-SF1. 1 hit.
TIGR01758. MDH_euk_cyt. 1 hit.
PROSITEPS00068. MDH. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio788384.

Entry information

Entry nameQ9VKX2_DROME
AccessionPrimary (citable) accession number: Q9VKX2
Entry history
Integrated into UniProtKB/TrEMBL: May 1, 2000
Last sequence update: October 1, 2002
Last modified: January 25, 2012
This is version 93 of the entry and version 2 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)