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Protein

Glutamate decarboxylase

Gene

MTR_3g064740

Organism
Medicago truncatula (Barrel medic) (Medicago tribuloides)
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

Catalytic activityi

L-glutamate = 4-aminobutanoate + CO2.UniRule annotation

Cofactori

pyridoxal 5'-phosphateUniRule annotation

GO - Molecular functioni

  1. glutamate decarboxylase activity Source: UniProtKB-EC
  2. pyridoxal phosphate binding Source: InterPro

GO - Biological processi

  1. glutamate metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

DecarboxylaseUniRule annotation, Lyase

Keywords - Ligandi

Pyridoxal phosphateUniRule annotation

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate decarboxylaseUniRule annotation (EC:4.1.1.15UniRule annotation)
Gene namesi
Ordered Locus Names:MTR_3g064740Imported
OrganismiMedicago truncatula (Barrel medic) (Medicago tribuloides)Imported
Taxonomic identifieri3880 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaeTrifolieaeMedicago
ProteomesiUP000002051 Componenti: Chromosome 3

Family & Domainsi

Sequence similaritiesi

Belongs to the group II decarboxylase family.UniRule annotation

Phylogenomic databases

KOiK01580.
OMAiENCRENM.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
InterProiIPR010107. Glutamate_decarboxylase.
IPR002129. PyrdxlP-dep_de-COase.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
[Graphical view]
PfamiPF00282. Pyridoxal_deC. 1 hit.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR01788. Glu-decarb-GAD. 1 hit.

Sequencei

Sequence statusi: Complete.

G7J8M7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVLSKTASES DVSVHSTFAS RYVRTSLPRF KMPEESIPKD AAYQIINDEL
60 70 80 90 100
MLDGNPRLNL ASFVTTWMEP ECDKLIMASI NKNYVDMDEY PVTTELQNRC
110 120 130 140 150
VNMIAHLFNA PLEENEAAVG VGTVGSSEAI MLAGLAFKRK WQNKRKQEGK
160 170 180 190 200
PYDKPNIVTG ANVQVCWEKF ARYFEVELKE VKLSEGYYVM DPAKAVELVD
210 220 230 240 250
ENTICVAAIL GSTLNGEFED VKRLNDLLVE KNKETGWDTP IHVDAASGGF
260 270 280 290 300
IAPFIYPELE WDFRLPLVKS INVSGHKYGL VYAGIGWAIW RSKEDLPEEL
310 320 330 340 350
IFHINYLGAD QPTFTLNFSK GSSQVIAQYY QLIRLGYEGY KNVMENCRDN
360 370 380 390 400
MIVLKEGLEK MGRFNIVSKD DGVPLVAFTL KDPHNFDEFQ ISDLLRRFGW
410 420 430 440 450
IVPAYSMPPD AQHITVLRVV IREDFSRTLA ERLVADIEKV LHELDSLTAK
460 470 480 490 500
IKMLSGTSSV TVHEVVKDNG QVVVAKKSAL ETQREITAIW KKFVLDRKKL

NDKMNGVC
Length:508
Mass (Da):57,501
Last modified:January 25, 2012 - v1
Checksum:i9FFCA655E302BA36
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC147472 Genomic DNA. No translation available.
CM001219 Genomic DNA. Translation: AES70904.1.
RefSeqiXP_003600653.1. XM_003600605.1.
UniGeneiMtr.2960.

Genome annotation databases

EnsemblPlantsiAES70904; AES70904; MTR_3g064740.
GeneIDi11408278.
KEGGimtr:MTR_3g064740.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC147472 Genomic DNA. No translation available.
CM001219 Genomic DNA. Translation: AES70904.1.
RefSeqiXP_003600653.1. XM_003600605.1.
UniGeneiMtr.2960.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAES70904; AES70904; MTR_3g064740.
GeneIDi11408278.
KEGGimtr:MTR_3g064740.

Phylogenomic databases

KOiK01580.
OMAiENCRENM.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
InterProiIPR010107. Glutamate_decarboxylase.
IPR002129. PyrdxlP-dep_de-COase.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
[Graphical view]
PfamiPF00282. Pyridoxal_deC. 1 hit.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR01788. Glu-decarb-GAD. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The Medicago genome provides insight into the evolution of rhizobial symbioses."
    Young N.D., Debelle F., Oldroyd G.E.D., Geurts R., Cannon S.B., Udvardi M.K., Benedito V.A., Mayer K.F.X., Gouzy J., Schoof H., Van de Peer Y., Proost S., Cook D.R., Meyers B.C., Spannagl M., Cheung F., De Mita S., Krishnakumar V.
    , Gundlach H., Zhou S., Mudge J., Bharti A.K., Murray J.D., Naoumkina M.A., Rosen B., Silverstein K.A.T., Tang H., Rombauts S., Zhao P.X., Zhou P., Barbe V., Bardou P., Bechner M., Bellec A., Berger A., Berges H., Bidwell S., Bisseling T., Choisne N., Couloux A., Denny R., Deshpande S., Dai X., Doyle J.J., Dudez A.-M., Farmer A.D., Fouteau S., Franken C., Gibelin C., Gish J., Goldstein S., Gonzalez A.J., Green P.J., Hallab A., Hartog M., Hua A., Humphray S.J., Jeong D.-H., Jing Y., Jocker A., Kenton S.M., Kim D.-J., Klee K., Lai H., Lang C., Lin S., Macmil S.L., Magdelenat G., Matthews L., McCorrison J., Monaghan E.L., Mun J.-H., Najar F.Z., Nicholson C., Noirot C., O'Bleness M., Paule C.R., Poulain J., Prion F., Qin B., Qu C., Retzel E.F., Riddle C., Sallet E., Samain S., Samson N., Sanders I., Saurat O., Scarpelli C., Schiex T., Segurens B., Severin A.J., Sherrier D.J., Shi R., Sims S., Singer S.R., Sinharoy S., Sterck L., Viollet A., Wang B.-B., Wang K., Wang M., Wang X., Warfsmann J., Weissenbach J., White D.D., White J.D., Wiley G.B., Wincker P., Xing Y., Yang L., Yao Z., Ying F., Zhai J., Zhou L., Zuber A., Denarie J., Dixon R.A., May G.D., Schwartz D.C., Rogers J., Quetier F., Town C.D., Roe B.A.
    Nature 480:520-524(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: A17Imported and cv. Jemalong A17Imported.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: A17.
  3. EnsemblPlants
    Submitted (JAN-2015) to UniProtKB
    Cited for: IDENTIFICATION.
    Strain: cv. Jemalong A17Imported.

Entry informationi

Entry nameiG7J8M7_MEDTR
AccessioniPrimary (citable) accession number: G7J8M7
Entry historyi
Integrated into UniProtKB/TrEMBL: January 25, 2012
Last sequence update: January 25, 2012
Last modified: April 1, 2015
This is version 20 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteomeImported

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.