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Protein

Glutamate decarboxylase

Gene

SELMODRAFT_444651

Organism
Selaginella moellendorffii (Spikemoss)
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
ORF Names:SELMODRAFT_444651Imported
OrganismiSelaginella moellendorffii (Spikemoss)Imported
Taxonomic identifieri88036 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaLycopodiidaeSelaginellalesSelaginellaceaeSelaginella
ProteomesiUP000001514 Componenti: Unassembled WGS sequence

Structurei

3D structure databases

ProteinModelPortaliD8SBV2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the group II decarboxylase family.UniRule annotation

Phylogenomic databases

InParanoidiD8SBV2.
KOiK01580.
OMAiLHEMPER.

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.

D8SBV2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVLTMTSEAD SSLQSTFASR YSQSSVSKYR IPDQETPKDA AYQIISDELM
60 70 80 90 100
LDGNPRLNLA SFVTTWMEPE CDKLVMASLN KNYIDMDEYP VTTELQDRCV
110 120 130 140 150
NMIARLFNAP VGDSEQAIGA GTIGSSEAIM LAGLALKRKW QNKRKAEGKP
160 170 180 190 200
WDKPNIVTGS NVQVCWEKFA RYFEVELKEV KLSKDYYVMD PHKAVEMVDE
210 220 230 240 250
NTICIAAILG STYNGEFEDV KLLNELLEKK NKETGWDTPI HVDAASGGFI
260 270 280 290 300
APFLYPDLEW DFRLPLVKSI NVSGHKYGLV YAGIGWVIWR GKEDLPEELV
310 320 330 340 350
FHINYLGADQ PTFTLNFSKG ASQIIAQYYQ LIRLGFRGYK SIMQNCQANA
360 370 380 390 400
KILADALVAT GRFVILSKEI GVPVVAFSLK DRKNHDEYEI ADHLRRYGWI
410 420 430 440 450
VPAYTMAPDA QDVTLLRVVV REDFSRTLAD RLVSDIVAVF KYLDAHPPRL
460 470 480 490 500
IQAVTEALAK DPEIKKELLD AEPGEVKAQL DLRKASVFED IRNSQRAFKV
510
WKKFALSKTN GVC
Length:513
Mass (Da):57,884
Last modified:October 4, 2010 - v1
Checksum:i1CC0A551B7BD146B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
GL377611 Genomic DNA. Translation: EFJ18071.1.
RefSeqiXP_002980886.1. XM_002980840.1.
UniGeneiSmo.1959.

Genome annotation databases

EnsemblPlantsiEFJ18071; EFJ18071; SELMODRAFT_444651.
GeneIDi9656977.
KEGGismo:SELMODRAFT_444651.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
GL377611 Genomic DNA. Translation: EFJ18071.1.
RefSeqiXP_002980886.1. XM_002980840.1.
UniGeneiSmo.1959.

3D structure databases

ProteinModelPortaliD8SBV2.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiEFJ18071; EFJ18071; SELMODRAFT_444651.
GeneIDi9656977.
KEGGismo:SELMODRAFT_444651.

Phylogenomic databases

InParanoidiD8SBV2.
KOiK01580.
OMAiLHEMPER.

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

  1. "The Selaginella genome identifies genetic changes associated with the evolution of vascular plants."
    Banks J.A., Nishiyama T., Hasebe M., Bowman J.L., Gribskov M., dePamphilis C., Albert V.A., Aono N., Aoyama T., Ambrose B.A., Ashton N.W., Axtell M.J., Barker E., Barker M.S., Bennetzen J.L., Bonawitz N.D., Chapple C., Cheng C.
    , Correa L.G., Dacre M., DeBarry J., Dreyer I., Elias M., Engstrom E.M., Estelle M., Feng L., Finet C., Floyd S.K., Frommer W.B., Fujita T., Gramzow L., Gutensohn M., Harholt J., Hattori M., Heyl A., Hirai T., Hiwatashi Y., Ishikawa M., Iwata M., Karol K.G., Koehler B., Kolukisaoglu U., Kubo M., Kurata T., Lalonde S., Li K., Li Y., Litt A., Lyons E., Manning G., Maruyama T., Michael T.P., Mikami K., Miyazaki S., Morinaga S., Murata T., Mueller-Roeber B., Nelson D.R., Obara M., Oguri Y., Olmstead R.G., Onodera N., Petersen B.L., Pils B., Prigge M., Rensing S.A., Riano-Pachon D.M., Roberts A.W., Sato Y., Scheller H.V., Schulz B., Schulz C., Shakirov E.V., Shibagaki N., Shinohara N., Shippen D.E., Soerensen I., Sotooka R., Sugimoto N., Sugita M., Sumikawa N., Tanurdzic M., Theissen G., Ulvskov P., Wakazuki S., Weng J.K., Willats W.W., Wipf D., Wolf P.G., Yang L., Zimmer A.D., Zhu Q., Mitros T., Hellsten U., Loque D., Otillar R., Salamov A., Schmutz J., Shapiro H., Lindquist E., Lucas S., Rokhsar D., Grigoriev I.V.
    Science 332:960-963(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Entry informationi

Entry nameiD8SBV2_SELML
AccessioniPrimary (citable) accession number: D8SBV2
Entry historyi
Integrated into UniProtKB/TrEMBL: October 4, 2010
Last sequence update: October 4, 2010
Last modified: January 6, 2015
This is version 22 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.