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Protein

Glutamate decarboxylase

Gene

gad

Organism
Synechocystis sp. PCC 6803 substr. PCC-P
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

Enzyme and pathway databases

BioCyciSSP1080230:GLM3-494-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate decarboxylaseUniRule annotation (EC:4.1.1.15UniRule annotation)
Gene namesi
Name:gadImported
ORF Names:SYNPCCP_0488Imported
OrganismiSynechocystis sp. PCC 6803 substr. PCC-PImported
Taxonomic identifieri1080230 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechocystis
ProteomesiUP000007107: Chromosome

Structurei

3D structure databases

ProteinModelPortaliH0PJX2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the group II decarboxylase family.UniRule annotation

Phylogenomic databases

KOiK01580.

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]
PANTHERiPTHR11999:SF1. PTHR11999:SF1. 1 hit.
PfamiPF00282. Pyridoxal_deC. 1 hit.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR01788. Glu-decarb-GAD. 1 hit.

Sequencei

Sequence statusi: Complete.

H0PJX2-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MVHKKIDLNQ LSEAESLLTP TYAARGLANS VSKYEMPETE MLPAIAYNLI
60 70 80 90 100
HDELGLDGNS RLNLATFVTT WMEPEARQLM ADTFDKNMID KDEYPQTAEI
110 120 130 140 150
ELRCVNILSR LWNAPASAEA TGCSTIGSSE AAMLGGMAMK WKWRQRRQAA
160 170 180 190 200
GKPGDRPNLV MGINVQVCWE KFCRYWEVEP RFVPMEGDRY HISPEEAVKL
210 220 230 240 250
IDENTIGVIG ILGSTFDGSY EPIEALNDAL ETLNQRTGWQ VPLHIDAASG
260 270 280 290 300
GFIAPFLDPD LRWDFRLPWV KSINTSGHKY GLVYPGVGWI IWRDKEELPE
310 320 330 340 350
ELIFHCNYLG GDLPNFALNF SRPGNQVVAQ YYNFLRLGKE GYRKIQQTCR
360 370 380 390 400
DTALYLSGKI AQLGPFELLT DGGDIPVFAW RLKDEVLANT CYTLYDMADK
410 420 430 440 450
LRERGWLVPA YRMPKNREDL VVQRIVVKEG FSRDMADLLL ADMERAIAYF
460
ASQPDHKPKQ EGSHFSH
Length:467
Mass (Da):53,041
Last modified:February 22, 2012 - v1
Checksum:i7C0BDFA030743153
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP012278 Genomic DNA. Translation: BAL34574.1.
RefSeqiWP_010871692.1. NC_017039.1.
YP_005385420.1. NC_017039.1.

Genome annotation databases

EnsemblBacteriaiBAL34574; BAL34574; SYNPCCP_0488.
GeneIDi11976113.
KEGGisyq:SYNPCCP_0488.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP012278 Genomic DNA. Translation: BAL34574.1.
RefSeqiWP_010871692.1. NC_017039.1.
YP_005385420.1. NC_017039.1.

3D structure databases

ProteinModelPortaliH0PJX2.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAL34574; BAL34574; SYNPCCP_0488.
GeneIDi11976113.
KEGGisyq:SYNPCCP_0488.

Phylogenomic databases

KOiK01580.

Enzyme and pathway databases

BioCyciSSP1080230:GLM3-494-MONOMER.

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]
PANTHERiPTHR11999:SF1. PTHR11999:SF1. 1 hit.
PfamiPF00282. Pyridoxal_deC. 1 hit.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR01788. Glu-decarb-GAD. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Identification of substrain-specific mutations by massively parallel whole-genome resequencing of Synechocystis sp. PCC 6803."
    Kanesaki Y., Shiwa Y., Tajima N., Suzuki M., Watanabe S., Sato N., Ikeuchi M., Yoshikawa H.
    DNA Res. 19:67-79(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Entry informationi

Entry nameiH0PJX2_9SYNC
AccessioniPrimary (citable) accession number: H0PJX2
Entry historyi
Integrated into UniProtKB/TrEMBL: February 22, 2012
Last sequence update: February 22, 2012
Last modified: February 4, 2015
This is version 21 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete 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.