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H0P291

- H0P291_9SYNC

UniProt

H0P291 - H0P291_9SYNC

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Protein

Glutamate decarboxylase

Gene

gad

Organism
Synechocystis sp. PCC 6803 substr. GT-I
Status
Unreviewed - Annotation score: 2 out of 5- Protein inferred from homologyi

Functioni

Catalytic activityi

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

Cofactori

Note: Pyridoxal phosphate.UniRule 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

BioCyciSSP1080228:GLM4-494-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate decarboxylaseUniRule annotation (EC:4.1.1.15UniRule annotation)
Gene namesi
Name:gadImported
ORF Names:SYNGTI_0488Imported
OrganismiSynechocystis sp. PCC 6803 substr. GT-IImported
Taxonomic identifieri1080228 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechocystis
ProteomesiUP000007109: Chromosome

Structurei

3D structure databases

ProteinModelPortaliH0P291.
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.

H0P291-1 [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
AP012276 Genomic DNA. Translation: BAL28235.1.
RefSeqiYP_005382250.1. NC_017038.1.

Genome annotation databases

EnsemblBacteriaiBAL28235; BAL28235; SYNGTI_0488.
GeneIDi11972902.
KEGGisyt:SYNGTI_0488.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP012276 Genomic DNA. Translation: BAL28235.1 .
RefSeqi YP_005382250.1. NC_017038.1.

3D structure databases

ProteinModelPortali H0P291.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAL28235 ; BAL28235 ; SYNGTI_0488 .
GeneIDi 11972902.
KEGGi syt:SYNGTI_0488.

Phylogenomic databases

KOi K01580.

Enzyme and pathway databases

BioCyci SSP1080228:GLM4-494-MONOMER.

Family and domain databases

Gene3Di 3.40.640.10. 1 hit.
InterProi IPR010107. Glutamate_decarboxylase.
IPR002129. PyrdxlP-dep_de-COase.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
[Graphical view ]
PANTHERi PTHR11999:SF1. PTHR11999:SF1. 1 hit.
Pfami PF00282. Pyridoxal_deC. 1 hit.
[Graphical view ]
SUPFAMi SSF53383. SSF53383. 1 hit.
TIGRFAMsi TIGR01788. Glu-decarb-GAD. 1 hit.
ProtoNeti Search...

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 nameiH0P291_9SYNC
AccessioniPrimary (citable) accession number: H0P291
Entry historyi
Integrated into UniProtKB/TrEMBL: February 22, 2012
Last sequence update: February 22, 2012
Last modified: November 26, 2014
This is version 19 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