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Protein

Gamma-glutamyl hydrolase 2

Gene

GGH2

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Cleaves the polyglutamate sidechains of folate polyglutamates in the vacuole. Is important for polyglutamyl tail length determination before vacuolar exit. Plays a role on folate stability and intracellular folate content. Has endopeptidase activity against 4-amino-10-methylpteroyl penta-, tetra-, tri- and di-gamma-L-glutamate substrates and is responsible for the production of folic acid, also called pteroylglutamic acid (PteGlu) from teroylpolyglutamates.1 Publication

Catalytic activityi

Hydrolysis of a gamma-glutamyl bond.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei155 – 1551NucleophilePROSITE-ProRule annotation
Active sitei268 – 2681Proton donorPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

  • glutamine metabolic process Source: InterPro
  • proteolysis Source: GOC
  • tetrahydrofolylpolyglutamate metabolic process Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Enzyme and pathway databases

BioCyciARA:GQT-2768-MONOMER.
BRENDAi3.4.19.9. 399.

Protein family/group databases

MEROPSiC26.003.

Names & Taxonomyi

Protein namesi
Recommended name:
Gamma-glutamyl hydrolase 2 (EC:3.4.19.9)
Short name:
AtGGH2
Alternative name(s):
Conjugase
GH
Gamma-Glu-X carboxypeptidase
Gene namesi
Name:GGH2
Synonyms:GGH, GGH1
Ordered Locus Names:At1g78680
ORF Names:F9K20.28
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 1

Organism-specific databases

TAIRiAT1G78680.

Subcellular locationi

GO - Cellular componenti

  • cell wall Source: UniProtKB
  • extracellular space Source: UniProtKB
  • vacuole Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Cell wall, Secreted, Vacuole

Pathology & Biotechi

Disruption phenotypei

No visible phenotype under normal growth conditions.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222Sequence analysisAdd
BLAST
Chaini23 – 347325Gamma-glutamyl hydrolase 2PRO_0000026542Add
BLAST

Proteomic databases

PaxDbiO65355.
PRIDEiO65355.

Expressioni

Tissue specificityi

Expressed in roots, in leaves, stems and siliques.1 Publication

Gene expression databases

ExpressionAtlasiO65355. baseline and differential.
GenevisibleiO65355. AT.

Interactioni

Protein-protein interaction databases

BioGridi29423. 1 interaction.
IntActiO65355. 1 interaction.
STRINGi3702.AT1G78680.1.

Structurei

3D structure databases

ProteinModelPortaliO65355.
SMRiO65355. Positions 51-340.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini45 – 341297Gamma-glutamyl hydrolasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase C26 family.Curated
Contains 1 gamma-glutamyl hydrolase domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG1559. Eukaryota.
ENOG410XQKI. LUCA.
HOGENOMiHOG000006721.
InParanoidiO65355.
OMAiACHQHRY.
PhylomeDBiO65355.

Family and domain databases

Gene3Di3.40.50.880. 1 hit.
InterProiIPR029062. Class_I_gatase-like.
IPR015527. Pept_C26_g-glut_hydrolase.
IPR011697. Peptidase_C26.
[Graphical view]
PANTHERiPTHR11315. PTHR11315. 1 hit.
PfamiPF07722. Peptidase_C26. 1 hit.
[Graphical view]
SUPFAMiSSF52317. SSF52317. 1 hit.
PROSITEiPS51275. PEPTIDASE_C26_GGH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 1 isoform i produced by alternative splicing. AlignAdd to basket

Note: A number of isoforms are produced. According to EST sequences.

Isoform 1 (identifier: O65355-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MWSYVWLPLV ALSLFKDSII MAKAATILLP SQTGFDISRS PVCSAPDPNL
60 70 80 90 100
NYRPVIGILS HPGDGASGRL SNATDASSIA ASYVKLAESG GARVIPLIFN
110 120 130 140 150
EPEEILFQKL ELVNGVILTG GWAKEGLYFE IVKKIFNKVL ERNDAGEHFP
160 170 180 190 200
IYAICLGFEL LTMIISQNRD IFEKMDARNS ASSLQFVENV NIQGTIFQRF
210 220 230 240 250
PPELLKKLGT DCLVMQNHRF GISPQSFEGN IALSNFFKIV TTCVDDNGKV
260 270 280 290 300
YVSTVQSTKY PVTGFQWHPE KNAFEWGSSK IPHSEDAIQV TQHAANHLVS
310 320 330 340
EARKSLNRPE SKKVLSNLIY NYKPTYCGYA GIGYDEVYIF TQQRSLL
Length:347
Mass (Da):38,642
Last modified:December 6, 2002 - v2
Checksum:iE81DFE8B4B5CAA4F
GO

Sequence cautioni

The sequence AAC33745.1 differs from that shown. Reason: Frameshift at positions 22, 24, 43 and 60. Curated
The sequence AAC83041.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti34 – 341G → A in AAC33745 (Ref. 4) Curated
Sequence conflicti64 – 641D → N in AAC33745 (Ref. 4) Curated
Sequence conflicti74 – 741T → I in AAC33745 (Ref. 4) Curated
Sequence conflicti77 – 771S → P in AAC33745 (Ref. 4) Curated
Sequence conflicti103 – 1031E → G in AAC33745 (Ref. 4) Curated
Sequence conflicti136 – 1361F → L in AAC33745 (Ref. 4) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC005679 Genomic DNA. Translation: AAC83041.1. Different initiation.
CP002684 Genomic DNA. Translation: AEE36137.1.
AY096428 mRNA. Translation: AAM20068.1.
AY070047 mRNA. Translation: AAL49804.1.
AF067141 mRNA. Translation: AAC33745.1. Frameshift.
PIRiF96815.
T52030.
RefSeqiNP_565186.2. NM_106515.3. [O65355-1]
UniGeneiAt.10894.

Genome annotation databases

EnsemblPlantsiAT1G78680.1; AT1G78680.1; AT1G78680. [O65355-1]
GeneIDi844204.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC005679 Genomic DNA. Translation: AAC83041.1. Different initiation.
CP002684 Genomic DNA. Translation: AEE36137.1.
AY096428 mRNA. Translation: AAM20068.1.
AY070047 mRNA. Translation: AAL49804.1.
AF067141 mRNA. Translation: AAC33745.1. Frameshift.
PIRiF96815.
T52030.
RefSeqiNP_565186.2. NM_106515.3. [O65355-1]
UniGeneiAt.10894.

3D structure databases

ProteinModelPortaliO65355.
SMRiO65355. Positions 51-340.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi29423. 1 interaction.
IntActiO65355. 1 interaction.
STRINGi3702.AT1G78680.1.

Protein family/group databases

MEROPSiC26.003.

Proteomic databases

PaxDbiO65355.
PRIDEiO65355.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT1G78680.1; AT1G78680.1; AT1G78680. [O65355-1]
GeneIDi844204.

Organism-specific databases

TAIRiAT1G78680.

Phylogenomic databases

eggNOGiKOG1559. Eukaryota.
ENOG410XQKI. LUCA.
HOGENOMiHOG000006721.
InParanoidiO65355.
OMAiACHQHRY.
PhylomeDBiO65355.

Enzyme and pathway databases

BioCyciARA:GQT-2768-MONOMER.
BRENDAi3.4.19.9. 399.

Miscellaneous databases

PROiO65355.

Gene expression databases

ExpressionAtlasiO65355. baseline and differential.
GenevisibleiO65355. AT.

Family and domain databases

Gene3Di3.40.50.880. 1 hit.
InterProiIPR029062. Class_I_gatase-like.
IPR015527. Pept_C26_g-glut_hydrolase.
IPR011697. Peptidase_C26.
[Graphical view]
PANTHERiPTHR11315. PTHR11315. 1 hit.
PfamiPF07722. Peptidase_C26. 1 hit.
[Graphical view]
SUPFAMiSSF52317. SSF52317. 1 hit.
PROSITEiPS51275. PEPTIDASE_C26_GGH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
    Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K.
    , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
    Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  2. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  3. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
    , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  4. "Cloning of a gamma-glutamyl hydrolase cDNA from Arabidopsis."
    Rickle S.A., Xu H., Liu C.Y., Morris P.F., Graham J.S.
    Plant Gene Register PGR98-146
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 13-347, CHARACTERIZATION.
    Strain: cv. Columbia.
  5. "A central role for gamma-glutamyl hydrolases in plant folate homeostasis."
    Akhtar T.A., Orsomando G., Mehrshahi P., Lara-Nunez A., Bennett M.J., Gregory J.F. III, Hanson A.D.
    Plant J. 64:256-266(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.

Entry informationi

Entry nameiGGH2_ARATH
AccessioniPrimary (citable) accession number: O65355
Secondary accession number(s): Q8VYT0, Q9ZV86
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: December 6, 2002
Last modified: November 11, 2015
This is version 119 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

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 one 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.