GGH1_ARATH
ID GGH1_ARATH Reviewed; 348 AA.
AC Q9SYL6; Q29Q19; Q93Z97;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 132.
DE RecName: Full=Gamma-glutamyl hydrolase 1;
DE Short=AtGGH1;
DE EC=3.4.19.9;
DE AltName: Full=Conjugase;
DE AltName: Full=GH;
DE AltName: Full=Gamma-Glu-X carboxypeptidase;
DE Flags: Precursor;
GN Name=GGH1; OrderedLocusNames=At1g78660; ORFNames=T30F21.1;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia; TISSUE=Rosette leaf;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA Shinn P., Chen H., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=21070406; DOI=10.1111/j.1365-313x.2010.04330.x;
RA Akhtar T.A., Orsomando G., Mehrshahi P., Lara-Nunez A., Bennett M.J.,
RA Gregory J.F. III, Hanson A.D.;
RT "A central role for gamma-glutamyl hydrolases in plant folate
RT homeostasis.";
RL Plant J. 64:256-266(2010).
CC -!- FUNCTION: Cleaves the polyglutamate sidechains of folate polyglutamates
CC in the vacuole. Is important for polyglutamyl tail length determination
CC before vacuolar exit. Plays a role in folate stability and
CC intracellular folate content. {ECO:0000269|PubMed:21070406}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6S)-5,6,7,8-tetrahydrofolyl-(gamma-L-Glu)(n) + (n-1) H2O =
CC (6S)-5,6,7,8-tetrahydrofolate + (n-1) L-glutamate;
CC Xref=Rhea:RHEA:56784, Rhea:RHEA-COMP:14738, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:57453, ChEBI:CHEBI:141005;
CC EC=3.4.19.9;
CC -!- SUBCELLULAR LOCATION: Vacuole {ECO:0000305|PubMed:21070406}. Secreted,
CC extracellular space {ECO:0000250}. Secreted, cell wall {ECO:0000250}.
CC Note=Extracellular or cell-wall bound.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9SYL6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9SYL6-2; Sequence=VSP_053262;
CC -!- TISSUE SPECIFICITY: Highly expressed in roots and at lower levels in
CC leaves, stems and siliques. {ECO:0000269|PubMed:21070406}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions. {ECO:0000269|PubMed:21070406}.
CC -!- SIMILARITY: Belongs to the peptidase C26 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL15332.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AC007260; AAD30570.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE36133.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE36134.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE36135.1; -; Genomic_DNA.
DR EMBL; AY057702; AAL15332.1; ALT_FRAME; mRNA.
DR EMBL; AK317198; BAH19882.1; -; mRNA.
DR EMBL; BT024737; ABD59075.1; -; mRNA.
DR PIR; D96815; D96815.
DR RefSeq; NP_177987.1; NM_106513.5. [Q9SYL6-1]
DR RefSeq; NP_849900.1; NM_179569.4. [Q9SYL6-2]
DR RefSeq; NP_974172.1; NM_202443.3. [Q9SYL6-1]
DR AlphaFoldDB; Q9SYL6; -.
DR SMR; Q9SYL6; -.
DR STRING; 3702.AT1G78660.3; -.
DR MEROPS; C26.002; -.
DR PaxDb; Q9SYL6; -.
DR PRIDE; Q9SYL6; -.
DR ProteomicsDB; 221835; -. [Q9SYL6-1]
DR EnsemblPlants; AT1G78660.1; AT1G78660.1; AT1G78660. [Q9SYL6-1]
DR EnsemblPlants; AT1G78660.2; AT1G78660.2; AT1G78660. [Q9SYL6-2]
DR EnsemblPlants; AT1G78660.3; AT1G78660.3; AT1G78660. [Q9SYL6-1]
DR GeneID; 844202; -.
DR Gramene; AT1G78660.1; AT1G78660.1; AT1G78660. [Q9SYL6-1]
DR Gramene; AT1G78660.2; AT1G78660.2; AT1G78660. [Q9SYL6-2]
DR Gramene; AT1G78660.3; AT1G78660.3; AT1G78660. [Q9SYL6-1]
DR KEGG; ath:AT1G78660; -.
DR Araport; AT1G78660; -.
DR TAIR; locus:2037583; AT1G78660.
DR eggNOG; KOG1559; Eukaryota.
DR InParanoid; Q9SYL6; -.
DR OMA; QNYTRNA; -.
DR OrthoDB; 877490at2759; -.
DR PhylomeDB; Q9SYL6; -.
DR PRO; PR:Q9SYL6; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SYL6; baseline and differential.
DR Genevisible; Q9SYL6; AT.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR GO; GO:0005773; C:vacuole; IDA:TAIR.
DR GO; GO:0034722; F:gamma-glutamyl-peptidase activity; IBA:GO_Central.
DR GO; GO:0008242; F:omega peptidase activity; IDA:TAIR.
DR GO; GO:0046900; P:tetrahydrofolylpolyglutamate metabolic process; IDA:TAIR.
DR Gene3D; 3.40.50.880; -; 1.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR015527; Pept_C26_g-glut_hydrolase.
DR InterPro; IPR011697; Peptidase_C26.
DR PANTHER; PTHR11315; PTHR11315; 1.
DR Pfam; PF07722; Peptidase_C26; 1.
DR SUPFAM; SSF52317; SSF52317; 1.
DR PROSITE; PS51275; PEPTIDASE_C26_GGH; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cell wall; Hydrolase; Reference proteome; Secreted;
KW Signal; Vacuole.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..348
FT /note="Gamma-glutamyl hydrolase 1"
FT /id="PRO_0000423721"
FT DOMAIN 46..342
FT /note="Gamma-glutamyl hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00607"
FT ACT_SITE 156
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00607"
FT ACT_SITE 269
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00607"
FT VAR_SEQ 2..18
FT /note="IDNNCLYKEELNRNSYS -> WRYICLPFFLLLWNDI (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:19423640, ECO:0000303|Ref.5"
FT /id="VSP_053262"
SQ SEQUENCE 348 AA; 39057 MW; 6C1E3F0A7EEE84C4 CRC64;
MIDNNCLYKE ELNRNSYSGL AKEASESILL PSESGFDGSR SPVCSSPDPN LNYRPVIGIL
SHPGDGASGR LTNDTSSTYI AASYVKFAEA GGARVIPLIY NEPEEVLFQK LELVNGVIFT
GGWAKKYDYF EIVKKIFTKA LERNDAGEHF PVYGICLGFE LMSIIISQNR DILERFDAED
NASSLQFVDN VNNDGTLFQR FPPELLKKLS TDCLVMQKHK YGITPANFQA NPALSSFFEI
LTTCIDENSK TYVSTVKAKR YPITGFQWHP EKNAFEWGSS AIPHSEDAIQ VTQHAASYLV
SEARKSLNRP ESQKVLSNLI YNYKPTYCGY AGRGYDEVYI FTQPRSRF
