GGH2_ARATH
ID GGH2_ARATH Reviewed; 347 AA.
AC O65355; Q8VYT0; Q9ZV86;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2002, sequence version 2.
DT 25-MAY-2022, entry version 151.
DE RecName: Full=Gamma-glutamyl hydrolase 2;
DE Short=AtGGH2;
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=GGH2; Synonyms=GGH, GGH1; OrderedLocusNames=At1g78680;
GN ORFNames=F9K20.28;
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].
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 [MRNA] OF 13-347, AND CHARACTERIZATION.
RC STRAIN=cv. Columbia;
RA Rickle S.A., Xu H., Liu C.Y., Morris P.F., Graham J.S.;
RT "Cloning of a gamma-glutamyl hydrolase cDNA from Arabidopsis.";
RL (er) Plant Gene Register PGR98-146(1998).
RN [5]
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 on folate stability and
CC intracellular folate content. Has endopeptidase activity against 4-
CC amino-10-methylpteroyl penta-, tetra-, tri- and di-gamma-L-glutamate
CC substrates and is responsible for the production of folic acid, also
CC called pteroylglutamic acid (PteGlu) from teroylpolyglutamates.
CC {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=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=O65355-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in roots, in leaves, stems and siliques.
CC {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=AAC33745.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAC83041.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC005679; AAC83041.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002684; AEE36137.1; -; Genomic_DNA.
DR EMBL; AY096428; AAM20068.1; -; mRNA.
DR EMBL; AY070047; AAL49804.1; -; mRNA.
DR EMBL; AF067141; AAC33745.1; ALT_FRAME; mRNA.
DR PIR; F96815; F96815.
DR PIR; T52030; T52030.
DR RefSeq; NP_565186.2; NM_106515.4. [O65355-1]
DR AlphaFoldDB; O65355; -.
DR SMR; O65355; -.
DR BioGRID; 29423; 1.
DR IntAct; O65355; 1.
DR STRING; 3702.AT1G78680.1; -.
DR MEROPS; C26.003; -.
DR PaxDb; O65355; -.
DR PRIDE; O65355; -.
DR ProteomicsDB; 221836; -. [O65355-1]
DR EnsemblPlants; AT1G78680.1; AT1G78680.1; AT1G78680. [O65355-1]
DR GeneID; 844204; -.
DR Gramene; AT1G78680.1; AT1G78680.1; AT1G78680. [O65355-1]
DR KEGG; ath:AT1G78680; -.
DR Araport; AT1G78680; -.
DR TAIR; locus:2037603; AT1G78680.
DR eggNOG; KOG1559; Eukaryota.
DR HOGENOM; CLU_058704_0_0_1; -.
DR InParanoid; O65355; -.
DR OrthoDB; 877490at2759; -.
DR PhylomeDB; O65355; -.
DR BRENDA; 3.4.19.9; 399.
DR PRO; PR:O65355; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; O65355; baseline and differential.
DR Genevisible; O65355; AT.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR GO; GO:0009505; C:plant-type cell wall; ISS:UniProtKB.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
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 1: Evidence at protein level;
KW Alternative splicing; Cell wall; Hydrolase; Reference proteome; Secreted;
KW Signal; Vacuole.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..347
FT /note="Gamma-glutamyl hydrolase 2"
FT /id="PRO_0000026542"
FT DOMAIN 45..341
FT /note="Gamma-glutamyl hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00607"
FT ACT_SITE 155
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00607"
FT ACT_SITE 268
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00607"
FT CONFLICT 34
FT /note="G -> A (in Ref. 4; AAC33745)"
FT /evidence="ECO:0000305"
FT CONFLICT 64
FT /note="D -> N (in Ref. 4; AAC33745)"
FT /evidence="ECO:0000305"
FT CONFLICT 74
FT /note="T -> I (in Ref. 4; AAC33745)"
FT /evidence="ECO:0000305"
FT CONFLICT 77
FT /note="S -> P (in Ref. 4; AAC33745)"
FT /evidence="ECO:0000305"
FT CONFLICT 103
FT /note="E -> G (in Ref. 4; AAC33745)"
FT /evidence="ECO:0000305"
FT CONFLICT 136
FT /note="F -> L (in Ref. 4; AAC33745)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 347 AA; 38642 MW; E81DFE8B4B5CAA4F CRC64;
MWSYVWLPLV ALSLFKDSII MAKAATILLP SQTGFDISRS PVCSAPDPNL NYRPVIGILS
HPGDGASGRL SNATDASSIA ASYVKLAESG GARVIPLIFN EPEEILFQKL ELVNGVILTG
GWAKEGLYFE IVKKIFNKVL ERNDAGEHFP IYAICLGFEL LTMIISQNRD IFEKMDARNS
ASSLQFVENV NIQGTIFQRF PPELLKKLGT DCLVMQNHRF GISPQSFEGN IALSNFFKIV
TTCVDDNGKV YVSTVQSTKY PVTGFQWHPE KNAFEWGSSK IPHSEDAIQV TQHAANHLVS
EARKSLNRPE SKKVLSNLIY NYKPTYCGYA GIGYDEVYIF TQQRSLL
