GGH3_ARATH
ID GGH3_ARATH Reviewed; 352 AA.
AC Q9ZV85; Q8LA07;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 25-MAY-2022, entry version 135.
DE RecName: Full=Probable gamma-glutamyl hydrolase 3;
DE Short=AtGGH3;
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=GGH3; OrderedLocusNames=At1g78670; ORFNames=F9K20.29;
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 [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). {ECO:0000250}.
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:0000250}. Secreted, extracellular
CC space {ECO:0000250}. Secreted, cell wall {ECO:0000250}.
CC Note=Extracellular or cell-wall bound.
CC -!- SIMILARITY: Belongs to the peptidase C26 family. {ECO:0000305}.
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DR EMBL; AC005679; AAC83042.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE36136.1; -; Genomic_DNA.
DR EMBL; AF389281; AAK63854.1; -; mRNA.
DR EMBL; BT000554; AAN18123.1; -; mRNA.
DR EMBL; AY088100; AAM65646.1; -; mRNA.
DR PIR; E96815; E96815.
DR RefSeq; NP_177988.1; NM_106514.4.
DR AlphaFoldDB; Q9ZV85; -.
DR SMR; Q9ZV85; -.
DR BioGRID; 29422; 1.
DR STRING; 3702.AT1G78670.1; -.
DR MEROPS; C26.A01; -.
DR PaxDb; Q9ZV85; -.
DR PRIDE; Q9ZV85; -.
DR ProteomicsDB; 221837; -.
DR EnsemblPlants; AT1G78670.1; AT1G78670.1; AT1G78670.
DR GeneID; 844203; -.
DR Gramene; AT1G78670.1; AT1G78670.1; AT1G78670.
DR KEGG; ath:AT1G78670; -.
DR Araport; AT1G78670; -.
DR TAIR; locus:2037573; AT1G78670.
DR eggNOG; KOG1559; Eukaryota.
DR HOGENOM; CLU_058704_0_0_1; -.
DR InParanoid; Q9ZV85; -.
DR OMA; IYNEPQE; -.
DR OrthoDB; 877490at2759; -.
DR PRO; PR:Q9ZV85; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9ZV85; baseline and differential.
DR Genevisible; Q9ZV85; AT.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0005773; C:vacuole; IBA:GO_Central.
DR GO; GO:0034722; F:gamma-glutamyl-peptidase activity; IBA:GO_Central.
DR GO; GO:0046900; P:tetrahydrofolylpolyglutamate metabolic process; IBA:GO_Central.
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 Cell wall; Hydrolase; Reference proteome; Secreted; Signal; Vacuole.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..352
FT /note="Probable gamma-glutamyl hydrolase 3"
FT /id="PRO_0000423722"
FT DOMAIN 49..352
FT /note="Gamma-glutamyl hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00607"
FT ACT_SITE 166
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00607"
FT ACT_SITE 279
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00607"
FT CONFLICT 8
FT /note="L -> I (in Ref. 4; AAM65646)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 352 AA; 39882 MW; 2427B147EC8B40E8 CRC64;
MWRFCFFLSL LFFDVSAVKS AESIFLPSQI GVEDSRVFES LSLSPVCSAA DPNLNYKPVI
GILTHPGEGR WDARLHSLKN YAYATNISYI AASYVKLAET GGARVIPLIY NEPEEILFQK
LELVNGVIFT GGWAKTGLYY DVVEKIFNKV MEKNDAGEHF PVYAMCLGFE ILSMIISQNR
DILERFNSVN YASSLQFFKN VNIEATVFQR FPPELLKKLS ADCLVMQNHY FGISPDNFQG
NPYLSSFFNI VTTSADKDSK TFVSTIRSKR YPVTAFQWHP EKNAFEWGSS EIPHSEDAIQ
VTQHAANYLV SEARKSMNRP SSEKVLSNLI YNYKPTYSGY KGSGDDEVYI FT
