GGHB_DICDI
ID GGHB_DICDI Reviewed; 347 AA.
AC Q54HL4;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 96.
DE RecName: Full=Gamma-glutamyl hydrolase B;
DE EC=3.4.19.9;
DE AltName: Full=Conjugase B;
DE AltName: Full=GH B;
DE AltName: Full=Gamma-Glu-X carboxypeptidase B;
DE Flags: Precursor;
GN Name=gghB; ORFNames=DDB_G0289365;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
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: Secreted, extracellular space {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase C26 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AAFI02000139; EAL62769.1; -; Genomic_DNA.
DR RefSeq; XP_636287.1; XM_631195.1.
DR AlphaFoldDB; Q54HL4; -.
DR SMR; Q54HL4; -.
DR STRING; 44689.DDB0266397; -.
DR MEROPS; C26.001; -.
DR PaxDb; Q54HL4; -.
DR EnsemblProtists; EAL62769; EAL62769; DDB_G0289365.
DR GeneID; 8627105; -.
DR KEGG; ddi:DDB_G0289365; -.
DR dictyBase; DDB_G0289365; gghB.
DR eggNOG; KOG1559; Eukaryota.
DR HOGENOM; CLU_058704_1_1_1; -.
DR InParanoid; Q54HL4; -.
DR OMA; QNYTRNA; -.
DR PhylomeDB; Q54HL4; -.
DR Reactome; R-DDI-6798695; Neutrophil degranulation.
DR PRO; PR:Q54HL4; -.
DR Proteomes; UP000002195; Chromosome 5.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR GO; GO:0005773; C:vacuole; IBA:GO_Central.
DR GO; GO:0034722; F:gamma-glutamyl-peptidase activity; IBA:GO_Central.
DR GO; GO:0008242; F:omega peptidase activity; ISS:UniProtKB.
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 3: Inferred from homology;
KW Glycoprotein; Hydrolase; Reference proteome; Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..347
FT /note="Gamma-glutamyl hydrolase B"
FT /id="PRO_0000327992"
FT DOMAIN 23..314
FT /note="Gamma-glutamyl hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00607"
FT ACT_SITE 128
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00607"
FT ACT_SITE 240
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00607"
FT CARBOHYD 152
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 158
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 201
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 273
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 314
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 318
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 347 AA; 40072 MW; C29CF0CEA3624EED CRC64;
MIKLFSLFIY LYLISNLKLI NTINNTPVIG ILTQPFPSSI NIKYGDNYLM ASYVKYVESA
GARVVPIFYN QDDESLTTIF KQINGILLPG GDVDFKTEIQ YVKTLTLIWD YVLDVNINGD
YFPLWGTCLG LEEIVSLQAE SFDVLTDFNA ENYSIPLNFS NIALESKIMK NCPTNIINSL
ANDPITMNNH HFGISPNTFD NNSLLNQFFN VLATNNDKSG NEFISLIESK DYPIYAIIWH
PEKSPYSWYS KDATDHSFNA ILACQYMSNF FVNETRKSNH KFNDEEVLFK SLIYNYNPTY
TFKETHVEQI YIFNTSTNNT KNDFNINQIF SKKLFIIIFI LIILFFK
