ID F1A4P6_DICPU Unreviewed; 267 AA.
AC F1A4P6;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=folate gamma-glutamyl hydrolase {ECO:0000256|ARBA:ARBA00012886, ECO:0000256|PROSITE-ProRule:PRU00607};
DE EC=3.4.19.9 {ECO:0000256|ARBA:ARBA00012886, ECO:0000256|PROSITE-ProRule:PRU00607};
DE Flags: Fragment;
GN ORFNames=DICPUDRAFT_51633 {ECO:0000313|EMBL:EGC28836.1};
OS Dictyostelium purpureum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=5786 {ECO:0000313|EMBL:EGC28836.1, ECO:0000313|Proteomes:UP000001064};
RN [1] {ECO:0000313|Proteomes:UP000001064}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=QSDP1 {ECO:0000313|Proteomes:UP000001064};
RX PubMed=21356102; DOI=10.1186/gb-2011-12-2-r20;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Sucgang R., Kuo A., Tian X., Salerno W., Parikh A., Feasley C.L., Dalin E.,
RA Tu H., Huang E., Barry K., Lindquist E., Shapiro H., Bruce D., Schmutz J.,
RA Salamov A., Fey P., Gaudet P., Anjard C., Babu M.M., Basu S.,
RA Bushmanova Y., van der Wel H., Katoh-Kurasawa M., Dinh C., Coutinho P.M.,
RA Saito T., Elias M., Schaap P., Kay R.R., Henrissat B., Eichinger L.,
RA Rivero F., Putnam N.H., West C.M., Loomis W.F., Chisholm R.L., Shaulsky G.,
RA Strassmann J.E., Queller D.C., Kuspa A., Grigoriev I.V.;
RT "Comparative genomics of the social amoebae Dictyostelium discoideum and
RT Dictyostelium purpureum.";
RL Genome Biol. 12:R20.1-R20.23(2011).
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; Evidence={ECO:0000256|PROSITE-ProRule:PRU00607};
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space
CC {ECO:0000256|ARBA:ARBA00004239}.
CC -!- SIMILARITY: Belongs to the peptidase C26 family.
CC {ECO:0000256|ARBA:ARBA00011083}.
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DR EMBL; GL871534; EGC28836.1; -; Genomic_DNA.
DR RefSeq; XP_003294636.1; XM_003294588.1.
DR AlphaFoldDB; F1A4P6; -.
DR STRING; 5786.F1A4P6; -.
DR MEROPS; C26.001; -.
DR EnsemblProtists; EGC28836; EGC28836; DICPUDRAFT_51633.
DR GeneID; 10507097; -.
DR KEGG; dpp:DICPUDRAFT_51633; -.
DR eggNOG; KOG1559; Eukaryota.
DR InParanoid; F1A4P6; -.
DR OMA; QNYTRNA; -.
DR OrthoDB; 102889at2759; -.
DR Proteomes; UP000001064; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005773; C:vacuole; IBA:GO_Central.
DR GO; GO:0034722; F:gamma-glutamyl-peptidase activity; IBA:GO_Central.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
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:SF0; GAMMA-GLUTAMYL HYDROLASE; 1.
DR PANTHER; PTHR11315; PROTEASE FAMILY C26 GAMMA-GLUTAMYL HYDROLASE; 1.
DR Pfam; PF07722; Peptidase_C26; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
DR PROSITE; PS51275; PEPTIDASE_C26_GGH; 1.
PE 3: Inferred from homology;
KW Glutamine amidotransferase {ECO:0000256|PROSITE-ProRule:PRU00605};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU00607}; Reference proteome {ECO:0000313|Proteomes:UP000001064};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..267
FT /note="folate gamma-glutamyl hydrolase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003265620"
FT ACT_SITE 137
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR615527-1,
FT ECO:0000256|PROSITE-ProRule:PRU00607"
FT ACT_SITE 253
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00607"
FT ACT_SITE 253
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR615527-1"
FT ACT_SITE 255
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT NON_TER 267
FT /evidence="ECO:0000313|EMBL:EGC28836.1"
SQ SEQUENCE 267 AA; 30716 MW; 44F0FDF37265D097 CRC64;
MNKIIVLFIY FFLFLNFLKT NCLKQDGCHH ALNDRPVIGI LSQPASSDKY KEYGYQYIAA
SYVKYVESAG ARVVPILYDQ DEDTLRKLLN SINGILLPGG GVYFDEQPIY NKSLYLIWNY
VIESNKRGDY FPLWGTCLGF EEIVSVAANT FDVLTSFNAS NYSIPLNLTD QVLNLSSNSL
LFKEMPLEML KTISNEPITM NNHRMGLSVE TFNNFTSLHQ FFDILSLNDD KSGNTFISVI
ESKEYPIYAV MFHPEKPLFE WYEKEDI
//
