ID F4W5X6_ACREC Unreviewed; 341 AA.
AC F4W5X6;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 31.
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};
GN ORFNames=G5I_00826 {ECO:0000313|EMBL:EGI70452.1};
OS Acromyrmex echinatior (Panamanian leafcutter ant) (Acromyrmex octospinosus
OS echinatior).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Acromyrmex.
OX NCBI_TaxID=103372 {ECO:0000313|Proteomes:UP000007755};
RN [1] {ECO:0000313|EMBL:EGI70452.1}
RP NUCLEOTIDE SEQUENCE.
RA Nygaard S., Zhang G.;
RT "The genome of the leaf-cutting ant Acromyrmex echinatior suggests key
RT adaptations to social evolution and fungus farming.";
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
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; GL887695; EGI70452.1; -; Genomic_DNA.
DR AlphaFoldDB; F4W5X6; -.
DR STRING; 103372.F4W5X6; -.
DR MEROPS; C26.A22; -.
DR EnsemblMetazoa; XM_011060097.1; XP_011058399.1; LOC105148388.
DR eggNOG; KOG1559; Eukaryota.
DR InParanoid; F4W5X6; -.
DR Proteomes; UP000007755; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0034722; F:gamma-glutamyl-peptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
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:UP000007755};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT ACT_SITE 144
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR615527-1,
FT ECO:0000256|PROSITE-ProRule:PRU00607"
FT ACT_SITE 255
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00607"
FT ACT_SITE 255
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR615527-1"
FT ACT_SITE 257
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 341 AA; 39242 MW; 017FA44DCC37E1ED CRC64;
MQTLADLVAR RESDMLVREG GGDGDGGGVV KTKEELNNRP IIGILTQEIS YNLNKTYPNQ
YHSYIAASYV KFVEGAGARA VPIWIGGNTL YYKDILSKVN GVLWPGGSTY FSQKEGYADA
GAKIYRIAKR INEEGKYFPI FGICLGFELL TYVAANRVAH RTQCSSNNQR LPLEFTPGYR
ESKLFKNAPL NVLRVLSEQN VTANYHHLCV TKKALRHVNL TDEFHVLSLN HDENGLEFIS
TLEHKQFPFY GLQFHPEKNL YEWVIGKRIP HSINATIASQ YFANFFVNEA RKNFNEFRKQ
EEQRSLIYNY PITYTALQNS SFQQCYMFKK SDRNNFFYRN L
//
