ID A0A087XTB2_POEFO Unreviewed; 319 AA.
AC A0A087XTB2;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 2.
DT 27-MAR-2024, entry version 42.
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};
OS Poecilia formosa (Amazon molly) (Limia formosa).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48698 {ECO:0000313|Ensembl:ENSPFOP00000009015.2, ECO:0000313|Proteomes:UP000028760};
RN [1] {ECO:0000313|Proteomes:UP000028760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=female {ECO:0000313|Proteomes:UP000028760};
RA Schartl M., Warren W.;
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPFOP00000009015.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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; AYCK01007899; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AYCK01007900; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_007559766.1; XM_007559704.2.
DR AlphaFoldDB; A0A087XTB2; -.
DR STRING; 48698.ENSPFOP00000009015; -.
DR Ensembl; ENSPFOT00000009027.1; ENSPFOP00000009015.2; ENSPFOG00000009003.1.
DR GeneID; 103143243; -.
DR KEGG; pfor:103143243; -.
DR eggNOG; KOG1559; Eukaryota.
DR GeneTree; ENSGT00490000043388; -.
DR OMA; QNYTRNA; -.
DR OrthoDB; 102889at2759; -.
DR Proteomes; UP000028760; 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:SF10; FOLATE 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:UP000028760};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..319
FT /note="folate gamma-glutamyl hydrolase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001833495"
FT ACT_SITE 135
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR615527-1,
FT ECO:0000256|PROSITE-ProRule:PRU00607"
FT ACT_SITE 245
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00607"
FT ACT_SITE 245
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR615527-1"
FT ACT_SITE 247
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 319 AA; 35930 MW; 6A11141E34293381 CRC64;
MRGPAAAGFS VLTAFLLCGP LLCAAARSQQ HNDRPIIGVL AQENLSDDQF ARGSSYIAAS
YVKFLESAGA RVAPIRINRT EEEYIKIFNS INGLLLPGGD VDIQTSQFSR AARIFYNLAL
KANDAGDYFP IWGTCQGFQQ LSVLTARKNL LTLTKTKAVA LPLILTPAAQ SSRLFRSFPR
DVLQSLANEN ITSNFHSWSL SIQNYTRNAK LKRFYRVLST NSDGEKEFIS TMEAYRYPFY
AVQWHPEKSP FEWIDKPGMV HTVSAVRISF YTGSFFVSEA LKSQHRFSNA AEEDRALIYN
FSPVYRGLNA IFIQNYYFD
//