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Database: UniProt
Entry: A0A1I8MZT6_MUSDO
LinkDB: A0A1I8MZT6_MUSDO
Original site: A0A1I8MZT6_MUSDO 
ID   A0A1I8MZT6_MUSDO        Unreviewed;       339 AA.
AC   A0A1I8MZT6;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 41.
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   Name=101892617 {ECO:0000313|EnsemblMetazoa:MDOA010071-PA};
GN   Synonyms=LOC101892617 {ECO:0000313|RefSeq:XP_005182858.1};
OS   Musca domestica (House fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Muscoidea;
OC   Muscidae; Musca.
OX   NCBI_TaxID=7370 {ECO:0000313|EnsemblMetazoa:MDOA010071-PA};
RN   [1] {ECO:0000313|EnsemblMetazoa:MDOA010071-PA}
RP   IDENTIFICATION.
RC   STRAIN=Aabys {ECO:0000313|EnsemblMetazoa:MDOA010071-PA};
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) to UniProtKB.
RN   [2] {ECO:0000313|RefSeq:XP_005182858.1}
RP   IDENTIFICATION.
RC   STRAIN=Aabys {ECO:0000313|RefSeq:XP_005182858.1};
RG   RefSeq;
RL   Submitted (NOV-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   RefSeq; XP_005182858.1; XM_005182801.3.
DR   STRING; 7370.A0A1I8MZT6; -.
DR   EnsemblMetazoa; MDOA010071-RA; MDOA010071-PA; MDOA010071.
DR   GeneID; 101892617; -.
DR   KEGG; mde:101892617; -.
DR   VEuPathDB; VectorBase:MDOA010071; -.
DR   eggNOG; KOG1559; Eukaryota.
DR   OrthoDB; 102889at2759; -.
DR   Proteomes; UP000095301; Unassembled WGS sequence.
DR   Proteomes; UP000694905; Unplaced.
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:UP000694905};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   ACT_SITE        130
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615527-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU00607"
FT   ACT_SITE        243
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00607"
FT   ACT_SITE        243
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615527-1"
FT   ACT_SITE        245
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ   SEQUENCE   339 AA;  39398 MW;  03C5BBFC48EC0F18 CRC64;
     MATCDRHQQE LQCNENFSPV IGILCIDIAS ALQKNYGKEN QSYLAASYVK YLEAAGARVI
     PIWNNRSQDY YESIMNKING ILLPGGAIYF NKKYCTKDMT SHCYDSSRCI FEIARQLNEQ
     GRHFPLWGTC LGYQMLLTHS AGVEDVRQDC TDMKQSLPVQ FEDQNVLKKS KLFANLDESM
     KEKMSKQPFG YHYHRYCITK GDLSLFKIEG QWRVLATNKD AKGLEFITLT EHVKFPFFGS
     QIHPERVFYE NLHDRDSCHQ CPSCYELNQY FAKFFVQQCR ANANRFEDHK ELVRYSINNF
     PLTFTGPEKL HWQLCYLFKA NTDYPNQVLE NGGDGESDK
//
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