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Database: UniProt
Entry: A0A084WA72_ANOSI
LinkDB: A0A084WA72_ANOSI
Original site: A0A084WA72_ANOSI 
ID   A0A084WA72_ANOSI        Unreviewed;       379 AA.
AC   A0A084WA72;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, 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=ZHAS_00015165 {ECO:0000313|EMBL:KFB47116.1};
OS   Anopheles sinensis (Mosquito).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Anophelinae; Anopheles.
OX   NCBI_TaxID=74873 {ECO:0000313|EMBL:KFB47116.1};
RN   [1] {ECO:0000313|EMBL:KFB47116.1, ECO:0000313|Proteomes:UP000030765}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=24438588; DOI=10.1186/1471-2164-15-42;
RA   Zhou D., Zhang D., Ding G., Shi L., Hou Q., Ye Y., Xu Y., Zhou H.,
RA   Xiong C., Li S., Yu J., Hong S., Yu X., Zou P., Chen C., Chang X., Wang W.,
RA   Lv Y., Sun Y., Ma L., Shen B., Zhu C.;
RT   "Genome sequence of Anopheles sinensis provides insight into genetics basis
RT   of mosquito competence for malaria parasites.";
RL   BMC Genomics 15:42-42(2014).
RN   [2] {ECO:0000313|EnsemblMetazoa:ASIC015165-PA}
RP   IDENTIFICATION.
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) 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; ATLV01022048; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; KE525327; KFB47116.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A084WA72; -.
DR   STRING; 74873.A0A084WA72; -.
DR   EnsemblMetazoa; ASIC015165-RA; ASIC015165-PA; ASIC015165.
DR   VEuPathDB; VectorBase:ASIC015165; -.
DR   VEuPathDB; VectorBase:ASIS003414; -.
DR   OMA; PVTANFH; -.
DR   Proteomes; UP000030765; 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:UP000030765};
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..379
FT                   /note="folate gamma-glutamyl hydrolase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001784701"
FT   ACT_SITE        148
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615527-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU00607"
FT   ACT_SITE        259
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00607"
FT   ACT_SITE        259
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615527-1"
FT   ACT_SITE        261
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ   SEQUENCE   379 AA;  42609 MW;  09CDF629EF358F15 CRC64;
     MTVTVALVLA VVLLLVTGPG QAKRLIDSQE RSLFDAAVVN DQPVVGILSQ ELSYLMTQNY
     GDDGYDSYIA ASYVKFVEGA GARVVPIWIN QPAEYYEQIM VNLNGVLFPG GATWFNQSNG
     YADAGRHIYD IAMRYNENGD YFPVWGTCLG FELLTYLAAN GSEHRAHCRS NSQALPLNFK
     DDFRKSRLFA SAPNEIVDIL SSEPVTANFH QYCVTEANMT AYGLEDNWRV MSVDKDWNGM
     EFISTIEHKR YPFYGIQFHP EKNIYEWVQN KNISHTANAV QAAQFFADFF IHEARKSDHR
     FPSETILDQH VIYNYQPIFT GLKRSSFEQC YMFSGKVLDE DQLGLADDAG SSASAVSLTC
     MLSVLTTLVT TIVRLHVHG
//
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