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Database: UniProt
Entry: C3Z747_BRAFL
LinkDB: C3Z747_BRAFL
Original site: C3Z747_BRAFL 
ID   C3Z747_BRAFL            Unreviewed;       298 AA.
AC   C3Z747;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 65.
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=BRAFLDRAFT_200938 {ECO:0000313|EMBL:EEN51643.1};
OS   Branchiostoma floridae (Florida lancelet) (Amphioxus).
OC   Eukaryota; Metazoa; Chordata; Cephalochordata; Leptocardii; Amphioxiformes;
OC   Branchiostomatidae; Branchiostoma.
OX   NCBI_TaxID=7739;
RN   [1] {ECO:0000313|EMBL:EEN51643.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN51643.1};
RC   TISSUE=Testes {ECO:0000313|EMBL:EEN51643.1};
RX   PubMed=18563158; DOI=10.1038/nature06967;
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Putnam N.H., Butts T., Ferrier D.E.K., Furlong R.F., Hellsten U.,
RA   Kawashima T., Robinson-Rechavi M., Shoguchi E., Terry A., Yu J.-K.,
RA   Benito-Gutierrez E.L., Dubchak I., Garcia-Fernandez J., Gibson-Brown J.J.,
RA   Grigoriev I.V., Horton A.C., de Jong P.J., Jurka J., Kapitonov V.V.,
RA   Kohara Y., Kuroki Y., Lindquist E., Lucas S., Osoegawa K., Pennacchio L.A.,
RA   Salamov A.A., Satou Y., Sauka-Spengler T., Schmutz J., Shin-I T.,
RA   Toyoda A., Bronner-Fraser M., Fujiyama A., Holland L.Z., Holland P.W.H.,
RA   Satoh N., Rokhsar D.S.;
RT   "The amphioxus genome and the evolution of the chordate karyotype.";
RL   Nature 453:1064-1071(2008).
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; GG666590; EEN51643.1; -; Genomic_DNA.
DR   RefSeq; XP_002595631.1; XM_002595585.1.
DR   AlphaFoldDB; C3Z747; -.
DR   MEROPS; C26.001; -.
DR   eggNOG; KOG1559; Eukaryota.
DR   InParanoid; C3Z747; -.
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}; Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   ACT_SITE        112
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615527-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU00607"
FT   ACT_SITE        224
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00607"
FT   ACT_SITE        224
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615527-1"
FT   ACT_SITE        226
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ   SEQUENCE   298 AA;  33119 MW;  566FA1BD0D5AAD04 CRC64;
     MQCSLFSHSF DLPMTGVIAQ ASGGAIAKFG KTYIPASYIK YLESAGARVV PIRVNLTTAE
     YTKLFNSLNG VLYPGGSVNM FTSGYAKSAK IFYDLAIKAF DEGDYFPVWG TCMGFQQLTA
     LTSDRNVLTT CKGTENKSYK LNFSKDYMSS RMFGKVPVDI LTDLATLPLT PNFHKYCLTP
     QIFTDDAKLK SFYKILSTNT DDDGMEFVSS MEAIKYPVYG VQWHPEKNNF EFGSVLKITH
     SDAATRVSQA MANFLVSEAR KSTHKFPTLA EEVAALIYNY APVYTGNVTI SDQTYFID
//
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