ID A0A0S4JKC5_BODSA Unreviewed; 390 AA.
AC A0A0S4JKC5;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, 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=BSAL_27610 {ECO:0000313|EMBL:CUG90578.1};
OS Bodo saltans (Flagellated protozoan).
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Eubodonida; Bodonidae; Bodo.
OX NCBI_TaxID=75058 {ECO:0000313|EMBL:CUG90578.1, ECO:0000313|Proteomes:UP000051952};
RN [1] {ECO:0000313|Proteomes:UP000051952}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lake Konstanz {ECO:0000313|Proteomes:UP000051952};
RG Pathogen Informatics;
RL Submitted (SEP-2015) 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; CYKH01001847; CUG90578.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S4JKC5; -.
DR VEuPathDB; TriTrypDB:BSAL_27610; -.
DR OMA; PVACRDH; -.
DR OrthoDB; 102889at2759; -.
DR Proteomes; UP000051952; 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:UP000051952};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT ACT_SITE 199
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR615527-1,
FT ECO:0000256|PROSITE-ProRule:PRU00607"
FT ACT_SITE 321
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00607"
FT ACT_SITE 321
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR615527-1"
FT ACT_SITE 323
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 390 AA; 42930 MW; 90501402ABB2F767 CRC64;
MCGIPVIQHK SACTTPTFPP FFSTAAQEMK LLRNYTTKLS ITAILLLLLQ YVSLTNALPN
QKQAPIMAIV VEPFAWNPPE CVSVWGRASP IQITPGGGSS TSPSSLRNTT VQAGCVWSIY
VDWLEASGIR VIPLPWNAPT ARMDYILDRV NGVLFPGGII QGDAPVTDAY FATVQYIFNR
AVAKYFMEDH DGFVVWGTCQ GFELLNAAAA GTMNVVESGF VGTDPSMLPV TFLPSADDND
GDRLYRGLDA PLREALTTTN STLNWHSKGV SPMAYNSTQY RDTLGALLQP LTVSYDATGR
SFVSSLQGIN DTIRVFATQF HPERPPYEFD NDVIGHDAST IGISQFLSLQ LRKWLSESNH
TFENATEANE LMIETYNRVN QGWGVQVYFI
//
