ID   Q9U1D6_LEIMA            Unreviewed;       241 AA.
AC   Q9U1D6;
DT   01-MAY-2000, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2000, sequence version 1.
DT   27-NOV-2024, entry version 54.
DE   RecName: Full=Protein N-terminal glutamine amidohydrolase {ECO:0000256|ARBA:ARBA00021247, ECO:0000256|RuleBase:RU367082};
DE            EC=3.5.1.122 {ECO:0000256|ARBA:ARBA00012718, ECO:0000256|RuleBase:RU367082};
DE   AltName: Full=Protein NH2-terminal glutamine deamidase {ECO:0000256|ARBA:ARBA00029677, ECO:0000256|RuleBase:RU367082};
GN   Name=L1648.12 {ECO:0000313|EMBL:CAB55374.1};
OS   Leishmania major.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX   NCBI_TaxID=5664 {ECO:0000313|EMBL:CAB55374.1};
RN   [1] {ECO:0000313|EMBL:CAB55374.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Friedlin {ECO:0000313|EMBL:CAB55374.1};
RX   PubMed=9477341;
RA   Ivens A.C., Lewis S.M., Bagherzadeh A., Zhang L., Chan H.M., Smith D.F.;
RT   "A physical map of the Leishmania major Friedlin genome.";
RL   Genome Res. 8:135-145(1998).
RN   [2] {ECO:0000313|EMBL:CAB55374.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Friedlin {ECO:0000313|EMBL:CAB55374.1};
RA   Murphy L., Harris D., Ivens A.C., Lawson D., Quail M., Rajandream M.A.,
RA   Barrell B.G.;
RL   Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Mediates the side-chain deamidation of N-terminal glutamine
CC       residues to glutamate, an important step in N-end rule pathway of
CC       protein degradation. Conversion of the resulting N-terminal glutamine
CC       to glutamate renders the protein susceptible to arginylation,
CC       polyubiquitination and degradation as specified by the N-end rule. Does
CC       not act on substrates with internal or C-terminal glutamine and does
CC       not act on non-glutamine residues in any position.
CC       {ECO:0000256|RuleBase:RU367082}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N-terminal L-glutaminyl-[protein] + H2O = N-terminal L-
CC         glutamyl-[protein] + NH4(+); Xref=Rhea:RHEA:50680, Rhea:RHEA-
CC         COMP:12668, Rhea:RHEA-COMP:12777, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:28938, ChEBI:CHEBI:64721, ChEBI:CHEBI:64722;
CC         EC=3.5.1.122; Evidence={ECO:0000256|ARBA:ARBA00001439,
CC         ECO:0000256|RuleBase:RU367082};
CC   -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245,
CC       ECO:0000256|RuleBase:RU367082}.
CC   -!- SIMILARITY: Belongs to the NTAQ1 family.
CC       {ECO:0000256|ARBA:ARBA00008985, ECO:0000256|RuleBase:RU367082}.
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DR   EMBL; AL117260; CAB55374.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9U1D6; -.
DR   GO; GO:0008418; F:protein-N-terminal asparagine amidohydrolase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0070773; F:protein-N-terminal glutamine amidohydrolase activity; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.10.620.10; Protein N-terminal glutamine amidohydrolase, alpha beta roll; 1.
DR   InterPro; IPR037132; N_Gln_amidohydro_ab_roll_sf.
DR   InterPro; IPR039733; NTAQ1.
DR   InterPro; IPR023128; Prot_N_Gln_amidohydro_ab_roll.
DR   PANTHER; PTHR13035:SF0; PROTEIN N-TERMINAL GLUTAMINE AMIDOHYDROLASE; 1.
DR   PANTHER; PTHR13035; UNCHARACTERIZED; 1.
DR   Pfam; PF09764; Nt_Gln_amidase; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU367082}.
FT   DOMAIN          7..240
FT                   /note="Protein N-terminal glutamine amidohydrolase alpha
FT                   beta roll"
FT                   /evidence="ECO:0000259|Pfam:PF09764"
SQ   SEQUENCE   241 AA;  27674 MW;  08592391B7CB046D CRC64;
     MAHPLYYAFC YCEENVYKFL EMISAMGDLF DRSCAVFMTS FCCAPCDEAL NEWTSVVPYR
     PCESSELRKD ITTWDYHVIA LVRATRTGKW YVVDQDSRLS PTWDADLGSL APHCIDLDKY
     VAQVLFLDTA VTNTVCSELT ELLNRVRYRV IERDDYLSFL RSDRSHMQKE PGVYRTLPPQ
     WPLINGCSTC VRDEVRRRAE SALSSLPSTL RANNLVCFIN AANTTIPGVI IDRHSFADFF
     R
//