ID   IPUF_PSESP              Reviewed;         295 AA.
AC   Q936S7;
DT   14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 50.
DE   RecName: Full=Gamma-glutamyl-L-1-hydroxyisopropylamide hydrolase;
DE            EC=3.4.-.-;
DE   AltName: Full=Gamma-glutamyl-L-alaninol hydrolase;
DE            Short=Galo hydrolase;
GN   Name=ipuF;
OS   Pseudomonas sp.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=306;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, DISRUPTION
RP   PHENOTYPE, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBSTRATE SPECIFICITY.
RC   STRAIN=KIE171;
RX   PubMed=11976110; DOI=10.1128/aem.68.5.2368-2375.2002;
RA   de Azevedo Waesch S.I., van der Ploeg J.R., Maire T., Lebreton A.,
RA   Kiener A., Leisinger T.;
RT   "Transformation of isopropylamine to L-alaninol by Pseudomonas sp. strain
RT   KIE171 involves N-glutamylated intermediates.";
RL   Appl. Environ. Microbiol. 68:2368-2375(2002).
CC   -!- FUNCTION: Involved in the degradation of isopropylamine, which is a
CC       constituent of the herbicides atrazine. Catalyzes the hydrolysis of
CC       gamma-glutamyl-L-alaninol (GALO) to L-alaninol and L-glutamate. It can
CC       also uses gamma-glutamyl-isopropylamide, gamma-glutamyl-ethylamide, L-
CC       glutamine, and gamma-glutamyl-p-nitroanilide.
CC       {ECO:0000269|PubMed:11976110}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=gamma-L-glutamyl-L-alaninol + H2O = L-alaninol + L-glutamate;
CC         Xref=Rhea:RHEA:45768, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985,
CC         ChEBI:CHEBI:85421, ChEBI:CHEBI:85422;
CC         Evidence={ECO:0000269|PubMed:11976110};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=65 mM for gamma-glutamyl-isopropylamide
CC         {ECO:0000269|PubMed:11976110};
CC         Vmax=1.5 umol/min/mg enzyme with gamma-glutamyl-isopropylamide as
CC         substrate {ECO:0000269|PubMed:11976110};
CC   -!- DISRUPTION PHENOTYPE: Cells lacking this gene are unable to transform
CC       isopropylamine to L-alaninol. {ECO:0000269|PubMed:11976110}.
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DR   EMBL; AJ311159; CAC81338.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q936S7; -.
DR   SMR; Q936S7; -.
DR   BioCyc; MetaCyc:MON-13566; -.
DR   SABIO-RK; Q936S7; -.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   CDD; cd01741; GATase1_1; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   InterPro; IPR044992; ChyE-like.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR017926; GATASE.
DR   PANTHER; PTHR42695; PTHR42695; 1.
DR   Pfam; PF00117; GATase; 1.
DR   SUPFAM; SSF52317; SSF52317; 1.
DR   PROSITE; PS51273; GATASE_TYPE_1; 1.
PE   1: Evidence at protein level;
KW   Hydrolase.
FT   CHAIN           1..295
FT                   /note="Gamma-glutamyl-L-1-hydroxyisopropylamide hydrolase"
FT                   /id="PRO_0000428950"
FT   DOMAIN          5..221
FT                   /note="Glutamine amidotransferase type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        104
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        200
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        202
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
SQ   SEQUENCE   295 AA;  32442 MW;  4BFA504549E0D5BD CRC64;
     MEKLRILICD GNTEADRASF KKFVGCAPSK QFESLLKNYN SQIRTEIAFP ADPGPLMTLP
     LGAYDGILIT GSNSHIYEAQ PGNLRQIEFA QKAFASGTPM FGVCWGMQLA VVAAGGEVLP
     SRVADCSCET PFATGVELTS YGSGHPMHHS RTSGFDVFSF HSDEVTRLPG GAVVTARNRN
     FIQAVEIKHG RSTFWGVQYH PELSGWDQAG FLRESARSLV EDGSYETLNH VEHAAQAISM
     FKAGAQISEE NLVHFEGVDT NSFEFRPLEI LNWLDHLVIP TAKRKFGWGG GWLQK