ID   NIT1_SYNYG              Reviewed;         272 AA.
AC   P0DP66;
DT   05-JUL-2017, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2017, sequence version 1.
DT   25-MAY-2022, entry version 12.
DE   RecName: Full=Deaminated glutathione amidase {ECO:0000305};
DE            Short=dGSH amidase {ECO:0000305};
DE            EC=3.5.1.128 {ECO:0000269|PubMed:28373563};
DE   AltName: Full=Nitrilase homolog 1;
DE            Short=syNit1 {ECO:0000303|PubMed:28373563};
GN   Name=nit1 {ECO:0000303|PubMed:28373563}; Synonyms=sll0601;
GN   OrderedLocusNames=SYNGTS_2407;
OS   Synechocystis sp. (strain PCC 6803 / GT-S).
OC   Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC   unclassified Synechocystis.
OX   NCBI_TaxID=1111707;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6803 / GT-S;
RX   PubMed=21803841; DOI=10.1093/dnares/dsr026;
RA   Tajima N., Sato S., Maruyama F., Kaneko T., Sasaki N.V., Kurokawa K.,
RA   Ohta H., Kanesaki Y., Yoshikawa H., Tabata S., Ikeuchi M., Sato N.;
RT   "Genomic structure of the cyanobacterium Synechocystis sp. PCC 6803 strain
RT   GT-S.";
RL   DNA Res. 18:393-399(2011).
RN   [2]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=PCC 6803 / GT-S;
RX   PubMed=28373563; DOI=10.1073/pnas.1613736114;
RA   Peracchi A., Veiga-da-Cunha M., Kuhara T., Ellens K.W., Paczia N.,
RA   Stroobant V., Seliga A.K., Marlaire S., Jaisson S., Bommer G.T., Sun J.,
RA   Huebner K., Linster C.L., Cooper A.J.L., Van Schaftingen E.;
RT   "Nit1 is a metabolite repair enzyme that hydrolyzes deaminated
RT   glutathione.";
RL   Proc. Natl. Acad. Sci. U.S.A. 114:E3233-E3242(2017).
CC   -!- FUNCTION: Hydrolyzes deaminated glutathione (dGSH, 2-oxoglutaramate) to
CC       alpha-ketoglutarate (alpha-KG) and cysteinylglycine (specific activity
CC       7.77 umol/min/mg), hydrolyzes alpha-ketoglutaramate (a-KGM, specific
CC       activity 2.13 umol/min/mg), has no activity on glutathione or L-
CC       glutamine. May function as a metabolite repair enzyme.
CC       {ECO:0000269|PubMed:28373563}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N-(4-oxoglutaryl)-L-cysteinylglycine = 2-oxoglutarate +
CC         L-cysteinylglycine; Xref=Rhea:RHEA:54532, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:16810, ChEBI:CHEBI:61694, ChEBI:CHEBI:138256;
CC         EC=3.5.1.128; Evidence={ECO:0000269|PubMed:28373563};
CC   -!- SIMILARITY: Belongs to the carbon-nitrogen hydrolase superfamily.
CC       NIT1/NIT2 family. {ECO:0000305}.
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DR   EMBL; AP012205; BAK51155.1; -; Genomic_DNA.
DR   AlphaFoldDB; P0DP66; -.
DR   SMR; P0DP66; -.
DR   KEGG; syy:SYNGTS_2407; -.
DR   BRENDA; 3.5.1.128; 6192.
DR   GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IEA:InterPro.
DR   GO; GO:0006807; P:nitrogen compound metabolic process; IEA:InterPro.
DR   CDD; cd07572; nit; 1.
DR   Gene3D; 3.60.110.10; -; 1.
DR   InterPro; IPR003010; C-N_Hydrolase.
DR   InterPro; IPR036526; C-N_Hydrolase_sf.
DR   InterPro; IPR045254; Nit1/2_C-N_Hydrolase.
DR   InterPro; IPR001110; UPF0012_CS.
DR   Pfam; PF00795; CN_hydrolase; 1.
DR   SUPFAM; SSF56317; SSF56317; 1.
DR   PROSITE; PS50263; CN_HYDROLASE; 1.
DR   PROSITE; PS01227; UPF0012; 1.
PE   1: Evidence at protein level;
KW   Hydrolase.
FT   CHAIN           1..272
FT                   /note="Deaminated glutathione amidase"
FT                   /id="PRO_0000440696"
FT   DOMAIN          1..253
FT                   /note="CN hydrolase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT   ACT_SITE        43
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT   ACT_SITE        115
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT   ACT_SITE        158
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
SQ   SEQUENCE   272 AA;  30191 MW;  7787BA9B2BE003A1 CRC64;
     MKPYLAAALQ MTSRPNLTEN LQEAEELIDL AVRQGAELVG LPENFAFLGN ETEKLEQATA
     IATATEKFLQ TMAQRFQVTI LAGGFPFPVA GEAGKAYNTA TLIAPNGQEL ARYHKVHLFD
     VNVPDGNTYW ESATVMAGQK YPPVYHSDSF GNLGLSICYD VRFPELYRYL SRQGADVLFV
     PAAFTAYTGK DHWQVLLQAR AIENTCYVIA PAQTGCHYER RHTHGHAMII DPWGVILADA
     GEKPGLAIAE INPDRLKQVR QQMPSLQHRV FV