ID   NIT1_SYNY3              Reviewed;         272 AA.
AC   P55175;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   25-MAY-2022, entry version 115.
DE   RecName: Full=Deaminated glutathione amidase {ECO:0000305};
DE            Short=dGSH amidase {ECO:0000305};
DE            EC=3.5.1.128 {ECO:0000250|UniProtKB:P0DP66};
DE   AltName: Full=Nitrilase homolog 1;
DE            Short=syNit1;
GN   OrderedLocusNames=sll0601;
OS   Synechocystis sp. (strain PCC 6803 / Kazusa).
OC   Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC   unclassified Synechocystis.
OX   NCBI_TaxID=1111708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27184 / PCC 6803 / N-1;
RX   PubMed=8590279; DOI=10.1093/dnares/2.4.153;
RA   Kaneko T., Tanaka A., Sato S., Kotani H., Sazuka T., Miyajima N.,
RA   Sugiura M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. I. Sequence features in the 1 Mb region
RT   from map positions 64% to 92% of the genome.";
RL   DNA Res. 2:153-166(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6803 / Kazusa;
RX   PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA   Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA   Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA   Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA   Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT   genome and assignment of potential protein-coding regions.";
RL   DNA Res. 3:109-136(1996).
CC   -!- FUNCTION: Hydrolyzes deaminated glutathione (dGSH, 2-oxoglutaramate) to
CC       alpha-ketoglutarate (alpha-KG) and cysteinylglycine, alpha-
CC       ketoglutaramate (a-KGM), and no activity on glutathione or L-glutamine.
CC       May function as a metabolite repair enzyme.
CC       {ECO:0000250|UniProtKB:P0DP66}.
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:0000250|UniProtKB:P0DP66};
CC   -!- SIMILARITY: Belongs to the carbon-nitrogen hydrolase superfamily.
CC       NIT1/NIT2 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BA000022; BAA10370.1; -; Genomic_DNA.
DR   PIR; S76524; S76524.
DR   AlphaFoldDB; P55175; -.
DR   SMR; P55175; -.
DR   IntAct; P55175; 2.
DR   STRING; 1148.1001639; -.
DR   PaxDb; P55175; -.
DR   EnsemblBacteria; BAA10370; BAA10370; BAA10370.
DR   KEGG; syn:sll0601; -.
DR   eggNOG; COG0388; Bacteria.
DR   InParanoid; P55175; -.
DR   OMA; GNTYRES; -.
DR   PhylomeDB; P55175; -.
DR   Proteomes; UP000001425; Chromosome.
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   3: Inferred from homology;
KW   Hydrolase; Reference proteome.
FT   CHAIN           1..272
FT                   /note="Deaminated glutathione amidase"
FT                   /id="PRO_0000213262"
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