NIT1_DICDI
ID NIT1_DICDI Reviewed; 291 AA.
AC Q557J5; Q86KI6;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 90.
DE RecName: Full=Deaminated glutathione amidase;
DE Short=dGSH amidase;
DE EC=3.5.1.128 {ECO:0000250|UniProtKB:Q8VDK1};
DE AltName: Full=Nitrilase homolog 1;
GN Name=nit1-1; ORFNames=DDB_G0273457;
GN and
GN Name=nit1-2; ORFNames=DDB_G0273519;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=12097910; DOI=10.1038/nature00847;
RA Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA Noegel A.A.;
RT "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL Nature 418:79-85(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: Catalyzes the hydrolysis of the amide bond in N-(4-
CC oxoglutarate)-L-cysteinylglycine (deaminated glutathione), a metabolite
CC repair reaction to dispose of the harmful deaminated glutathione.
CC {ECO:0000250|UniProtKB:Q8VDK1}.
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:Q8VDK1};
CC -!- SIMILARITY: Belongs to the carbon-nitrogen hydrolase superfamily.
CC NIT1/NIT2 family. {ECO:0000305}.
CC -!- CAUTION: The gene for this protein is duplicated in strains AX3 and
CC AX4. These strains contain a duplication of a segment of 750 kb of
CC chromosome 2 compared to the corresponding sequence in strain AX2.
CC {ECO:0000305}.
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DR EMBL; AAFI02000010; EAL70683.1; -; Genomic_DNA.
DR EMBL; AAFI02000010; EAL70714.1; -; Genomic_DNA.
DR RefSeq; XP_644610.1; XM_639518.1.
DR RefSeq; XP_644640.1; XM_639548.1.
DR AlphaFoldDB; Q557J5; -.
DR SMR; Q557J5; -.
DR STRING; 44689.DDB0302490; -.
DR PaxDb; Q557J5; -.
DR EnsemblProtists; EAL70683; EAL70683; DDB_G0273519.
DR EnsemblProtists; EAL70714; EAL70714; DDB_G0273457.
DR GeneID; 8618974; -.
DR GeneID; 8619003; -.
DR KEGG; ddi:DDB_G0273457; -.
DR KEGG; ddi:DDB_G0273519; -.
DR dictyBase; DDB_G0273457; nit1-1.
DR dictyBase; DDB_G0273519; nit1-2.
DR eggNOG; KOG0807; Eukaryota.
DR HOGENOM; CLU_030130_1_2_1; -.
DR InParanoid; Q557J5; -.
DR OMA; MTCYDVR; -.
DR PhylomeDB; Q557J5; -.
DR PRO; PR:Q557J5; -.
DR Proteomes; UP000002195; Chromosome 2.
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..291
FT /note="Deaminated glutathione amidase"
FT /id="PRO_0000332972"
FT DOMAIN 13..268
FT /note="CN hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT ACT_SITE 52
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT ACT_SITE 130
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT ACT_SITE 172
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
SQ SEQUENCE 291 AA; 33191 MW; ECD77CA01EE558B8 CRC64;
MIRNSKILMN KLKRIGLGQI TSTNNKEDNF RKCKEMIEKA VENKVNLFCL PECFAFISGG
IHQFESRDNA EYLDQKGGII ERYKDLAKQN NIWLSLGGFH EKILDDPNDM IYNTHLIIDS
NGVIVCEYRK MHLFDVDIPS KGVKMNESKV VKGGNDLVVC DSPVGKLGLS ICYDLRFPEL
YLSLRRMDAQ ILLVPSAFMK STGEAHWKPL LQARAIENQT YVIAAAQTGD HHSKRSSYGH
SMIIDPWGKV LHDLPDNLND IAFVDIDLDY ISTCRENIPV FNHKKLNNYK I
