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NILP2_ARATH
ID   NILP2_ARATH             Reviewed;         307 AA.
AC   Q94JV5; Q9LE50;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 127.
DE   RecName: Full=Deaminated glutathione amidase, chloroplastic/cytosolic {ECO:0000305};
DE            Short=dGSH amidase {ECO:0000303|PubMed:30692244};
DE            EC=3.5.1.128 {ECO:0000269|PubMed:30692244};
DE   AltName: Full=Nitrilase-like protein 2 {ECO:0000303|PubMed:12435743};
DE   AltName: Full=Protein nitrilase 1 homolog {ECO:0000303|PubMed:30692244};
DE            Short=AtNit1 {ECO:0000303|PubMed:30692244};
DE            Short=Protein Nit1 homolog {ECO:0000303|PubMed:30692244};
DE   Flags: Precursor;
GN   Name=NLP2 {ECO:0000303|PubMed:12435743};
GN   Synonyms=NIT1 {ECO:0000303|PubMed:30692244};
GN   OrderedLocusNames=At4g08790 {ECO:0000312|Araport:AT4G08790};
GN   ORFNames=T32A17.100 {ECO:0000312|EMBL:CAB82115.1};
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA   Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA   Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA   de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA   Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA   Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA   Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA   Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA   Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA   Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA   Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA   Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA   Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA   Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA   Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA   Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA   Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA   Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA   Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA   Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA   Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA   Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA   Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA   de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA   Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA   Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA   Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA   Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA   Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA   Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA   Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA   Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA   O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA   Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA   Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL   Nature 402:769-777(1999).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [4]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=12435743; DOI=10.1074/jbc.m205699200;
RA   Piotrowski M., Janowitz T., Kneifel H.;
RT   "Plant C-N hydrolases and the identification of a plant N-
RT   carbamoylputrescine amidohydrolase involved in polyamine biosynthesis.";
RL   J. Biol. Chem. 278:1708-1712(2003).
RN   [5]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
RP   LOCATION (ISOFORMS 1 AND 2), ALTERNATIVE INITIATION, DISRUPTION PHENOTYPE,
RP   AND MUTAGENESIS OF MET-29.
RX   PubMed=30692244; DOI=10.1042/bcj20180931;
RA   Niehaus T.D., Patterson J.A., Alexander D.C., Folz J.S., Pyc M.,
RA   MacTavish B.S., Bruner S.D., Mullen R.T., Fiehn O., Hanson A.D.;
RT   "The metabolite repair enzyme Nit1 is a dual-targeted amidase that disposes
RT   of damaged glutathione in Arabidopsis.";
RL   Biochem. J. 476:683-697(2019).
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       (PubMed:30692244). Possesses amidase activity toward deaminated
CC       ophthalmate in vitro (PubMed:30692244). {ECO:0000269|PubMed:30692244}.
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:30692244};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54533;
CC         Evidence={ECO:0000269|PubMed:30692244};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N-(4-carboxy-4-oxobutanoyl)-L-ethylglycylglycine = 2-
CC         oxoglutarate + N-(2-aminobutanoyl)glycine; Xref=Rhea:RHEA:17125,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:16810, ChEBI:CHEBI:144697,
CC         ChEBI:CHEBI:144699; Evidence={ECO:0000269|PubMed:30692244};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17126;
CC         Evidence={ECO:0000269|PubMed:30692244};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=35 uM for N-(4-oxoglutarate)-L-cysteinylglycine
CC         {ECO:0000269|PubMed:30692244};
CC         KM=6.7 uM for ophthalmate {ECO:0000269|PubMed:30692244};
CC         Vmax=7.9 umol/min/mg enzyme with N-(4-oxoglutarate)-L-
CC         cysteinylglycine as substrate {ECO:0000269|PubMed:30692244};
CC         Vmax=5.6 umol/min/mg enzyme with ophthalmate as substrate
CC         {ECO:0000269|PubMed:30692244};
CC         Note=kcat is 4.2 sec(-1) with N-(4-oxoglutarate)-L-cysteinylglycine
CC         as substrate (PubMed:30692244). kcat is 3.0 sec(-1) with ophthalmate
CC         as substrate (PubMed:30692244). {ECO:0000269|PubMed:30692244};
CC   -!- SUBCELLULAR LOCATION: [Isoform 1]: Plastid, chloroplast
CC       {ECO:0000269|PubMed:30692244}.
CC   -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm
CC       {ECO:0000269|PubMed:30692244}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative initiation; Named isoforms=2;
CC       Name=1 {ECO:0000305}; Synonyms=Full-length, FL
CC       {ECO:0000303|PubMed:30692244};
CC         IsoId=Q94JV5-1; Sequence=Displayed;
CC       Name=2 {ECO:0000305}; Synonyms=Truncated, Tr
CC       {ECO:0000303|PubMed:30692244};
CC         IsoId=Q94JV5-2; Sequence=VSP_060389;
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC       conditions, but the accumuluation of N-(4-oxoglutarate)-L-
CC       cysteinylglycine (deaminated glutathione) in mutant plants is up to 70-
CC       fold higher than in the wild type. {ECO:0000269|PubMed:30692244}.
CC   -!- SIMILARITY: Belongs to the nitrilase superfamily. NIT1/NIT2 family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAB78004.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=CAB82115.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AL161512; CAB78004.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL161813; CAB82115.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002687; AEE82678.1; -; Genomic_DNA.
DR   EMBL; AF372904; AAK49620.1; -; mRNA.
DR   EMBL; AY133544; AAM91374.1; -; mRNA.
DR   PIR; D85088; D85088.
DR   RefSeq; NP_567340.1; NM_116949.4. [Q94JV5-1]
DR   AlphaFoldDB; Q94JV5; -.
DR   SMR; Q94JV5; -.
DR   BioGRID; 11748; 1.
DR   IntAct; Q94JV5; 1.
DR   STRING; 3702.AT4G08790.1; -.
DR   iPTMnet; Q94JV5; -.
DR   PaxDb; Q94JV5; -.
DR   PRIDE; Q94JV5; -.
DR   ProMEX; Q94JV5; -.
DR   ProteomicsDB; 251171; -. [Q94JV5-1]
DR   EnsemblPlants; AT4G08790.1; AT4G08790.1; AT4G08790. [Q94JV5-1]
DR   GeneID; 826449; -.
DR   Gramene; AT4G08790.1; AT4G08790.1; AT4G08790. [Q94JV5-1]
DR   KEGG; ath:AT4G08790; -.
DR   Araport; AT4G08790; -.
DR   TAIR; locus:2138208; AT4G08790.
DR   eggNOG; KOG0807; Eukaryota.
DR   HOGENOM; CLU_030130_1_2_1; -.
DR   InParanoid; Q94JV5; -.
DR   OMA; MTCYDVR; -.
DR   OrthoDB; 1154369at2759; -.
DR   PhylomeDB; Q94JV5; -.
DR   BioCyc; ARA:AT4G08790-MON; -.
DR   BRENDA; 3.5.1.128; 399.
DR   PRO; PR:Q94JV5; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; Q94JV5; baseline and differential.
DR   Genevisible; Q94JV5; AT.
DR   GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR   GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR   GO; GO:0009536; C:plastid; HDA:TAIR.
DR   GO; GO:0050406; F:[acetyl-CoA carboxylase]-phosphatase activity; IEA:RHEA.
DR   GO; GO:0110050; F:deaminated glutathione amidase activity; IDA:TAIR.
DR   GO; GO:0110051; P:metabolite repair; IDA:TAIR.
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   Pfam; PF00795; CN_hydrolase; 1.
DR   SUPFAM; SSF56317; SSF56317; 1.
DR   PROSITE; PS50263; CN_HYDROLASE; 1.
PE   1: Evidence at protein level;
KW   Alternative initiation; Chloroplast; Cytoplasm; Hydrolase; Plastid;
KW   Reference proteome; Transit peptide.
FT   TRANSIT         1..36
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           37..307
FT                   /note="Deaminated glutathione amidase,
FT                   chloroplastic/cytosolic"
FT                   /id="PRO_0000426705"
FT   DOMAIN          37..286
FT                   /note="CN hydrolase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT   ACT_SITE        76
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT   ACT_SITE        147
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT   ACT_SITE        188
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT   VAR_SEQ         1..28
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000269|PubMed:30692244"
FT                   /id="VSP_060389"
FT   MUTAGEN         29
FT                   /note="M->L: No cytoplasmic localization."
FT                   /evidence="ECO:0000269|PubMed:30692244"
SQ   SEQUENCE   307 AA;  33971 MW;  EFB45469A2779D81 CRC64;
     MNAYSVSLDF TKPSLFTRIT LSSQIPLTMA TTVNKTVRVA AAQMTSVNDL MTNFATCSRL
     VQEAALAGAK LICFPENFSF VGDKEGESVK IAEPLDGPVM ERYCSLARDS NIWLSLGGFQ
     ERFDDTHLCN THVVIDDAGM IRDTYQKMHL FDVDVPGGSS YKESSFTVPG TKIVSVDSPV
     GRLGLTVCYD LRFPKIYQQL RFEQKAQVLL VPSAFTKVTG EAHWEILLRA RAIETQCYVI
     AAAQAGKHNE KRESYGDTLI IDPWGTVVGR LPDRVSTGIV VADIDFSLID SVRTKMPIDK
     QRVSIDL
 
 
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