NILP1_ARATH
ID NILP1_ARATH Reviewed; 299 AA.
AC Q8VYF5; Q9ZQH4;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-OCT-2019, sequence version 2.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=N-carbamoylputrescine amidase {ECO:0000303|PubMed:12435743};
DE EC=3.5.1.53 {ECO:0000269|PubMed:12435743};
DE AltName: Full=Nitrilase-like protein 1 {ECO:0000303|PubMed:12435743};
GN Name=CPA {ECO:0000303|PubMed:12435743};
GN Synonyms=NLP1 {ECO:0000303|PubMed:12435743}; OrderedLocusNames=At2g27450;
GN ORFNames=F10A12.13;
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(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] (ISOFORM 1).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, SUBUNIT, INDUCTION, TISSUE SPECIFICITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, GENE FAMILY, AND NOMENCLATURE (ISOFORM 2).
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).
CC -!- FUNCTION: Involved in polyamine biosynthesis (PubMed:12435743).
CC Catalyzes the hydrolysis of N-carbamoylputrescine to produce putrescine
CC and ammonia (PubMed:12435743). {ECO:0000269|PubMed:12435743}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 H(+) + H2O + N-carbamoylputrescine = CO2 + NH4(+) +
CC putrescine; Xref=Rhea:RHEA:22284, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:58318, ChEBI:CHEBI:326268; EC=3.5.1.53;
CC Evidence={ECO:0000269|PubMed:12435743};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22285;
CC Evidence={ECO:0000269|PubMed:12435743};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=135 uM for N-carbamoylputrescine {ECO:0000269|PubMed:12435743};
CC Vmax=86 nmol/sec/mg enzyme {ECO:0000269|PubMed:12435743};
CC Note=Determined for isoform 2.;
CC pH dependence:
CC Optimum pH is 8-9. {ECO:0000269|PubMed:12435743};
CC Temperature dependence:
CC Optimum temperature is 40 degrees Celsius.
CC {ECO:0000269|PubMed:12435743};
CC -!- PATHWAY: Amine and polyamine biosynthesis; putrescine biosynthesis via
CC agmatine pathway; putrescine from N-carbamoylputrescine (amidase
CC route): step 1/1. {ECO:0000305}.
CC -!- SUBUNIT: Homooctamer (isoform 2). {ECO:0000269|PubMed:12435743}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=2;
CC IsoId=Q8VYF5-2; Sequence=Displayed;
CC Name=1;
CC IsoId=Q8VYF5-1; Sequence=VSP_060388;
CC -!- TISSUE SPECIFICITY: [Isoform 2]: Expressed in roots, stems, leaves and
CC flowers. {ECO:0000269|PubMed:12435743}.
CC -!- INDUCTION: [Isoform 2]: Not induced by osmotic stress.
CC {ECO:0000269|PubMed:12435743}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to a competing donor splice
CC site. Used for enzyme characterization.
CC -!- SIMILARITY: Belongs to the carbon-nitrogen hydrolase superfamily.
CC {ECO:0000305}.
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DR EMBL; AC006232; AAD15597.2; -; Genomic_DNA.
DR EMBL; CP002685; AEC07997.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC07998.1; -; Genomic_DNA.
DR EMBL; AY072113; AAL59935.1; -; mRNA.
DR EMBL; AY122963; AAM67496.1; -; mRNA.
DR EMBL; AY086056; AAM63266.1; -; mRNA.
DR PIR; A84673; A84673.
DR RefSeq; NP_565650.1; NM_128305.2. [Q8VYF5-2]
DR RefSeq; NP_850101.1; NM_179770.1. [Q8VYF5-1]
DR AlphaFoldDB; Q8VYF5; -.
DR SMR; Q8VYF5; -.
DR BioGRID; 2642; 3.
DR STRING; 3702.AT2G27450.2; -.
DR PaxDb; Q8VYF5; -.
DR PRIDE; Q8VYF5; -.
DR ProteomicsDB; 250533; -. [Q8VYF5-2]
DR EnsemblPlants; AT2G27450.1; AT2G27450.1; AT2G27450. [Q8VYF5-2]
DR EnsemblPlants; AT2G27450.2; AT2G27450.2; AT2G27450. [Q8VYF5-1]
DR GeneID; 817290; -.
DR Gramene; AT2G27450.1; AT2G27450.1; AT2G27450. [Q8VYF5-2]
DR Gramene; AT2G27450.2; AT2G27450.2; AT2G27450. [Q8VYF5-1]
DR KEGG; ath:AT2G27450; -.
DR Araport; AT2G27450; -.
DR TAIR; locus:2038623; AT2G27450.
DR eggNOG; KOG0806; Eukaryota.
DR InParanoid; Q8VYF5; -.
DR OMA; NAPYFCQ; -.
DR OrthoDB; 996578at2759; -.
DR PhylomeDB; Q8VYF5; -.
DR BioCyc; MetaCyc:MON-1841; -.
DR SABIO-RK; Q8VYF5; -.
DR UniPathway; UPA00534; UER00286.
DR PRO; PR:Q8VYF5; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q8VYF5; baseline and differential.
DR Genevisible; Q8VYF5; AT.
DR GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IBA:GO_Central.
DR GO; GO:0050126; F:N-carbamoylputrescine amidase activity; IDA:TAIR.
DR GO; GO:0009446; P:putrescine biosynthetic process; TAS:TAIR.
DR GO; GO:0033388; P:putrescine biosynthetic process from arginine; IBA:GO_Central.
DR Gene3D; 3.60.110.10; -; 1.
DR InterPro; IPR003010; C-N_Hydrolase.
DR InterPro; IPR036526; C-N_Hydrolase_sf.
DR InterPro; IPR017755; N-carbamoylputrescine_amidase.
DR Pfam; PF00795; CN_hydrolase; 1.
DR SUPFAM; SSF56317; SSF56317; 1.
DR TIGRFAMs; TIGR03381; agmatine_aguB; 1.
DR PROSITE; PS50263; CN_HYDROLASE; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Hydrolase; Polyamine biosynthesis;
KW Reference proteome.
FT CHAIN 1..299
FT /note="N-carbamoylputrescine amidase"
FT /id="PRO_0000261601"
FT DOMAIN 10..268
FT /note="CN hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT ACT_SITE 49
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT ACT_SITE 122
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT ACT_SITE 159
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT VAR_SEQ 32
FT /note="R -> RFVSLSSSLPLSNYQSLPSSSSFKFPYA (in isoform 1)"
FT /evidence="ECO:0000305"
FT /id="VSP_060388"
SQ SEQUENCE 299 AA; 33533 MW; E21E6EA09F22AB38 CRC64;
METEGRRREV VVSSLQFACS DDISTNVAAA ERLVREAHAK GANIILIQEL FEGYYFCQAQ
REDFFKRAKP YKNHPTIARM QKLAKELGVV IPVSFFEEAN TAHYNSIAII DADGTDLGIY
RKSHIPDGPG YQEKFYFNPG DTGFKVFQTK FAKIGVAICW DQWFPEAARA MVLQGAEILF
YPTAIGSEPQ DQGLDSRDHW RRVMQGHAGA NVVPLVASNR IGKEIIETEH GPSQITFYGT
SFIAGPTGEI VAEADDKSEA VLVAQFDLDM IKSKRQSWGV FRDRRPDLYK VLLTMDGNL
