NIC1_ARATH
ID NIC1_ARATH Reviewed; 244 AA.
AC Q8S8F9; F4IJK3; Q8LFK8; Q9ZQ55;
DT 07-JAN-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Nicotinamidase 1 {ECO:0000305};
DE Short=AtNIC1 {ECO:0000303|PubMed:17335512};
DE EC=3.5.1.19 {ECO:0000269|PubMed:17335512};
DE AltName: Full=Nicotinamide deamidase 1;
GN Name=NIC1 {ECO:0000303|PubMed:17335512};
GN Synonyms=PNC1 {ECO:0000303|PubMed:17335512};
GN OrderedLocusNames=At2g22570 {ECO:0000312|Araport:AT2G22570};
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).
RC STRAIN=cv. Columbia;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [6]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE
RP SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=17335512; DOI=10.1111/j.1365-313x.2006.03013.x;
RA Wang G., Pichersky E.;
RT "Nicotinamidase participates in the salvage pathway of NAD biosynthesis in
RT Arabidopsis.";
RL Plant J. 49:1020-1029(2007).
CC -!- FUNCTION: Catalyzes the deamidation of nicotinamide, an early step in
CC the NAD(+) salvage pathway. Prevents the accumulation of intracellular
CC nicotinamide, a known inhibitor of poly(ADP-ribose) polymerases (PARP
CC enzymes). {ECO:0000269|PubMed:17335512}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + nicotinamide = NH4(+) + nicotinate;
CC Xref=Rhea:RHEA:14545, ChEBI:CHEBI:15377, ChEBI:CHEBI:17154,
CC ChEBI:CHEBI:28938, ChEBI:CHEBI:32544; EC=3.5.1.19;
CC Evidence={ECO:0000269|PubMed:17335512};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=118 uM for nicotinamide {ECO:0000269|PubMed:17335512};
CC Note=kcat is 0.93 sec(-1) with nicotinamide as substrate.
CC {ECO:0000269|PubMed:17335512};
CC pH dependence:
CC Optimum pH is 6.5-7.0. {ECO:0000269|PubMed:17335512};
CC -!- PATHWAY: Cofactor biosynthesis; nicotinate biosynthesis; nicotinate
CC from nicotinamide: step 1/1. {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8S8F9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8S8F9-2; Sequence=VSP_057303, VSP_057304;
CC -!- TISSUE SPECIFICITY: Expressed in roots and stems, and at lower levels
CC in flowers, siliques and leaves. {ECO:0000269|PubMed:17335512}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but mutant plants have decreased endogenous levels of NAD
CC and NADP and display abnormal hypersensitivity to exogenous treatment
CC with abscisic acid (ABA) and sodium chloride (NaCl).
CC {ECO:0000269|PubMed:17335512}.
CC -!- SIMILARITY: Belongs to the isochorismatase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD15566.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC006340; AAD15566.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC006592; AAM15300.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC07323.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC07324.1; -; Genomic_DNA.
DR EMBL; BT002359; AAN86192.1; -; mRNA.
DR EMBL; BX821676; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AY084790; AAM61357.1; -; mRNA.
DR PIR; C84614; C84614.
DR RefSeq; NP_565539.1; NM_127823.3. [Q8S8F9-1]
DR RefSeq; NP_973511.1; NM_201782.3. [Q8S8F9-2]
DR AlphaFoldDB; Q8S8F9; -.
DR SMR; Q8S8F9; -.
DR STRING; 3702.AT2G22570.1; -.
DR PaxDb; Q8S8F9; -.
DR PRIDE; Q8S8F9; -.
DR ProteomicsDB; 250531; -. [Q8S8F9-1]
DR EnsemblPlants; AT2G22570.1; AT2G22570.1; AT2G22570. [Q8S8F9-1]
DR EnsemblPlants; AT2G22570.2; AT2G22570.2; AT2G22570. [Q8S8F9-2]
DR GeneID; 816789; -.
DR Gramene; AT2G22570.1; AT2G22570.1; AT2G22570. [Q8S8F9-1]
DR Gramene; AT2G22570.2; AT2G22570.2; AT2G22570. [Q8S8F9-2]
DR KEGG; ath:AT2G22570; -.
DR Araport; AT2G22570; -.
DR TAIR; locus:2041298; AT2G22570.
DR eggNOG; ENOG502QR6S; Eukaryota.
DR HOGENOM; CLU_100758_0_0_1; -.
DR InParanoid; Q8S8F9; -.
DR OMA; FCERNWP; -.
DR PhylomeDB; Q8S8F9; -.
DR UniPathway; UPA00830; UER00790.
DR PRO; PR:Q8S8F9; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q8S8F9; baseline and differential.
DR Genevisible; Q8S8F9; AT.
DR GO; GO:0008936; F:nicotinamidase activity; IDA:TAIR.
DR GO; GO:0019365; P:pyridine nucleotide salvage; IMP:TAIR.
DR GO; GO:0009737; P:response to abscisic acid; IMP:TAIR.
DR Gene3D; 3.40.50.850; -; 1.
DR InterPro; IPR000868; Isochorismatase-like.
DR InterPro; IPR036380; Isochorismatase-like_sf.
DR InterPro; IPR044717; NIC1.
DR PANTHER; PTHR47297; PTHR47297; 1.
DR Pfam; PF00857; Isochorismatase; 1.
DR SUPFAM; SSF52499; SSF52499; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Hydrolase; Pyridine nucleotide biosynthesis;
KW Reference proteome.
FT CHAIN 1..244
FT /note="Nicotinamidase 1"
FT /id="PRO_0000431487"
FT VAR_SEQ 157..175
FT /note="IVVVGICTDICVFDFVATA -> VSFSFDKMLSFDVEQVYCF (in
FT isoform 2)"
FT /id="VSP_057303"
FT VAR_SEQ 176..244
FT /note="Missing (in isoform 2)"
FT /id="VSP_057304"
FT CONFLICT 152
FT /note="K -> N (in Ref. 5; AAM61357)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 244 AA; 27023 MW; 1903299865FA776C CRC64;
MANHETIFDQ LKKQIPVDEE EPLILNRDSS VGLVIVDVVN GFCTIGSGNM APTKHNEQIS
KMVEESAKLA REFCDRKWPV LAFIDSHHPD IPERPYPPHC IIGTEESELV PALKWLESED
CATLRRKDCI NGFVGSMESD GSNVFVDWVK EKQIKVIVVV GICTDICVFD FVATALSARN
HGVLSPVEDV VVYSRGCATF DLPLHVAKDI KGAQAHPQEL MHHVGLYMAK GRGAQVVSKI
SFET
