NIC3_ARATH
ID NIC3_ARATH Reviewed; 198 AA.
AC Q9FMX8;
DT 07-JAN-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Nicotinamidase 3 {ECO:0000305};
DE Short=AtNIC3 {ECO:0000303|PubMed:17587307};
DE EC=3.5.1.19 {ECO:0000269|PubMed:17587307};
DE AltName: Full=Nicotinamide deamidase 3;
GN Name=NIC3 {ECO:0000303|PubMed:17587307};
GN OrderedLocusNames=At5g23220 {ECO:0000312|Araport:AT5G23220};
GN ORFNames=MKD15.8 {ECO:0000312|EMBL:BAB11177.1};
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=9501997; DOI=10.1093/dnares/4.6.401;
RA Nakamura Y., Sato S., Kaneko T., Kotani H., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. III. Sequence
RT features of the regions of 1,191,918 bp covered by seventeen physically
RT assigned P1 clones.";
RL DNA Res. 4:401-414(1997).
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 FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=17587307; DOI=10.1111/j.1365-313x.2007.03151.x;
RA Hunt L., Holdsworth M.J., Gray J.E.;
RT "Nicotinamidase activity is important for germination.";
RL Plant J. 51:341-351(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:17587307}.
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:17587307};
CC -!- PATHWAY: Cofactor biosynthesis; nicotinate biosynthesis; nicotinate
CC from nicotinamide: step 1/1. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the isochorismatase 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; AB007648; BAB11177.1; -; Genomic_DNA.
DR EMBL; CP002688; AED93138.1; -; Genomic_DNA.
DR EMBL; BT002920; AAO22736.1; -; mRNA.
DR EMBL; BT004341; AAO42335.1; -; mRNA.
DR RefSeq; NP_197713.1; NM_122228.3.
DR AlphaFoldDB; Q9FMX8; -.
DR SMR; Q9FMX8; -.
DR IntAct; Q9FMX8; 1.
DR STRING; 3702.AT5G23220.1; -.
DR PaxDb; Q9FMX8; -.
DR PRIDE; Q9FMX8; -.
DR ProteomicsDB; 251163; -.
DR EnsemblPlants; AT5G23220.1; AT5G23220.1; AT5G23220.
DR GeneID; 832386; -.
DR Gramene; AT5G23220.1; AT5G23220.1; AT5G23220.
DR KEGG; ath:AT5G23220; -.
DR Araport; AT5G23220; -.
DR TAIR; locus:2166948; AT5G23220.
DR eggNOG; ENOG502QQB1; Eukaryota.
DR HOGENOM; CLU_068979_8_3_1; -.
DR InParanoid; Q9FMX8; -.
DR OMA; CEENCIV; -.
DR OrthoDB; 1344853at2759; -.
DR PhylomeDB; Q9FMX8; -.
DR BioCyc; ARA:AT5G23220-MON; -.
DR UniPathway; UPA00830; UER00790.
DR PRO; PR:Q9FMX8; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FMX8; baseline and differential.
DR Genevisible; Q9FMX8; AT.
DR GO; GO:0008936; F:nicotinamidase activity; IDA:TAIR.
DR GO; GO:0019363; P:pyridine nucleotide biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.850; -; 1.
DR InterPro; IPR000868; Isochorismatase-like.
DR InterPro; IPR036380; Isochorismatase-like_sf.
DR Pfam; PF00857; Isochorismatase; 1.
DR SUPFAM; SSF52499; SSF52499; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Pyridine nucleotide biosynthesis; Reference proteome.
FT CHAIN 1..198
FT /note="Nicotinamidase 3"
FT /id="PRO_0000431489"
SQ SEQUENCE 198 AA; 22230 MW; 89095E8DF4644EF9 CRC64;
MASSSTRKYE TRKRDPNSKI AALLVIDMQN HFSSMAKPIL NNVLTTIDIC RRASVPVFFT
RHNHKSPTDH GMLGEWCNGD VILDGTTDSE IIQEIQGQVT GPDEMVEKNT YSAFNKTRLQ
ENLEKIGVKE VIVIGVMTNL CCETTAREAF IKGFRVFFST DATATFNEEL HEATLMNLAF
GFAYLVDCDK LRRSLLGN
