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NAGS1_ARATH
ID   NAGS1_ARATH             Reviewed;         609 AA.
AC   Q84JF4; O81008;
DT   18-SEP-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 132.
DE   RecName: Full=Probable amino-acid acetyltransferase NAGS1, chloroplastic;
DE            EC=2.3.1.1;
DE   AltName: Full=N-acetylglutamate synthase 1;
DE   Flags: Precursor;
GN   Name=NAGS1; OrderedLocusNames=At2g22910; ORFNames=T20K9.12;
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].
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).
CC   -!- FUNCTION: N-acetylglutamate synthase involved in arginine biosynthesis.
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + L-glutamate = CoA + H(+) + N-acetyl-L-glutamate;
CC         Xref=Rhea:RHEA:24292, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985,
CC         ChEBI:CHEBI:44337, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.1.1;
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-
CC       L-ornithine from L-glutamate: step 1/4.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the acetyltransferase family. ArgA subfamily.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC32438.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AC004786; AAC32438.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002685; AEC07372.1; -; Genomic_DNA.
DR   EMBL; BT004254; AAO42258.1; -; mRNA.
DR   EMBL; BT006149; AAP04134.1; -; mRNA.
DR   PIR; D84618; D84618.
DR   RefSeq; NP_179875.2; NM_127856.4.
DR   AlphaFoldDB; Q84JF4; -.
DR   SMR; Q84JF4; -.
DR   BioGRID; 2175; 2.
DR   IntAct; Q84JF4; 2.
DR   STRING; 3702.AT2G22910.1; -.
DR   PaxDb; Q84JF4; -.
DR   PRIDE; Q84JF4; -.
DR   ProteomicsDB; 251042; -.
DR   EnsemblPlants; AT2G22910.1; AT2G22910.1; AT2G22910.
DR   GeneID; 816822; -.
DR   Gramene; AT2G22910.1; AT2G22910.1; AT2G22910.
DR   KEGG; ath:AT2G22910; -.
DR   Araport; AT2G22910; -.
DR   TAIR; locus:2059165; AT2G22910.
DR   eggNOG; KOG2436; Eukaryota.
DR   HOGENOM; CLU_024773_1_0_1; -.
DR   InParanoid; Q84JF4; -.
DR   OMA; RWHEICD; -.
DR   OrthoDB; 1224477at2759; -.
DR   PhylomeDB; Q84JF4; -.
DR   BioCyc; ARA:AT2G22910-MON; -.
DR   UniPathway; UPA00068; UER00106.
DR   PRO; PR:Q84JF4; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q84JF4; baseline and differential.
DR   Genevisible; Q84JF4; AT.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0004042; F:acetyl-CoA:L-glutamate N-acetyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0103045; F:methione N-acyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd04237; AAK_NAGS-ABP; 1.
DR   Gene3D; 3.40.1160.10; -; 1.
DR   HAMAP; MF_01105; N_acetyl_glu_synth; 1.
DR   InterPro; IPR036393; AceGlu_kinase-like_sf.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR001048; Asp/Glu/Uridylate_kinase.
DR   InterPro; IPR000182; GNAT_dom.
DR   InterPro; IPR033719; NAGS_kin.
DR   InterPro; IPR010167; NH2A_AcTrfase.
DR   PANTHER; PTHR30602; PTHR30602; 1.
DR   Pfam; PF00696; AA_kinase; 1.
DR   Pfam; PF00583; Acetyltransf_1; 1.
DR   SUPFAM; SSF53633; SSF53633; 2.
DR   SUPFAM; SSF55729; SSF55729; 1.
DR   TIGRFAMs; TIGR01890; N-Ac-Glu-synth; 1.
DR   PROSITE; PS51186; GNAT; 1.
PE   2: Evidence at transcript level;
KW   Acyltransferase; Amino-acid biosynthesis; Arginine biosynthesis;
KW   Chloroplast; Plastid; Reference proteome; Transferase; Transit peptide.
FT   TRANSIT         1..67
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           68..609
FT                   /note="Probable amino-acid acetyltransferase NAGS1,
FT                   chloroplastic"
FT                   /id="PRO_0000423406"
FT   DOMAIN          446..594
FT                   /note="N-acetyltransferase"
SQ   SEQUENCE   609 AA;  67179 MW;  BF1475A19D0BAA43 CRC64;
     MTERGAMVVS SSTCYVPFRC PQARKDFAFV EPSKKLNPNR VLIKPPVYTY SPALTAAKCN
     IFDYAETGEN LVGDKQFVRW FREAWPYLWA HRSCTFVVTI SGDVLDGPYC DLVLKDIAFL
     HHLGIKFVLV PGTQVQIDQL LAERGREPTY VGRYRVTDSA SLQAAKEAAG AISVMIEAKL
     SPGPSIYNIR RHGDSSRLHE TGVRVDTGNF FAAKRRGVVD GVDFGATGLV KKIDVDRIRE
     RLDSGSVVLL RNLGHSSTGE VLNCNTYEVA TACALAIGAD KLICIMDGPV LDENGHLVRF
     LTLQEADTLV RKRAQQSEIA ANYVKAVGDG GISSFPEPLG YNGMVTTPNN HIGRPIWEKL
     SPTFQNGVGF DNGNGLWSGE QGFAIGGEER ISRLNGYLSE LAAAAFVCRG GVKRVHLLDG
     TISGVLLLEL FKRDGMGTMV ASDVYEGNRE AKVEDLAGIR QIIKPLEESG ALVRRTDEEL
     LRALDSFVVV EREGHIIACA ALFPFFEEKC GEVAAIAVAS DCRGQGQGDK LLDYIEKKAS
     ALGLEMLFLL TTRTADWFVR RGFQECPIEM IPEARRERIN LSRRSKYYMK KLLPDRSGIS
     VVRTFQYDS
 
 
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