ARGC_ARATH
ID ARGC_ARATH Reviewed; 401 AA.
AC Q93Z70; O82187;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 2.
DT 25-MAY-2022, entry version 140.
DE RecName: Full=Probable N-acetyl-gamma-glutamyl-phosphate reductase, chloroplastic;
DE Short=AGPR;
DE EC=1.2.1.38;
DE AltName: Full=N-acetyl-glutamate semialdehyde dehydrogenase;
DE Short=NAGSA dehydrogenase;
DE Flags: Precursor;
GN OrderedLocusNames=At2g19940; ORFNames=F6F22.3;
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).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.19 ANGSTROMS) OF 43-401, AND SUBUNIT.
RG Center for eukaryotic structural genomics (CESG);
RT "X-ray structure of gene product from Arabidopsis thaliana At2g19940.";
RL Submitted (FEB-2005) to the PDB data bank.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N-acetyl-L-glutamate 5-semialdehyde + NADP(+) + phosphate =
CC H(+) + N-acetyl-L-glutamyl 5-phosphate + NADPH; Xref=Rhea:RHEA:21588,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29123, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:57936, ChEBI:CHEBI:58349; EC=1.2.1.38;
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-
CC L-ornithine from L-glutamate: step 3/4.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|Ref.4}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the NAGSA dehydrogenase family. Type 1
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC62122.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC005169; AAC62122.2; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC06946.2; -; Genomic_DNA.
DR EMBL; AY058082; AAL24190.1; -; mRNA.
DR EMBL; AY090309; AAL90970.1; -; mRNA.
DR PIR; A84583; A84583.
DR RefSeq; NP_849993.5; NM_179662.6.
DR PDB; 1XYG; X-ray; 2.19 A; A/B/C/D=43-401.
DR PDB; 2Q49; X-ray; 2.19 A; A/B/C/D=43-401.
DR PDBsum; 1XYG; -.
DR PDBsum; 2Q49; -.
DR AlphaFoldDB; Q93Z70; -.
DR SMR; Q93Z70; -.
DR BioGRID; 1868; 7.
DR IntAct; Q93Z70; 1.
DR STRING; 3702.AT2G19940.2; -.
DR PaxDb; Q93Z70; -.
DR PRIDE; Q93Z70; -.
DR ProteomicsDB; 244446; -.
DR DNASU; 816513; -.
DR GeneID; 816513; -.
DR KEGG; ath:AT2G19940; -.
DR Araport; AT2G19940; -.
DR TAIR; locus:2051980; AT2G19940.
DR eggNOG; KOG4354; Eukaryota.
DR HOGENOM; CLU_688090_0_0_1; -.
DR InParanoid; Q93Z70; -.
DR OrthoDB; 656144at2759; -.
DR PhylomeDB; Q93Z70; -.
DR UniPathway; UPA00068; UER00108.
DR EvolutionaryTrace; Q93Z70; -.
DR PRO; PR:Q93Z70; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q93Z70; baseline and differential.
DR Genevisible; Q93Z70; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0005730; C:nucleolus; HDA:TAIR.
DR GO; GO:0005507; F:copper ion binding; HDA:TAIR.
DR GO; GO:0003942; F:N-acetyl-gamma-glutamyl-phosphate reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniPathway.
DR HAMAP; MF_00150; ArgC_type1; 1.
DR InterPro; IPR023013; AGPR_AS.
DR InterPro; IPR000706; AGPR_type-1.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR000534; Semialdehyde_DH_NAD-bd.
DR InterPro; IPR012280; Semialdhyde_DH_dimer_dom.
DR Pfam; PF01118; Semialdhyde_dh; 1.
DR Pfam; PF02774; Semialdhyde_dhC; 1.
DR SMART; SM00859; Semialdhyde_dh; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR01850; argC; 1.
DR PROSITE; PS01224; ARGC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Arginine biosynthesis; Chloroplast;
KW NADP; Oxidoreductase; Plastid; Reference proteome; Transit peptide.
FT TRANSIT 1..48
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 49..401
FT /note="Probable N-acetyl-gamma-glutamyl-phosphate
FT reductase, chloroplastic"
FT /id="PRO_0000002066"
FT ACT_SITE 205
FT /evidence="ECO:0000250"
FT STRAND 59..64
FT /evidence="ECO:0007829|PDB:1XYG"
FT HELIX 69..79
FT /evidence="ECO:0007829|PDB:1XYG"
FT STRAND 82..90
FT /evidence="ECO:0007829|PDB:1XYG"
FT TURN 93..96
FT /evidence="ECO:0007829|PDB:1XYG"
FT HELIX 99..102
FT /evidence="ECO:0007829|PDB:1XYG"
FT HELIX 104..106
FT /evidence="ECO:0007829|PDB:1XYG"
FT HELIX 117..119
FT /evidence="ECO:0007829|PDB:1XYG"
FT HELIX 122..124
FT /evidence="ECO:0007829|PDB:1XYG"
FT STRAND 126..130
FT /evidence="ECO:0007829|PDB:1XYG"
FT TURN 134..136
FT /evidence="ECO:0007829|PDB:1XYG"
FT HELIX 137..142
FT /evidence="ECO:0007829|PDB:1XYG"
FT STRAND 149..152
FT /evidence="ECO:0007829|PDB:1XYG"
FT TURN 156..158
FT /evidence="ECO:0007829|PDB:1XYG"
FT HELIX 162..169
FT /evidence="ECO:0007829|PDB:1XYG"
FT HELIX 176..179
FT /evidence="ECO:0007829|PDB:1XYG"
FT HELIX 187..195
FT /evidence="ECO:0007829|PDB:1XYG"
FT STRAND 198..201
FT /evidence="ECO:0007829|PDB:1XYG"
FT HELIX 205..219
FT /evidence="ECO:0007829|PDB:1XYG"
FT STRAND 225..227
FT /evidence="ECO:0007829|PDB:1XYG"
FT STRAND 229..235
FT /evidence="ECO:0007829|PDB:1XYG"
FT HELIX 236..239
FT /evidence="ECO:0007829|PDB:1XYG"
FT HELIX 245..247
FT /evidence="ECO:0007829|PDB:1XYG"
FT HELIX 249..252
FT /evidence="ECO:0007829|PDB:1XYG"
FT HELIX 266..278
FT /evidence="ECO:0007829|PDB:1XYG"
FT STRAND 285..287
FT /evidence="ECO:0007829|PDB:1XYG"
FT STRAND 289..295
FT /evidence="ECO:0007829|PDB:1XYG"
FT STRAND 297..305
FT /evidence="ECO:0007829|PDB:1XYG"
FT HELIX 311..322
FT /evidence="ECO:0007829|PDB:1XYG"
FT STRAND 326..330
FT /evidence="ECO:0007829|PDB:1XYG"
FT HELIX 339..341
FT /evidence="ECO:0007829|PDB:1XYG"
FT TURN 342..344
FT /evidence="ECO:0007829|PDB:1XYG"
FT STRAND 348..354
FT /evidence="ECO:0007829|PDB:1XYG"
FT STRAND 360..367
FT /evidence="ECO:0007829|PDB:1XYG"
FT TURN 369..374
FT /evidence="ECO:0007829|PDB:1XYG"
FT HELIX 375..385
FT /evidence="ECO:0007829|PDB:1XYG"
FT TURN 390..393
FT /evidence="ECO:0007829|PDB:1XYG"
SQ SEQUENCE 401 AA; 44136 MW; 70A1CFECD1EAD162 CRC64;
MSTASAFSSI QGCWFKGERK IRVADKRAKR LTLGSHVASP SSMSFRVSAS SSVKPEKDIR
IGLLGASGYT GAEIVRLLAN HPHFQVTLMT ADRKAGQSME SVFPHLRAQK LPTLVSVKDA
DFSTVDAVFC CLPHGTTQEI IKELPTALKI VDLSADFRLR NIAEYEEWYG QPHKAVELQK
EVVYGLTEIL REDIKKARLV ANPGCYPTTI QLPLVPLLKA NLIKHENIII DAKSGVSGAG
RGAKEANLYS EIAEGISSYG VTRHRHVPEI EQGLSDVAQS KVTVSFTPHL MPMIRGMQST
IYVEMAPGVR TEDLHQQLKT SYEDEEFVKV LDEGVVPRTH NVRGSNYCHM SVFPDRIPGR
AIIISVIDNL VKGASGQALQ NLNIMLGYPE TTGLLHQPLF P
