ARGC_ORYSJ
ID ARGC_ORYSJ Reviewed; 415 AA.
AC Q6AV34; Q10GQ5;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 115.
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=Os03g0617900, LOC_Os03g42110; ORFNames=OSJNBa0063J18.8;
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16109971; DOI=10.1101/gr.3869505;
RG The rice chromosome 3 sequencing consortium;
RA Buell C.R., Yuan Q., Ouyang S., Liu J., Zhu W., Wang A., Maiti R., Haas B.,
RA Wortman J., Pertea M., Jones K.M., Kim M., Overton L., Tsitrin T.,
RA Fadrosh D., Bera J., Weaver B., Jin S., Johri S., Reardon M., Webb K.,
RA Hill J., Moffat K., Tallon L., Van Aken S., Lewis M., Utterback T.,
RA Feldblyum T., Zismann V., Iobst S., Hsiao J., de Vazeille A.R.,
RA Salzberg S.L., White O., Fraser C.M., Yu Y., Kim H., Rambo T., Currie J.,
RA Collura K., Kernodle-Thompson S., Wei F., Kudrna K., Ammiraju J.S.S.,
RA Luo M., Goicoechea J.L., Wing R.A., Henry D., Oates R., Palmer M.,
RA Pries G., Saski C., Simmons J., Soderlund C., Nelson W., de la Bastide M.,
RA Spiegel L., Nascimento L., Huang E., Preston R., Zutavern T., Palmer L.,
RA O'Shaughnessy A., Dike S., McCombie W.R., Minx P., Cordum H., Wilson R.,
RA Jin W., Lee H.R., Jiang J., Jackson S.;
RT "Sequence, annotation, and analysis of synteny between rice chromosome 3
RT and diverged grass species.";
RL Genome Res. 15:1284-1291(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 50-415, AND SUBUNIT.
RX PubMed=16240442; DOI=10.1002/prot.20679;
RA Nonaka T., Kita A., Miura-Ohnuma J., Katoh E., Inagaki N., Yamazaki T.,
RA Miki K.;
RT "Crystal structure of putative N-acetyl-gamma-glutamyl-phosphate reductase
RT (AK071544) from rice (Oryza sativa).";
RL Proteins 61:1137-1140(2005).
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|PubMed:16240442}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the NAGSA dehydrogenase family. Type 1
CC subfamily. {ECO:0000305}.
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DR EMBL; AC107206; AAT77050.1; -; Genomic_DNA.
DR EMBL; DP000009; ABF97646.1; -; Genomic_DNA.
DR EMBL; AP008209; BAF12582.1; -; Genomic_DNA.
DR EMBL; AP014959; BAS85284.1; -; Genomic_DNA.
DR EMBL; AK071544; BAG92548.1; -; mRNA.
DR RefSeq; XP_015632676.1; XM_015777190.1.
DR PDB; 2CVO; X-ray; 2.20 A; A/B/C/D=50-415.
DR PDBsum; 2CVO; -.
DR AlphaFoldDB; Q6AV34; -.
DR SMR; Q6AV34; -.
DR BioGRID; 802495; 1.
DR STRING; 4530.OS03T0617900-01; -.
DR PaxDb; Q6AV34; -.
DR PRIDE; Q6AV34; -.
DR EnsemblPlants; Os03t0617900-01; Os03t0617900-01; Os03g0617900.
DR GeneID; 4333458; -.
DR Gramene; Os03t0617900-01; Os03t0617900-01; Os03g0617900.
DR KEGG; osa:4333458; -.
DR eggNOG; KOG4354; Eukaryota.
DR HOGENOM; CLU_006384_2_1_1; -.
DR InParanoid; Q6AV34; -.
DR OMA; PHLTPMI; -.
DR OrthoDB; 656144at2759; -.
DR PlantReactome; R-OSA-1119263; Arginine biosynthesis.
DR PlantReactome; R-OSA-1119273; Lysine biosynthesis I.
DR PlantReactome; R-OSA-1119283; Lysine biosynthesis II.
DR PlantReactome; R-OSA-1119295; Homoserine biosynthesis.
DR PlantReactome; R-OSA-1119539; Ornithine biosynthesis.
DR PlantReactome; R-OSA-1119622; Arginine biosynthesis II (acetyl cycle).
DR UniPathway; UPA00068; UER00108.
DR EvolutionaryTrace; Q6AV34; -.
DR Proteomes; UP000000763; Chromosome 3.
DR Proteomes; UP000059680; Chromosome 3.
DR Genevisible; Q6AV34; OS.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
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..74
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 75..415
FT /note="Probable N-acetyl-gamma-glutamyl-phosphate
FT reductase, chloroplastic"
FT /id="PRO_0000247610"
FT REGION 48..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..66
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 219
FT /evidence="ECO:0000250"
FT STRAND 73..79
FT /evidence="ECO:0007829|PDB:2CVO"
FT HELIX 83..92
FT /evidence="ECO:0007829|PDB:2CVO"
FT STRAND 96..104
FT /evidence="ECO:0007829|PDB:2CVO"
FT TURN 107..110
FT /evidence="ECO:0007829|PDB:2CVO"
FT HELIX 113..116
FT /evidence="ECO:0007829|PDB:2CVO"
FT HELIX 118..120
FT /evidence="ECO:0007829|PDB:2CVO"
FT HELIX 131..133
FT /evidence="ECO:0007829|PDB:2CVO"
FT HELIX 136..138
FT /evidence="ECO:0007829|PDB:2CVO"
FT STRAND 140..144
FT /evidence="ECO:0007829|PDB:2CVO"
FT STRAND 147..149
FT /evidence="ECO:0007829|PDB:2CVO"
FT HELIX 150..156
FT /evidence="ECO:0007829|PDB:2CVO"
FT STRAND 163..166
FT /evidence="ECO:0007829|PDB:2CVO"
FT TURN 170..172
FT /evidence="ECO:0007829|PDB:2CVO"
FT HELIX 176..183
FT /evidence="ECO:0007829|PDB:2CVO"
FT HELIX 190..193
FT /evidence="ECO:0007829|PDB:2CVO"
FT HELIX 201..210
FT /evidence="ECO:0007829|PDB:2CVO"
FT STRAND 212..215
FT /evidence="ECO:0007829|PDB:2CVO"
FT HELIX 219..233
FT /evidence="ECO:0007829|PDB:2CVO"
FT STRAND 239..241
FT /evidence="ECO:0007829|PDB:2CVO"
FT STRAND 243..249
FT /evidence="ECO:0007829|PDB:2CVO"
FT HELIX 250..253
FT /evidence="ECO:0007829|PDB:2CVO"
FT HELIX 259..261
FT /evidence="ECO:0007829|PDB:2CVO"
FT HELIX 263..266
FT /evidence="ECO:0007829|PDB:2CVO"
FT HELIX 280..292
FT /evidence="ECO:0007829|PDB:2CVO"
FT STRAND 299..309
FT /evidence="ECO:0007829|PDB:2CVO"
FT STRAND 311..319
FT /evidence="ECO:0007829|PDB:2CVO"
FT HELIX 325..336
FT /evidence="ECO:0007829|PDB:2CVO"
FT STRAND 342..344
FT /evidence="ECO:0007829|PDB:2CVO"
FT HELIX 353..355
FT /evidence="ECO:0007829|PDB:2CVO"
FT TURN 356..358
FT /evidence="ECO:0007829|PDB:2CVO"
FT STRAND 362..368
FT /evidence="ECO:0007829|PDB:2CVO"
FT STRAND 374..381
FT /evidence="ECO:0007829|PDB:2CVO"
FT TURN 383..388
FT /evidence="ECO:0007829|PDB:2CVO"
FT HELIX 389..400
FT /evidence="ECO:0007829|PDB:2CVO"
FT TURN 404..407
FT /evidence="ECO:0007829|PDB:2CVO"
SQ SEQUENCE 415 AA; 44786 MW; 7AD9E6788B065016 CRC64;
MGSTALGGGA PARLGLAPKD GVFGSNLKQC GGFMLKTTPK VGSSSVRVRA SVASSPQKQH
SPKTSGVKSG EEVRIAVLGA SGYTGAEIVR LLANHPQFRI KVMTADRKAG EQFGSVFPHL
ITQDLPNLVA VKDADFSNVD AVFCCLPHGT TQEIIKGLPQ ELKIVDLSAD FRLRDINEYA
EWYGHSHRAP ELQQEAVYGL TEVLRNEIRN ARLVANPGCY PTSIQLPLVP LIKAKLIKVS
NIIIDAKSGV SGAGRGAKEA NLYTEIAEGI HAYGIKGHRH VPEIEQGLSE AAESKVTISF
TPNLICMKRG MQSTMFVEMA PGVTANDLYQ HLKSTYEGEE FVKLLNGSSV PHTRHVVGSN
YCFMNVFEDR IPGRAIIISV IDNLVKGASG QAVQNLNLMM GLPENTGLQY QPLFP
