ARGC_SHIFL
ID ARGC_SHIFL Reviewed; 334 AA.
AC P59310;
DT 12-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 12-FEB-2003, sequence version 1.
DT 25-MAY-2022, entry version 135.
DE RecName: Full=N-acetyl-gamma-glutamyl-phosphate reductase {ECO:0000255|HAMAP-Rule:MF_00150};
DE Short=AGPR {ECO:0000255|HAMAP-Rule:MF_00150};
DE EC=1.2.1.38 {ECO:0000255|HAMAP-Rule:MF_00150};
DE AltName: Full=N-acetyl-glutamate semialdehyde dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00150};
DE Short=NAGSA dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00150};
GN Name=argC {ECO:0000255|HAMAP-Rule:MF_00150};
GN OrderedLocusNames=SF4035, S3711;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
CC -!- FUNCTION: Catalyzes the NADPH-dependent reduction of N-acetyl-5-
CC glutamyl phosphate to yield N-acetyl-L-glutamate 5-semialdehyde.
CC {ECO:0000255|HAMAP-Rule:MF_00150}.
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 Evidence={ECO:0000255|HAMAP-Rule:MF_00150};
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-
CC L-ornithine from L-glutamate: step 3/4. {ECO:0000255|HAMAP-
CC Rule:MF_00150}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00150}.
CC -!- SIMILARITY: Belongs to the NAGSA dehydrogenase family. Type 1
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00150}.
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DR EMBL; AE005674; AAN45465.1; -; Genomic_DNA.
DR EMBL; AE014073; AAP18737.1; -; Genomic_DNA.
DR RefSeq; NP_709758.1; NC_004337.2.
DR RefSeq; WP_000935388.1; NZ_WPGW01000012.1.
DR PDB; 3DR3; X-ray; 2.00 A; A=1-334.
DR PDBsum; 3DR3; -.
DR AlphaFoldDB; P59310; -.
DR SMR; P59310; -.
DR STRING; 198214.SF4035; -.
DR EnsemblBacteria; AAN45465; AAN45465; SF4035.
DR EnsemblBacteria; AAP18737; AAP18737; S3711.
DR GeneID; 1026505; -.
DR GeneID; 58388791; -.
DR KEGG; sfl:SF4035; -.
DR KEGG; sfx:S3711; -.
DR PATRIC; fig|198214.7.peg.4757; -.
DR HOGENOM; CLU_006384_0_1_6; -.
DR OMA; PHLTPMI; -.
DR OrthoDB; 951261at2; -.
DR UniPathway; UPA00068; UER00108.
DR EvolutionaryTrace; P59310; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003942; F:N-acetyl-gamma-glutamyl-phosphate reductase activity; IEA:UniProtKB-UniRule.
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-UniRule.
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; Cytoplasm;
KW NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..334
FT /note="N-acetyl-gamma-glutamyl-phosphate reductase"
FT /id="PRO_0000112446"
FT ACT_SITE 154
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00150"
FT STRAND 2..7
FT /evidence="ECO:0007829|PDB:3DR3"
FT TURN 8..10
FT /evidence="ECO:0007829|PDB:3DR3"
FT HELIX 12..23
FT /evidence="ECO:0007829|PDB:3DR3"
FT STRAND 27..35
FT /evidence="ECO:0007829|PDB:3DR3"
FT TURN 39..42
FT /evidence="ECO:0007829|PDB:3DR3"
FT HELIX 45..48
FT /evidence="ECO:0007829|PDB:3DR3"
FT HELIX 50..52
FT /evidence="ECO:0007829|PDB:3DR3"
FT TURN 53..55
FT /evidence="ECO:0007829|PDB:3DR3"
FT STRAND 59..65
FT /evidence="ECO:0007829|PDB:3DR3"
FT HELIX 66..68
FT /evidence="ECO:0007829|PDB:3DR3"
FT STRAND 74..78
FT /evidence="ECO:0007829|PDB:3DR3"
FT HELIX 82..94
FT /evidence="ECO:0007829|PDB:3DR3"
FT STRAND 98..101
FT /evidence="ECO:0007829|PDB:3DR3"
FT STRAND 107..109
FT /evidence="ECO:0007829|PDB:3DR3"
FT HELIX 111..117
FT /evidence="ECO:0007829|PDB:3DR3"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:3DR3"
FT HELIX 125..130
FT /evidence="ECO:0007829|PDB:3DR3"
FT TURN 136..138
FT /evidence="ECO:0007829|PDB:3DR3"
FT HELIX 141..144
FT /evidence="ECO:0007829|PDB:3DR3"
FT STRAND 147..150
FT /evidence="ECO:0007829|PDB:3DR3"
FT HELIX 154..168
FT /evidence="ECO:0007829|PDB:3DR3"
FT STRAND 179..184
FT /evidence="ECO:0007829|PDB:3DR3"
FT HELIX 186..189
FT /evidence="ECO:0007829|PDB:3DR3"
FT HELIX 199..201
FT /evidence="ECO:0007829|PDB:3DR3"
FT STRAND 203..206
FT /evidence="ECO:0007829|PDB:3DR3"
FT TURN 209..211
FT /evidence="ECO:0007829|PDB:3DR3"
FT HELIX 214..222
FT /evidence="ECO:0007829|PDB:3DR3"
FT STRAND 227..237
FT /evidence="ECO:0007829|PDB:3DR3"
FT STRAND 239..247
FT /evidence="ECO:0007829|PDB:3DR3"
FT HELIX 253..264
FT /evidence="ECO:0007829|PDB:3DR3"
FT STRAND 270..272
FT /evidence="ECO:0007829|PDB:3DR3"
FT STRAND 274..276
FT /evidence="ECO:0007829|PDB:3DR3"
FT HELIX 280..282
FT /evidence="ECO:0007829|PDB:3DR3"
FT TURN 283..285
FT /evidence="ECO:0007829|PDB:3DR3"
FT STRAND 289..296
FT /evidence="ECO:0007829|PDB:3DR3"
FT STRAND 299..306
FT /evidence="ECO:0007829|PDB:3DR3"
FT TURN 308..313
FT /evidence="ECO:0007829|PDB:3DR3"
FT HELIX 314..325
FT /evidence="ECO:0007829|PDB:3DR3"
FT TURN 329..333
FT /evidence="ECO:0007829|PDB:3DR3"
SQ SEQUENCE 334 AA; 35938 MW; 45FCA247E797257A CRC64;
MLNTLIVGAS GYAGAELVTY VNRHPHMNIT ALTVSAQSND AGKLISDLHP QLKGIVELPL
QPMSDISEFS PGVDVVFLAT AHEVSHDLAP QFLEAGCVVF DLSGAFRVND ATFYEKYYGF
THQYPELLEQ AAYGLAEWCG NKLKEANLIA VPGCYPTAAQ LALKPLIDAD LLDLNQWPVI
NATSGVSGAG RKAAISNSFC EVSLQPYGVF THRHQPEIAT HLGADVIFTP HLGNFPRGIL
ETITCRLKSG VTQAQVAQAL QQAYAHKPLV RLYDKGVPAL KNVVGLPFCD IGFAVQGEHL
IIVATEDNLL KGAAAQAVQC ANIRFGYAET QSLI
