ARGC_SALTY
ID ARGC_SALTY Reviewed; 334 AA.
AC Q8ZKL8;
DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 128.
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}; OrderedLocusNames=STM4121;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
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; AE006468; AAL22960.1; -; Genomic_DNA.
DR RefSeq; NP_463001.1; NC_003197.2.
DR RefSeq; WP_000935340.1; NC_003197.2.
DR PDB; 2G17; X-ray; 2.30 A; A=1-334.
DR PDBsum; 2G17; -.
DR AlphaFoldDB; Q8ZKL8; -.
DR SMR; Q8ZKL8; -.
DR STRING; 99287.STM4121; -.
DR PaxDb; Q8ZKL8; -.
DR DNASU; 1255648; -.
DR EnsemblBacteria; AAL22960; AAL22960; STM4121.
DR GeneID; 1255648; -.
DR KEGG; stm:STM4121; -.
DR PATRIC; fig|99287.12.peg.4343; -.
DR HOGENOM; CLU_006384_0_1_6; -.
DR OMA; PHLTPMI; -.
DR PhylomeDB; Q8ZKL8; -.
DR BioCyc; SENT99287:STM4121-MON; -.
DR UniPathway; UPA00068; UER00108.
DR EvolutionaryTrace; Q8ZKL8; -.
DR Proteomes; UP000001014; 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_0000112444"
FT ACT_SITE 154
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00150"
FT STRAND 2..7
FT /evidence="ECO:0007829|PDB:2G17"
FT TURN 8..10
FT /evidence="ECO:0007829|PDB:2G17"
FT HELIX 12..23
FT /evidence="ECO:0007829|PDB:2G17"
FT STRAND 27..35
FT /evidence="ECO:0007829|PDB:2G17"
FT TURN 39..42
FT /evidence="ECO:0007829|PDB:2G17"
FT HELIX 45..48
FT /evidence="ECO:0007829|PDB:2G17"
FT HELIX 50..52
FT /evidence="ECO:0007829|PDB:2G17"
FT TURN 53..55
FT /evidence="ECO:0007829|PDB:2G17"
FT STRAND 59..64
FT /evidence="ECO:0007829|PDB:2G17"
FT HELIX 66..68
FT /evidence="ECO:0007829|PDB:2G17"
FT STRAND 75..78
FT /evidence="ECO:0007829|PDB:2G17"
FT HELIX 82..94
FT /evidence="ECO:0007829|PDB:2G17"
FT STRAND 98..101
FT /evidence="ECO:0007829|PDB:2G17"
FT STRAND 107..109
FT /evidence="ECO:0007829|PDB:2G17"
FT HELIX 111..118
FT /evidence="ECO:0007829|PDB:2G17"
FT HELIX 125..130
FT /evidence="ECO:0007829|PDB:2G17"
FT HELIX 136..138
FT /evidence="ECO:0007829|PDB:2G17"
FT HELIX 140..143
FT /evidence="ECO:0007829|PDB:2G17"
FT STRAND 147..150
FT /evidence="ECO:0007829|PDB:2G17"
FT HELIX 154..168
FT /evidence="ECO:0007829|PDB:2G17"
FT STRAND 179..184
FT /evidence="ECO:0007829|PDB:2G17"
FT HELIX 186..189
FT /evidence="ECO:0007829|PDB:2G17"
FT HELIX 199..201
FT /evidence="ECO:0007829|PDB:2G17"
FT STRAND 203..206
FT /evidence="ECO:0007829|PDB:2G17"
FT TURN 209..211
FT /evidence="ECO:0007829|PDB:2G17"
FT HELIX 214..222
FT /evidence="ECO:0007829|PDB:2G17"
FT STRAND 227..237
FT /evidence="ECO:0007829|PDB:2G17"
FT STRAND 239..247
FT /evidence="ECO:0007829|PDB:2G17"
FT HELIX 253..264
FT /evidence="ECO:0007829|PDB:2G17"
FT STRAND 270..272
FT /evidence="ECO:0007829|PDB:2G17"
FT STRAND 274..276
FT /evidence="ECO:0007829|PDB:2G17"
FT HELIX 280..282
FT /evidence="ECO:0007829|PDB:2G17"
FT TURN 283..285
FT /evidence="ECO:0007829|PDB:2G17"
FT STRAND 289..296
FT /evidence="ECO:0007829|PDB:2G17"
FT STRAND 299..306
FT /evidence="ECO:0007829|PDB:2G17"
FT TURN 308..313
FT /evidence="ECO:0007829|PDB:2G17"
FT HELIX 314..325
FT /evidence="ECO:0007829|PDB:2G17"
FT TURN 329..333
FT /evidence="ECO:0007829|PDB:2G17"
SQ SEQUENCE 334 AA; 35949 MW; 9F4663CAFF5A1145 CRC64;
MLNTLIVGAS GYAGAELVSY VNRHPHMTIT ALTVSAQSND AGKLISDLHP QLKGIVDLPL
QPMSDVRDFS ADVDVVFLAT AHEVSHDLAP QFLQAGCVVF DLSGAFRVND RAFYEKYYGF
THQYPELLEQ AVYGLAEWNV DKLNTANLIA VPGCYPTAAQ LSLKPLIDGG LLDLTQWPVI
NATSGVSGAG RKAAISNSFC EVSLQPYGVF THRHQPEIAV HLGAEVIFTP HLGNFPRGIL
ETITCRLKAG VTHAQVADVL QKAYGDKPLV RLYDKGVPAL KNVVGLPFCD IGFAVQGEHL
IVVATEDNLL KGAAAQAVQC ANIRFGFAET QSLI
