ARGC_MORPR
ID ARGC_MORPR Reviewed; 336 AA.
AC Q9K4Z6;
DT 12-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 90.
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};
OS Moritella profunda.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Moritellaceae; Moritella.
OX NCBI_TaxID=111291;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=2674;
RX PubMed=10692366; DOI=10.1128/jb.182.6.1609-1615.2000;
RA Xu Y., Liang Z., Legrain C., Ruger H.J., Glansdorff N.;
RT "Evolution of arginine biosynthesis in the bacterial domain: novel gene-
RT enzyme relationships from psychrophilic Moritella strains (Vibrionaceae)
RT and evolutionary significance of N-alpha-acetyl ornithinase.";
RL J. Bacteriol. 182:1609-1615(2000).
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; AJ252020; CAB95014.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9K4Z6; -.
DR SMR; Q9K4Z6; -.
DR UniPathway; UPA00068; UER00108.
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 3: Inferred from homology;
KW Amino-acid biosynthesis; Arginine biosynthesis; Cytoplasm; NADP;
KW Oxidoreductase.
FT CHAIN 1..336
FT /note="N-acetyl-gamma-glutamyl-phosphate reductase"
FT /id="PRO_0000112421"
FT ACT_SITE 156
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00150"
SQ SEQUENCE 336 AA; 36107 MW; 1B3A2F068CE84C5E CRC64;
MLKTILVGAT GYTGAELAHY ITKHPELELA GLYVSEHSLD AGKPFSSLYG HLLGVVDQTI
EPLAVSNIKN ICDDVDIVVL ATAHEVSHDI AAEFLAQDTV VFDLSGAFRV NDPAFYENYY
GFKHNFDKEL QSAVYGLAEW ASADIAEANL IAVPGCYPTA SLSALKPLAK HGLISTDQKP
IINAVSGVSG AGRKASLASA FCEVSHAPYG VFNHRHQPEI STHLGHEVIF TPHLGSFKRG
ILATINVKLA AGVTPEQVTA AYQEAYQDQP MVRLLPSGWP SIKAVEKTAY CDLAWQQQGQ
DLIVVSAIDN LLKGAAAQAM QCINIRFGFA MTTSLV
