ARGC_MORAB
ID ARGC_MORAB Reviewed; 336 AA.
AC Q9K4Z1;
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 abyssi.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Moritellaceae; Moritella.
OX NCBI_TaxID=111292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=2693;
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; AJ252021; CAB95020.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9K4Z1; -.
DR SMR; Q9K4Z1; -.
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_0000112420"
FT ACT_SITE 156
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00150"
SQ SEQUENCE 336 AA; 36238 MW; DD8CE3FB79938A20 CRC64;
MLKTILVGAT GYTGAELAHY ITKHPELELA GLYVSEHSLD AGKPFSSLYG HLLGVVDQTI
QPLALSNIKH ICDDVDIVVL ATAHEVSHDI AAEFLAQGTV VFDLSGAFRV NDPAFYEKYY
GFKHNFDKEL KSAVYGLAEW ASADIAEANL IAVPGCYPTA SLSALKPLAQ HGLIAAEQKP
IINAVSGVSG AGRKASLASA FCEVSHAPYG VFNHRHQPEI STHLGHEVIF TPHLGSFKRG
ILATINVKLV AGVTPEQVTA AYQEAYQDQP MVRLLPRRTP SIKAVEKTAY YDLAWQQQGQ
DLIVVSAIDN LLKGAAAQAM QCINIRFGFA MTTSLV
