ARGC_GEOSE
ID ARGC_GEOSE Reviewed; 345 AA.
AC Q07906;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 2.
DT 25-MAY-2022, entry version 112.
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 Geobacillus stearothermophilus (Bacillus stearothermophilus).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX NCBI_TaxID=1422;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-84, AND TRANSCRIPTIONAL REGULATION.
RC STRAIN=NCIMB 8224 / CCM 2186 / NCA C-1235.1 / VKM B-718;
RX PubMed=8804405; DOI=10.1007/bf02173206;
RA Savchenko A., Charlier D.R.M., Dion M., Weigel P., Hallet J.-N.,
RA Holtham C., Baumberg S., Glansdorff N., Sakanyan V.;
RT "The arginine operon of Bacillus stearothermophilus: characterization of
RT the control region and its interaction with the heterologous B. subtilis
RT arginine repressor.";
RL Mol. Gen. Genet. 252:69-78(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 52-345.
RC STRAIN=NCIMB 8224 / CCM 2186 / NCA C-1235.1 / VKM B-718;
RX PubMed=8473852; DOI=10.1099/00221287-139-3-393;
RA Sakanyan V., Charlier D.R.M., Legrain C., Kochikyan A., Mett I.,
RA Pierard P., Glansdorff N.;
RT "Primary structure, partial purification and regulation of key enzymes of
RT the acetyl cycle of arginine biosynthesis in Bacillus stearothermophilus:
RT dual function of ornithine acetyltransferase.";
RL J. Gen. Microbiol. 139:393-402(1993).
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 -!- INDUCTION: Expression of the argCJBD operon is regulated by ArgR. This
CC binding is arginine dependent. {ECO:0000269|PubMed:8804405}.
CC -!- SIMILARITY: Belongs to the NAGSA dehydrogenase family. Type 1
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00150}.
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DR EMBL; L06036; AAA22196.1; -; Genomic_DNA.
DR PIR; S72490; S72490.
DR AlphaFoldDB; Q07906; -.
DR SMR; Q07906; -.
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 2: Evidence at transcript level;
KW Amino-acid biosynthesis; Arginine biosynthesis; Cytoplasm; NADP;
KW Oxidoreductase.
FT CHAIN 1..345
FT /note="N-acetyl-gamma-glutamyl-phosphate reductase"
FT /id="PRO_0000112384"
FT ACT_SITE 149
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00150"
SQ SEQUENCE 345 AA; 37455 MW; F488A7108E602FDD CRC64;
MMNVAIIGAT GYSGAELFRL LYGHPHVSQC DVFSSSQDGI HLSESFPHVG AVDGAVLHKL
EIEALAKYDA VFFATPPGVS GEWAPALVDR GVKVIDLSGD FRLKDGAVYA QWYGREAAPS
AYLERAVYGL TEWNREAVRG AVLLSNPGCY PTATLLGLAP LVKEGLIKED SIIVDAKSGV
SGAGRKAGLG THFSEVNENV KIYKVNAHQH IPEIEQALQT WNEAVAPITF STHLIPMTRG
IMATIYAKAK QSISPNDLVD LYKTSYEGSP FVRIRQLGQF PATKDVYGSN YCDIGLAYDE
RTERVTVVSV IDNLMKGAAG QAVQNFNLMM GWDEAEGLRS LPIYP
