ID H0TF11_9BRAD Unreviewed; 325 AA.
AC H0TF11;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 24-JAN-2024, entry version 55.
DE RecName: Full=N-acetyl-gamma-glutamyl-phosphate reductase {ECO:0000256|HAMAP-Rule:MF_00150};
DE Short=AGPR {ECO:0000256|HAMAP-Rule:MF_00150};
DE EC=1.2.1.38 {ECO:0000256|HAMAP-Rule:MF_00150};
DE AltName: Full=N-acetyl-glutamate semialdehyde dehydrogenase {ECO:0000256|HAMAP-Rule:MF_00150};
DE Short=NAGSA dehydrogenase {ECO:0000256|HAMAP-Rule:MF_00150};
GN Name=argC {ECO:0000256|HAMAP-Rule:MF_00150,
GN ECO:0000313|EMBL:CCE05049.1};
GN ORFNames=BRAS3843_1260027 {ECO:0000313|EMBL:CCE05049.1};
OS Bradyrhizobium sp. STM 3843.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=551947 {ECO:0000313|EMBL:CCE05049.1, ECO:0000313|Proteomes:UP000002686};
RN [1] {ECO:0000313|Proteomes:UP000002686}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=STM3843 {ECO:0000313|Proteomes:UP000002686};
RX PubMed=24704842; DOI=10.3390/genes3010035;
RA Mornico D., Miche L., Bena G., Nouwen N., Vermeglio A., Vallenet D.,
RA Smith A.A., Giraud E., Medigue C., Moulin L.;
RT "Comparative genomics of aeschynomene symbionts: insights into the
RT ecological lifestyle of nod-independent photosynthetic bradyrhizobia.";
RL Genes (Basel) 3:35-61(2011).
CC -!- FUNCTION: Catalyzes the NADPH-dependent reduction of N-acetyl-5-
CC glutamyl phosphate to yield N-acetyl-L-glutamate 5-semialdehyde.
CC {ECO:0000256|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:0000256|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:0000256|HAMAP-
CC Rule:MF_00150}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00150}.
CC -!- SIMILARITY: Belongs to the NAGSA dehydrogenase family. Type 1
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_00150}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CCE05049.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CAFK01000031; CCE05049.1; -; Genomic_DNA.
DR RefSeq; WP_008967573.1; NZ_CAFK01000031.1.
DR AlphaFoldDB; H0TF11; -.
DR OrthoDB; 9801289at2; -.
DR UniPathway; UPA00068; UER00108.
DR Proteomes; UP000002686; Unassembled WGS sequence.
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:0070401; F:NADP+ 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 Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR HAMAP; MF_00150; ArgC_type1; 1.
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 NCBIfam; TIGR01850; argC; 1.
DR PANTHER; PTHR32338:SF10; N-ACETYL-GAMMA-GLUTAMYL-PHOSPHATE REDUCTASE, CHLOROPLASTIC-RELATED; 1.
DR PANTHER; PTHR32338; N-ACETYL-GAMMA-GLUTAMYL-PHOSPHATE REDUCTASE, CHLOROPLASTIC-RELATED-RELATED; 1.
DR Pfam; PF01118; Semialdhyde_dh; 1.
DR Pfam; PF02774; Semialdhyde_dhC; 1.
DR SMART; SM00859; Semialdhyde_dh; 1.
DR SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW Rule:MF_00150};
KW Arginine biosynthesis {ECO:0000256|ARBA:ARBA00022571, ECO:0000256|HAMAP-
KW Rule:MF_00150}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00150};
KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|HAMAP-Rule:MF_00150};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_00150}; Reference proteome {ECO:0000313|Proteomes:UP000002686}.
FT DOMAIN 4..123
FT /note="Semialdehyde dehydrogenase NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00859"
FT ACT_SITE 131
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00150"
SQ SEQUENCE 325 AA; 34033 MW; C94870DF1CADFE26 CRC64;
MSIRVGIVGI SGFGGGEAMR LVASHPSFEL VYAAGEGSAG SRLVDRFPGV PAKLAELVIE
KWDPVALPKL DVLFASLPTG ASAEALARVP RDVKIVDIGG DHRYVEGWAY GLADVWPAEI
EGQIRVANPG CFPAATLNAL APLLVNKLIE PGNIVIDVKT GISGAGRGGA DSKFGYAESN
ENLLPYGLLK HVHMPEIAKT IERLSGGSAA GLVFTPHLVP MTRGVLATIY CRGRATTDQC
LDAARRFYAG RAFVRVTDKP PQTKWATGSN LAFVSYAADP ERNLVIAMGV VDNLGKGAAG
QAVQNANLIC GLPETAGLDG APVWP
//
