ID S9RYG5_9RHOB Unreviewed; 342 AA.
AC S9RYG5;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 61.
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 ORFNames=thalar_01826 {ECO:0000313|EMBL:EPX79009.1};
OS Litoreibacter arenae DSM 19593.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Litoreibacter.
OX NCBI_TaxID=1123360 {ECO:0000313|EMBL:EPX79009.1, ECO:0000313|Proteomes:UP000015351};
RN [1] {ECO:0000313|Proteomes:UP000015351}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19593 {ECO:0000313|Proteomes:UP000015351};
RX PubMed=24501650; DOI=10.4056/sigs.4258318;
RA Riedel T., Fiebig A., Petersen J., Gronow S., Kyrpides N.C., Goker M.,
RA Klenk H.P.;
RT "Genome sequence of the Litoreibacter arenae type strain (DSM 19593(T)), a
RT member of the Roseobacter clade isolated from sea sand.";
RL Stand. Genomic Sci. 9:117-127(2013).
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:EPX79009.1}.
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; AONI01000010; EPX79009.1; -; Genomic_DNA.
DR RefSeq; WP_021100389.1; NZ_KE557306.1.
DR AlphaFoldDB; S9RYG5; -.
DR STRING; 1123360.thalar_01826; -.
DR PATRIC; fig|1123360.3.peg.1809; -.
DR eggNOG; COG0002; Bacteria.
DR HOGENOM; CLU_006384_0_1_5; -.
DR OrthoDB; 9801289at2; -.
DR UniPathway; UPA00068; UER00108.
DR Proteomes; UP000015351; 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:UP000015351}.
FT DOMAIN 4..141
FT /note="Semialdehyde dehydrogenase NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00859"
FT ACT_SITE 149
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00150"
SQ SEQUENCE 342 AA; 36829 MW; 310D9A73F9C46220 CRC64;
MTHKIAILGA SGYTGAELVR LISTHPSMSI AALSADRKAG MEMADVFPHL RHLDLPTLVT
IDEIDFSGID LCFCALPHKT SQEVILKLPK TLKIVDLSAD FRLRDPDAYK QWYGNDHAAL
EMQKEAVYGL TEFYRDDIAK ARLVAGTGCN AATGQFALRP LIAGGVIDLD DIILDLKVGV
SGAGRSLKEN LLHAELSEGS NAYAIGGTHR HLGEFDQEFS AIAGRPVKVQ FTPHLVPMNR
GILATVYVKG DAAEIHATLA EAYSDEPFIE ILPFGEAPST HETRGSNFVH IGVTGDRIEG
RAIVTAALDN LTKGSSGQAL QNANLMLGLE ETEGLMMAPL FP
//
