ID A0A0Q4QNY1_9BACL Unreviewed; 353 AA.
AC A0A0Q4QNY1;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 32.
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=ASF12_13705 {ECO:0000313|EMBL:KQO04583.1};
OS Paenibacillus sp. Leaf72.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1736234 {ECO:0000313|EMBL:KQO04583.1, ECO:0000313|Proteomes:UP000051722};
RN [1] {ECO:0000313|EMBL:KQO04583.1, ECO:0000313|Proteomes:UP000051722}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf72 {ECO:0000313|EMBL:KQO04583.1,
RC ECO:0000313|Proteomes:UP000051722};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQO04583.1, ECO:0000313|Proteomes:UP000051722}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf72 {ECO:0000313|EMBL:KQO04583.1,
RC ECO:0000313|Proteomes:UP000051722};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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:KQO04583.1}.
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DR EMBL; LMLV01000023; KQO04583.1; -; Genomic_DNA.
DR RefSeq; WP_056038678.1; NZ_LMLV01000023.1.
DR AlphaFoldDB; A0A0Q4QNY1; -.
DR STRING; 1736234.ASF12_13705; -.
DR OrthoDB; 9801289at2; -.
DR UniPathway; UPA00068; UER00108.
DR Proteomes; UP000051722; 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:UP000051722}.
FT DOMAIN 10..149
FT /note="Semialdehyde dehydrogenase NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00859"
FT ACT_SITE 156
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00150"
SQ SEQUENCE 353 AA; 38928 MW; 362F21290CB1DF65 CRC64;
MSVTRSSVKR VAILGGNGFT GGELYRLLKR HPYFKVDFVS SESKAGLPLD KFFVSSARQK
RADGGKFQKL ASLSGHYDFI FSCLPTGVLP RHIDHIAEHA EYVINVSGDY RLNDQELLRQ
YYPESLSHPA QGGSHYFIPE FSDINLEAKV VNLPGCMAVA TIYTLFPLLA ANLIEPRVIS
DAKTGSSGGG KASTEHHAER AHNFRPYKVH GHRHRPEIEF ALEEHLERSV ELQFSVHSLD
LPRGILVTSY SLLKEHASEI DVKKAFYGAY AAKPFVHYFN SKNGSYSYPM IKTTAGTNYA
EVGAYVEGRN CVSIASIDNL IKGAAGQAIQ AANLYSGIAE EAGLQFELEG AWP
//
