ID D4ML69_9FIRM Unreviewed; 315 AA.
AC D4ML69;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 24-JAN-2024, entry version 60.
DE RecName: Full=N-acetyl-gamma-glutamyl-phosphate reductase {ECO:0000256|HAMAP-Rule:MF_01110};
DE Short=AGPR {ECO:0000256|HAMAP-Rule:MF_01110};
DE EC=1.2.1.38 {ECO:0000256|HAMAP-Rule:MF_01110};
DE AltName: Full=N-acetyl-glutamate semialdehyde dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01110};
DE Short=NAGSA dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01110};
GN Name=argC {ECO:0000256|HAMAP-Rule:MF_01110};
GN ORFNames=ES1_15480 {ECO:0000313|EMBL:CBL34502.1};
OS [Eubacterium] siraeum V10Sc8a.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Oscillospiraceae incertae sedis.
OX NCBI_TaxID=717961 {ECO:0000313|EMBL:CBL34502.1, ECO:0000313|Proteomes:UP000007050};
RN [1] {ECO:0000313|EMBL:CBL34502.1, ECO:0000313|Proteomes:UP000007050}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=V10Sc8a {ECO:0000313|EMBL:CBL34502.1,
RC ECO:0000313|Proteomes:UP000007050};
RG metaHIT consortium -- http://www.metahit.eu/;
RA Pajon A., Turner K., Parkhill J., Duncan S., Flint H.;
RT "The genome sequence of Eubacterium siraeum V10Sc8a.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CBL34502.1, ECO:0000313|Proteomes:UP000007050}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=V10Sc8a {ECO:0000313|EMBL:CBL34502.1,
RC ECO:0000313|Proteomes:UP000007050};
RA Pajon A.;
RL Submitted (MAR-2010) 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_01110}.
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_01110};
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_01110}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01110}.
CC -!- SIMILARITY: Belongs to the NAGSA dehydrogenase family. Type 2
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_01110}.
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DR EMBL; FP929059; CBL34502.1; -; Genomic_DNA.
DR AlphaFoldDB; D4ML69; -.
DR KEGG; esr:ES1_15480; -.
DR PATRIC; fig|717961.3.peg.1641; -.
DR HOGENOM; CLU_077118_0_0_9; -.
DR UniPathway; UPA00068; UER00108.
DR Proteomes; UP000007050; Chromosome.
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:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR HAMAP; MF_01110; ArgC_type2; 1.
DR InterPro; IPR010136; AGPR_type-2.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR000534; Semialdehyde_DH_NAD-bd.
DR NCBIfam; TIGR01851; argC_other; 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 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_01110};
KW Arginine biosynthesis {ECO:0000256|ARBA:ARBA00022571, ECO:0000256|HAMAP-
KW Rule:MF_01110}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01110};
KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|HAMAP-Rule:MF_01110};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_01110}.
FT DOMAIN 4..105
FT /note="Semialdehyde dehydrogenase NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00859"
FT ACT_SITE 116
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01110"
SQ SEQUENCE 315 AA; 34715 MW; A0D4970A43B9E6FD CRC64;
MSVKVYIDGQ EGTTGLKILE RFKDRNDIEI MKIDEDKRKD NDERKKFICS SDFTFLCLPD
AAAREAVELA KGSNVRIIDA STAHRTNPDW AYGFPELSKQ HREKIAASSR VAVPGCYASG
FISLVYPLVK AGIMPSDYPV VAHAVSGYSG AGKKAIAVYE SDEKPEEFYS PRQYALPQEH
KHLPEMMKIS GLDYKPVFNP LICDYFSGMV VTVPVLTRLL PKKYTLADIH KAFTEHYADA
NLVKVMPVMG EGVLENGFLA ANTLSGKNNM EIFVCGNDDR IVLCSRLDNL GKGASGAAVQ
CLNIMMGIDE TTGLV
//
