ID A0A2P1NI65_9BURK Unreviewed; 313 AA.
AC A0A2P1NI65;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 24-JAN-2024, entry version 24.
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 ECO:0000313|EMBL:AVP56745.1};
GN ORFNames=C7H73_02990 {ECO:0000313|EMBL:AVP56745.1};
OS Pulveribacter suum.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Pulveribacter.
OX NCBI_TaxID=2116657 {ECO:0000313|EMBL:AVP56745.1, ECO:0000313|Proteomes:UP000241829};
RN [1] {ECO:0000313|Proteomes:UP000241829}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC2-7 {ECO:0000313|Proteomes:UP000241829};
RA Kim S.-J., Heo J., Ahn J.-H., Kwon S.-W.;
RT "Genome sequencing of Melaminivora sp. strain SC2-7.";
RL Submitted (MAR-2018) 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; CP027792; AVP56745.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P1NI65; -.
DR KEGG; melm:C7H73_02990; -.
DR OrthoDB; 9801289at2; -.
DR UniPathway; UPA00068; UER00108.
DR Proteomes; UP000241829; 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; IPR023013; AGPR_AS.
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 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.
DR PROSITE; PS01224; ARGC; 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}; Reference proteome {ECO:0000313|Proteomes:UP000241829}.
FT DOMAIN 6..113
FT /note="Semialdehyde dehydrogenase NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00859"
FT ACT_SITE 124
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01110,
FT ECO:0000256|PROSITE-ProRule:PRU10010"
SQ SEQUENCE 313 AA; 33461 MW; 4EF7496A7B7DFCC6 CRC64;
MSQVHKVFID GEAGTTGLQI RERLQSLPQV QLVSIAPELR KDAAAKRDLV AGVDMVVLCL
HDDAARESAA MVDALQAETG RAIKIIDAST AHRTADGWVF GFPELCAGQA HAVRSATRVS
NPGCYATGAI ALLRPLVDAG LLPPDHPVAL PSVSGYSGGG RAMIEAYEAG SAAPYELYAL
GLSHKHLPEI LKYTGMQRRP IFVPSVGNFR QGMLVQLPLH LDLLPGKPTA ADLHDALAAH
YAKSNTPEQW VQVLPPTEDG KLEPTALNDT NRLELRVFPN EDHRHALLVA RLDNLGKGAS
GAAVQNLKLM LGL
//
