ID A0A1A6DYA8_9BURK Unreviewed; 306 AA.
AC A0A1A6DYA8;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 24-JAN-2024, entry version 33.
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:TSE37161.1};
GN ORFNames=A9O67_00595 {ECO:0000313|EMBL:OBS31661.1}, Tfont_01257
GN {ECO:0000313|EMBL:TSE37161.1};
OS Tepidimonas fonticaldi.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; Tepidimonas.
OX NCBI_TaxID=1101373 {ECO:0000313|EMBL:OBS31661.1, ECO:0000313|Proteomes:UP000091969};
RN [1] {ECO:0000313|EMBL:OBS31661.1, ECO:0000313|Proteomes:UP000091969}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PL17 {ECO:0000313|EMBL:OBS31661.1,
RC ECO:0000313|Proteomes:UP000091969};
RA Pinnaka A.K.;
RT "Genome sequence of Tepidimonas fonticaldi PL17.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:TSE37161.1, ECO:0000313|Proteomes:UP000316388}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AT-A2 {ECO:0000313|EMBL:TSE37161.1,
RC ECO:0000313|Proteomes:UP000316388};
RA Da Costa M.S., Froufe H.J.C., Egas C., Albuquerque L.;
RT "Tepidimonas fonticaldi AT-A2 draft genome.";
RL Submitted (JUL-2019) 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}.
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:OBS31661.1}.
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DR EMBL; LZDH01000012; OBS31661.1; -; Genomic_DNA.
DR EMBL; VJOO01000009; TSE37161.1; -; Genomic_DNA.
DR RefSeq; WP_068606985.1; NZ_VJOO01000009.1.
DR AlphaFoldDB; A0A1A6DYA8; -.
DR STRING; 1101373.A9O67_00595; -.
DR OrthoDB; 9801289at2; -.
DR UniPathway; UPA00068; UER00108.
DR Proteomes; UP000091969; Unassembled WGS sequence.
DR Proteomes; UP000316388; 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: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}.
FT DOMAIN 3..110
FT /note="Semialdehyde dehydrogenase NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00859"
FT ACT_SITE 121
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01110,
FT ECO:0000256|PROSITE-ProRule:PRU10010"
SQ SEQUENCE 306 AA; 32610 MW; 9F2030142F8967F4 CRC64;
MAHIFIDGEA GTTGLQIRER LQGLAGVTLL SIDPERRKDP QAKRERMAQA DLVILCLHDE
AARESVAMID ALRAETGRAP RIIDASTAHR VAPGWVYGFA ELAPGQAEAI RAADRVANPG
CYATGAIALI RPLVDAGLIP PDHPLCLPSV SGYTGGGRTM IEAYESGRAP AFELYALGLE
HKHLPEIMAY TGLQRRPLFV PSVGNFAQGM LVQLPLHLDA LPGQVRPADL HDALAAHYAG
SAWVSVEPPT ADGKLDAVAL AGSDRLELRV YGNDARRHAL LVARLDNLGK GASGAAVQNL
RLMLDV
//
