ID H1SEY4_9BURK Unreviewed; 315 AA.
AC H1SEY4;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 24-JAN-2024, entry version 43.
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=OR16_34398 {ECO:0000313|EMBL:EHP38929.1};
OS Cupriavidus basilensis OR16.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=1127483 {ECO:0000313|EMBL:EHP38929.1, ECO:0000313|Proteomes:UP000005808};
RN [1] {ECO:0000313|EMBL:EHP38929.1, ECO:0000313|Proteomes:UP000005808}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OR16 {ECO:0000313|EMBL:EHP38929.1,
RC ECO:0000313|Proteomes:UP000005808};
RX PubMed=22461549; DOI=10.1128/JB.06752-11;
RA Cserhati M., Kriszt B., Szoboszlay S., Toth A., Szabo I., Tancsics A.,
RA Nagy I., Horvath B., Nagy I., Kukolya J.;
RT "De Novo Genome Project of Cupriavidus basilensis OR16.";
RL J. Bacteriol. 194:2109-2110(2012).
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:EHP38929.1}.
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DR EMBL; AHJE01000103; EHP38929.1; -; Genomic_DNA.
DR RefSeq; WP_006162742.1; NZ_AHJE01000103.1.
DR AlphaFoldDB; H1SEY4; -.
DR PATRIC; fig|1127483.3.peg.6869; -.
DR OrthoDB; 9801289at2; -.
DR UniPathway; UPA00068; UER00108.
DR Proteomes; UP000005808; 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; 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; 33988 MW; 9A8B12F23B7283B3 CRC64;
MVFKVFVDGQ EGTTGLRLLD YLSGRSDVEL LRIADDKRKD PAERARFLNA ADVAFLCLPD
VASREAVALV TNPNTCVIDA STAFRTTDSW AYGLPELTRG QREKIRTSKR IAVPGCHASA
FLMAVRPLVE AGVMQADYPV SAFSLTGYSG GGKQMIAEFE AGGNPKLDSP RPYSLGLAHK
HLPEMRVQAG LAQAPIFNPI VGNFLKGLAV TVPVYPDRLA RQVTPEQIAD IYRKHYEGEQ
FVRVMPVGDE ANLDGGFFDV QASNDTNRVD LFVFGSAERI VLMARLDNLG KGAAGAAVQC
MNVHVGADEA TGLSA
//
