ID R7WTC7_9NOCA Unreviewed; 351 AA.
AC R7WTC7;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 46.
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=Rrhod_0029 {ECO:0000313|EMBL:EOM78493.1};
OS Rhodococcus rhodnii LMG 5362.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=1273125 {ECO:0000313|EMBL:EOM78493.1, ECO:0000313|Proteomes:UP000013525};
RN [1] {ECO:0000313|EMBL:EOM78493.1, ECO:0000313|Proteomes:UP000013525}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 5362 {ECO:0000313|EMBL:EOM78493.1,
RC ECO:0000313|Proteomes:UP000013525};
RX PubMed=23788540;
RA Pachebat J.A., van Keulen G., Whitten M.M., Girdwood S., Del Sol R.,
RA Dyson P.J., Facey P.D.;
RT "Draft Genome Sequence of Rhodococcus rhodnii Strain LMG5362, a Symbiont of
RT Rhodnius prolixus (Hemiptera, Reduviidae, Triatominae), the Principle
RT Vector of Trypanosoma cruzi.";
RL Genome Announc. 1:e00329-13(2013).
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:EOM78493.1}.
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DR EMBL; APMY01000003; EOM78493.1; -; Genomic_DNA.
DR RefSeq; WP_010836110.1; NZ_APMY01000003.1.
DR AlphaFoldDB; R7WTC7; -.
DR PATRIC; fig|1273125.3.peg.30; -.
DR eggNOG; COG0002; Bacteria.
DR OrthoDB; 9801289at2; -.
DR UniPathway; UPA00068; UER00108.
DR Proteomes; UP000013525; 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; IPR023013; AGPR_AS.
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.
DR PROSITE; PS01224; ARGC; 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:UP000013525}.
FT DOMAIN 10..147
FT /note="Semialdehyde dehydrogenase NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00859"
FT ACT_SITE 157
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00150,
FT ECO:0000256|PROSITE-ProRule:PRU10010"
SQ SEQUENCE 351 AA; 35692 MW; 3F039A83BFB96812 CRC64;
MTDHAPTPIR VAVAGASGYA GGEVLRLLLG HPLFLDGTLT IGTLTAGDNA GTTLGSHHPH
LLPLADRVLA DTSVETLAGH DVVFLALPHG NSARYANELP DSVVLVDCGA DFRLRDADAW
TRFYGGEYAG SWPYGLPELP GARDALRGAT RIAVPGCYPT AASLAFAPAV EAGIVEPRVR
IVAVSGTSGA GRAPKVAQLG SEVIGSARAY GVGGLHRHTP EIVQNLSAVA GGHVDVSFTP
VLVPMSRGIL ATCSAPTTVD AGEAHAVYTK AYRDEPFVHV LPEGTFPQTK SVVGSNAVQI
GVAVDADAGE LVVVAAIDNL TKGTAGGAVQ SMNLALGLPE TAGLSTVGVA P
//
