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Database: UniProt
Entry: A0A0G0MJF0_9BACT
LinkDB: A0A0G0MJF0_9BACT
Original site: A0A0G0MJF0_9BACT 
ID   A0A0G0MJF0_9BACT        Unreviewed;       286 AA.
AC   A0A0G0MJF0;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   SubName: Full=N-acetyl-gamma-glutamyl-phosphate reductase {ECO:0000313|EMBL:KKR04139.1};
GN   ORFNames=UT31_C0002G0008 {ECO:0000313|EMBL:KKR04139.1};
OS   Parcubacteria group bacterium GW2011_GWF2_39_13b.
OC   Bacteria.
OX   NCBI_TaxID=1618962 {ECO:0000313|EMBL:KKR04139.1, ECO:0000313|Proteomes:UP000034319};
RN   [1] {ECO:0000313|EMBL:KKR04139.1, ECO:0000313|Proteomes:UP000034319}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA   Wilkins M.J., Williams K.H., Banfield J.F.;
RT   "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT   radiation of phyla.";
RL   Nature 0:0-0(2015).
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:KKR04139.1}.
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DR   EMBL; LBWH01000002; KKR04139.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G0MJF0; -.
DR   PATRIC; fig|1618962.3.peg.32; -.
DR   Proteomes; UP000034319; Unassembled WGS sequence.
DR   GO; GO:0003942; F:N-acetyl-gamma-glutamyl-phosphate reductase activity; IEA:InterPro.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR023013; AGPR_AS.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR000534; Semialdehyde_DH_NAD-bd.
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.
DR   PROSITE; PS01224; ARGC; 1.
PE   4: Predicted;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW   Arginine biosynthesis {ECO:0000256|ARBA:ARBA00022571};
KW   NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          3..98
FT                   /note="Semialdehyde dehydrogenase NAD-binding"
FT                   /evidence="ECO:0000259|SMART:SM00859"
FT   ACT_SITE        106
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10010"
SQ   SEQUENCE   286 AA;  31602 MW;  3AF479C75EA244D5 CRC64;
     MIQVAVIGTR TLGKILIQIL RKHPKATIVY TANSQESSGN LANADCMFLA LPHGQSHIFI
     AKNQSLLKGR KIIDSGDDFR LKWVYGLPEF NRPAIKTAMQ IACPGCYATS VLLGLGPLIG
     KLSTTAIDIA ATSGISGAGL KKRAKDNFFS YKTGQIHEHL PEIKMISGTT DIIFAPLRCD
     NTNFGIVSSI FIHGLKKERN IANLYRRFYD CEPCVRIVNH DIQTADIIGT AYCDIHVQWP
     NQNTLLIISA LDNTLKGGAS QAIQNFNLMF GFNEFMGLEK YLKNRP
//
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