ID A0A172Q8A1_9STRE Unreviewed; 340 AA.
AC A0A172Q8A1;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 32.
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=A0O21_06360 {ECO:0000313|EMBL:AND79671.1};
OS Streptococcus pantholopis.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1811193 {ECO:0000313|EMBL:AND79671.1, ECO:0000313|Proteomes:UP000077317};
RN [1] {ECO:0000313|EMBL:AND79671.1, ECO:0000313|Proteomes:UP000077317}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TA 26 {ECO:0000313|EMBL:AND79671.1,
RC ECO:0000313|Proteomes:UP000077317};
RX PubMed=27226124; DOI=10.1099/ijsem.0.001189;
RA Bai X., Xiong Y., Lu S., Jin D., Lai X., Yang J., Niu L., Hu S., Meng X.,
RA Pu J., Ye C., Xu J.;
RT "Streptococcuspantholopis sp. nov., isolated from faeces of the Tibetan
RT antelope (Pantholops hodgsonii).";
RL Int. J. Syst. Evol. Microbiol. 66:3281-3286(2016).
RN [2] {ECO:0000313|Proteomes:UP000077317}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TA 26 {ECO:0000313|Proteomes:UP000077317};
RA Bai X.;
RT "Streptococcus antelopensis sp. nov., isolated from the feces of the
RT Tibetan antelope (Pantholops hodgsonii) in Hoh Xil National Nature Reserve,
RT Qinghai, China.";
RL Submitted (MAR-2016) 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_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}.
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DR EMBL; CP014699; AND79671.1; -; Genomic_DNA.
DR RefSeq; WP_067063074.1; NZ_CP014699.1.
DR AlphaFoldDB; A0A172Q8A1; -.
DR STRING; 1811193.A0O21_06360; -.
DR KEGG; spat:A0O21_06360; -.
DR OrthoDB; 9801289at2; -.
DR UniPathway; UPA00068; UER00108.
DR Proteomes; UP000077317; 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: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:UP000077317}.
FT DOMAIN 2..140
FT /note="Semialdehyde dehydrogenase NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00859"
FT ACT_SITE 146
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00150,
FT ECO:0000256|PROSITE-ProRule:PRU10010"
SQ SEQUENCE 340 AA; 37234 MW; FE44C6C882DD76B0 CRC64;
MKVSIVGVTG YSGLELVRLL NNHKNAEIVS IHASKDIGSS LSDIYPYLKG ICDLKIDAVD
SQSIMEKADL VFLATPSGVA KDLACDFVAA DFPLIDLSGD HRLPASLYER WYQKTAQTDS
VLARFTYALS EYTDLKGKRF IANPGCYATA AELALIPLLK AQAIDLTSII VDAKSGLTGA
GKALSASSHF VNVHDNYVTY KLNRHQHIPE IVQELQLFDS QLQHIQFSTS LLPVNRGIMA
TCYVKLKQPL SHEAITALYQ DCYADKFFVR IQQELPELHN VIGSNFADIG FAYNPPTNVL
TVVSVIDNLI KGAAGQAVQN FNLMCGFDEK TGLLAVPSYL
//
