ID N6WFT1_9ACTO Unreviewed; 357 AA.
AC N6WFT1;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 51.
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 ECO:0000313|EMBL:ENO19089.1};
GN ORFNames=HMPREF9004_0008 {ECO:0000313|EMBL:ENO19089.1};
OS Schaalia cardiffensis F0333.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Schaalia.
OX NCBI_TaxID=888050 {ECO:0000313|EMBL:ENO19089.1, ECO:0000313|Proteomes:UP000013015};
RN [1] {ECO:0000313|EMBL:ENO19089.1, ECO:0000313|Proteomes:UP000013015}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0333 {ECO:0000313|EMBL:ENO19089.1,
RC ECO:0000313|Proteomes:UP000013015};
RA Aqrawi P., Ayvaz T., Bess C., Blankenburg K., Coyle M., Deng J., Forbes L.,
RA Fowler G., Francisco L., Fu Q., Gibbs R., Gross S., Gubbala S., Hale W.,
RA Hemphill L., Highlander S., Hirani K., Jackson L., Jakkamsetti A.,
RA Javaid M., Jayaseelan J.C., Jiang H., Joshi V., Korchina V., Kovar C.,
RA Lara F., Lee S., Liu Y., Mata R., Mathew T., Munidasa M., Muzny D.,
RA Nazareth L., Ngo R., Nguyen L., Nguyen N., Okwuonu G., Ongeri F.,
RA Palculict T., Patil S., Petrosino J., Pham C., Pham P., Pu L.-L., Qin X.,
RA Qu J., Reid J., Ross M., Ruth R., Saada N., San Lucas F., Santibanez J.,
RA Shang Y., Simmons D., Song X.-Z., Tang L.-Y., Thornton R., Warren J.,
RA Weissenberger G., Wilczek-Boney K., Worley K., Youmans B., Zhang J.,
RA Zhang L., Zhao Z., Zhou C., Zhu D., Zhu Y.;
RT "Reference genome for the Human Microbiome Project.";
RL Submitted (MAR-2013) 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}.
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:ENO19089.1}.
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DR EMBL; AQHZ01000001; ENO19089.1; -; Genomic_DNA.
DR AlphaFoldDB; N6WFT1; -.
DR STRING; 888050.HMPREF9004_0008; -.
DR PATRIC; fig|888050.3.peg.8; -.
DR eggNOG; COG0002; Bacteria.
DR HOGENOM; CLU_006384_0_0_11; -.
DR UniPathway; UPA00068; UER00108.
DR Proteomes; UP000013015; 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:UP000013015}.
FT DOMAIN 6..141
FT /note="Semialdehyde dehydrogenase NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00859"
FT ACT_SITE 159
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00150,
FT ECO:0000256|PROSITE-ProRule:PRU10010"
SQ SEQUENCE 357 AA; 36792 MW; D910479B85E0F37F CRC64;
MHMSLKAAIA GASGYAGGEV ARLLAAHLEI EVTTLTAASS AGRLFGELHP QIGSLAELEI
QETSVETLSG HDLVILALPH GHSAALAEEL DASGDGALVL DCAADHRLIK AEDWAEYYGG
EFSPAWTYGM PELIHAREPL ARAQRELLAA TRRIAVPGCN VTAVTLALQP AVHAGLVDVS
HIVATLAVGY SGAGKSMKPH LLASQALGNM APYAVGGTHR HIPEIIQNLV LAGGDKESMR
LSFTPVLVPT SRGILATVVA PLAEGVKEES VKEAYTIYED EALITVTPDG VWPTSGPVTG
TGLARVKAVI DAKAGTLIAI AAIDNLGKGT AAAAVQSANI ALGLEEYLGV PMIGVAP
//
