ID A0A0H3DXQ2_BACA1 Unreviewed; 345 AA.
AC A0A0H3DXQ2;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 42.
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:ADP31601.1};
GN OrderedLocusNames=BATR1942_03225 {ECO:0000313|EMBL:ADP31601.1};
OS Bacillus atrophaeus (strain 1942).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=720555 {ECO:0000313|EMBL:ADP31601.1, ECO:0000313|Proteomes:UP000006867};
RN [1] {ECO:0000313|Proteomes:UP000006867}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1942 {ECO:0000313|Proteomes:UP000006867};
RA Gibbons H.S., Broomall S., McNew L.A., Daligault H., Chapman C., Bruce D.,
RA Karavis M., McGregor P., Hong C., Park K.H., Akmal A., Feldman A.,
RA Lin J.S., Chang W.E., Higgs B.W., Demirev P., Lindquist J., Liem A.,
RA Fochler E., Tapia R., Bishop-Lilly K., Detter C., Han C., Sozhamannan S.,
RA Rosenzweig C.N., Skowronski E.;
RT "Genomic signatures of strain selection and enhancement in Bacillus
RT atrophaeus subsp. Globigii, a historical biowarfare simulant.";
RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADP31601.1, ECO:0000313|Proteomes:UP000006867}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1942 {ECO:0000313|EMBL:ADP31601.1,
RC ECO:0000313|Proteomes:UP000006867};
RX PubMed=21464989; DOI=10.1371/journal.pone.0017836;
RA Gibbons H.S., Broomall S.M., McNew L.A., Daligault H., Chapman C.,
RA Bruce D., Karavis M., Krepps M., McGregor P.A., Hong C., Park K.H.,
RA Akmal A., Feldman A., Lin J.S., Chang W.E., Higgs B.W., Demirev P.,
RA Lindquist J., Liem A., Fochler E., Read T.D., Tapia R., Johnson S.,
RA Bishop-Lilly K.A., Detter C., Han C., Sozhamannan S., Rosenzweig C.N.,
RA Skowronski E.W.;
RT "Genomic signatures of strain selection and enhancement in Bacillus
RT atrophaeus var. globigii, a historical biowarfare simulant.";
RL PLoS ONE 6:E17836-E17836(2011).
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; CP002207; ADP31601.1; -; Genomic_DNA.
DR RefSeq; WP_013390468.1; NC_014639.1.
DR AlphaFoldDB; A0A0H3DXQ2; -.
DR GeneID; 23409192; -.
DR KEGG; bae:BATR1942_03225; -.
DR eggNOG; COG0002; Bacteria.
DR HOGENOM; CLU_006384_0_1_9; -.
DR OrthoDB; 9801289at2; -.
DR UniPathway; UPA00068; UER00108.
DR Proteomes; UP000006867; 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}.
FT DOMAIN 2..141
FT /note="Semialdehyde dehydrogenase NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00859"
FT ACT_SITE 149
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00150,
FT ECO:0000256|PROSITE-ProRule:PRU10010"
SQ SEQUENCE 345 AA; 38220 MW; 88654D45A89EE029 CRC64;
MKIGIVGATG YGGAELVRIL KNHPHAEECI LYSSSGQGNA YSETYPHMSG LVHQTLQPIN
MNTIKHEADV MFLATPPGVS SELTPQLAVA GIPVIDLSGD LRIQEPEVYE KWYKRTAAPE
QTIEETVYGL SEINREHIKK AKLIANPGCF PTAVLLGLAP LVQNKLLDES FLIVDAKTGV
SGAGRKASMG THFSELNDNL KIYKVNEHQH TPEIEQLLKE WHPAMENITF SAHLVPMTRG
IMATMYTQIK TNMSGDDLQS LYSEFYQDSY FVRVRPQGHF PATKEVWGSN FCDIGITIDE
RTNRVTVVSV IDNLMKGASG QAVQNLNIMN GWKEETGLTM TPIYP
//
