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Database: UniProt
Entry: A0A161J2W6_9MICO
LinkDB: A0A161J2W6_9MICO
Original site: A0A161J2W6_9MICO 
ID   A0A161J2W6_9MICO        Unreviewed;       349 AA.
AC   A0A161J2W6;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 34.
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=A6122_1026 {ECO:0000313|EMBL:AND16175.1};
OS   Rathayibacter tritici.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Rathayibacter.
OX   NCBI_TaxID=33888 {ECO:0000313|EMBL:AND16175.1, ECO:0000313|Proteomes:UP000077071};
RN   [1] {ECO:0000313|EMBL:AND16175.1, ECO:0000313|Proteomes:UP000077071}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCPPB 1953 {ECO:0000313|EMBL:AND16175.1,
RC   ECO:0000313|Proteomes:UP000077071};
RA   Park J., Lee H.-H., Lee S.-W., Seo Y.-S.;
RT   "Complete genome sequence of Rathayibacter tritici NCPPB 1953.";
RL   Submitted (MAY-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; CP015515; AND16175.1; -; Genomic_DNA.
DR   RefSeq; WP_068252429.1; NZ_PSWT01000054.1.
DR   AlphaFoldDB; A0A161J2W6; -.
DR   STRING; 33888.A6122_1026; -.
DR   KEGG; rtn:A6122_1026; -.
DR   PATRIC; fig|33888.3.peg.1131; -.
DR   OrthoDB; 9801289at2; -.
DR   UniPathway; UPA00068; UER00108.
DR   Proteomes; UP000077071; 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:UP000077071}.
FT   DOMAIN          4..133
FT                   /note="Semialdehyde dehydrogenase NAD-binding"
FT                   /evidence="ECO:0000259|SMART:SM00859"
FT   ACT_SITE        152
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00150,
FT                   ECO:0000256|PROSITE-ProRule:PRU10010"
SQ   SEQUENCE   349 AA;  35740 MW;  6D24409596A457FE CRC64;
     MSFSVAVAGA SGYAGGELLR LLADHLEFEV RTVTAHANAG QPLSAVHPHL RSLRDLVLVD
     TTTENLAGHD VVFLALPHGK SGEITATLPE GVLVVDCGAD HRLTDPQDWA DYYGGDFAGA
     WPYGLPELLI GGGGRKQREA LAGVRRIAVP GCNVTAITLG LAPGLHAGVI EPSDLVSVLA
     VGPSGAGKSL RTDLLASELL GSAHAYGLGG AHRHNPEIRQ NLLLAGAGPV SISFTPVLVP
     MSRGILATST ARLAPGVSAQ DVRAAWETAY GDETFVQLLP EGSFPRTADV VGANTALIGL
     AVDERARRVV VVSAIDNLVK GTAGAAVQSS NIALGLPESL GLSVNGVAP
//
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