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Database: UniProt
Entry: A0A0D8HF83_9ACTN
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ID   A0A0D8HF83_9ACTN        Unreviewed;       362 AA.
AC   A0A0D8HF83;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   24-JAN-2024, entry version 37.
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:KJF16583.1};
GN   ORFNames=AXFE_25510 {ECO:0000313|EMBL:KJF16583.1};
OS   Acidithrix ferrooxidans.
OC   Bacteria; Actinomycetota; Acidimicrobiia; Acidimicrobiales;
OC   Acidimicrobiaceae; Acidithrix.
OX   NCBI_TaxID=1280514 {ECO:0000313|EMBL:KJF16583.1, ECO:0000313|Proteomes:UP000032360};
RN   [1] {ECO:0000313|EMBL:KJF16583.1, ECO:0000313|Proteomes:UP000032360}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Py-F3 {ECO:0000313|EMBL:KJF16583.1,
RC   ECO:0000313|Proteomes:UP000032360};
RA   Poehlein A., Eisen S., Schloemann M., Johnson B.D., Daniel R., Muehling M.;
RT   "Draft genome of the acidophilic iron oxidizer Acidithrix ferrooxidans
RT   strain Py-F3.";
RL   Submitted (JAN-2015) 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:KJF16583.1}.
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DR   EMBL; JXYS01000079; KJF16583.1; -; Genomic_DNA.
DR   RefSeq; WP_052606255.1; NZ_JXYS01000079.1.
DR   AlphaFoldDB; A0A0D8HF83; -.
DR   STRING; 1280514.AXFE_25510; -.
DR   PATRIC; fig|1280514.3.peg.3348; -.
DR   OrthoDB; 9801289at2; -.
DR   UniPathway; UPA00068; UER00108.
DR   Proteomes; UP000032360; 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:UP000032360}.
FT   DOMAIN          2..146
FT                   /note="Semialdehyde dehydrogenase NAD-binding"
FT                   /evidence="ECO:0000259|SMART:SM00859"
FT   ACT_SITE        154
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00150,
FT                   ECO:0000256|PROSITE-ProRule:PRU10010"
SQ   SEQUENCE   362 AA;  38150 MW;  15C3D4A90E843CFA CRC64;
     MKAVIFGASG YGGAELIRSL GVHPSFEVVG LSGGANAGAT LGEIYPHLET SSFGEMVLFD
     TDGLCDFIEH NQVDLAFLAL PNNTATKIVP RIIDKVSCVI DLSADFRLKD PSLYESYYGY
     VHPEPKLLEE AVYGLCELNR SQLIGAKLIA APGCYVTAST LALFPFLDQS IIDSNNVVIS
     AVSGVSGAGR GSSVANLFSE IDSNVMAYGL FGHRHRPEIE QNLGSSVLFI PHLVPMTRGI
     LATCFGDLSG EVAGELGLSH VSDITAKSSL LSRYLNGLLS DFYSGDQFVE VLAPGVSPRT
     KSTLGTNNAL VSVSYDAQTN KVIVLAAIDN MVKGAAGQAI QAANIAFGLA EDAGLSKVSF
     YP
//
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