ID T0ZAA5_9ZZZZ Unreviewed; 265 AA.
AC T0ZAA5;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=N-acetyl-gamma-glutamyl-phosphate reductase {ECO:0000313|EMBL:EQD26054.1};
DE EC=2.7.2.8 {ECO:0000313|EMBL:EQD26054.1};
DE Flags: Fragment;
GN ORFNames=B1A_22029 {ECO:0000313|EMBL:EQD26054.1};
OS mine drainage metagenome.
OC unclassified sequences; metagenomes; ecological metagenomes.
OX NCBI_TaxID=410659 {ECO:0000313|EMBL:EQD26054.1};
RN [1] {ECO:0000313|EMBL:EQD26054.1}
RP NUCLEOTIDE SEQUENCE.
RA Mendez C., Richter M., Ferrer M., Sanchez J.;
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EQD26054.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=24430486; DOI=10.1038/ismej.2013.242;
RA Mendez-Garcia C., Mesa V., Sprenger R.R., Richter M., Diez M.S., Solano J.,
RA Bargiela R., Golyshina O.V., Manteca A., Ramos J.L., Gallego J.R.,
RA Llorente I., Martins Dos Santos V.A., Jensen O.N., Pelaez A.I., Sanchez J.,
RA Ferrer M.;
RT "Microbial stratification in low pH oxic and suboxic macroscopic growths
RT along an acid mine drainage.";
RL ISME J. 8:1259-1274(2014).
CC -!- PATHWAY: Amino-acid biosynthesis. {ECO:0000256|ARBA:ARBA00029440}.
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:EQD26054.1}.
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DR EMBL; AUZX01016281; EQD26054.1; -; Genomic_DNA.
DR AlphaFoldDB; T0ZAA5; -.
DR GO; GO:0003991; F:acetylglutamate kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0003942; F:N-acetyl-gamma-glutamyl-phosphate reductase activity; IEA:InterPro.
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-KW.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 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 4: Predicted;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Arginine biosynthesis {ECO:0000256|ARBA:ARBA00022571};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Transferase {ECO:0000313|EMBL:EQD26054.1}.
FT DOMAIN 1..69
FT /note="Semialdehyde dehydrogenase NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00859"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EQD26054.1"
SQ SEQUENCE 265 AA; 28351 MW; F668B496332DABB3 CRC64;
ESLDPAAVAT RSADVVVLAL PNGKAAPYVE AIDTAAPDTL IVDLSADYRF DKAWYYGLPE
LTRAHYAGQR RISNPGCYAT AMQLALAPLR GLLGGMPACF GVSGYSGAGT TPSDKNDADK
LRDNLMPYQL TGHLHEREVT HRLGQPVAFM PHVAAYFRGI TLTVHAPLAS PLDGVAALRA
LFRDAYAHEP LLRVRDDPPW VSRIAGRHHA EIGGFALGDD GRRAVLVVTL DNLLKGAATQ
ALQNLNRALG HPELEGIPLD AAARP
//
