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Database: UniProt
Entry: H8GU67_DEIGI
LinkDB: H8GU67_DEIGI
Original site: H8GU67_DEIGI 
ID   H8GU67_DEIGI            Unreviewed;       252 AA.
AC   H8GU67;
DT   16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT   16-MAY-2012, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   SubName: Full=N-acetyl-gamma-glutamyl-phosphate reductase 2 {ECO:0000313|EMBL:AFD24209.1};
GN   Name=clpP {ECO:0000313|EMBL:AFD24209.1};
GN   OrderedLocusNames=DGo_CA0282 {ECO:0000313|EMBL:AFD24209.1};
OS   Deinococcus gobiensis (strain DSM 21396 / JCM 16679 / CGMCC 1.7299 / I-0).
OC   Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=745776 {ECO:0000313|EMBL:AFD24209.1, ECO:0000313|Proteomes:UP000007575};
RN   [1] {ECO:0000313|EMBL:AFD24209.1, ECO:0000313|Proteomes:UP000007575}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21396 / JCM 16679 / CGMCC 1.7299 / I-0
RC   {ECO:0000313|Proteomes:UP000007575};
RX   PubMed=22470573; DOI=10.1371/journal.pone.0034458;
RA   Yuan M., Chen M., Zhang W., Lu W., Wang J., Yang M., Zhao P., Tang R.,
RA   Li X., Hao Y., Zhou Z., Zhan Y., Yu H., Teng C., Yan Y., Ping S., Wang Y.,
RA   Lin M.;
RT   "Genome sequence and transcriptome analysis of the radioresistant bacterium
RT   Deinococcus gobiensis: insights into the extreme environmental
RT   adaptations.";
RL   PLoS ONE 7:E34458-E34458(2012).
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DR   EMBL; CP002191; AFD24209.1; -; Genomic_DNA.
DR   AlphaFoldDB; H8GU67; -.
DR   STRING; 745776.DGo_CA0282; -.
DR   KEGG; dgo:DGo_CA0282; -.
DR   PATRIC; fig|745776.4.peg.289; -.
DR   eggNOG; COG0002; Bacteria.
DR   HOGENOM; CLU_077118_0_0_0; -.
DR   Proteomes; UP000007575; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0003942; F:N-acetyl-gamma-glutamyl-phosphate reductase activity; IEA:InterPro.
DR   GO; GO:0006526; P:arginine biosynthetic process; IEA:InterPro.
DR   InterPro; IPR023013; AGPR_AS.
DR   InterPro; IPR010136; AGPR_type-2.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   NCBIfam; TIGR01851; argC_other; 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   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   NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   ACT_SITE        64
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10010"
SQ   SEQUENCE   252 AA;  26804 MW;  1473907CAD2FB8BE CRC64;
     MSILCLHDDA AREAAALTTN PAARLLDAST AHRVNPEWVF GFPELNADQP ARIREARHVA
     NPGCYSTGAI ALLAPLTSRG LLPANFPVHI QGHSGYTGGG RALVDAHEQD LDHPMRGDFL
     GYGLALDHKH IPETMRYGGL TRTPIFTPNV GAWAQGMTVT IPLHLGELNV TAGALHAALA
     EHYAGQRHVR VYAQADNPAV LDPQTLNGTN TLELFVYPAQ DGERAVLAAR LDNLGKGAGG
     AAVQNLELML GL
//
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