ARGC_THET2
ID ARGC_THET2 Reviewed; 345 AA.
AC P96136;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2004, sequence version 3.
DT 25-MAY-2022, entry version 137.
DE RecName: Full=N-acetyl-gamma-glutamyl-phosphate reductase {ECO:0000255|HAMAP-Rule:MF_00150};
DE Short=AGPR {ECO:0000255|HAMAP-Rule:MF_00150};
DE EC=1.2.1.38 {ECO:0000255|HAMAP-Rule:MF_00150};
DE AltName: Full=N-acetyl-glutamate semialdehyde dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00150, ECO:0000303|PubMed:9493385};
DE Short=NAGSA dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00150, ECO:0000303|PubMed:9493385};
GN Name=argC {ECO:0000255|HAMAP-Rule:MF_00150, ECO:0000303|PubMed:9493385};
GN OrderedLocusNames=TT_C0836;
OS Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=262724;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PATHWAY.
RC STRAIN=ATCC BAA-163 / DSM 7039 / HB27;
RX PubMed=9493385; DOI=10.1099/00221287-144-2-479;
RA Baetens M.C.Y., Legrain C., Boyen A., Glansdorff N.;
RT "Genes and enzymes of the acetyl cycle of arginine biosynthesis in the
RT extreme thermophilic bacterium Thermus thermophilus HB27.";
RL Microbiology 144:479-492(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC BAA-163 / DSM 7039 / HB27;
RX PubMed=11004195; DOI=10.1128/jb.182.20.5911-5915.2000;
RA Sanchez R., Roovers M., Glansdorff N.;
RT "Organization and expression of a Thermus thermophilus arginine cluster:
RT presence of unidentified open reading frames and absence of a Shine-
RT Dalgarno sequence.";
RL J. Bacteriol. 182:5911-5915(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-163 / DSM 7039 / HB27;
RX PubMed=15064768; DOI=10.1038/nbt956;
RA Henne A., Brueggemann H., Raasch C., Wiezer A., Hartsch T., Liesegang H.,
RA Johann A., Lienard T., Gohl O., Martinez-Arias R., Jacobi C.,
RA Starkuviene V., Schlenczeck S., Dencker S., Huber R., Klenk H.-P.,
RA Kramer W., Merkl R., Gottschalk G., Fritz H.-J.;
RT "The genome sequence of the extreme thermophile Thermus thermophilus.";
RL Nat. Biotechnol. 22:547-553(2004).
CC -!- FUNCTION: Catalyzes the NADPH-dependent reduction of N-acetyl-5-
CC glutamyl phosphate to yield N-acetyl-L-glutamate 5-semialdehyde.
CC {ECO:0000255|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:0000255|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:0000255|HAMAP-
CC Rule:MF_00150, ECO:0000305|PubMed:9493385}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00150}.
CC -!- SIMILARITY: Belongs to the NAGSA dehydrogenase family. Type 1
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00150}.
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DR EMBL; Y10525; CAA71550.1; -; Genomic_DNA.
DR EMBL; Y18353; CAA77142.1; -; Genomic_DNA.
DR EMBL; AE017221; AAS81182.1; -; Genomic_DNA.
DR RefSeq; WP_011173267.1; NC_005835.1.
DR AlphaFoldDB; P96136; -.
DR SMR; P96136; -.
DR STRING; 262724.TT_C0836; -.
DR EnsemblBacteria; AAS81182; AAS81182; TT_C0836.
DR GeneID; 3168562; -.
DR KEGG; tth:TT_C0836; -.
DR eggNOG; COG0002; Bacteria.
DR HOGENOM; CLU_006384_0_1_0; -.
DR OMA; PHLTPMI; -.
DR UniPathway; UPA00068; UER00108.
DR Proteomes; UP000000592; 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:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniRule.
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 Pfam; PF01118; Semialdhyde_dh; 1.
DR Pfam; PF02774; Semialdhyde_dhC; 1.
DR SMART; SM00859; Semialdhyde_dh; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR01850; argC; 1.
DR PROSITE; PS01224; ARGC; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Arginine biosynthesis; Cytoplasm; NADP;
KW Oxidoreductase.
FT CHAIN 1..345
FT /note="N-acetyl-gamma-glutamyl-phosphate reductase"
FT /id="PRO_0000112468"
FT ACT_SITE 142
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00150"
FT CONFLICT 183
FT /note="F -> L (in Ref. 1; CAA71550 and 2; CAA77142)"
FT /evidence="ECO:0000305"
FT CONFLICT 234
FT /note="P -> H (in Ref. 1; CAA71550 and 2; CAA77142)"
FT /evidence="ECO:0000305"
FT CONFLICT 243..272
FT /note="ILVTAEAEVEGAWSQESLEALYRDFYAGEP -> SWSPRGRGGGRLEPGEPR
FT GALPGLLRRGA (in Ref. 1; CAA71550 and 2; CAA77142)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 345 AA; 37634 MW; BD67CC4DC17A6407 CRC64;
MGILGASGYG GAELLRLLKA HPEVELVGFS SRKYEGRPLE AAWPQLWDGR LFAAQEEVLE
RAEVVFLALP NGLSMEIAPE ALKAGKRVVD LSGDFRLPPE VYEAWYRIPH KSPDLYREAV
YGLPELHREE LKGARLVANP GCYVTAATLA LAPLAAEGVL KGAFVVGLSG VSGAGREAEG
TAFAEVNENL KPYKAGGTHR HIPEMERNLG RILAQGRRVR THGEARAVRL SFTPHLVPMT
RGILVTAEAE VEGAWSQESL EALYRDFYAG EPFVRVLKGL PETKATLGSN RVDVRPLYEE
RTGRVLVFAA LDNLVKGMAG QAVQNLNLML GLPEETALPK EGLWP
