ID ARGC_METMP Reviewed; 343 AA.
AC Q6M102;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 01-MAY-2013, entry version 71.
DE RecName: Full=N-acetyl-gamma-glutamyl-phosphate reductase;
DE Short=AGPR;
DE EC=1.2.1.38;
DE AltName: Full=N-acetyl-glutamate semialdehyde dehydrogenase;
DE Short=NAGSA dehydrogenase;
GN Name=argC; OrderedLocusNames=MMP0116;
OS Methanococcus maripaludis (strain S2 / LL).
OC Archaea; Euryarchaeota; Methanococci; Methanococcales;
OC Methanococcaceae; Methanococcus.
OX NCBI_TaxID=267377;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S2 / LL;
RX PubMed=15466049; DOI=10.1128/JB.186.20.6956-6969.2004;
RA Hendrickson E.L., Kaul R., Zhou Y., Bovee D., Chapman P., Chung J.,
RA Conway de Macario E., Dodsworth J.A., Gillett W., Graham D.E.,
RA Hackett M., Haydock A.K., Kang A., Land M.L., Levy R., Lie T.J.,
RA Major T.A., Moore B.C., Porat I., Palmeiri A., Rouse G.,
RA Saenphimmachak C., Soell D., Van Dien S., Wang T., Whitman W.B.,
RA Xia Q., Zhang Y., Larimer F.W., Olson M.V., Leigh J.A.;
RT "Complete genome sequence of the genetically tractable
RT hydrogenotrophic methanogen Methanococcus maripaludis.";
RL J. Bacteriol. 186:6956-6969(2004).
CC -!- CATALYTIC ACTIVITY: N-acetyl-L-glutamate 5-semialdehyde + NADP(+)
CC + phosphate = N-acetyl-5-glutamyl phosphate + NADPH.
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-
CC acetyl-L-ornithine from L-glutamate: step 3/4.
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- SIMILARITY: Belongs to the NAGSA dehydrogenase family. Type 1
CC subfamily.
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DR EMBL; BX950229; CAF29672.1; -; Genomic_DNA.
DR RefSeq; NP_987236.1; NC_005791.1.
DR ProteinModelPortal; Q6M102; -.
DR STRING; 267377.MMP0116; -.
DR EnsemblBacteria; CAF29672; CAF29672; MMP0116.
DR GeneID; 2761790; -.
DR KEGG; mmp:MMP0116; -.
DR eggNOG; COG0002; -.
DR HOGENOM; HOG000254902; -.
DR KO; K00145; -.
DR OMA; VCRIAVH; -.
DR ProtClustDB; PRK00436; -.
DR BioCyc; MMAR267377:GJ77-137-MONOMER; -.
DR UniPathway; UPA00068; UER00108.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003942; F:N-acetyl-gamma-glutamyl-phosphate reductase activity; IEA:HAMAP.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0006526; P:arginine biosynthetic process; IEA:HAMAP.
DR Gene3D; 3.40.50.720; -; 1.
DR HAMAP; MF_00150; ArgC_type1; 1; -.
DR InterPro; IPR023013; AGPR_AS.
DR InterPro; IPR000706; AGPR_type-1.
DR InterPro; IPR016040; NAD(P)-bd_dom.
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 TIGRFAMs; TIGR01850; argC; 1.
DR PROSITE; PS01224; ARGC; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Arginine biosynthesis; Complete proteome;
KW Cytoplasm; NADP; Oxidoreductase.
FT CHAIN 1 343 N-acetyl-gamma-glutamyl-phosphate
FT reductase.
FT /FTId=PRO_0000112489.
FT ACT_SITE 149 149 By similarity.
SQ SEQUENCE 343 AA; 37784 MW; E16F55C2ADE76AEF CRC64;
MKTVSIIGGT GYTGSELLRL LSNHDEVEVV NVTSRKEAGK NLTDYHPQVR NLSNYNDLKF
QNIAPEDIDS DIVFCATPHG ASMAIVPTLH EKGINVIDLS GDYRFEDIDM YESWYGLKHS
GKIDSAVYGL PELHREKIKK SKTIANPGCY PTGAILSMAP LVANDLVEDR IIFDSKSGVS
GAGVEASQTT HFANVNENIG PYKITKHRHS PEIGKELQYL ANKNLKVSFT PHLLPVTRGI
LTTAHSFLKE DISPIDVIEI YEEFYKDEFF IRIFEEGMPS LTGVRGTNFC DIGGFEIDQY
GRIVVVSAID NLVKGASGQA IQNMNIIMGF DEKEGLGVGG LKP
//
