ARGC_THEMA
ID ARGC_THEMA Reviewed; 339 AA.
AC Q9X2A2;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 25-MAY-2022, entry version 145.
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};
DE Short=NAGSA dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00150};
GN Name=argC {ECO:0000255|HAMAP-Rule:MF_00150}; OrderedLocusNames=TM_1782;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
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}.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE000512; AAD36845.1; -; Genomic_DNA.
DR PIR; A72211; A72211.
DR RefSeq; NP_229579.1; NC_000853.1.
DR RefSeq; WP_004082328.1; NZ_CP011107.1.
DR PDB; 1VKN; X-ray; 1.80 A; A/B/C/D=1-339.
DR PDBsum; 1VKN; -.
DR AlphaFoldDB; Q9X2A2; -.
DR SMR; Q9X2A2; -.
DR STRING; 243274.THEMA_05290; -.
DR EnsemblBacteria; AAD36845; AAD36845; TM_1782.
DR KEGG; tma:TM1782; -.
DR eggNOG; COG0002; Bacteria.
DR InParanoid; Q9X2A2; -.
DR OMA; PHLTPMI; -.
DR OrthoDB; 951261at2; -.
DR UniPathway; UPA00068; UER00108.
DR EvolutionaryTrace; Q9X2A2; -.
DR Proteomes; UP000008183; 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 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Arginine biosynthesis; Cytoplasm;
KW NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..339
FT /note="N-acetyl-gamma-glutamyl-phosphate reductase"
FT /id="PRO_0000112466"
FT ACT_SITE 145
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00150"
FT STRAND 2..8
FT /evidence="ECO:0007829|PDB:1VKN"
FT HELIX 12..23
FT /evidence="ECO:0007829|PDB:1VKN"
FT STRAND 27..33
FT /evidence="ECO:0007829|PDB:1VKN"
FT TURN 36..39
FT /evidence="ECO:0007829|PDB:1VKN"
FT HELIX 42..45
FT /evidence="ECO:0007829|PDB:1VKN"
FT HELIX 47..49
FT /evidence="ECO:0007829|PDB:1VKN"
FT HELIX 60..66
FT /evidence="ECO:0007829|PDB:1VKN"
FT STRAND 68..72
FT /evidence="ECO:0007829|PDB:1VKN"
FT HELIX 78..83
FT /evidence="ECO:0007829|PDB:1VKN"
FT STRAND 90..96
FT /evidence="ECO:0007829|PDB:1VKN"
FT TURN 97..99
FT /evidence="ECO:0007829|PDB:1VKN"
FT HELIX 103..110
FT /evidence="ECO:0007829|PDB:1VKN"
FT HELIX 117..119
FT /evidence="ECO:0007829|PDB:1VKN"
FT STRAND 122..124
FT /evidence="ECO:0007829|PDB:1VKN"
FT HELIX 127..134
FT /evidence="ECO:0007829|PDB:1VKN"
FT STRAND 138..141
FT /evidence="ECO:0007829|PDB:1VKN"
FT HELIX 145..159
FT /evidence="ECO:0007829|PDB:1VKN"
FT STRAND 166..175
FT /evidence="ECO:0007829|PDB:1VKN"
FT HELIX 176..179
FT /evidence="ECO:0007829|PDB:1VKN"
FT HELIX 185..187
FT /evidence="ECO:0007829|PDB:1VKN"
FT HELIX 189..192
FT /evidence="ECO:0007829|PDB:1VKN"
FT HELIX 206..218
FT /evidence="ECO:0007829|PDB:1VKN"
FT STRAND 223..235
FT /evidence="ECO:0007829|PDB:1VKN"
FT STRAND 237..244
FT /evidence="ECO:0007829|PDB:1VKN"
FT HELIX 249..260
FT /evidence="ECO:0007829|PDB:1VKN"
FT STRAND 266..268
FT /evidence="ECO:0007829|PDB:1VKN"
FT HELIX 277..280
FT /evidence="ECO:0007829|PDB:1VKN"
FT STRAND 286..293
FT /evidence="ECO:0007829|PDB:1VKN"
FT TURN 294..297
FT /evidence="ECO:0007829|PDB:1VKN"
FT STRAND 298..305
FT /evidence="ECO:0007829|PDB:1VKN"
FT TURN 307..312
FT /evidence="ECO:0007829|PDB:1VKN"
FT HELIX 313..323
FT /evidence="ECO:0007829|PDB:1VKN"
FT TURN 328..331
FT /evidence="ECO:0007829|PDB:1VKN"
SQ SEQUENCE 339 AA; 37936 MW; E3152D5D4E4EA116 CRC64;
MIRAGIIGAT GYTGLELVRL LKNHPEAKIT YLSSRTYAGK KLEEIFPSTL ENSILSEFDP
EKVSKNCDVL FTALPAGASY DLVRELKGVK IIDLGADFRF DDPGVYREWY GKELSGYENI
KRVYGLPELH REEIKNAQVV GNPGCYPTSV ILALAPALKH NLVDPETILV DAKSGVSGAG
RKEKVDYLFS EVNESLRPYN VAKHRHVPEM EQELGKISGK KVNVVFTPHL VPMTRGILST
IYVKTDKSLE EIHEAYLEFY KNEPFVHVLP MGIYPSTKWC YGSNHVFIGM QMEERTNTLI
LMSAIDNLVK GASGQAVQNM NIMFGLDETK GLEFTPIYP
