ARGC_BACSU
ID ARGC_BACSU Reviewed; 345 AA.
AC P23715; O08146; P70953;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 3.
DT 03-AUG-2022, entry version 153.
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=BSU11190;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / EMG50;
RX PubMed=2117746; DOI=10.1093/nar/18.15.4595;
RA Smith M.C.M., Mountain A., Baumberg S.;
RT "Nucleotide sequence of the Bacillus subtilis argC gene encoding N-
RT acetylglutamate-gamma-semialdehyde dehydrogenase.";
RL Nucleic Acids Res. 18:4595-4595(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=8025667; DOI=10.1099/13500872-140-5-1023;
RA O'Reilly M., Devine K.M.;
RT "Sequence and analysis of the citrulline biosynthetic operon argC-F from
RT Bacillus subtilis.";
RL Microbiology 140:1023-1025(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9025291; DOI=10.1099/00221287-143-1-175;
RA Levine A., Vannier F., Roche B., Autret S., Mavel D., Seror S.J.;
RT "A 10.3 kbp segment from nprB to argJ at the 102 degrees region of the
RT Bacillus subtilis chromosome.";
RL Microbiology 143:175-177(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9353931; DOI=10.1099/00221287-143-10-3305;
RA Medina N., Vannier F., Roche B., Autret S., Levine A., Seror S.J.;
RT "Sequencing of regions downstream of addA (98 degrees) and citG (289
RT degrees) in Bacillus subtilis.";
RL Microbiology 143:3305-3308(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [6]
RP SEQUENCE REVISION TO 235 AND 340.
RX PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT 168 reference genome a decade later.";
RL Microbiology 155:1758-1775(2009).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-56.
RX PubMed=3106155; DOI=10.1016/0378-1119(86)90384-7;
RA Smith M.C.M., Mountain A., Baumberg S.;
RT "Sequence analysis of the Bacillus subtilis argC promoter region.";
RL Gene 49:53-60(1986).
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}.
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DR EMBL; X52834; CAA37016.1; -; Genomic_DNA.
DR EMBL; Z26919; CAA81543.1; -; Genomic_DNA.
DR EMBL; Z79580; CAB01842.1; -; Genomic_DNA.
DR EMBL; Y09476; CAA70638.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB12960.2; -; Genomic_DNA.
DR EMBL; M15420; AAA22248.1; -; Genomic_DNA.
DR PIR; I40372; I40372.
DR RefSeq; NP_389001.2; NC_000964.3.
DR RefSeq; WP_003245768.1; NZ_JNCM01000035.1.
DR RefSeq; WP_009966985.1; NZ_CM000487.1.
DR AlphaFoldDB; P23715; -.
DR SMR; P23715; -.
DR IntAct; P23715; 3.
DR MINT; P23715; -.
DR STRING; 224308.BSU11190; -.
DR PaxDb; P23715; -.
DR PRIDE; P23715; -.
DR EnsemblBacteria; CAB12960; CAB12960; BSU_11190.
DR GeneID; 936389; -.
DR KEGG; bsu:BSU11190; -.
DR PATRIC; fig|224308.179.peg.1204; -.
DR eggNOG; COG0002; Bacteria.
DR InParanoid; P23715; -.
DR OMA; PHLTPMI; -.
DR PhylomeDB; P23715; -.
DR BioCyc; BSUB:BSU11190-MON; -.
DR UniPathway; UPA00068; UER00108.
DR Proteomes; UP000001570; 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; Reference proteome.
FT CHAIN 1..345
FT /note="N-acetyl-gamma-glutamyl-phosphate reductase"
FT /id="PRO_0000112385"
FT ACT_SITE 149
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00150"
FT CONFLICT 235
FT /note="V -> F (in Ref. 1; CAA37016 and 2; CAA81543)"
FT /evidence="ECO:0000305"
FT CONFLICT 340
FT /note="I -> II (in Ref. 2; CAA81543, 3; CAB01842 and 4;
FT CAA70638)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 345 AA; 37960 MW; 35B40ADC17633EA4 CRC64;
MKIGIVGATG YGGTELVRIL SHHPHAEECI LYSSSGEGNV YSEGYPHLTG LADQQLKPID
MNTIKHEIDI MFLAAPPGVS SELTPKLADA GITVIDLSGD LRIKEPAEYE KWYKRTAAPK
AVIQEAVYGL AELNQLQIQQ AKLIANPGCF PTAVLLGLAP LAQKKLLDES FVIVDAKTGV
SGAGRKASMG THFSELNDNF KIYKVNEHQH TPEIEQALNE WQPGLGPITF SAHLVPMTRG
IMATMYTRLT CDLTADDLHD LYSEFYQDSY FVRVRPKGQY PQTKEVYGSN FCDIAVTLDE
RTNRVTIVSV IDNLMKGAAG QAVQNFNLMN GWNEETGLTI TPIYP
