(data stored in ACNUC7421 zone)

SWISSPROT: C8W631_DESAS

ID   C8W631_DESAS            Unreviewed;       346 AA.
AC   C8W631;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 77.
DE   RecName: Full=N-acetyl-gamma-glutamyl-phosphate reductase {ECO:0000256|HAMAP-Rule:MF_00150};
DE            Short=AGPR {ECO:0000256|HAMAP-Rule:MF_00150};
DE            EC=1.2.1.38 {ECO:0000256|HAMAP-Rule:MF_00150};
DE   AltName: Full=N-acetyl-glutamate semialdehyde dehydrogenase {ECO:0000256|HAMAP-Rule:MF_00150};
DE            Short=NAGSA dehydrogenase {ECO:0000256|HAMAP-Rule:MF_00150};
GN   Name=argC {ECO:0000256|HAMAP-Rule:MF_00150};
GN   OrderedLocusNames=Dtox_0566 {ECO:0000313|EMBL:ACV61486.1};
OS   Desulfotomaculum acetoxidans (strain ATCC 49208 / DSM 771 / VKM
OS   B-1644) (Desulfofarcimen acetoxidans).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae;
OC   Desulfofarcimen.
OX   NCBI_TaxID=485916 {ECO:0000313|EMBL:ACV61486.1, ECO:0000313|Proteomes:UP000002217};
RN   [1] {ECO:0000313|EMBL:ACV61486.1, ECO:0000313|Proteomes:UP000002217}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49208 / DSM 771 / VKM B-1644
RC   {ECO:0000313|Proteomes:UP000002217};
RX   PubMed=21304664; DOI=10.4056/sigs.39508;
RA   Spring S., Lapidus A., Schroder M., Gleim D., Sims D., Meincke L.,
RA   Glavina Del Rio T., Tice H., Copeland A., Cheng J.F., Lucas S.,
RA   Chen F., Nolan M., Bruce D., Goodwin L., Pitluck S., Ivanova N.,
RA   Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Chain P., Saunders E.,
RA   Brettin T., Detter J.C., Goker M., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Han C.;
RT   "Complete genome sequence of Desulfotomaculum acetoxidans type strain
RT   (5575).";
RL   Stand. Genomic Sci. 1:242-253(2009).
CC   -!- FUNCTION: Catalyzes the NADPH-dependent reduction of N-acetyl-5-
CC       glutamyl phosphate to yield N-acetyl-L-glutamate 5-semialdehyde.
CC       {ECO:0000256|HAMAP-Rule:MF_00150, ECO:0000256|SAAS:SAAS01081944}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N-acetyl-L-glutamate 5-semialdehyde + NADP(+) + phosphate
CC         = H(+) + N-acetyl-L-glutamyl 5-phosphate + NADPH;
CC         Xref=Rhea:RHEA:21588, ChEBI:CHEBI:15378, ChEBI:CHEBI:29123,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57783, ChEBI:CHEBI:57936,
CC         ChEBI:CHEBI:58349; EC=1.2.1.38; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00150, ECO:0000256|SAAS:SAAS01127949};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-
CC       acetyl-L-ornithine from L-glutamate: step 3/4. {ECO:0000256|HAMAP-
CC       Rule:MF_00150, ECO:0000256|SAAS:SAAS01096212}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00150,
CC       ECO:0000256|SAAS:SAAS01087196}.
CC   -!- SIMILARITY: Belongs to the NAGSA dehydrogenase family. Type 1
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_00150,
CC       ECO:0000256|SAAS:SAAS00591558}.
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DR   EMBL; CP001720; ACV61486.1; -; Genomic_DNA.
DR   RefSeq; WP_015756205.1; NC_013216.1.
DR   STRING; 485916.Dtox_0566; -.
DR   EnsemblBacteria; ACV61486; ACV61486; Dtox_0566.
DR   KEGG; dae:Dtox_0566; -.
DR   eggNOG; ENOG4105C0N; Bacteria.
DR   eggNOG; COG0002; LUCA.
DR   HOGENOM; HOG000254902; -.
DR   KO; K00145; -.
DR   OMA; PHLTPMI; -.
DR   OrthoDB; 951261at2; -.
DR   BioCyc; DACE485916:G1GFV-573-MONOMER; -.
DR   UniPathway; UPA00068; UER00108.
DR   Proteomes; UP000002217; 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;
DR   PRODOM; C8W631.
DR   SWISS-2DPAGE; C8W631.
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00150,
KW   ECO:0000256|SAAS:SAAS00333562};
KW   Arginine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00150,
KW   ECO:0000256|SAAS:SAAS01096209};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002217};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00150,
KW   ECO:0000256|SAAS:SAAS01087102};
KW   NADP {ECO:0000256|HAMAP-Rule:MF_00150, ECO:0000256|SAAS:SAAS00333569};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00150,
KW   ECO:0000256|SAAS:SAAS00333583, ECO:0000313|EMBL:ACV61486.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002217}.
FT   DOMAIN        3    142       Semialdhyde_dh. {ECO:0000259|SMART:
FT                                SM00859}.
FT   ACT_SITE    150    150       {ECO:0000256|HAMAP-Rule:MF_00150,
FT                                ECO:0000256|PROSITE-ProRule:PRU10010}.
SQ   SEQUENCE   346 AA;  38067 MW;  D5D10A281818AAFD CRC64;
     MIKAAIIGAT GYAGAELVRI LSRHPQVRLT AITSQSYAGQ AFWQVYPHLY KYIDLTCEEM
     DLINIINQSD VIFAALPHGH AMPIVLEAVK QNKKIIDLGA DFRIDDPVVY ESWYKVTHTA
     VDLLAEAVYG LPEINRNRIK EARILANPGC YPTSAILGLA PLLARGLIEP ESIIIDSKSG
     VSGAGRSLSL NTHYSEVNES IKAYNIGQHR HTPEIEQEIS KIAGQKITLS FTPHLTPMIR
     GILSTIYAKL KIEALDMDLG QLYRDFYQEE PFVRVLPEGC LPRTKDVSGS NFCDVAVVKD
     KRTGRAVVVS AIDNLLKGAS GQAVQNMNIM FGFAEATGID DPSLYP
//

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