(data stored in ACNUC7421 zone)

SWISSPROT: C1AT02_RHOOB

ID   C1AT02_RHOOB            Unreviewed;       351 AA.
AC   C1AT02;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   07-JUN-2017, entry version 71.
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   ECO:0000313|EMBL:BAH48934.1};
GN   OrderedLocusNames=ROP_06870 {ECO:0000313|EMBL:BAH48934.1};
OS   Rhodococcus opacus (strain B4).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=632772 {ECO:0000313|EMBL:BAH48934.1, ECO:0000313|Proteomes:UP000002212};
RN   [1] {ECO:0000313|EMBL:BAH48934.1, ECO:0000313|Proteomes:UP000002212}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B4 {ECO:0000313|EMBL:BAH48934.1,
RC   ECO:0000313|Proteomes:UP000002212};
RA   Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA   Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT   "Comparison of the complete genome sequences of Rhodococcus
RT   erythropolis PR4 and Rhodococcus opacus B4.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CATALYTIC ACTIVITY: N-acetyl-L-glutamate 5-semialdehyde + NADP(+)
CC       + phosphate = N-acetyl-5-glutamyl phosphate + NADPH.
CC       {ECO:0000256|HAMAP-Rule:MF_00150, ECO:0000256|SAAS:SAAS00694068}.
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:SAAS00694085}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00150,
CC       ECO:0000256|SAAS:SAAS00016011}.
CC   -!- SIMILARITY: Belongs to the NAGSA dehydrogenase family. Type 1
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_00150,
CC       ECO:0000256|SAAS:SAAS00661402}.
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DR   EMBL; AP011115; BAH48934.1; -; Genomic_DNA.
DR   RefSeq; WP_012687936.1; NC_012522.1.
DR   STRING; 632772.ROP_06870; -.
DR   EnsemblBacteria; BAH48934; BAH48934; ROP_06870.
DR   KEGG; rop:ROP_06870; -.
DR   PATRIC; fig|632772.20.peg.748; -.
DR   eggNOG; ENOG4105C0N; Bacteria.
DR   eggNOG; COG0002; LUCA.
DR   HOGENOM; HOG000254904; -.
DR   KO; K00145; -.
DR   OMA; TFVPHLT; -.
DR   OrthoDB; POG091H0412; -.
DR   UniPathway; UPA00068; UER00108.
DR   Proteomes; UP000002212; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003942; F:N-acetyl-gamma-glutamyl-phosphate reductase activity; IEA:UniProtKB-HAMAP.
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-HAMAP.
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   SUPFAM; SSF51735; SSF51735; 1.
DR   TIGRFAMs; TIGR01850; argC; 1.
DR   PROSITE; PS01224; ARGC; 1.
PE   3: Inferred from homology;
DR   PRODOM; C1AT02.
DR   SWISS-2DPAGE; C1AT02.
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00150,
KW   ECO:0000256|SAAS:SAAS00132374};
KW   Arginine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00150,
KW   ECO:0000256|SAAS:SAAS00694062};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002212};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00150,
KW   ECO:0000256|SAAS:SAAS00015975};
KW   NADP {ECO:0000256|HAMAP-Rule:MF_00150, ECO:0000256|SAAS:SAAS00132389};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00150,
KW   ECO:0000256|SAAS:SAAS00132381, ECO:0000313|EMBL:BAH48934.1}.
FT   DOMAIN       10    147       Semialdhyde_dh. {ECO:0000259|SMART:
FT                                SM00859}.
FT   ACT_SITE    157    157       {ECO:0000256|HAMAP-Rule:MF_00150,
FT                                ECO:0000256|PROSITE-ProRule:PRU10010}.
SQ   SEQUENCE   351 AA;  35731 MW;  4B27C8C873FD95EB CRC64;
     MTEHAGKPIR IAVAGASGYA GGEVLRLLLG HPSYADGSLV IGALTAGGNA GSTLGSHHPH
     LLPLADRVLE DTTVDTLSGH DVVFLGLPHG NSAQYAKDLP ESTVIIDCGA DFRLTNAEDW
     ERYYKSPHAG SWPYGLPELP GAREKLAGAT RIAVPGCFPT VSSLAMAPAV AAGVVEPRVT
     IVAVTGASGA GRAPKADLLG SEVMGSVRAY GVGGVHRHTP EIIQNLSELA GERVTVSFTP
     VLAPMPRGIL ATCTAVTTAT EDEVRAIYEK AYADEPFVHV LPRGVLPQTG AVVGSNAVQI
     AVAVDADAGQ IVVVAVIDNL AKGTAGGAVQ SMNLALGLPE TAGLSTVGVA P
//

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