(data stored in SCRATCH zone)

SWISSPROT: C1AT00_RHOOB

ID   C1AT00_RHOOB            Unreviewed;       308 AA.
AC   C1AT00;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   08-MAY-2019, entry version 76.
DE   RecName: Full=Acetylglutamate kinase {ECO:0000256|HAMAP-Rule:MF_00082};
DE            EC=2.7.2.8 {ECO:0000256|HAMAP-Rule:MF_00082};
DE   AltName: Full=N-acetyl-L-glutamate 5-phosphotransferase {ECO:0000256|HAMAP-Rule:MF_00082};
DE   AltName: Full=NAG kinase {ECO:0000256|HAMAP-Rule:MF_00082};
DE            Short=NAGK {ECO:0000256|HAMAP-Rule:MF_00082};
GN   Name=argB {ECO:0000256|HAMAP-Rule:MF_00082,
GN   ECO:0000313|EMBL:BAH48932.1};
GN   OrderedLocusNames=ROP_06850 {ECO:0000313|EMBL:BAH48932.1};
OS   Rhodococcus opacus (strain B4).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=632772 {ECO:0000313|EMBL:BAH48932.1, ECO:0000313|Proteomes:UP000002212};
RN   [1] {ECO:0000313|EMBL:BAH48932.1, ECO:0000313|Proteomes:UP000002212}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B4 {ECO:0000313|EMBL:BAH48932.1,
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 ATP-dependent phosphorylation of N-acetyl-
CC       L-glutamate. {ECO:0000256|HAMAP-Rule:MF_00082,
CC       ECO:0000256|SAAS:SAAS01159244}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-
CC         phosphate; Xref=Rhea:RHEA:14629, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:44337, ChEBI:CHEBI:57936, ChEBI:CHEBI:456216;
CC         EC=2.7.2.8; Evidence={ECO:0000256|HAMAP-Rule:MF_00082,
CC         ECO:0000256|SAAS:SAAS01124576};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-
CC       acetyl-L-ornithine from L-glutamate: step 2/4. {ECO:0000256|HAMAP-
CC       Rule:MF_00082, ECO:0000256|SAAS:SAAS01090818}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00082,
CC       ECO:0000256|SAAS:SAAS01159235}.
CC   -!- SIMILARITY: Belongs to the acetylglutamate kinase family. ArgB
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_00082,
CC       ECO:0000256|SAAS:SAAS01076971}.
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DR   EMBL; AP011115; BAH48932.1; -; Genomic_DNA.
DR   RefSeq; WP_012687934.1; NC_012522.1.
DR   EnsemblBacteria; BAH48932; BAH48932; ROP_06850.
DR   KEGG; rop:ROP_06850; -.
DR   PATRIC; fig|632772.20.peg.746; -.
DR   eggNOG; ENOG4105CAS; Bacteria.
DR   eggNOG; COG0548; LUCA.
DR   HOGENOM; HOG000233259; -.
DR   KO; K00930; -.
DR   OMA; PKTECCI; -.
DR   OrthoDB; 901370at2; -.
DR   UniPathway; UPA00068; UER00107.
DR   Proteomes; UP000002212; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003991; F:acetylglutamate kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0042450; P:arginine biosynthetic process via ornithine; IEA:UniProtKB-UniRule.
DR   CDD; cd04250; AAK_NAGK-C; 1.
DR   Gene3D; 3.40.1160.10; -; 1.
DR   HAMAP; MF_00082; ArgB; 1.
DR   InterPro; IPR036393; AceGlu_kinase-like_sf.
DR   InterPro; IPR004662; AcgluKinase_fam.
DR   InterPro; IPR037528; ArgB.
DR   InterPro; IPR001048; Asp/Glu/Uridylate_kinase.
DR   InterPro; IPR001057; Glu/AcGlu_kinase.
DR   InterPro; IPR041727; NAGK-C.
DR   Pfam; PF00696; AA_kinase; 1.
DR   PIRSF; PIRSF000728; NAGK; 1.
DR   PRINTS; PR00474; GLU5KINASE.
DR   SUPFAM; SSF53633; SSF53633; 1.
DR   TIGRFAMs; TIGR00761; argB; 1.
PE   3: Inferred from homology;
DR   PRODOM; C1AT00.
DR   SWISS-2DPAGE; C1AT00.
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00082,
KW   ECO:0000256|SAAS:SAAS01090837};
KW   Arginine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00082,
KW   ECO:0000256|SAAS:SAAS01090853};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00082,
KW   ECO:0000256|SAAS:SAAS00088659};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002212};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00082,
KW   ECO:0000256|SAAS:SAAS01159248};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00082,
KW   ECO:0000256|SAAS:SAAS00461199, ECO:0000313|EMBL:BAH48932.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00082,
KW   ECO:0000256|SAAS:SAAS00461200};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00082,
KW   ECO:0000256|SAAS:SAAS00461129, ECO:0000313|EMBL:BAH48932.1}.
FT   DOMAIN       33    273       AA_kinase. {ECO:0000259|Pfam:PF00696}.
FT   REGION       73     74       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00082}.
FT   BINDING      95     95       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00082}.
FT   BINDING     194    194       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00082}.
FT   SITE         38     38       Transition state stabilizer.
FT                                {ECO:0000256|HAMAP-Rule:MF_00082}.
FT   SITE        255    255       Transition state stabilizer.
FT                                {ECO:0000256|HAMAP-Rule:MF_00082}.
SQ   SEQUENCE   308 AA;  32084 MW;  3974BD2D7A8AFE7B CRC64;
     MTAASEALTG ITDHQKAHVL AEALPWLQQF RDKVVVVKYG GNAMVDDALK TAFAADMAFL
     RTVGIQPVVV HGGGPQINAM LGKLGMTGEF KGGFRVTTPE VMDVVRMVLF GQVGRELVGL
     INAHGPYAVG ISGEDAHLFT ATKRTVMVEG TPTDIGLVGD VTTVNPEAVL DLIRAGRIPV
     VSTIAPDSDG VVHNINADTA AAALAEAIGA EKLVVLTDVE GLYTNWPDRD SLATEIDVDA
     LAQLLPSLDA GMVPKMEACL RAVRGGVPTA HVIDGRLAHS VLLELFTGEG IGTMVTPAPT
     SPTEGVAP
//

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