(data stored in SCRATCH zone)

SWISSPROT: D4YYT6_SPHJU

ID   D4YYT6_SPHJU            Unreviewed;       305 AA.
AC   D4YYT6;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   08-MAY-2019, entry version 61.
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:BAI95518.1};
GN   OrderedLocusNames=SJA_C1-06840 {ECO:0000313|EMBL:BAI95518.1};
OS   Sphingobium japonicum (strain DSM 16413 / CCM 7287 / MTCC 6362 / UT26
OS   / NBRC 101211 / UT26S).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingobium.
OX   NCBI_TaxID=452662 {ECO:0000313|EMBL:BAI95518.1, ECO:0000313|Proteomes:UP000007753};
RN   [1] {ECO:0000313|EMBL:BAI95518.1, ECO:0000313|Proteomes:UP000007753}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16413 / CCM 7287 / MTCC 6362 / UT26 / NBRC 101211 / UT26S
RC   {ECO:0000313|Proteomes:UP000007753};
RX   PubMed=20817768; DOI=10.1128/JB.00961-10;
RA   Nagata Y., Ohtsubo Y., Endo R., Ichikawa N., Ankai A., Oguchi A.,
RA   Fukui S., Fujita N., Tsuda M.;
RT   "Complete genome sequence of the representative gamma-
RT   hexachlorocyclohexane-degrading bacterium Sphingobium japonicum
RT   UT26.";
RL   J. Bacteriol. 192:5852-5853(2010).
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; AP010803; BAI95518.1; -; Genomic_DNA.
DR   RefSeq; WP_013039207.1; NC_014006.1.
DR   STRING; 452662.SJA_C1-06840; -.
DR   EnsemblBacteria; BAI95518; BAI95518; SJA_C1-06840.
DR   GeneID; 29272356; -.
DR   KEGG; sjp:SJA_C1-06840; -.
DR   eggNOG; ENOG4105CAS; Bacteria.
DR   eggNOG; COG0548; LUCA.
DR   HOGENOM; HOG000233259; -.
DR   KO; K00930; -.
DR   OMA; PKTECCI; -.
DR   UniPathway; UPA00068; UER00107.
DR   Proteomes; UP000007753; Chromosome 1.
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; D4YYT6.
DR   SWISS-2DPAGE; D4YYT6.
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:UP000007753};
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:BAI95518.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00082,
KW   ECO:0000256|SAAS:SAAS00461200};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007753};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00082,
KW   ECO:0000256|SAAS:SAAS00461129, ECO:0000313|EMBL:BAI95518.1}.
FT   DOMAIN       35    280       AA_kinase. {ECO:0000259|Pfam:PF00696}.
FT   REGION       75     76       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00082}.
FT   BINDING      97     97       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00082}.
FT   BINDING     203    203       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00082}.
FT   SITE         40     40       Transition state stabilizer.
FT                                {ECO:0000256|HAMAP-Rule:MF_00082}.
FT   SITE        263    263       Transition state stabilizer.
FT                                {ECO:0000256|HAMAP-Rule:MF_00082}.
SQ   SEQUENCE   305 AA;  31842 MW;  625CE2ED5E0FD7E9 CRC64;
     MRPRMNSKHS PDPALLAKAE TLVEALPYMQ RYAGKTFVVK YGGHAMGDPE AARDFAEDVV
     LMKAVGINVV VVHGGGPQIG AMLKKLGVES QFVGGLRVTD KETAQIAEMV LAGSINKEIV
     GWISGAGGRA VGISGKDGGL VLCEKVLGKR EADPNSGIER NVDLGFVGDP VRVDRSILDT
     LTQNGIIPVV APVGIGADGH TYNVNADTMA GAIAAELQAA RFFLLTDVAG VLDKQGQLLT
     DLDPEAINGL EADGTISGGM IPKLETCVRA VEGGVDAAVI LDGRVPHAML LEIFTDRGAG
     TLVRR
//

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