(data stored in ACNUC7421 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   30-AUG-2017, entry version 53.
DE   RecName: Full=Acetylglutamate kinase {ECO:0000256|SAAS:SAAS00384253};
DE            EC=2.7.2.- {ECO:0000256|SAAS:SAAS00701608};
DE            EC=2.7.2.8 {ECO:0000256|SAAS:SAAS00384213};
GN   Name=argB {ECO:0000313|EMBL:BAI95518.1};
GN   OrderedLocusNames=SJA_C1-06840 {ECO:0000313|EMBL:BAI95518.1};
OS   Sphingobium japonicum (strain 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=NBRC 101211 / UT26S {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|SAAS:SAAS00701626}.
CC   -!- CATALYTIC ACTIVITY: ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-
CC       glutamate 5-phosphate. {ECO:0000256|SAAS:SAAS00384289}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-
CC       acetyl-L-ornithine from L-glutamate: step 2/4.
CC       {ECO:0000256|SAAS:SAAS00384237}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|SAAS:SAAS00384301}.
CC   -!- SIMILARITY: Belongs to the acetylglutamate kinase family. ArgB
CC       subfamily. {ECO:0000256|SAAS:SAAS00701617}.
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DR   EMBL; AP010803; BAI95518.1; -; Genomic_DNA.
DR   RefSeq; WP_013039207.1; NC_014006.1.
DR   ProteinModelPortal; D4YYT6; -.
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   OrthoDB; POG091H063W; -.
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-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   HAMAP; MF_00082_B; ArgB_B; 1.
DR   InterPro; IPR004662; AcgluKinase.
DR   InterPro; IPR001048; Asp/Glu/Uridylate_kinase.
DR   InterPro; IPR001057; Glu/AcGlu_kinase.
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|SAAS:SAAS00701594};
KW   Arginine biosynthesis {ECO:0000256|SAAS:SAAS00088592};
KW   ATP-binding {ECO:0000256|SAAS:SAAS00651454};
KW   Complete proteome {ECO:0000313|Proteomes:UP000007753};
KW   Cytoplasm {ECO:0000256|SAAS:SAAS00461202};
KW   Kinase {ECO:0000256|SAAS:SAAS00651459, ECO:0000313|EMBL:BAI95518.1};
KW   Nucleotide-binding {ECO:0000256|SAAS:SAAS00651462};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007753};
KW   Transferase {ECO:0000256|SAAS:SAAS00651468,
KW   ECO:0000313|EMBL:BAI95518.1}.
FT   DOMAIN       35    280       AA_kinase. {ECO:0000259|Pfam:PF00696}.
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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