(data stored in SCRATCH zone)

SWISSPROT: C8W633_DESAS

ID   C8W633_DESAS            Unreviewed;       295 AA.
AC   C8W633;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 68.
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   OrderedLocusNames=Dtox_0568 {ECO:0000313|EMBL:ACV61488.1};
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:ACV61488.1, ECO:0000313|Proteomes:UP000002217};
RN   [1] {ECO:0000313|EMBL:ACV61488.1, 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 ATP-dependent phosphorylation of N-acetyl-
CC       L-glutamate. {ECO:0000256|HAMAP-Rule:MF_00082,
CC       ECO:0000256|SAAS:SAAS01076979}.
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   -!- 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; CP001720; ACV61488.1; -; Genomic_DNA.
DR   RefSeq; WP_015756207.1; NC_013216.1.
DR   STRING; 485916.Dtox_0568; -.
DR   EnsemblBacteria; ACV61488; ACV61488; Dtox_0568.
DR   KEGG; dae:Dtox_0568; -.
DR   eggNOG; ENOG4105CAS; Bacteria.
DR   eggNOG; COG0548; LUCA.
DR   HOGENOM; HOG000233259; -.
DR   KO; K00930; -.
DR   OMA; PKTECCI; -.
DR   OrthoDB; 901370at2; -.
DR   BioCyc; DACE485916:G1GFV-575-MONOMER; -.
DR   UniPathway; UPA00068; UER00107.
DR   Proteomes; UP000002217; 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; IPR041727; NAGK-C.
DR   Pfam; PF00696; AA_kinase; 1.
DR   PIRSF; PIRSF000728; NAGK; 1.
DR   SUPFAM; SSF53633; SSF53633; 1.
DR   TIGRFAMs; TIGR00761; argB; 1.
PE   3: Inferred from homology;
DR   PRODOM; C8W633.
DR   SWISS-2DPAGE; C8W633.
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:UP000002217};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00082};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00082,
KW   ECO:0000256|SAAS:SAAS00461199, ECO:0000313|EMBL:ACV61488.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00082,
KW   ECO:0000256|SAAS:SAAS00461200};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002217};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00082,
KW   ECO:0000256|SAAS:SAAS00461129, ECO:0000313|EMBL:ACV61488.1}.
FT   DOMAIN       24    271       AA_kinase. {ECO:0000259|Pfam:PF00696}.
FT   REGION       64     65       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00082}.
FT   BINDING      86     86       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00082}.
FT   BINDING     190    190       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00082}.
FT   SITE         29     29       Transition state stabilizer.
FT                                {ECO:0000256|HAMAP-Rule:MF_00082}.
FT   SITE        253    253       Transition state stabilizer.
FT                                {ECO:0000256|HAMAP-Rule:MF_00082}.
SQ   SEQUENCE   295 AA;  31492 MW;  94E2F74D8166FB7E CRC64;
     MLTALEKAGI LVEALPYIKK FYGKTVIIKY GGHAMINEQL KQAVLTDAVL MKFVGMHPVI
     VHGGGPEITG MLKRVGKVSE FVGGLRVTDR ETMEIVEMVL VGKINKDIVA LINRFGGRAV
     GLCGKDAGLF KAVKKPGTLR LPDGSTQEVD IGFVGDISRV NPQIVVNLIG EGYIPVIAPV
     AVGDGGESYN VNADYAAGKL AEALKADKFI NLTDVEGILR DRNDLSSLIS TLHVDEVPEL
     IRQGIIDGGM IPKVECCIEA IKGGVPQAHI LDGRVQHSIL LEVFTDQGVG TMVVS
//

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