(data stored in ACNUC10821 zone)

SWISSPROT: C8U2K2_ECO10

ID   C8U2K2_ECO10            Unreviewed;       297 AA.
AC   C8U2K2;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 49.
DE   RecName: Full=Carbamate kinase {ECO:0000256|PIRNR:PIRNR000723};
GN   Name=ybcF {ECO:0000313|EMBL:BAI29360.1};
GN   OrderedLocusNames=ECO103_0493 {ECO:0000313|EMBL:BAI29360.1};
OS   Escherichia coli O103:H2 (strain 12009 / EHEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585395 {ECO:0000313|EMBL:BAI29360.1, ECO:0000313|Proteomes:UP000000959};
RN   [1] {ECO:0000313|EMBL:BAI29360.1, ECO:0000313|Proteomes:UP000000959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12009 / EHEC {ECO:0000313|Proteomes:UP000000959};
RX   PubMed=19815525; DOI=10.1073/pnas.0903585106;
RA   Ogura Y., Ooka T., Iguchi A., Toh H., Asadulghani M., Oshima K.,
RA   Kodama T., Abe H., Nakayama K., Kurokawa K., Tobe T., Hattori M.,
RA   Hayashi T.;
RT   "Comparative genomics reveal the mechanism of the parallel evolution
RT   of O157 and non-O157 enterohemorrhagic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:17939-17944(2009).
CC   -!- SIMILARITY: Belongs to the carbamate kinase family.
CC       {ECO:0000256|PIRNR:PIRNR000723}.
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DR   EMBL; AP010958; BAI29360.1; -; Genomic_DNA.
DR   RefSeq; WP_000855356.1; NC_013353.1.
DR   EnsemblBacteria; BAI29360; BAI29360; ECO103_0493.
DR   KEGG; eoh:ECO103_0493; -.
DR   HOGENOM; HOG000277403; -.
DR   KO; K00926; -.
DR   OMA; ESQGFIG; -.
DR   BioCyc; ECOL585395:ECO103_RS02575-MONOMER; -.
DR   Proteomes; UP000000959; Chromosome.
DR   GO; GO:0008804; F:carbamate kinase activity; IEA:InterPro.
DR   GO; GO:0006525; P:arginine metabolic process; IEA:InterPro.
DR   CDD; cd04235; AAK_CK; 1.
DR   Gene3D; 3.40.1160.10; -; 1.
DR   InterPro; IPR036393; AceGlu_kinase-like_sf.
DR   InterPro; IPR001048; Asp/Glu/Uridylate_kinase.
DR   InterPro; IPR003964; Carb_kinase.
DR   PANTHER; PTHR30409; PTHR30409; 1.
DR   Pfam; PF00696; AA_kinase; 1.
DR   PIRSF; PIRSF000723; Carbamate_kin; 1.
DR   SUPFAM; SSF53633; SSF53633; 1.
DR   TIGRFAMs; TIGR00746; arcC; 1.
PE   3: Inferred from homology;
DR   PRODOM; C8U2K2.
DR   SWISS-2DPAGE; C8U2K2.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000959};
KW   Kinase {ECO:0000256|PIRNR:PIRNR000723, ECO:0000313|EMBL:BAI29360.1};
KW   Transferase {ECO:0000256|PIRNR:PIRNR000723}.
FT   DOMAIN        2    277       AA_kinase. {ECO:0000259|Pfam:PF00696}.
SQ   SEQUENCE   297 AA;  31705 MW;  FC4CF8ABA26EA698 CRC64;
     MKTLVVALGG NALLQRGEAL TAENQYRNIA SAVPALARLA RSYRLAIVHG NGPQVGLLAL
     QNLAWKEVDP YPLDVLVAES QGMIGYMLAQ SLSAQPQMPP VTTVLTRIEV SPDDPAFLQP
     EKFIGPVYQP EEQKALEAAY GWQMKRDGKY LRRVVASPQP RKILDSEAIE LLLKEGHVVI
     CSGGGGVPVT EDGAGSEAVI DKDLAAALLA EQINADGLVI LTDADAVYEN WGTPQQRAIR
     HATPDELAPF AKAYGSMGPK VTAVSGYVRS RGKPAWIGAL SRIEETLAGE AGTCISL
//

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