(data stored in ACNUC7421 zone)

HOGENOM: DICDC_1_PE1010

ID   DICDC_1_PE1010                       STANDARD;      PRT;   214 AA.
AC   DICDC_1_PE1010; C6CBP4;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Adenylate kinase; Short=AK; EC=2.7.4 3;AltName:
DE   Full=ATP-AMP transphosphorylase; (DICDC_1.PE1010).
GN   Name=adk; OrderedLocusNames=Dd703_1024;
OS   DICKEYA DADANTII ECH703.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Dickeya.
OX   NCBI_TaxID=579405;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS DICDC_1.PE1010.
CC       Dickeya dadantii Ech703, complete genome.
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:C6CBP4_DICDC
CC   -!- FUNCTION: Catalyzes the reversible transfer of the terminal
CC       phosphate group between ATP and AMP. This small ubiquitous enzyme
CC       involved in the energy metabolism and nucleotide synthesis, is
CC       essential for maintenance and cell growth (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + AMP = 2 ADP.
CC   -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway;
CC       AMP from ADP: step 1/1.
CC   -!- SUBUNIT: Monomer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- DOMAIN: Consists of three domains, a large central CORE domain and
CC       two small peripheral domains, AMP binding and LID. The LID domain
CC       closes over the site of phosphoryl transfer upon ATP binding (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the adenylate kinase family.
CC   -!- GENE_FAMILY: HOG000238772 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; C6CBP4; -.
DR   EMBL; CP001654; ACS84829.1; -; Genomic_DNA.
DR   RefSeq; YP_002986651.1; NC_012880.1.
DR   ProteinModelPortal; C6CBP4; -.
DR   STRING; C6CBP4; -.
DR   GeneID; 8088146; -.
DR   GenomeReviews; CP001654_GR; Dd703_1024.
DR   KEGG; dda:Dd703_1024; -.
DR   OMA; CANGFLF; -.
DR   ProtClustDB; CLSK2549338; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004017; F:adenylate kinase activity; IEA:HAMAP.
DR   GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR   GO; GO:0009165; P:nucleotide biosynthetic process; IEA:HAMAP.
DR   HAMAP; MF_00235; Adenylate_kinase_Adk; 1; -.
DR   InterPro; IPR006259; Adenyl_kin_sub.
DR   InterPro; IPR000850; Adenylate_kin.
DR   InterPro; IPR007862; Adenylate_kinase_lid-dom.
DR   PANTHER; PTHR23359; Adenylate_kin; 1.
DR   Pfam; PF00406; ADK; 1.
DR   Pfam; PF05191; ADK_lid; 1.
DR   PRINTS; PR00094; ADENYLTKNASE.
DR   TIGRFAMs; TIGR01351; Adk; 1.
DR   PROSITE; PS00113; ADENYLATE_KINASE; 1.
DR   HOGENOMDNA; DICDC_1.PE1010; -.
KW   adenylate kinase;
KW   ATP-binding; Complete proteome; Cytoplasm; Kinase;
KW   Nucleotide biosynthesis; Nucleotide-binding; Transferase.
SQ   SEQUENCE   214 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MRIILLGAPG AGKGTQAQFI MEKYGIPQIS TGDMLRAAVK AGTELGKQAK EIMDAGKLVT
     DELVIALVKE RIAQDDCRNG FLLDGFPRTI PQADAMKEAG ISVDNVIEFD VPDELIVERI
     IGRRVHAASG RVYHVKFNPP KVEGKDDATG EDLSVRKDDQ EDTVRKRLVE YHQQTAPLVD
     YYQQEAAAGN TRYHKIDGTR AVSDVSAELA RILG
//

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