(data stored in ACNUC7421 zone)

HOGENOM: ACIAD_1_PE1001

ID   ACIAD_1_PE1001                       STANDARD;      PRT;   219 AA.
AC   ACIAD_1_PE1001; Q6FD71;
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; (ACIAD_1.PE1001).
GN   Name=adk; OrderedLocusNames=ACIAD1105;
OS   ACINETOBACTER SP. ADP1.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Moraxellaceae; Acinetobacter.
OX   NCBI_TaxID=62977;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS ACIAD_1.PE1001.
CC       Acinetobacter sp. ADP1 chromosome, complete genome.
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:KAD_ACIAD
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; Q6FD71; -.
DR   EMBL; CR543861; CAG67988.1; -; Genomic_DNA.
DR   RefSeq; YP_045810.1; NC_005966.1.
DR   ProteinModelPortal; Q6FD71; -.
DR   SMR; Q6FD71; 1-215.
DR   STRING; Q6FD71; -.
DR   GeneID; 2878206; -.
DR   GenomeReviews; CR543861_GR; ACIAD1105.
DR   KEGG; aci:ACIAD1105; -.
DR   NMPDR; fig|62977.3.peg.1303; -.
DR   eggNOG; COG0563; -.
DR   OMA; CANGFLF; -.
DR   PhylomeDB; Q6FD71; -.
DR   ProtClustDB; PRK00279; -.
DR   BioCyc; ASP62977:ACIAD1105-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004017; F:adenylate kinase activity; IEA:EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0009165; P:nucleotide biosynthetic process; IEA:UniProtKB-KW.
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; ACIAD_1.PE1001; -.
KW   ATP-binding; Complete proteome; Cytoplasm; Kinase;
KW   Nucleotide biosynthesis; Nucleotide-binding; Transferase.
SQ   SEQUENCE   219 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MRIILLGPPG AGKGTQAQLI CKRYDIPQIS TGDMLRAAIR EGTELGLKAK SVMESGGLVS
     DELIIGLVKE RIAQPDCENG CIFDGFPRTI PQAEALENAG ITIDHVIEIA VPDEEIVKRL
     SGRRQHPASG RVYHIEYNPP KVEGKDDVTG EELVQRPDDL EETIRKRLGS YHSETEQLVG
     FYQGRAASGE NAPTYNKLDG LRTIDVVQKD LFAILDETK
//

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