(data stored in ACNUC7421 zone)

HOGENOM: THEEB_1_PE100

ID   THEEB_1_PE100                        STANDARD;      PRT;   195 AA.
AC   THEEB_1_PE100; Q8DML4;
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; (THEEB_1.PE100).
GN   Name=adk; OrderedLocusNames=tlr0100;
OS   THERMOSYNECHOCOCCUS ELONGATUS BP-1.
OC   Bacteria; Cyanobacteria; Chroococcales; Thermosynechococcus.
OX   NCBI_TaxID=197221;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS THEEB_1.PE100.
CC       Thermosynechococcus elongatus BP-1, complete genome.
CC       genome.
CC   -!- ANNOTATIONS ORIGIN:KAD_THEEB
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; Q8DML4; -.
DR   EMBL; BA000039; BAC07653.1; -; Genomic_DNA.
DR   RefSeq; NP_680891.1; NC_004113.1.
DR   ProteinModelPortal; Q8DML4; -.
DR   STRING; Q8DML4; -.
DR   GeneID; 1010391; -.
DR   GenomeReviews; BA000039_GR; tlr0100.
DR   KEGG; tel:tlr0100; -.
DR   NMPDR; fig|197221.1.peg.100; -.
DR   eggNOG; COG0563; -.
DR   OMA; VLGRYSC; -.
DR   BioCyc; TELO197221:TLR0100-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; IPR000850; Adenylate_kin.
DR   PANTHER; PTHR23359; Adenylate_kin; 1.
DR   Pfam; PF00406; ADK; 1.
DR   PRINTS; PR00094; ADENYLTKNASE.
DR   PROSITE; PS00113; ADENYLATE_KINASE; 1.
DR   HOGENOMDNA; THEEB_1.PE100; -.
KW   adenylate kinase;
KW   ATP-binding; Complete proteome; Cytoplasm; Kinase;
KW   Nucleotide biosynthesis; Nucleotide-binding; Reference proteome;
KW   Transferase.
SQ   SEQUENCE   195 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MRLILFGGPG SGKGTQAAIL TTLLGIPHIS TGDILRAERA AGTLLGQQAQ SYMDRGELVP
     DQVIVDMVAN RLQQPDTAAG WLLDGFPRNG AQAAVFEEML KSIHQDYDYL LFLDVPAAIL
     QERALNRAKQ AVNGQQRSDD TPETILKRLQ VYERETLPMI QQYMSHPKFV PIDGTRTIEE
     VTAAIQARIG EVNRV
//

If you have problems or comments...

PBIL Back to PBIL home page