(data stored in ACNUC8465 zone)

HOGENOM: UNCTG_1_PE102

ID   UNCTG_1_PE102                        STANDARD;      PRT;   212 AA.
AC   UNCTG_1_PE102; B1GZA3;
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; (UNCTG_1.PE102).
GN   Name=adk; OrderedLocusNames=TGRD_102;
OS   UNCULTURED TERMITE GROUP 1 BACTERIUM PHYLOTYPE RS-D17.
OC   Bacteria; Elusimicrobia; environmental samples.
OX   NCBI_TaxID=471821;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS UNCTG_1.PE102.
CC       Uncultured Termite group 1 bacterium phylotype Rs-D17, complete genome.
CC       1..870428 annotated by Ensembl
CC   -!- ANNOTATIONS ORIGIN:KAD_UNCTG
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; B1GZA3; -.
DR   EMBL; AP009510; BAG13585.1; -; Genomic_DNA.
DR   RefSeq; YP_001956046.1; NS_000191.1.
DR   ProteinModelPortal; B1GZA3; -.
DR   STRING; B1GZA3; -.
DR   GeneID; 6373505; -.
DR   GenomeReviews; AP009510_GR; TGRD_102.
DR   KEGG; rsd:TGRD_102; -.
DR   OMA; HEEFHPP; -.
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   SUPFAM; SSF57774; Adenylate_kinase_Znf_lid; 1.
DR   TIGRFAMs; TIGR01351; Adk; 1.
DR   PROSITE; PS00113; ADENYLATE_KINASE; 1.
DR   HOGENOMDNA; UNCTG_1.PE102; -.
KW   ATP-AMP transphosphorylase;
KW   ATP-binding; Complete proteome; Cytoplasm; Kinase;
KW   Nucleotide biosynthesis; Nucleotide-binding; Transferase.
SQ   SEQUENCE   212 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MNYIILGPPG AGKGTQAKKI AVKFGILHLS TGDMFREAKK SDESISKLLS SGQLVPDEIV
     VNMVRKRLEK NNIKKGFLLD GFPRTVKQTG ELDRMLMSEN IKIDSVFLIS VPFEEAAKRI
     AGRIVCACGA SYHTMLLPPK EFGKCDCCGG VLFHRSDDKE EDIIRDRFSV YEKQTKPLIE
     YYKESGLLIY IDGLKSESDV FEQISGCIIN GE
//

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