(data stored in ACNUC7421 zone)

HOGENOM: BACFN_1_PE1051

ID   BACFN_1_PE1051                       STANDARD;      PRT;   635 AA.
AC   BACFN_1_PE1051; Q64XA6;
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; (BACFN_1.PE1051).
GN   Name=adk; OrderedLocusNames=BF1120;
OS   BACTEROIDES FRAGILIS NCTC 9343.
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=272559;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS BACFN_1.PE1051.
CC       Bacteroides fragilis NCTC 9343 chromosome, complete genome.
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:KAD_BACFR
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: HOG000253523 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; Q64XA6; -.
DR   EMBL; AP006841; BAD47870.1; -; Genomic_DNA.
DR   RefSeq; YP_098404.1; NC_006347.1.
DR   ProteinModelPortal; Q64XA6; -.
DR   GeneID; 3081739; -.
DR   GenomeReviews; AP006841_GR; BF1120.
DR   KEGG; bfr:BF1120; -.
DR   OMA; PAVEGIC; -.
DR   ProtClustDB; PRK00279; -.
DR   BioCyc; BFRA295405:BF1120-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; BACFN_1.PE1051; -.
KW   ATP-binding; Complete proteome; Cytoplasm; Kinase;
KW   Nucleotide biosynthesis; Nucleotide-binding; Transferase.
SQ   SEQUENCE   635 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MTDILKHLDL NSADGTQLNL DALYQIAPSA FTEVRDDKTG AISRKVNFEV FRQLLGDHAT
     DGEGEMYQFT WVGKNAARAE AAKPTDKTLR PVVEDSMDWD NTKNIYIEGD NLEVLKLLQR
     SYMGKVKMIY IDPPYNTGND FVYHDDFART AAEEDLEAGS VDELGNRFRK NTDTNGKFHS
     DWCSMIYSRL LVARSLLTED GVIFISIDDN EQRNLKNICD EVFGSSNFLA QIVWERAYSP
     INLMKHFSPS HDYVLCYAKN LDSAVCKGIA RSSEADNRYT NPDNDPRGVW KASDLSVGPA
     VEENIYTITT PSGRNVEPPA GRSWRLSRKA FRERLQDNRI WFGPDGNSVP AMKRFLSELR
     KTGITPMTIW KYTEVDHSQG ATQKLAKLFD GKKVFDYPKP VELIKRIISL YSDSNSIILD
     FFSGSATTAH AVMEQNALDG GCRQFIMVQL EEDFSESSDG YKMGFKTICD AAKERIRRAG
     AKIKADSPLT TQNIDTGFRV FRLDESNYEE VSISPNDYQQ DQLNLFADNI KQDRTDLDLL
     FGAMLAWGVT LDLPMTQEEV DGCTIYTVND GDLVACFTER ITDNVVAAMA DKTPLRVLFR
     DSCFAQDDQK INIYEQFKQL MDWTDDEAFK NIKVI
//

If you have problems or comments...

PBIL Back to PBIL home page