ID A7XUY8_9BACI Unreviewed; 149 AA.
AC A7XUY8;
DT 23-OCT-2007, integrated into UniProtKB/TrEMBL.
DT 23-OCT-2007, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=Adenylate kinase {ECO:0000256|RuleBase:RU003331};
DE EC=2.7.4.3 {ECO:0000256|RuleBase:RU003331};
DE Flags: Fragment;
GN Name=adk {ECO:0000313|EMBL:ABU52798.1};
OS Bacillus sp. AH624.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=460960 {ECO:0000313|EMBL:ABU52798.1};
RN [1] {ECO:0000313|EMBL:ABU52798.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=AH624 {ECO:0000313|EMBL:ABU52798.1};
RX PubMed=17997177; DOI=10.1016/j.mimet.2007.10.001;
RA Olsen J.S., Skogan G., Fykse E.M., Rawlinson E.L., Tomaso H., Granum P.E.,
RA Blatny J.M.;
RT "Genetic distribution of 295 Bacillus cereus group members based on adk-
RT screening in combination with MLST (Multilocus Sequence Typing) used for
RT validating a primer targeting a chromosomal locus in B. anthracis.";
RL J. Microbiol. Methods 71:265-274(2007).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=AMP + ATP = 2 ADP; Xref=Rhea:RHEA:12973, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:456215, ChEBI:CHEBI:456216; EC=2.7.4.3;
CC Evidence={ECO:0000256|ARBA:ARBA00000582,
CC ECO:0000256|RuleBase:RU003331};
CC -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245,
CC ECO:0000256|RuleBase:RU003331}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|RuleBase:RU003331}.
CC -!- SIMILARITY: Belongs to the adenylate kinase family.
CC {ECO:0000256|ARBA:ARBA00007220, ECO:0000256|RuleBase:RU003330}.
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DR EMBL; EF553926; ABU52798.1; -; Genomic_DNA.
DR AlphaFoldDB; A7XUY8; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004017; F:adenylate kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd01428; ADK; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR HAMAP; MF_00235; Adenylate_kinase_Adk; 1.
DR InterPro; IPR006259; Adenyl_kin_sub.
DR InterPro; IPR000850; Adenylat/UMP-CMP_kin.
DR InterPro; IPR033690; Adenylat_kinase_CS.
DR InterPro; IPR007862; Adenylate_kinase_lid-dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR NCBIfam; TIGR01351; adk; 1.
DR PANTHER; PTHR23359; NUCLEOTIDE KINASE; 1.
DR PANTHER; PTHR23359:SF206; UMP-CMP KINASE; 1.
DR Pfam; PF00406; ADK; 1.
DR Pfam; PF05191; ADK_lid; 1.
DR PRINTS; PR00094; ADENYLTKNASE.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00113; ADENYLATE_KINASE; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU003331};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU003330};
KW Nucleotide biosynthesis {ECO:0000256|ARBA:ARBA00022727};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU003331};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003330}.
FT DOMAIN 78..113
FT /note="Adenylate kinase active site lid"
FT /evidence="ECO:0000259|Pfam:PF05191"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ABU52798.1"
FT NON_TER 149
FT /evidence="ECO:0000313|EMBL:ABU52798.1"
SQ SEQUENCE 149 AA; 16684 MW; 95831ACE019F32A6 CRC64;
KSFIDKGALV PDEVTIGIVR ERLSQEDCIK GFLLDGFPRT VAQASALEEI MKDLGKKIDY
VLNINVDSGL LLKRLTGRRI CKECGATYHL EFNPPAKADV CDKCGGELYQ RSDDNEETVA
NRLDVNIKQT KPLLDFYEEL GYLQSINGE
//
