KADA_PYRFU
ID KADA_PYRFU Reviewed; 196 AA.
AC Q8U020;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Adenylate kinase {ECO:0000255|HAMAP-Rule:MF_00234};
DE Short=AK {ECO:0000255|HAMAP-Rule:MF_00234};
DE EC=2.7.4.3 {ECO:0000255|HAMAP-Rule:MF_00234};
DE AltName: Full=ATP-AMP transphosphorylase {ECO:0000255|HAMAP-Rule:MF_00234};
GN Name=adkA {ECO:0000255|HAMAP-Rule:MF_00234}; OrderedLocusNames=PF1800;
OS Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=186497;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA DiRuggiero J., Robb F.T.;
RT "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT horikoshii inferred from complete genomic sequences.";
RL Genetics 152:1299-1305(1999).
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:0000255|HAMAP-Rule:MF_00234};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00234}.
CC -!- SIMILARITY: Belongs to the archaeal adenylate kinase family.
CC {ECO:0000255|HAMAP-Rule:MF_00234}.
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DR EMBL; AE009950; AAL81924.1; -; Genomic_DNA.
DR RefSeq; WP_011012941.1; NZ_CP023154.1.
DR AlphaFoldDB; Q8U020; -.
DR SMR; Q8U020; -.
DR STRING; 186497.PF1800; -.
DR PRIDE; Q8U020; -.
DR EnsemblBacteria; AAL81924; AAL81924; PF1800.
DR GeneID; 41713619; -.
DR KEGG; pfu:PF1800; -.
DR PATRIC; fig|186497.12.peg.1871; -.
DR eggNOG; arCOG01039; Archaea.
DR HOGENOM; CLU_119371_0_0_2; -.
DR OMA; HRDEMRK; -.
DR OrthoDB; 79684at2157; -.
DR PhylomeDB; Q8U020; -.
DR Proteomes; UP000001013; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004017; F:adenylate kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00234; Adenylate_kinase_AdkA; 1.
DR InterPro; IPR023477; Adenylate_kinase_AdkA.
DR InterPro; IPR027417; P-loop_NTPase.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Reference proteome;
KW Transferase.
FT CHAIN 1..196
FT /note="Adenylate kinase"
FT /id="PRO_0000131822"
FT BINDING 9..17
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00234"
SQ SEQUENCE 196 AA; 22294 MW; 0564D18B65426EE5 CRC64;
MPFVVIITGI PGVGKSTITR LALQRTKAKF RLINFGDLMF EEAVKAGLVK HRDEMRKLPL
KIQRELQMKA AKKITEMAKE HPILVDTHAT IKTPHGYMLG LPYEVVKTLN PNFIVIIEAT
PSEILGRRLR DLKRDRDVET EEQIQRHQDL NRAAAIAYAM HSNALIKIIE NHEDKGLEEA
VNELVKILDL AVNEYA