KADA_PYRHO
ID KADA_PYRHO Reviewed; 196 AA.
AC O59443;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Adenylate kinase;
DE Short=AK;
DE EC=2.7.4.3;
DE AltName: Full=ATP-AMP transphosphorylase;
GN Name=adkA; OrderedLocusNames=PH1753;
OS Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS 100139 / OT-3).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=70601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT "Complete sequence and gene organization of the genome of a hyper-
RT thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL DNA Res. 5:55-76(1998).
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the archaeal adenylate kinase family.
CC {ECO:0000305}.
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DR EMBL; BA000001; BAA30867.1; -; Genomic_DNA.
DR PIR; D71184; D71184.
DR RefSeq; WP_010885817.1; NC_000961.1.
DR AlphaFoldDB; O59443; -.
DR SMR; O59443; -.
DR STRING; 70601.3258184; -.
DR EnsemblBacteria; BAA30867; BAA30867; BAA30867.
DR GeneID; 1442598; -.
DR KEGG; pho:PH1753; -.
DR eggNOG; arCOG01039; Archaea.
DR OMA; HRDEMRK; -.
DR OrthoDB; 79684at2157; -.
DR Proteomes; UP000000752; 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; Transferase.
FT CHAIN 1..196
FT /note="Adenylate kinase"
FT /id="PRO_0000131823"
FT BINDING 9..17
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 196 AA; 22413 MW; 26C834A1BE944D5F CRC64;
MPFVVIITGI PGVGKSTITK LALQRTRAKF KLINFGDLMF EEALKLKLVK HRDEMRKLPL
EVQRELQMNA AKKIAEMAKN YPILLDTHAT IKTPHGYLLG LPYEVIKILN PNFIVIIEAT
PSEILGRRLR DLKRDRDVET EEQIQRHQDL NRAAAITYAM HSNALIKIIE NHEDKGLEEA
VNELVKILDL AVKEYA