KAD6_PYRHO
ID KAD6_PYRHO Reviewed; 180 AA.
AC O58998;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Putative adenylate kinase {ECO:0000255|HAMAP-Rule:MF_00039};
DE Short=AK {ECO:0000255|HAMAP-Rule:MF_00039};
DE EC=2.7.4.3 {ECO:0000255|HAMAP-Rule:MF_00039};
DE AltName: Full=ATP-AMP transphosphorylase {ECO:0000255|HAMAP-Rule:MF_00039};
GN OrderedLocusNames=PH1255;
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 -!- FUNCTION: Broad-specificity nucleoside monophosphate (NMP) kinase that
CC catalyzes the reversible transfer of the terminal phosphate group
CC between nucleoside triphosphates and monophosphates.
CC {ECO:0000255|HAMAP-Rule:MF_00039}.
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_00039};
CC -!- SIMILARITY: Belongs to the adenylate kinase family. AK6 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00039}.
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DR EMBL; BA000001; BAA30356.1; -; Genomic_DNA.
DR PIR; B71070; B71070.
DR RefSeq; WP_010885344.1; NC_000961.1.
DR AlphaFoldDB; O58998; -.
DR BMRB; O58998; -.
DR SMR; O58998; -.
DR STRING; 70601.3257673; -.
DR EnsemblBacteria; BAA30356; BAA30356; BAA30356.
DR GeneID; 1443579; -.
DR KEGG; pho:PH1255; -.
DR eggNOG; arCOG01038; Archaea.
DR OMA; QCEIFGT; -.
DR OrthoDB; 110798at2157; -.
DR Proteomes; UP000000752; Chromosome.
DR GO; GO:0004017; F:adenylate kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00039; Adenylate_kinase_AK6; 1.
DR InterPro; IPR020618; Adenyl_kinase_AK6.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR12595; PTHR12595; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 3: Inferred from homology;
KW ATP-binding; Kinase; Nucleotide-binding; Transferase.
FT CHAIN 1..180
FT /note="Putative adenylate kinase"
FT /id="PRO_0000153913"
FT REGION 30..50
FT /note="NMP"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00039"
FT REGION 99..109
FT /note="LID"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00039"
FT BINDING 10..15
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00039"
FT BINDING 96
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00039"
FT BINDING 100
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00039"
SQ SEQUENCE 180 AA; 20178 MW; A82E4C0E9D7C3067 CRC64;
MLIAITGTPG VGKTTVAKLL AKKLNYEYVS LKDFALEKGC GRRVNDEVEV EIDELAYFIE
RELKGKNAVL DGHLSHLMPV DLVVVLRAHP KLIGERLRER GYDREKIGEN VEAELVDAVL
IEAIEEHENV IEVDTTNKSP EDVVEEIVSL INSGIKKRVG IVDWSEVYDE IIPYLRLGGE
