KAD6_NATPD
ID KAD6_NATPD Reviewed; 168 AA.
AC Q3IRT0;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 82.
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 Name=adk2 {ECO:0000312|EMBL:CAI49162.1}; OrderedLocusNames=NP_2142A;
OS Natronomonas pharaonis (strain ATCC 35678 / DSM 2160 / CIP 103997 / JCM
OS 8858 / NBRC 14720 / NCIMB 2260 / Gabara) (Halobacterium pharaonis).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Natronomonas.
OX NCBI_TaxID=348780;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 / NCIMB
RC 2260 / Gabara;
RX PubMed=16169924; DOI=10.1101/gr.3952905;
RA Falb M., Pfeiffer F., Palm P., Rodewald K., Hickmann V., Tittor J.,
RA Oesterhelt D.;
RT "Living with two extremes: conclusions from the genome sequence of
RT Natronomonas pharaonis.";
RL Genome Res. 15:1336-1343(2005).
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; CR936257; CAI49162.1; -; Genomic_DNA.
DR RefSeq; WP_011322790.1; NC_007426.1.
DR AlphaFoldDB; Q3IRT0; -.
DR SMR; Q3IRT0; -.
DR STRING; 348780.NP_2142A; -.
DR EnsemblBacteria; CAI49162; CAI49162; NP_2142A.
DR GeneID; 3701362; -.
DR KEGG; nph:NP_2142A; -.
DR eggNOG; arCOG01038; Archaea.
DR HOGENOM; CLU_079096_0_1_2; -.
DR OMA; QCEIFGT; -.
DR OrthoDB; 110798at2157; -.
DR Proteomes; UP000002698; 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; Reference proteome; Transferase.
FT CHAIN 1..168
FT /note="Putative adenylate kinase"
FT /id="PRO_1000003093"
FT REGION 28..51
FT /note="NMP"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00039"
FT REGION 97..107
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 94
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00039"
FT BINDING 98
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00039"
SQ SEQUENCE 168 AA; 17825 MW; 2E2D717A9409E976 CRC64;
MRVAVTGTPG TGKTTATEAV ETALDVIHLN ERIREEGLDA GRDEERDSLV ADLDAVEAAL
AGEDDALIES HLAHHVDADR VVVLRCRPDI LQERLVDRGE PAAKAAENAE AEALDVVLSE
AVAEHGRESV YEIDTTEASP SAVAEAIEAV IDGERAPAVG TVDFTEHL
