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Database: UniProt
Entry: B9LNJ7_HALLT
LinkDB: B9LNJ7_HALLT
Original site: B9LNJ7_HALLT 
ID   B9LNJ7_HALLT            Unreviewed;       180 AA.
AC   B9LNJ7;
DT   24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   24-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 73.
DE   RecName: Full=Putative adenylate kinase {ECO:0000256|HAMAP-Rule:MF_00039};
DE            Short=AK {ECO:0000256|HAMAP-Rule:MF_00039};
DE            EC=2.7.4.3 {ECO:0000256|HAMAP-Rule:MF_00039};
DE   AltName: Full=ATP-AMP transphosphorylase {ECO:0000256|HAMAP-Rule:MF_00039};
GN   OrderedLocusNames=Hlac_1343 {ECO:0000313|EMBL:ACM56935.1};
OS   Halorubrum lacusprofundi (strain ATCC 49239 / DSM 5036 / JCM 8891 / ACAM
OS   34).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Halorubraceae; Halorubrum.
OX   NCBI_TaxID=416348 {ECO:0000313|EMBL:ACM56935.1, ECO:0000313|Proteomes:UP000000740};
RN   [1] {ECO:0000313|EMBL:ACM56935.1, ECO:0000313|Proteomes:UP000000740}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49239 / DSM 5036 / JCM 8891 / ACAM 34
RC   {ECO:0000313|Proteomes:UP000000740};
RX   PubMed=27617060; DOI=10.1186/s40793-016-0194-2;
RA   Anderson I.J., DasSarma P., Lucas S., Copeland A., Lapidus A.,
RA   Del Rio T.G., Tice H., Dalin E., Bruce D.C., Goodwin L., Pitluck S.,
RA   Sims D., Brettin T.S., Detter J.C., Han C.S., Larimer F., Hauser L.,
RA   Land M., Ivanova N., Richardson P., Cavicchioli R., DasSarma S.,
RA   Woese C.R., Kyrpides N.C.;
RT   "Complete genome sequence of the Antarctic Halorubrum lacusprofundi type
RT   strain ACAM 34.";
RL   Stand. Genomic Sci. 11:70-70(2016).
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:0000256|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:0000256|ARBA:ARBA00000582, ECO:0000256|HAMAP-
CC         Rule:MF_00039};
CC   -!- SIMILARITY: Belongs to the adenylate kinase family. AK6 subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_00039}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00039}.
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DR   EMBL; CP001365; ACM56935.1; -; Genomic_DNA.
DR   RefSeq; WP_015910077.1; NC_012029.1.
DR   AlphaFoldDB; B9LNJ7; -.
DR   GeneID; 7399438; -.
DR   KEGG; hla:Hlac_1343; -.
DR   eggNOG; arCOG01038; Archaea.
DR   HOGENOM; CLU_079096_0_1_2; -.
DR   Proteomes; UP000000740; Chromosome 1.
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; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   HAMAP; MF_00039; Adenylate_kinase_AK6; 1.
DR   InterPro; IPR020618; Adenyl_kinase_AK6.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR12595:SF0; ADENYLATE KINASE ISOENZYME 6; 1.
DR   PANTHER; PTHR12595; POS9-ACTIVATING FACTOR FAP7-RELATED; 1.
DR   Pfam; PF13238; AAA_18; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00039};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00039, ECO:0000313|EMBL:ACM56935.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00039};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000740};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00039}.
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          109..119
FT                   /note="LID"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00039"
FT   BINDING         22..27
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00039"
FT   BINDING         106
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00039"
FT   BINDING         110
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00039"
SQ   SEQUENCE   180 AA;  19849 MW;  BDDB561FED409B2F CRC64;
     MSGTERDEAD SPIRVAVTGT PGTGKSTATA LLADEYDVIH LNDRIKGDDD LWTERDADRD
     TLVADLDAVR EHLGDWSGVL DSHLAHRFDV DRVVVLRCHP ETIERRLRER GESDATAEEN
     AESEALDVIL SEAVAEHGMD NVYEIDTTDR DPESVADAIR AAIEGDREPS AGTVDFMDYI
//
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