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Database: UniProt
Entry: A0A161XLQ6_9EURY
LinkDB: A0A161XLQ6_9EURY
Original site: A0A161XLQ6_9EURY 
ID   A0A161XLQ6_9EURY        Unreviewed;       169 AA.
AC   A0A161XLQ6;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 23.
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   ORFNames=A4G99_05750 {ECO:0000313|EMBL:KZN23984.1};
OS   Haladaptatus sp. R4.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Haladaptataceae; Haladaptatus.
OX   NCBI_TaxID=1679489 {ECO:0000313|EMBL:KZN23984.1, ECO:0000313|Proteomes:UP000076599};
RN   [1] {ECO:0000313|EMBL:KZN23984.1, ECO:0000313|Proteomes:UP000076599}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R4 {ECO:0000313|EMBL:KZN23984.1,
RC   ECO:0000313|Proteomes:UP000076599};
RA   Mukhopadhyay S.K.;
RT   "Genome sequence of halophilic archaea.";
RL   Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
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: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KZN23984.1}.
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DR   EMBL; LWHG01000021; KZN23984.1; -; Genomic_DNA.
DR   RefSeq; WP_066142667.1; NZ_LWHG01000021.1.
DR   AlphaFoldDB; A0A161XLQ6; -.
DR   STRING; 1679489.A4G99_05750; -.
DR   OrthoDB; 8730at2157; -.
DR   Proteomes; UP000076599; Unassembled WGS sequence.
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:KZN23984.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00039};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00039}.
FT   REGION          28..51
FT                   /note="NMP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00039"
FT   REGION          98..108
FT                   /note="LID"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00039"
FT   BINDING         10..15
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00039"
FT   BINDING         95
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00039"
FT   BINDING         99
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00039"
SQ   SEQUENCE   169 AA;  18537 MW;  D4D1EC6B018D3A16 CRC64;
     MRVAVTGTPG TGKTTATELV ESDLDVVHLN DAIREEGLHD GEDEERGSLY ANLDAIREWL
     ASRGDDLLVD SHLAHHFDAD RVVVLRCHPE ELSKRLRERG ESDAKAEENA ESEALDVILS
     ETVAEHGPDS TYEIDTTDRT PEAVASDIEA VVRGERAPSA GTVDYLEYL
//
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