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Database: UniProt
Entry: A0A1C8ZRW3_9CREN
LinkDB: A0A1C8ZRW3_9CREN
Original site: A0A1C8ZRW3_9CREN 
ID   A0A1C8ZRW3_9CREN        Unreviewed;       193 AA.
AC   A0A1C8ZRW3;
DT   30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=Adenylate kinase {ECO:0000256|ARBA:ARBA00019926, ECO:0000256|HAMAP-Rule:MF_00234};
DE            Short=AK {ECO:0000256|HAMAP-Rule:MF_00234};
DE            EC=2.7.4.3 {ECO:0000256|ARBA:ARBA00012955, ECO:0000256|HAMAP-Rule:MF_00234};
DE   AltName: Full=ATP-AMP transphosphorylase {ECO:0000256|ARBA:ARBA00033336, ECO:0000256|HAMAP-Rule:MF_00234};
GN   Name=adkA {ECO:0000256|HAMAP-Rule:MF_00234};
GN   ORFNames=BFU36_02585 {ECO:0000313|EMBL:AOL15795.1};
OS   Sulfolobus sp. A20.
OC   Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=1891280 {ECO:0000313|EMBL:AOL15795.1, ECO:0000313|Proteomes:UP000094286};
RN   [1] {ECO:0000313|Proteomes:UP000094286}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A20 {ECO:0000313|Proteomes:UP000094286};
RA   Dai X.;
RT   "Genome sequencing of Sulfolobus sp. A20 from Costa Rica and comparative
RT   analyses of central carbon, nitrogen and sulfur metabolism in various
RT   Sulfolobus strains.";
RL   Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
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_00234};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00234}.
CC   -!- SIMILARITY: Belongs to the archaeal adenylate kinase family.
CC       {ECO:0000256|ARBA:ARBA00007088, ECO:0000256|HAMAP-Rule:MF_00234}.
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DR   EMBL; CP017006; AOL15795.1; -; Genomic_DNA.
DR   RefSeq; WP_069282036.1; NZ_CP017006.1.
DR   AlphaFoldDB; A0A1C8ZRW3; -.
DR   STRING; 1891280.BFU36_02585; -.
DR   GeneID; 28694710; -.
DR   KEGG; sula:BFU36_02585; -.
DR   OrthoDB; 26198at2157; -.
DR   Proteomes; UP000094286; 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; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   HAMAP; MF_00234; Adenylate_kinase_AdkA; 1.
DR   InterPro; IPR023477; Adenylate_kinase_AdkA.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF13207; AAA_17; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00234};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00234};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00234, ECO:0000313|EMBL:AOL15795.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00234};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00234}.
FT   BINDING         8..16
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00234"
SQ   SEQUENCE   193 AA;  21082 MW;  57667938FB8307F2 CRC64;
     MKVGIVTGIP GVGKTTVLSL VDKILIEKEI PHKIVNYGDY MLNTGIKEGY VKSRDEIRKL
     PLDKQKELQT LAAKRINEDL SKINGIGLVD THAVIRTPAG YLPGLPKHVV EVLSPNVIFL
     IEADPKIILE RQKRDSTRSR VDYSDINVIS EVINFARYAA VASAVLVGAS VKVVNNLEGD
     PSVAANEIIS TLM
//
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