KADA_SULAC
ID KADA_SULAC Reviewed; 194 AA.
AC P35028; Q4JB64;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 2.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Adenylate kinase;
DE Short=AK;
DE EC=2.7.4.3;
DE AltName: Full=ATP-AMP transphosphorylase;
GN Name=adkA; Synonyms=adk; OrderedLocusNames=Saci_0573;
OS Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC
OS 15157 / NCIMB 11770).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfolobus.
OX NCBI_TaxID=330779;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX PubMed=8274029; DOI=10.1006/abbi.1993.1607;
RA Kath T., Schmid R., Schaefer G.;
RT "Identification, cloning, and expression of the gene for adenylate kinase
RT from the thermoacidophilic archaebacterium Sulfolobus acidocaldarius.";
RL Arch. Biochem. Biophys. 307:405-410(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX PubMed=15995215; DOI=10.1128/jb.187.14.4992-4999.2005;
RA Chen L., Bruegger K., Skovgaard M., Redder P., She Q., Torarinsson E.,
RA Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.;
RT "The genome of Sulfolobus acidocaldarius, a model organism of the
RT Crenarchaeota.";
RL J. Bacteriol. 187:4992-4999(2005).
RN [3]
RP PROTEIN SEQUENCE OF 1-41, AND CHARACTERIZATION.
RC STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX PubMed=8489243; DOI=10.1006/abbi.1993.1229;
RA Lacher K., Schaefer G.;
RT "Archaebacterial adenylate kinase from the thermoacidophile Sulfolobus
RT acidocaldarius: purification, characterization, and partial sequence.";
RL Arch. Biochem. Biophys. 302:391-397(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-9.
RC STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX PubMed=10381320; DOI=10.1006/mpev.1998.0607;
RA Yang D., Kusser I., Koepke A.K., Koop B.F., Matheson A.T.;
RT "The structure and evolution of the ribosomal proteins encoded in the spc
RT operon of the archaeon (Crenarchaeota) Sulfolobus acidocaldarius.";
RL Mol. Phylogenet. Evol. 12:177-185(1999).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-6.
RC STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX PubMed=7495856; DOI=10.1016/0167-4781(95)00165-d;
RA Kath T., Schaefer G.;
RT "A secY homologous gene in the crenarchaeon Sulfolobus acidocaldarius.";
RL Biochim. Biophys. Acta 1264:155-158(1995).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.57 ANGSTROMS).
RX PubMed=9733648; DOI=10.1006/jmbi.1998.2003;
RA Vonrhein C., Boenisch H., Schaefer G., Schulz G.E.;
RT "The structure of a trimeric archaeal adenylate kinase.";
RL J. Mol. Biol. 282:167-179(1998).
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 -!- SUBUNIT: Homotrimer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the archaeal adenylate kinase family.
CC {ECO:0000305}.
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DR EMBL; X73564; CAA51967.1; -; Genomic_DNA.
DR EMBL; CP000077; AAY79965.1; -; Genomic_DNA.
DR EMBL; Y07778; CAA69101.1; -; Genomic_DNA.
DR RefSeq; WP_011277467.1; NC_007181.1.
DR PDB; 1NKS; X-ray; 2.57 A; A/B/C/D/E/F=1-194.
DR PDBsum; 1NKS; -.
DR AlphaFoldDB; P35028; -.
DR SMR; P35028; -.
DR STRING; 330779.Saci_0573; -.
DR EnsemblBacteria; AAY79965; AAY79965; Saci_0573.
DR GeneID; 3473211; -.
DR KEGG; sai:Saci_0573; -.
DR PATRIC; fig|330779.12.peg.552; -.
DR eggNOG; arCOG01039; Archaea.
DR HOGENOM; CLU_119371_0_0_2; -.
DR OMA; HRDEMRK; -.
DR BRENDA; 2.7.4.3; 6160.
DR EvolutionaryTrace; P35028; -.
DR Proteomes; UP000001018; 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; -; 1.
DR HAMAP; MF_00234; Adenylate_kinase_AdkA; 1.
DR InterPro; IPR023477; Adenylate_kinase_AdkA.
DR InterPro; IPR027417; P-loop_NTPase.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; Direct protein sequencing; Kinase;
KW Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..194
FT /note="Adenylate kinase"
FT /id="PRO_0000131825"
FT BINDING 8..16
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT STRAND 2..8
FT /evidence="ECO:0007829|PDB:1NKS"
FT HELIX 14..26
FT /evidence="ECO:0007829|PDB:1NKS"
FT TURN 27..29
FT /evidence="ECO:0007829|PDB:1NKS"
FT STRAND 32..36
FT /evidence="ECO:0007829|PDB:1NKS"
FT HELIX 37..46
FT /evidence="ECO:0007829|PDB:1NKS"
FT TURN 47..49
FT /evidence="ECO:0007829|PDB:1NKS"
FT HELIX 54..57
FT /evidence="ECO:0007829|PDB:1NKS"
FT HELIX 62..82
FT /evidence="ECO:0007829|PDB:1NKS"
FT STRAND 85..92
FT /evidence="ECO:0007829|PDB:1NKS"
FT STRAND 94..98
FT /evidence="ECO:0007829|PDB:1NKS"
FT STRAND 101..106
FT /evidence="ECO:0007829|PDB:1NKS"
FT HELIX 108..114
FT /evidence="ECO:0007829|PDB:1NKS"
FT STRAND 117..123
FT /evidence="ECO:0007829|PDB:1NKS"
FT HELIX 126..135
FT /evidence="ECO:0007829|PDB:1NKS"
FT TURN 137..139
FT /evidence="ECO:0007829|PDB:1NKS"
FT HELIX 147..168
FT /evidence="ECO:0007829|PDB:1NKS"
FT STRAND 171..176
FT /evidence="ECO:0007829|PDB:1NKS"
FT HELIX 183..193
FT /evidence="ECO:0007829|PDB:1NKS"
SQ SEQUENCE 194 AA; 21110 MW; C0AA552D8E541900 CRC64;
MKIGIVTGIP GVGKSTVLAK VKEILDNQGI NNKIINYGDF MLATALKLGY AKDRDEMRKL
SVEKQKKLQI DAAKGIAEEA RAGGEGYLFI DTHAVIRTPS GYLPGLPSYV ITEINPSVIF
LLEADPKIIL SRQKRDTTRN RNDYSDESVI LETINFARYA ATASAVLAGS TVKVIVNVEG
DPSIAANEII RSMK
