KADA_AERPE
ID KADA_AERPE Reviewed; 202 AA.
AC Q9YDD2;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2007, sequence version 2.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Adenylate kinase;
DE Short=AK;
DE EC=2.7.4.3;
DE AltName: Full=ATP-AMP transphosphorylase;
GN Name=adkA; OrderedLocusNames=APE_0981.1;
OS Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 /
OS K1).
OC Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC Desulfurococcaceae; Aeropyrum.
OX NCBI_TaxID=272557;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1;
RX PubMed=10382966; DOI=10.1093/dnares/6.2.83;
RA Kawarabayasi Y., Hino Y., Horikawa H., Yamazaki S., Haikawa Y., Jin-no K.,
RA Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A.,
RA Fukui S., Nagai Y., Nishijima K., Nakazawa H., Takamiya M., Masuda S.,
RA Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A.,
RA Aoki K., Kubota K., Nakamura Y., Nomura N., Sako Y., Kikuchi H.;
RT "Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon,
RT Aeropyrum pernix K1.";
RL DNA Res. 6:83-101(1999).
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the archaeal adenylate kinase family.
CC {ECO:0000305}.
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DR EMBL; BA000002; BAA79965.2; -; Genomic_DNA.
DR PIR; E72695; E72695.
DR PDB; 6LN3; X-ray; 2.00 A; A=1-202.
DR PDBsum; 6LN3; -.
DR AlphaFoldDB; Q9YDD2; -.
DR SMR; Q9YDD2; -.
DR STRING; 272557.APE_0981.1; -.
DR EnsemblBacteria; BAA79965; BAA79965; APE_0981.1.
DR KEGG; ape:APE_0981.1; -.
DR eggNOG; arCOG01039; Archaea.
DR Proteomes; UP000002518; 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; IPR003593; AAA+_ATPase.
DR InterPro; IPR023477; Adenylate_kinase_AdkA.
DR InterPro; IPR027417; P-loop_NTPase.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; Kinase; Nucleotide-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..202
FT /note="Adenylate kinase"
FT /id="PRO_0000131812"
FT BINDING 12..20
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT STRAND 4..11
FT /evidence="ECO:0007829|PDB:6LN3"
FT HELIX 18..31
FT /evidence="ECO:0007829|PDB:6LN3"
FT STRAND 35..40
FT /evidence="ECO:0007829|PDB:6LN3"
FT HELIX 41..51
FT /evidence="ECO:0007829|PDB:6LN3"
FT HELIX 58..63
FT /evidence="ECO:0007829|PDB:6LN3"
FT HELIX 66..87
FT /evidence="ECO:0007829|PDB:6LN3"
FT STRAND 92..97
FT /evidence="ECO:0007829|PDB:6LN3"
FT STRAND 100..104
FT /evidence="ECO:0007829|PDB:6LN3"
FT STRAND 107..112
FT /evidence="ECO:0007829|PDB:6LN3"
FT HELIX 114..120
FT /evidence="ECO:0007829|PDB:6LN3"
FT STRAND 123..129
FT /evidence="ECO:0007829|PDB:6LN3"
FT HELIX 132..141
FT /evidence="ECO:0007829|PDB:6LN3"
FT HELIX 148..150
FT /evidence="ECO:0007829|PDB:6LN3"
FT HELIX 152..171
FT /evidence="ECO:0007829|PDB:6LN3"
FT TURN 172..175
FT /evidence="ECO:0007829|PDB:6LN3"
FT STRAND 177..182
FT /evidence="ECO:0007829|PDB:6LN3"
FT HELIX 188..199
FT /evidence="ECO:0007829|PDB:6LN3"
SQ SEQUENCE 202 AA; 21948 MW; 41E55846683A0891 CRC64;
MRHPFKVVVV TGVPGVGKTT VIKELQGLAE KEGVKLHIVN FGSFMLDTAV KLGLVEDRDK
IRTLPLRRQL ELQREAAKRI VAEASKALGG DGVLIIDTHA LVKTVAGYWP GLPKHVLDEL
KPDMIAVVEA SPEEVAARQA RDTTRYRVDI GGVEGVKRLM ENARAASIAS AIQYASTVAI
VENREGEAAK AAEELLRLIK NL