KAD_VIBCH
ID KAD_VIBCH Reviewed; 214 AA.
AC Q9KTB7;
DT 04-MAY-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Adenylate kinase {ECO:0000255|HAMAP-Rule:MF_00235};
DE Short=AK {ECO:0000255|HAMAP-Rule:MF_00235};
DE EC=2.7.4.3 {ECO:0000255|HAMAP-Rule:MF_00235};
DE AltName: Full=ATP-AMP transphosphorylase {ECO:0000255|HAMAP-Rule:MF_00235};
DE AltName: Full=ATP:AMP phosphotransferase {ECO:0000255|HAMAP-Rule:MF_00235};
DE AltName: Full=Adenylate monophosphate kinase {ECO:0000255|HAMAP-Rule:MF_00235};
GN Name=adk {ECO:0000255|HAMAP-Rule:MF_00235}; OrderedLocusNames=VC_0986;
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
CC -!- FUNCTION: Catalyzes the reversible transfer of the terminal phosphate
CC group between ATP and AMP. Plays an important role in cellular energy
CC homeostasis and in adenine nucleotide metabolism. {ECO:0000255|HAMAP-
CC Rule:MF_00235}.
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:0000255|HAMAP-Rule:MF_00235};
CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; AMP
CC from ADP: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00235}.
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00235}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00235}.
CC -!- DOMAIN: Consists of three domains, a large central CORE domain and two
CC small peripheral domains, NMPbind and LID, which undergo movements
CC during catalysis. The LID domain closes over the site of phosphoryl
CC transfer upon ATP binding. Assembling and dissambling the active center
CC during each catalytic cycle provides an effective means to prevent ATP
CC hydrolysis. {ECO:0000255|HAMAP-Rule:MF_00235}.
CC -!- SIMILARITY: Belongs to the adenylate kinase family. {ECO:0000255|HAMAP-
CC Rule:MF_00235}.
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DR EMBL; AE003852; AAF94147.1; -; Genomic_DNA.
DR PIR; C82255; C82255.
DR RefSeq; NP_230632.1; NC_002505.1.
DR RefSeq; WP_001220222.1; NZ_LT906614.1.
DR PDB; 4NP6; X-ray; 2.00 A; A/B/C/D=1-214.
DR PDBsum; 4NP6; -.
DR AlphaFoldDB; Q9KTB7; -.
DR SMR; Q9KTB7; -.
DR STRING; 243277.VC_0986; -.
DR DNASU; 2614239; -.
DR EnsemblBacteria; AAF94147; AAF94147; VC_0986.
DR GeneID; 57739673; -.
DR KEGG; vch:VC_0986; -.
DR PATRIC; fig|243277.26.peg.939; -.
DR eggNOG; COG0563; Bacteria.
DR HOGENOM; CLU_032354_1_2_6; -.
DR OMA; FHNRMRV; -.
DR BioCyc; VCHO:VC0986-MON; -.
DR UniPathway; UPA00588; UER00649.
DR Proteomes; UP000000584; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004017; F:adenylate kinase activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004550; F:nucleoside diphosphate kinase activity; IBA:GO_Central.
DR GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway.
DR GO; GO:0009132; P:nucleoside diphosphate metabolic process; IBA:GO_Central.
DR GO; GO:0009123; P:nucleoside monophosphate metabolic process; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd01428; ADK; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00235; Adenylate_kinase_Adk; 1.
DR InterPro; IPR006259; Adenyl_kin_sub.
DR InterPro; IPR000850; Adenylat/UMP-CMP_kin.
DR InterPro; IPR033690; Adenylat_kinase_CS.
DR InterPro; IPR007862; Adenylate_kinase_lid-dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR23359; PTHR23359; 1.
DR Pfam; PF05191; ADK_lid; 1.
DR PRINTS; PR00094; ADENYLTKNASE.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR01351; adk; 1.
DR PROSITE; PS00113; ADENYLATE_KINASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; Kinase; Nucleotide biosynthesis;
KW Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..214
FT /note="Adenylate kinase"
FT /id="PRO_0000158882"
FT REGION 30..59
FT /note="NMP"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235"
FT REGION 122..159
FT /note="LID"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235"
FT BINDING 10..15
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235"
FT BINDING 31
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235"
FT BINDING 36
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235"
FT BINDING 57..59
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235"
FT BINDING 85..88
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235"
FT BINDING 92
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235"
FT BINDING 123
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235"
FT BINDING 132..133
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235"
FT BINDING 156
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235"
FT BINDING 167
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235"
FT BINDING 200
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235"
FT STRAND 1..7
FT /evidence="ECO:0007829|PDB:4NP6"
FT HELIX 14..24
FT /evidence="ECO:0007829|PDB:4NP6"
FT STRAND 28..30
FT /evidence="ECO:0007829|PDB:4NP6"
FT HELIX 31..41
FT /evidence="ECO:0007829|PDB:4NP6"
FT HELIX 44..54
FT /evidence="ECO:0007829|PDB:4NP6"
FT HELIX 61..71
FT /evidence="ECO:0007829|PDB:4NP6"
FT HELIX 75..77
FT /evidence="ECO:0007829|PDB:4NP6"
FT STRAND 80..85
FT /evidence="ECO:0007829|PDB:4NP6"
FT HELIX 90..97
FT /evidence="ECO:0007829|PDB:4NP6"
FT TURN 98..100
FT /evidence="ECO:0007829|PDB:4NP6"
FT STRAND 104..110
FT /evidence="ECO:0007829|PDB:4NP6"
FT HELIX 113..120
FT /evidence="ECO:0007829|PDB:4NP6"
FT STRAND 123..125
FT /evidence="ECO:0007829|PDB:4NP6"
FT TURN 127..129
FT /evidence="ECO:0007829|PDB:4NP6"
FT STRAND 132..134
FT /evidence="ECO:0007829|PDB:4NP6"
FT TURN 135..137
FT /evidence="ECO:0007829|PDB:4NP6"
FT TURN 147..149
FT /evidence="ECO:0007829|PDB:4NP6"
FT HELIX 157..159
FT /evidence="ECO:0007829|PDB:4NP6"
FT HELIX 161..187
FT /evidence="ECO:0007829|PDB:4NP6"
FT STRAND 190..197
FT /evidence="ECO:0007829|PDB:4NP6"
FT HELIX 202..212
FT /evidence="ECO:0007829|PDB:4NP6"
SQ SEQUENCE 214 AA; 23277 MW; D7600C1DC0A3E95B CRC64;
MRIILLGAPG AGKGTQAQFI MEKFGIPQIS TGDMLRAAIK AGTELGKQAK AVIDAGQLVS
DDIILGLIKE RIAQADCEKG FLLDGFPRTI PQADGLKEMG INVDYVIEFD VADDVIVERM
AGRRAHLPSG RTYHVVYNPP KVEGKDDVTG EDLVIREDDK EETVRARLNV YHTQTAPLIE
YYGKEAAAGK TQYLKFDGTK QVSEVSADIA KALA
