KADH_TRIVA
ID KADH_TRIVA Reviewed; 229 AA.
AC P49983;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Adenylate kinase;
DE Short=AK;
DE EC=2.7.4.3;
DE AltName: Full=ATP-AMP transphosphorylase;
DE AltName: Full=ATP:AMP phosphotransferase;
DE AltName: Full=Adenylate monophosphate kinase;
DE Flags: Precursor;
OS Trichomonas vaginalis.
OC Eukaryota; Metamonada; Parabasalia; Trichomonadida; Trichomonadidae;
OC Trichomonas.
OX NCBI_TaxID=5722;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 10-48, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=ATCC 30001 / NIH-C1;
RX PubMed=7808479; DOI=10.1016/0166-6851(94)90156-2;
RA Laenge S., Rozario C., Mueller M.;
RT "Primary structure of the hydrogenosomal adenylate kinase of Trichomonas
RT vaginalis and its phylogenetic relationships.";
RL Mol. Biochem. Parasitol. 66:297-308(1994).
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.
CC {ECO:0000250|UniProtKB:P69441}.
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:0000250|UniProtKB:P69441};
CC -!- SUBCELLULAR LOCATION: Hydrogenosome {ECO:0000269|PubMed:7808479}.
CC -!- SIMILARITY: Belongs to the adenylate kinase family. {ECO:0000305}.
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DR EMBL; U07203; AAC46483.1; -; Genomic_DNA.
DR AlphaFoldDB; P49983; -.
DR SMR; P49983; -.
DR STRING; 5722.XP_001305871.1; -.
DR PRIDE; P49983; -.
DR VEuPathDB; TrichDB:TVAG_489800; -.
DR eggNOG; KOG3078; Eukaryota.
DR GO; GO:0042566; C:hydrogenosome; IEA:UniProtKB-SubCell.
DR GO; GO:0004017; F:adenylate kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; IPR036193; ADK_active_lid_dom_sf.
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 SUPFAM; SSF57774; SSF57774; 1.
DR TIGRFAMs; TIGR01351; adk; 1.
DR PROSITE; PS00113; ADENYLATE_KINASE; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Direct protein sequencing; Hydrogenosome; Kinase;
KW Nucleotide-binding; Transferase.
FT PROPEP 1..9
FT /evidence="ECO:0000269|PubMed:7808479"
FT /id="PRO_0000016552"
FT CHAIN 10..229
FT /note="Adenylate kinase"
FT /id="PRO_0000016553"
FT REGION 45..74
FT /note="NMP"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT REGION 141..178
FT /note="LID"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 25..30
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 46
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 51
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 72..74
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 100..103
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 107
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 142
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 175
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 186
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 214
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P69441"
SQ SEQUENCE 229 AA; 25550 MW; B9C472398B796985 CRC64;
MLSTLAKRFA SGKKDRMVVF FGPPGVGKGT QAKLLEKEFN LYQISTGDAL RAEIRGQTPL
GKRVKGIIES GGLVDDDTIM DILQACMQKN TDNNGYIFDG IPRTIGQVEK LDALLAKMGT
PLTHVLYLSV NIDELRERVC GRLFHPGSGR VYHKVTNPPK KPMTDDITGE PLIIRKDDTP
EVFNQRMNQY FGTFQPCIDY YSKKGILQTF PVDGQPIDVV HKKLHAALQ
