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KAD1_BOVIN
ID   KAD1_BOVIN              Reviewed;         194 AA.
AC   P00570; Q5E9G9;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   27-JUN-2006, sequence version 2.
DT   03-AUG-2022, entry version 143.
DE   RecName: Full=Adenylate kinase isoenzyme 1 {ECO:0000255|HAMAP-Rule:MF_03171};
DE            Short=AK 1 {ECO:0000255|HAMAP-Rule:MF_03171};
DE            EC=2.7.4.3 {ECO:0000255|HAMAP-Rule:MF_03171};
DE            EC=2.7.4.6 {ECO:0000255|HAMAP-Rule:MF_03171};
DE   AltName: Full=ATP-AMP transphosphorylase 1 {ECO:0000255|HAMAP-Rule:MF_03171};
DE   AltName: Full=ATP:AMP phosphotransferase {ECO:0000255|HAMAP-Rule:MF_03171};
DE   AltName: Full=Adenylate monophosphate kinase {ECO:0000255|HAMAP-Rule:MF_03171};
DE   AltName: Full=Myokinase {ECO:0000255|HAMAP-Rule:MF_03171};
GN   Name=AK1 {ECO:0000255|HAMAP-Rule:MF_03171};
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=6089869; DOI=10.1021/bi00306a012;
RA   Kuby S.A., Palmieri R.H., Frischat A., Fischer A.H., Wu L.H., Maland L.,
RA   Manship M.;
RT   "Studies on adenosine triphosphate transphosphorylases. Amino acid sequence
RT   of rabbit muscle ATP-AMP transphosphorylase.";
RL   Biochemistry 23:2393-2399(1984).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Thymus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the reversible transfer of the terminal phosphate
CC       group between ATP and AMP. Also displays broad nucleoside diphosphate
CC       kinase activity. Plays an important role in cellular energy homeostasis
CC       and in adenine nucleotide metabolism. {ECO:0000255|HAMAP-
CC       Rule:MF_03171}.
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_03171};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2'-deoxyribonucleoside 5'-diphosphate + ATP = a 2'-
CC         deoxyribonucleoside 5'-triphosphate + ADP; Xref=Rhea:RHEA:44640,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61560, ChEBI:CHEBI:73316,
CC         ChEBI:CHEBI:456216; EC=2.7.4.6; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_03171};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ribonucleoside 5'-diphosphate + ATP = a ribonucleoside 5'-
CC         triphosphate + ADP; Xref=Rhea:RHEA:18113, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:57930, ChEBI:CHEBI:61557, ChEBI:CHEBI:456216; EC=2.7.4.6;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_03171};
CC   -!- SUBUNIT: Monomer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
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_03171}.
CC   -!- SIMILARITY: Belongs to the adenylate kinase family. AK1 subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_03171}.
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DR   EMBL; BT020951; AAX08968.1; -; mRNA.
DR   EMBL; BC114796; AAI14797.1; -; mRNA.
DR   PIR; A00681; KIBOA.
DR   RefSeq; NP_001013600.1; NM_001013582.1.
DR   RefSeq; XP_005213229.1; XM_005213172.1.
DR   AlphaFoldDB; P00570; -.
DR   BMRB; P00570; -.
DR   SMR; P00570; -.
DR   STRING; 9913.ENSBTAP00000050234; -.
DR   PaxDb; P00570; -.
DR   PeptideAtlas; P00570; -.
DR   PRIDE; P00570; -.
DR   Ensembl; ENSBTAT00000054038; ENSBTAP00000050234; ENSBTAG00000006305.
DR   Ensembl; ENSBTAT00000085834; ENSBTAP00000068153; ENSBTAG00000006305.
DR   GeneID; 280715; -.
DR   KEGG; bta:280715; -.
DR   CTD; 203; -.
DR   VEuPathDB; HostDB:ENSBTAG00000006305; -.
DR   VGNC; VGNC:25770; AK1.
DR   eggNOG; KOG3079; Eukaryota.
DR   GeneTree; ENSGT00940000158325; -.
DR   HOGENOM; CLU_032354_0_3_1; -.
DR   InParanoid; P00570; -.
DR   OMA; TQCDRMI; -.
DR   OrthoDB; 1378291at2759; -.
DR   TreeFam; TF354283; -.
DR   BRENDA; 2.7.4.3; 908.
DR   Proteomes; UP000009136; Chromosome 11.
DR   Bgee; ENSBTAG00000006305; Expressed in longissimus thoracis muscle and 104 other tissues.
DR   ExpressionAtlas; P00570; baseline and differential.
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-KW.
DR   GO; GO:0004550; F:nucleoside diphosphate kinase activity; ISS:UniProtKB.
DR   GO; GO:0006172; P:ADP biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0046033; P:AMP metabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0046034; P:ATP metabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006165; P:nucleoside diphosphate phosphorylation; ISS:UniProtKB.
DR   GO; GO:0009142; P:nucleoside triphosphate biosynthetic process; ISS:UniProtKB.
DR   CDD; cd01428; ADK; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_00235; Adenylate_kinase_Adk; 1.
DR   HAMAP; MF_03171; Adenylate_kinase_AK1; 1.
DR   InterPro; IPR000850; Adenylat/UMP-CMP_kin.
DR   InterPro; IPR033690; Adenylat_kinase_CS.
DR   InterPro; IPR028582; AK1.
DR   InterPro; IPR006267; AK1/5.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR23359; PTHR23359; 1.
DR   PRINTS; PR00094; ADENYLTKNASE.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR01360; aden_kin_iso1; 1.
DR   PROSITE; PS00113; ADENYLATE_KINASE; 1.
PE   1: Evidence at protein level;
KW   Acetylation; ATP-binding; Cytoplasm; Direct protein sequencing; Kinase;
KW   Nucleotide-binding; Phosphoprotein; Reference proteome; Transferase.
FT   CHAIN           1..194
FT                   /note="Adenylate kinase isoenzyme 1"
FT                   /id="PRO_0000158909"
FT   REGION          38..67
FT                   /note="NMP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03171"
FT   REGION          131..141
FT                   /note="LID"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03171"
FT   BINDING         18..23
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03171"
FT   BINDING         39
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03171"
FT   BINDING         44
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03171"
FT   BINDING         65..67
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03171"
FT   BINDING         94..97
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03171"
FT   BINDING         101
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03171"
FT   BINDING         132
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03171"
FT   BINDING         138
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03171"
FT   BINDING         149
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03171"
FT   BINDING         177
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03171"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:P00568"
FT   MOD_RES         38
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P00568"
FT   CONFLICT        8
FT                   /note="T -> A (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        85
FT                   /note="D -> N (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        98
FT                   /note="E -> Q (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        126
FT                   /note="T -> Q (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   194 AA;  21664 MW;  8F6EA93FBE3D3798 CRC64;
     MEEKLKKTKI IFVVGGPGSG KGTQCEKIVQ KYGYTHLSTG DLLRAEVSSG SARGKMLSEI
     MEKGQLVPLE TVLDMLRDAM VAKVDTSKGF LIDGYPREVQ QGEEFERRIA QPTLLLYVDA
     GPETMTKRLL KRGETSGRVD DNEETIKKRL ETYYKATEPV IAFYEKRGIV RKVNAEGSVD
     NVFSQVCTHL DALK
 
 
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