ID A0A151MFA9_ALLMI Unreviewed; 911 AA.
AC A0A151MFA9;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=Adenylate kinase isoenzyme 1 {ECO:0000256|HAMAP-Rule:MF_03171};
DE Short=AK 1 {ECO:0000256|HAMAP-Rule:MF_03171};
DE EC=2.7.4.3 {ECO:0000256|HAMAP-Rule:MF_03171};
DE EC=2.7.4.6 {ECO:0000256|HAMAP-Rule:MF_03171};
DE AltName: Full=ATP-AMP transphosphorylase 1 {ECO:0000256|HAMAP-Rule:MF_03171};
DE AltName: Full=ATP:AMP phosphotransferase {ECO:0000256|HAMAP-Rule:MF_03171};
DE AltName: Full=Adenylate monophosphate kinase {ECO:0000256|HAMAP-Rule:MF_03171};
DE AltName: Full=Myokinase {ECO:0000256|HAMAP-Rule:MF_03171};
GN Name=ST6GALNAC6 {ECO:0000313|EMBL:KYO23207.1};
GN Synonyms=AK1 {ECO:0000256|HAMAP-Rule:MF_03171};
GN ORFNames=Y1Q_0005636 {ECO:0000313|EMBL:KYO23207.1};
OS Alligator mississippiensis (American alligator).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC Alligator.
OX NCBI_TaxID=8496 {ECO:0000313|EMBL:KYO23207.1};
RN [1] {ECO:0000313|EMBL:KYO23207.1, ECO:0000313|Proteomes:UP000050525}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KSC_2009_1 {ECO:0000313|EMBL:KYO23207.1};
RX PubMed=22293439; DOI=10.1186/gb-2012-13-1-415;
RA St John J.A., Braun E.L., Isberg S.R., Miles L.G., Chong A.Y., Gongora J.,
RA Dalzell P., Moran C., Bed'hom B., Abzhanov A., Burgess S.C., Cooksey A.M.,
RA Castoe T.A., Crawford N.G., Densmore L.D., Drew J.C., Edwards S.V.,
RA Faircloth B.C., Fujita M.K., Greenwold M.J., Hoffmann F.G., Howard J.M.,
RA Iguchi T., Janes D.E., Khan S.Y., Kohno S., de Koning A.J., Lance S.L.,
RA McCarthy F.M., McCormack J.E., Merchant M.E., Peterson D.G., Pollock D.D.,
RA Pourmand N., Raney B.J., Roessler K.A., Sanford J.R., Sawyer R.H.,
RA Schmidt C.J., Triplett E.W., Tuberville T.D., Venegas-Anaya M.,
RA Howard J.T., Jarvis E.D., Guillette L.J.Jr., Glenn T.C., Green R.E.,
RA Ray D.A.;
RT "Sequencing three crocodilian genomes to illuminate the evolution of
RT archosaurs and amniotes.";
RL Genome Biol. 13:415-415(2012).
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:0000256|HAMAP-
CC Rule:MF_03171}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ADP + thiamine diphosphate = AMP + thiamine triphosphate;
CC Xref=Rhea:RHEA:69180, ChEBI:CHEBI:58937, ChEBI:CHEBI:58938,
CC ChEBI:CHEBI:456215, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000256|ARBA:ARBA00034400};
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:0000256|HAMAP-Rule:MF_03171};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + GDP = ADP + GTP; Xref=Rhea:RHEA:27686,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:37565, ChEBI:CHEBI:58189,
CC ChEBI:CHEBI:456216; EC=2.7.4.6;
CC Evidence={ECO:0000256|ARBA:ARBA00034442};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + UDP = ADP + UTP; Xref=Rhea:RHEA:25098,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:46398, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:456216; EC=2.7.4.6;
CC Evidence={ECO:0000256|ARBA:ARBA00034451};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + dGDP = ADP + dGTP; Xref=Rhea:RHEA:27690,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58595, ChEBI:CHEBI:61429,
CC ChEBI:CHEBI:456216; EC=2.7.4.6;
CC Evidence={ECO:0000256|ARBA:ARBA00034407};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + dTDP = ADP + dTTP; Xref=Rhea:RHEA:27682,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:37568, ChEBI:CHEBI:58369,
CC ChEBI:CHEBI:456216; EC=2.7.4.6;
CC Evidence={ECO:0000256|ARBA:ARBA00034432};
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:0000256|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:0000256|HAMAP-Rule:MF_03171};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-triphosphate + AMP = a ribonucleoside 5'-
CC diphosphate + ADP; Xref=Rhea:RHEA:13749, ChEBI:CHEBI:57930,
CC ChEBI:CHEBI:61557, ChEBI:CHEBI:456215, ChEBI:CHEBI:456216;
CC EC=2.7.4.10; Evidence={ECO:0000256|ARBA:ARBA00034410};
CC -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245, ECO:0000256|HAMAP-
CC Rule:MF_03171}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|HAMAP-Rule:MF_03171}. Membrane
CC {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane protein
CC {ECO:0000256|ARBA:ARBA00004606}.
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:0000256|HAMAP-Rule:MF_03171}.
CC -!- SIMILARITY: Belongs to the adenylate kinase family. AK1 subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_03171}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 29 family.
CC {ECO:0000256|ARBA:ARBA00006003}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KYO23207.1}.
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DR EMBL; AKHW03006215; KYO23207.1; -; Genomic_DNA.
DR eggNOG; KOG3079; Eukaryota.
DR Proteomes; UP000050525; Unassembled WGS sequence.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004017; F:adenylate kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004550; F:nucleoside diphosphate kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0046899; F:nucleoside triphosphate adenylate kinase activity; IEA:RHEA.
DR GO; GO:0008373; F:sialyltransferase activity; IEA:InterPro.
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:0009142; P:nucleoside triphosphate biosynthetic process; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0006486; P:protein glycosylation; IEA:InterPro.
DR CDD; cd01428; ADK; 2.
DR CDD; cd22978; DD_AK5; 1.
DR Gene3D; 3.90.1480.20; Glycosyl transferase family 29; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR HAMAP; MF_00235; Adenylate_kinase_Adk; 2.
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; IPR001675; Glyco_trans_29.
DR InterPro; IPR038578; GT29-like_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR NCBIfam; TIGR01360; aden_kin_iso1; 1.
DR PANTHER; PTHR23359:SF59; ADENYLATE KINASE ISOENZYME 1; 1.
DR PANTHER; PTHR23359; NUCLEOTIDE KINASE; 1.
DR Pfam; PF00406; ADK; 2.
DR Pfam; PF00777; Glyco_transf_29; 1.
DR PRINTS; PR00094; ADENYLTKNASE.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS00113; ADENYLATE_KINASE; 2.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_03171};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_03171};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW ECO:0000313|EMBL:KYO23207.1};
KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_03171};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_03171};
KW Reference proteome {ECO:0000313|Proteomes:UP000050525};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_03171};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 9..27
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 255..309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 634..668
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 742..771
FT /note="NMPbind"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03171"
FT REGION 835..845
FT /note="LID"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03171"
FT BINDING 722..727
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03171"
FT BINDING 743
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03171"
FT BINDING 748
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03171"
FT BINDING 769..771
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03171"
FT BINDING 798..801
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03171"
FT BINDING 805
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03171"
FT BINDING 836
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03171"
FT BINDING 842
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03171"
FT BINDING 853
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03171"
FT BINDING 881
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03171"
SQ SEQUENCE 911 AA; 101452 MW; 8284A619F6A3803E CRC64;
MSNNTGQHTA IFVVLFALVM LLIIYSSNNG NEVFHYASLR SKSHRPPNLK KWGLRNGYLP
VYGNKTLNSH CHQCVIITSS SHLLGSKLGS EINQVLKKPQ EFVNKTPETI FIFWGPPSKM
QRSLLRIIQH VSMSFPNMSA YVVSSGRMKQ FDDLFRGETG KDRQKSRSWL STGWFTMVIA
VELCDKVHVY GMVPPNYCSK RSQPHKMPYH YYEPKGPDEC TIYIHNERSR KGNHHRFITE
KRGERLWYKP SEPGAQRSCD ALKKGHPGLP PPQRLLSRGP RLQDDLRVPG LGGVRPRGAP
GSGPAARPRX XXXREIPQLF QSMLTGLMYS RPEDPISYLE CCLQKVRELG GPEKVQWDTF
LGPEQHCFPS LSGGQGKKPF FQPDPGVGPY HWCLQVPTCG CLPPIQSQFS IESDSDMTES
TGLIQEYDVF DPSRPRPKII FVIGGPGSGK GTQSTKIAAH FGLICISVGE ILRSQMLHHA
TSDRKWELIA QIIANGELAP PETTIEELKQ QFLKQQDARG FVVDGFPREI GQAFTFEEQI
GSPDLVVFLA CSSQRFRQRL EKRALEQGRL DDNPHAIERR VDTFKQNVPL IVKYYQEKGV
VIRFDADREE DDIFADISSV VQAQLYPDGM DKAGSLPWAE LDSPYSASAE GQQEEEEGEE
GQAGHAGQLA GANRPFLLPV SSDSSIPALS LKIFAQVPSG WQQAGKEKLK NHKIIFVVGG
PGSGKGTQCE KIVEKYGYTH LSTGDLLRAE VGSGSERGKK LSAIMEKGEL VPLDTVLDML
RDAMVAKADV SKGFLIDGYP REVKQGEEFE KKIGPPTLLL YVDAGKDTMV KRLLKRGETS
GRADDNEETI KMRLETYYKA TEPVIAFYES RGVVRKLNAE GTVDDVFKQC SLEPGLASTA
SKGQGPEKSL P
//
