ID A0A3B4G5U0_9CICH Unreviewed; 449 AA.
AC A0A3B4G5U0;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Adenylate kinase 8 {ECO:0000256|ARBA:ARBA00029501};
DE EC=2.7.4.3 {ECO:0000256|ARBA:ARBA00012955};
DE EC=2.7.4.6 {ECO:0000256|ARBA:ARBA00012966};
DE AltName: Full=ATP-AMP transphosphorylase 8 {ECO:0000256|ARBA:ARBA00042874};
OS Pundamilia nyererei.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Pundamilia.
OX NCBI_TaxID=303518 {ECO:0000313|Ensembl:ENSPNYP00000018245.1, ECO:0000313|Proteomes:UP000261460};
RN [1] {ECO:0000313|Ensembl:ENSPNYP00000018245.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: Nucleoside monophosphate (NMP) kinase that catalyzes the
CC reversible transfer of the terminal phosphate group between nucleoside
CC triphosphates and monophosphates. Has highest activity toward AMP, and
CC weaker activity toward dAMP, CMP and dCMP. Also displays broad
CC nucleoside diphosphate kinase activity.
CC {ECO:0000256|ARBA:ARBA00037483}.
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|ARBA:ARBA00000582};
CC -!- SIMILARITY: Belongs to the adenylate kinase family.
CC {ECO:0000256|RuleBase:RU003330}.
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DR AlphaFoldDB; A0A3B4G5U0; -.
DR STRING; 303518.ENSPNYP00000018245; -.
DR Ensembl; ENSPNYT00000018698.1; ENSPNYP00000018245.1; ENSPNYG00000013764.1.
DR GeneTree; ENSGT00940000164784; -.
DR Proteomes; UP000261460; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:0006139; P:nucleobase-containing compound metabolic process; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd01428; ADK; 1.
DR CDD; cd22979; DD_AK8; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR HAMAP; MF_00235; Adenylate_kinase_Adk; 1.
DR InterPro; IPR000850; Adenylat/UMP-CMP_kin.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR23359:SF81; ADENYLATE KINASE 8; 1.
DR PANTHER; PTHR23359; NUCLEOTIDE KINASE; 1.
DR Pfam; PF00406; ADK; 1.
DR PRINTS; PR00094; ADENYLTKNASE.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
PE 3: Inferred from homology;
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU003330};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003330};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 97..119
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 376..406
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 449 AA; 50355 MW; D94FE44BB4078BF0 CRC64;
MDETVRPLRI PPQAFVYADK HNVAQLVQVK VQLLVIDQPV DPISYLIGLL QRSSDDGEVA
VVSLMAFISW DHADLWTSTH THTHTHTHTH SLTSVRVCVC VCVCVCVCVC VCVLLQGWVL
EGIPQTRLQA LSLQQGGVIP EHVVMLEAAD DVLMERSCGR LVDAITGDIY HRTFILPDDD
IITQRLEKGR SLTDQQRLAK PHRYCCEVTG LRSAYQHVLK VIDSDQPHAD IYQQVLAFVR
TRQRSRTPRI LLLGPPGSGR SRQAQLLSEK YGMVDVSCGR LLRSVAAAGS SRGAEVQAYL
DDRRPVSDSL LLQVLEERLN RPDCTRGGWI LHGFPCDLQQ ARSLQESHQQ PNRVFFLELT
DDVCLERLSL RATDPVSGQS FHPVTRPAPS SEVQHRLKTR PEDSMESVTQ RLKQYRLHSA
SVYPEAIHIN ADQDPHSVFE AVASRLTSE
//
