ID A0A0E3S3H4_9EURY Unreviewed; 186 AA.
AC A0A0E3S3H4;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=Putative adenylate kinase {ECO:0000256|HAMAP-Rule:MF_00039};
DE Short=AK {ECO:0000256|HAMAP-Rule:MF_00039};
DE EC=2.7.4.3 {ECO:0000256|HAMAP-Rule:MF_00039};
DE AltName: Full=ATP-AMP transphosphorylase {ECO:0000256|HAMAP-Rule:MF_00039};
GN ORFNames=MSLAZ_2238 {ECO:0000313|EMBL:AKB75499.1};
OS Methanosarcina lacustris Z-7289.
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=1434111 {ECO:0000313|EMBL:AKB75499.1, ECO:0000313|Proteomes:UP000033072};
RN [1] {ECO:0000313|EMBL:AKB75499.1, ECO:0000313|Proteomes:UP000033072}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Z-7289 {ECO:0000313|EMBL:AKB75499.1,
RC ECO:0000313|Proteomes:UP000033072};
RA Henriksen J.R., Luke J., Reinhart S., Benedict M.N., Youngblut N.D.,
RA Metcalf M.E., Whitaker R.J., Metcalf W.W.;
RT "Methanogenic archaea and the global carbon cycle.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Broad-specificity nucleoside monophosphate (NMP) kinase that
CC catalyzes the reversible transfer of the terminal phosphate group
CC between nucleoside triphosphates and monophosphates.
CC {ECO:0000256|HAMAP-Rule:MF_00039}.
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, ECO:0000256|HAMAP-
CC Rule:MF_00039};
CC -!- SIMILARITY: Belongs to the adenylate kinase family. AK6 subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_00039}.
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DR EMBL; CP009515; AKB75499.1; -; Genomic_DNA.
DR RefSeq; WP_048127053.1; NZ_CP009515.1.
DR AlphaFoldDB; A0A0E3S3H4; -.
DR STRING; 1434111.MSLAZ_2238; -.
DR GeneID; 24807056; -.
DR KEGG; mls:MSLAZ_2238; -.
DR PATRIC; fig|1434111.4.peg.2981; -.
DR HOGENOM; CLU_079096_0_1_2; -.
DR OrthoDB; 8730at2157; -.
DR Proteomes; UP000033072; Chromosome.
DR GO; GO:0004017; F:adenylate kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR HAMAP; MF_00039; Adenylate_kinase_AK6; 1.
DR InterPro; IPR020618; Adenyl_kinase_AK6.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR12595:SF0; ADENYLATE KINASE ISOENZYME 6; 1.
DR PANTHER; PTHR12595; POS9-ACTIVATING FACTOR FAP7-RELATED; 1.
DR Pfam; PF13238; AAA_18; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00039};
KW Kinase {ECO:0000256|HAMAP-Rule:MF_00039, ECO:0000313|EMBL:AKB75499.1};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00039};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00039}.
FT REGION 30..53
FT /note="NMP"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00039"
FT REGION 108..118
FT /note="LID"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00039"
FT BINDING 10..15
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00039"
FT BINDING 105
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00039"
FT BINDING 109
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00039"
SQ SEQUENCE 186 AA; 21299 MW; 4E0BBF42F5CAFADB CRC64;
MLIGLTGTPG TGKTSVSKLL EKRRQWKVIY LNDLIKEEHL YTEVDEKRDS VVADMELIRS
RLLELTDEME RESASKVVIL ESHLAHYIAD IIIVLRAYPP ELIKRLEKRG YSEEKVNENA
EAESIDLILA EAFEWCEKVF EVNTTDRTAE ETAGDVEKII DHLLSGKEDE LHEYSPGSLD
WIDSVP
//
