ID   KAD6_METBF              Reviewed;         182 AA.
AC   Q46FV0;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   01-OCT-2014, entry version 45.
DE   RecName: Full=Putative adenylate kinase {ECO:0000255|HAMAP-Rule:MF_00039};
DE            Short=AK {ECO:0000255|HAMAP-Rule:MF_00039};
DE            EC=2.7.4.3 {ECO:0000255|HAMAP-Rule:MF_00039};
DE   AltName: Full=ATP-AMP transphosphorylase {ECO:0000255|HAMAP-Rule:MF_00039};
GN   OrderedLocusNames=Mbar_A0258;
OS   Methanosarcina barkeri (strain Fusaro / DSM 804).
OC   Archaea; Euryarchaeota; Methanomicrobia; Methanosarcinales;
OC   Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=269797;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fusaro / DSM 804;
RX   PubMed=16980466; DOI=10.1128/JB.00810-06;
RA   Maeder D.L., Anderson I., Brettin T.S., Bruce D.C., Gilna P.,
RA   Han C.S., Lapidus A., Metcalf W.W., Saunders E., Tapia R.,
RA   Sowers K.R.;
RT   "The Methanosarcina barkeri genome: comparative analysis with
RT   Methanosarcina acetivorans and Methanosarcina mazei reveals extensive
RT   rearrangement within methanosarcinal genomes.";
RL   J. Bacteriol. 188:7922-7931(2006).
CC   -!- FUNCTION: Broad-specificity nucleoside monophosphate (NMP) kinase
CC       that catalyzes the reversible transfer of the terminal phosphate
CC       group between nucleoside triphosphates and monophosphates.
CC       {ECO:0000255|HAMAP-Rule:MF_00039}.
CC   -!- CATALYTIC ACTIVITY: ATP + AMP = 2 ADP. {ECO:0000255|HAMAP-
CC       Rule:MF_00039}.
CC   -!- SIMILARITY: Belongs to the adenylate kinase family. AK6 subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00039}.
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DR   EMBL; CP000099; AAZ69242.1; -; Genomic_DNA.
DR   RefSeq; WP_011305297.1; NC_007355.1.
DR   RefSeq; YP_303822.1; NC_007355.1.
DR   ProteinModelPortal; Q46FV0; -.
DR   STRING; 269797.Mbar_A0258; -.
DR   EnsemblBacteria; AAZ69242; AAZ69242; Mbar_A0258.
DR   GeneID; 3624967; -.
DR   KEGG; mba:Mbar_A0258; -.
DR   eggNOG; COG1936; -.
DR   HOGENOM; HOG000224471; -.
DR   OMA; IDVTHRT; -.
DR   BioCyc; MBAR269797:GHUW-266-MONOMER; -.
DR   GO; GO:0004017; F:adenylate kinase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_00039; Adenylate_kinase_AK6; 1.
DR   InterPro; IPR020618; Adenyl_kinase_AK6.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   SUPFAM; SSF52540; SSF52540; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Complete proteome; Kinase; Nucleotide-binding;
KW   Reference proteome; Transferase.
FT   CHAIN         1    182       Putative adenylate kinase.
FT                                /FTId=PRO_1000003091.
FT   NP_BIND      10     15       ATP. {ECO:0000255|HAMAP-Rule:MF_00039}.
FT   REGION       30     53       NMPbind. {ECO:0000255|HAMAP-
FT                                Rule:MF_00039}.
FT   REGION      104    114       LID. {ECO:0000255|HAMAP-Rule:MF_00039}.
FT   BINDING     101    101       ATP. {ECO:0000255|HAMAP-Rule:MF_00039}.
FT   BINDING     105    105       ATP. {ECO:0000255|HAMAP-Rule:MF_00039}.
SQ   SEQUENCE   182 AA;  21069 MW;  6EE6678F65AE38CA CRC64;
     MLIGLTGTPG TGKTSVSKFL ERKRHWKVIH LNEMIKEEHL YTEVDEVRDA VIADMELVRQ
     RLEEIIGGKE NEVIILESHL AHYIADIVII LRVYPPELKM RLKARGYSEE KIRENIEAEA
     LDVILVEAFE WCKKVFEINT TGKSIEETEQ HIEKIIDHIL SGNEEELPEY KPGSIDWIDL
     VP
//