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KGUA_OLEA2
ID   KGUA_OLEA2              Reviewed;         206 AA.
AC   Q30XT1;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Guanylate kinase {ECO:0000255|HAMAP-Rule:MF_00328};
DE            EC=2.7.4.8 {ECO:0000255|HAMAP-Rule:MF_00328};
DE   AltName: Full=GMP kinase {ECO:0000255|HAMAP-Rule:MF_00328};
GN   Name=gmk {ECO:0000255|HAMAP-Rule:MF_00328}; OrderedLocusNames=Dde_2719;
OS   Oleidesulfovibrio alaskensis (strain ATCC BAA-1058 / DSM 17464 / G20)
OS   (Desulfovibrio alaskensis).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC   Desulfovibrionaceae; Oleidesulfovibrio.
OX   NCBI_TaxID=207559;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1058 / DSM 17464 / G20;
RX   PubMed=21685289; DOI=10.1128/jb.05400-11;
RA   Hauser L.J., Land M.L., Brown S.D., Larimer F., Keller K.L.,
RA   Rapp-Giles B.J., Price M.N., Lin M., Bruce D.C., Detter J.C., Tapia R.,
RA   Han C.S., Goodwin L.A., Cheng J.F., Pitluck S., Copeland A., Lucas S.,
RA   Nolan M., Lapidus A.L., Palumbo A.V., Wall J.D.;
RT   "Complete genome sequence and updated annotation of Desulfovibrio
RT   alaskensis G20.";
RL   J. Bacteriol. 193:4268-4269(2011).
CC   -!- FUNCTION: Essential for recycling GMP and indirectly, cGMP.
CC       {ECO:0000255|HAMAP-Rule:MF_00328}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + GMP = ADP + GDP; Xref=Rhea:RHEA:20780,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:58115, ChEBI:CHEBI:58189,
CC         ChEBI:CHEBI:456216; EC=2.7.4.8; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00328};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00328}.
CC   -!- SIMILARITY: Belongs to the guanylate kinase family. {ECO:0000255|HAMAP-
CC       Rule:MF_00328}.
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DR   EMBL; CP000112; ABB39515.1; -; Genomic_DNA.
DR   RefSeq; WP_011368541.1; NC_007519.1.
DR   AlphaFoldDB; Q30XT1; -.
DR   SMR; Q30XT1; -.
DR   STRING; 207559.Dde_2719; -.
DR   EnsemblBacteria; ABB39515; ABB39515; Dde_2719.
DR   KEGG; dde:Dde_2719; -.
DR   eggNOG; COG0194; Bacteria.
DR   HOGENOM; CLU_001715_1_0_7; -.
DR   OMA; EWAVVHG; -.
DR   OrthoDB; 1502854at2; -.
DR   Proteomes; UP000002710; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004385; F:guanylate kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_00328; Guanylate_kinase; 1.
DR   InterPro; IPR008145; GK/Ca_channel_bsu.
DR   InterPro; IPR008144; Guanylate_kin-like_dom.
DR   InterPro; IPR017665; Guanylate_kinase.
DR   InterPro; IPR020590; Guanylate_kinase_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00625; Guanylate_kin; 1.
DR   SMART; SM00072; GuKc; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR03263; guanyl_kin; 1.
DR   PROSITE; PS00856; GUANYLATE_KINASE_1; 1.
DR   PROSITE; PS50052; GUANYLATE_KINASE_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Reference proteome;
KW   Transferase.
FT   CHAIN           1..206
FT                   /note="Guanylate kinase"
FT                   /id="PRO_0000266318"
FT   DOMAIN          7..185
FT                   /note="Guanylate kinase-like"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00328"
FT   BINDING         14..21
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00328"
SQ   SEQUENCE   206 AA;  23732 MW;  6DA521CABD8CF894 CRC64;
     MVRPRSGIVL VLCAPSGTGK TTLTRRLLEE FPRFAFSVSY TTRQPRAGEE HGREYNFVDE
     ETFIRLRDEG FFAEWAEVHG NFYGTPLEDT RQLLARGRDV LFDIDVQGAA QLRGSLKQGC
     YVFILPPSGA ELERRLRARG TDPEDTIRRR LANARRELQQ AHWFNAWIVN DNLEQAYDEL
     RAAYLAATLS PTCRPELVDE LLQDWR
 
 
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