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Database: UniProt
Entry: A0A3R8U2I1_9PSED
LinkDB: A0A3R8U2I1_9PSED
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ID   A0A3R8U2I1_9PSED        Unreviewed;       206 AA.
AC   A0A3R8U2I1;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   13-SEP-2023, entry version 18.
DE   RecName: Full=Guanylate kinase {ECO:0000256|ARBA:ARBA00016296, ECO:0000256|HAMAP-Rule:MF_00328};
DE            EC=2.7.4.8 {ECO:0000256|ARBA:ARBA00012961, ECO:0000256|HAMAP-Rule:MF_00328};
DE   AltName: Full=GMP kinase {ECO:0000256|ARBA:ARBA00030128, ECO:0000256|HAMAP-Rule:MF_00328};
GN   Name=gmk {ECO:0000256|HAMAP-Rule:MF_00328};
GN   ORFNames=EGJ27_05160 {ECO:0000313|EMBL:RRV09161.1};
OS   Pseudomonas sp. v388.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=2479849 {ECO:0000313|EMBL:RRV09161.1, ECO:0000313|Proteomes:UP000268166};
RN   [1] {ECO:0000313|EMBL:RRV09161.1, ECO:0000313|Proteomes:UP000268166}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=v388 {ECO:0000313|Proteomes:UP000268166};
RA   D'Souza A.W., Potter R.F., Wallace M., Shupe A., Patel S., Sun S., Gul D.,
RA   Kwon J.H., Andleeb S., Burnham C.-A.D., Dantas G.;
RT   "Transmission dynamics of multidrug resistant bacteria on intensive care
RT   unit surfaces.";
RL   Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Essential for recycling GMP and indirectly, cGMP.
CC       {ECO:0000256|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:0000256|HAMAP-
CC         Rule:MF_00328};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00328}.
CC   -!- SIMILARITY: Belongs to the guanylate kinase family.
CC       {ECO:0000256|ARBA:ARBA00005790, ECO:0000256|HAMAP-Rule:MF_00328}.
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:RRV09161.1}.
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DR   EMBL; RHQN01000002; RRV09161.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3R8U2I1; -.
DR   OrthoDB; 9808150at2; -.
DR   Proteomes; UP000268166; Unassembled WGS sequence.
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   CDD; cd00071; GMPK; 1.
DR   Gene3D; 3.30.63.10; Guanylate Kinase phosphate binding domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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   NCBIfam; TIGR03263; guanyl_kin; 1.
DR   PANTHER; PTHR23117:SF13; GUANYLATE KINASE; 1.
DR   PANTHER; PTHR23117; GUANYLATE KINASE-RELATED; 1.
DR   Pfam; PF00625; Guanylate_kin; 1.
DR   SMART; SM00072; GuKc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00856; GUANYLATE_KINASE_1; 1.
DR   PROSITE; PS50052; GUANYLATE_KINASE_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00328}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00328};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_00328};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00328}; Reference proteome {ECO:0000313|Proteomes:UP000268166};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00328}.
FT   DOMAIN          6..184
FT                   /note="Guanylate kinase-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50052"
FT   BINDING         13..20
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00328"
SQ   SEQUENCE   206 AA;  23463 MW;  F12514B3593BC75A CRC64;
     MTHSTGTLYI ISAPSGAGKT SLVKALIDAQ PQIRVSVSHT TRAMRPGEAD GVNYHFVERA
     EFVRMIEHGD FLEQAEVFGN LYGTSQSRLQ QTLDEGHDLI LEIDWQGAQQ VRRQMPHARS
     IFILPPTQQA LRQRLTNRGQ DSDEIIDARM REAVSEMSHY VEYEYIVVND DFGSALEDLK
     AIFRANRLSQ THQQEQYSEL FQQLLA
//
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