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Database: UniProt
Entry: A0A0Q0AMW7_PSESX
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Original site: A0A0Q0AMW7_PSESX 
ID   A0A0Q0AMW7_PSESX        Unreviewed;       214 AA.
AC   A0A0Q0AMW7;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 36.
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=ALO94_04556 {ECO:0000313|EMBL:KPY65420.1}, ALP50_00986
GN   {ECO:0000313|EMBL:RMT36879.1};
OS   Pseudomonas syringae pv. spinaceae.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX   NCBI_TaxID=264459 {ECO:0000313|EMBL:KPY65420.1, ECO:0000313|Proteomes:UP000050384};
RN   [1] {ECO:0000313|EMBL:KPY65420.1, ECO:0000313|Proteomes:UP000050384}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ICMP16929 {ECO:0000313|EMBL:KPY65420.1,
RC   ECO:0000313|Proteomes:UP000050384};
RA   Thakur S., Wang P.W., Gong Y., Weir B.S., Guttman D.S.;
RT   "Genome announcement of multiple Pseudomonas syringae strains.";
RL   Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:RMT36879.1, ECO:0000313|Proteomes:UP000280047}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ICMP 16928 {ECO:0000313|EMBL:RMT36879.1,
RC   ECO:0000313|Proteomes:UP000280047};
RA   Dillon M., Thakur S., Almeida R.N.D., Weir B.S., Guttman D.S.;
RT   "Recombination of ecologically and evolutionarily significant loci
RT   maintains genetic cohesion in the Pseudomonas syringae species complex.";
RL   Submitted (AUG-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:KPY65420.1}.
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DR   EMBL; LJRI01001304; KPY65420.1; -; Genomic_DNA.
DR   EMBL; RBTF01000044; RMT36879.1; -; Genomic_DNA.
DR   RefSeq; WP_057428261.1; NZ_RBTF01000044.1.
DR   AlphaFoldDB; A0A0Q0AMW7; -.
DR   PATRIC; fig|264459.3.peg.7070; -.
DR   Proteomes; UP000050384; Unassembled WGS sequence.
DR   Proteomes; UP000280047; 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};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00328}.
FT   DOMAIN          6..192
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   214 AA;  24345 MW;  BD9F7B15186D1D95 CRC64;
     MTHITGTLYI ISAPSGAGKT SLVKALMDAQ QEPQHGAQAK IRVSVSHTTR AMRPGEVDGV
     NYNFVDRAEF VRMIEHGDFL EQAEVFGNLY GTSQSHLQQT LDEGHDLILE IDWQGARQVR
     TQMPQARSIF ILPPSQHALR QRLTNRGQDS DEIIEARMRE AVSEMSHYNE YEYVVVNDDF
     AGALEDLKSI FRANRLTQQH QQEQYSELFQ ELLA
//
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