ID H6L711_SAPGL Unreviewed; 206 AA.
AC H6L711;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 64.
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 ECO:0000313|EMBL:AFC26602.1};
GN OrderedLocusNames=SGRA_3886 {ECO:0000313|EMBL:AFC26602.1};
OS Saprospira grandis (strain Lewin).
OC Bacteria; Bacteroidota; Saprospiria; Saprospirales; Saprospiraceae;
OC Saprospira.
OX NCBI_TaxID=984262 {ECO:0000313|EMBL:AFC26602.1, ECO:0000313|Proteomes:UP000007519};
RN [1] {ECO:0000313|EMBL:AFC26602.1, ECO:0000313|Proteomes:UP000007519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lewin {ECO:0000313|EMBL:AFC26602.1,
RC ECO:0000313|Proteomes:UP000007519};
RX PubMed=22675601; DOI=10.4056/sigs.2445005;
RA Saw J.H., Yuryev A., Kanbe M., Hou S., Young A.G., Aizawa S., Alam M.;
RT "Complete genome sequencing and analysis of Saprospira grandis str. Lewin,
RT a predatory marine bacterium.";
RL Stand. Genomic Sci. 6:84-93(2012).
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}.
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DR EMBL; CP002831; AFC26602.1; -; Genomic_DNA.
DR RefSeq; WP_015694187.1; NC_016940.1.
DR AlphaFoldDB; H6L711; -.
DR STRING; 984262.SGRA_3886; -.
DR KEGG; sgn:SGRA_3886; -.
DR eggNOG; COG0194; Bacteria.
DR HOGENOM; CLU_001715_1_1_10; -.
DR OrthoDB; 9808150at2; -.
DR Proteomes; UP000007519; 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 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; 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; 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:UP000007519};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00328}.
FT DOMAIN 5..185
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000259|PROSITE:PS50052"
FT BINDING 12..19
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00328"
SQ SEQUENCE 206 AA; 23503 MW; B4653C6016860B69 CRC64;
MQQEAKLIIF TAPSGAGKTT IVKHLLKTRK DLAFSISACT RSQRYGEVNG MDYYFLSLQD
FKRRIEADEF VEWEEVYDNQ FYGTLKEEVE RLLALGKSVL FDIDVKGAVN IQKHYPERSL
SIFVKPPSAD TLFARLRGRK TEDEESLRKR IARASDELTY ECKFDYTLVN DNLEVALAEA
EKVVEAFISE GNSGLEKLKH GNGHHA
//
