ID A0A0F3LBB5_9CAUL Unreviewed; 213 AA.
AC A0A0F3LBB5;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
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=VH88_10980 {ECO:0000313|EMBL:KJV40860.1};
OS Brevundimonas sp. KM4.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Brevundimonas.
OX NCBI_TaxID=1628191 {ECO:0000313|EMBL:KJV40860.1, ECO:0000313|Proteomes:UP000033583};
RN [1] {ECO:0000313|EMBL:KJV40860.1, ECO:0000313|Proteomes:UP000033583}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KM4 {ECO:0000313|EMBL:KJV40860.1,
RC ECO:0000313|Proteomes:UP000033583};
RA Sulaiman J., Priya K., Chan K.-G.;
RT "Draft genome sequence of Brevundimonas sp. KM4.";
RL Submitted (MAR-2015) 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:KJV40860.1}.
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DR EMBL; JZRG01000018; KJV40860.1; -; Genomic_DNA.
DR RefSeq; WP_039247959.1; NZ_JZRG01000018.1.
DR AlphaFoldDB; A0A0F3LBB5; -.
DR GeneID; 34016059; -.
DR PATRIC; fig|1628191.3.peg.876; -.
DR Proteomes; UP000033583; 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 10..189
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000259|PROSITE:PS50052"
FT BINDING 17..24
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00328"
SQ SEQUENCE 213 AA; 24151 MW; 9CA6D8DD8D8A7EB4 CRC64;
MSNERSPRRG VLLIVASPSG AGKTSLCRRL MADHGGLELS VSMTTRGIRP GEVHGRDYNF
VGHDEFQRLI DEDAFLEWAD VHGNRYGSPR GPVDKALAEG RDVLFDIDWQ GARDVAEKCP
EDAVRVFILP PSLEELRRRL VTRSQDADDV IERRVANAKG EIEHCDAFDY VLVNEDFDRS
YAELAHIYHA ERSRRFRNLW VGDYKAALLN EAV
//
