KGUA_BDEBA
ID KGUA_BDEBA Reviewed; 185 AA.
AC P60549;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2004, sequence version 1.
DT 03-AUG-2022, entry version 90.
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=Bd1568;
OS Bdellovibrio bacteriovorus (strain ATCC 15356 / DSM 50701 / NCIMB 9529 /
OS HD100).
OC Bacteria; Proteobacteria; Oligoflexia; Bdellovibrionales;
OC Bdellovibrionaceae; Bdellovibrio.
OX NCBI_TaxID=264462;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15356 / DSM 50701 / NCIMB 9529 / HD100;
RX PubMed=14752164; DOI=10.1126/science.1093027;
RA Rendulic S., Jagtap P., Rosinus A., Eppinger M., Baar C., Lanz C.,
RA Keller H., Lambert C., Evans K.J., Goesmann A., Meyer F., Sockett R.E.,
RA Schuster S.C.;
RT "A predator unmasked: life cycle of Bdellovibrio bacteriovorus from a
RT genomic perspective.";
RL Science 303:689-692(2004).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAE79446.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BX842650; CAE79446.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_038448884.1; NC_005363.1.
DR AlphaFoldDB; P60549; -.
DR SMR; P60549; -.
DR STRING; 264462.Bd1568; -.
DR EnsemblBacteria; CAE79446; CAE79446; Bd1568.
DR KEGG; bba:Bd1568; -.
DR eggNOG; COG0194; Bacteria.
DR HOGENOM; CLU_001715_1_1_7; -.
DR OrthoDB; 1502854at2; -.
DR Proteomes; UP000008080; 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..185
FT /note="Guanylate kinase"
FT /id="PRO_0000170502"
FT DOMAIN 3..181
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00328"
FT BINDING 10..17
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00328"
SQ SEQUENCE 185 AA; 21180 MW; F17BF3E8B2E54B9E CRC64;
MKTRMIIVAA PSGAGKSSFV ERITREDSRL VDIVTFTTRS IRQGETPGLQ YNFIDHADFE
QKIKEGFFVE WAKVHTNFYG TSYSSLETAW NQGKTAIMDI DIQGVATFKS KFPDAKTVFI
HPPSIDELRR RIEKRDGKVP ADIEVRMANA EKEIREASKF DYQIVNDVFE KSYGEFKKIV
EDLLA
