KGUA_CLOAB
ID KGUA_CLOAB Reviewed; 209 AA.
AC Q97ID0;
DT 10-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 106.
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=CA_C1718;
OS Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710
OS / VKM B-1787).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=272562;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX PubMed=11466286; DOI=10.1128/jb.183.16.4823-4838.2001;
RA Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R.,
RA Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F.,
RA Doucette-Stamm L.A., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V.,
RA Smith D.R.;
RT "Genome sequence and comparative analysis of the solvent-producing
RT bacterium Clostridium acetobutylicum.";
RL J. Bacteriol. 183:4823-4838(2001).
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}.
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DR EMBL; AE001437; AAK79684.1; -; Genomic_DNA.
DR PIR; A97112; A97112.
DR RefSeq; NP_348344.1; NC_003030.1.
DR RefSeq; WP_010965025.1; NC_003030.1.
DR AlphaFoldDB; Q97ID0; -.
DR SMR; Q97ID0; -.
DR STRING; 272562.CA_C1718; -.
DR EnsemblBacteria; AAK79684; AAK79684; CA_C1718.
DR GeneID; 44998213; -.
DR KEGG; cac:CA_C1718; -.
DR PATRIC; fig|272562.8.peg.1920; -.
DR eggNOG; COG0194; Bacteria.
DR HOGENOM; CLU_001715_1_2_9; -.
DR OMA; EWAVVHG; -.
DR OrthoDB; 1502854at2; -.
DR Proteomes; UP000000814; 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..209
FT /note="Guanylate kinase"
FT /id="PRO_0000170524"
FT DOMAIN 5..182
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00328"
FT BINDING 12..19
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00328"
SQ SEQUENCE 209 AA; 23771 MW; 178B646B82843163 CRC64;
MSKKGLLIVI SGPSGAGKGT ICKALMKEQQ FWLSVSATTR EPREKEVEGK SYYFLTVDEF
KSKISEDGFL EYAEVYGNYY GTPKKSVCEK IDNGENVILE IDIQGALKVK ENYPEGVFIF
ILPPSMEELK KRIIGRGSET EKSLMTRFKS AYKEINYVSK YNYAIINDTV ENAVTKINSI
IVAEKCRVDR IKDNIIDSKE GKIHEQFYD
