ID A0A1S8LMY2_9CLOT Unreviewed; 209 AA.
AC A0A1S8LMY2;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
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_2 {ECO:0000313|EMBL:OOL93262.1};
GN Synonyms=gmk {ECO:0000256|HAMAP-Rule:MF_00328}, gmk_1
GN {ECO:0000313|EMBL:URZ00818.1};
GN ORFNames=CLAUR_008060 {ECO:0000313|EMBL:URZ00818.1}, CROST_022950
GN {ECO:0000313|EMBL:URZ11578.1}, CROST_03980
GN {ECO:0000313|EMBL:OOL93262.1};
OS Clostridium felsineum.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=36839 {ECO:0000313|EMBL:OOL93262.1};
RN [1] {ECO:0000313|EMBL:OOL93262.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 7320 {ECO:0000313|EMBL:OOL93262.1};
RA Poehlein A., Montoya Solano J.D., Flitsch S., Krabben P., Duerre P.,
RA Daniel R.;
RT "Microbial solvent formation.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:URZ11578.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DSM 7320 {ECO:0000313|EMBL:URZ11578.1};
RA Poehlein A., Schoch T., Duerre P., Daniel R.;
RT "Genome sequence of C. roseum typestrain.";
RL Submitted (APR-2022) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:URZ00818.1, ECO:0000313|Proteomes:UP000190175}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 793 {ECO:0000313|EMBL:URZ00818.1,
RC ECO:0000313|Proteomes:UP000190175};
RA Poehlein A., Schoch T., Duerre P., Daniel R.;
RT "Genome sequence of Clostridium aurantibutyricum DSM 793.";
RL Submitted (APR-2022) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Essential for recycling GMP and indirectly, cGMP.
CC {ECO:0000256|ARBA:ARBA00003531, 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;
CC Evidence={ECO:0000256|ARBA:ARBA00000283, 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LZYV01000025; OOL93262.1; -; Genomic_DNA.
DR EMBL; CP096988; URZ00818.1; -; Genomic_DNA.
DR EMBL; CP096983; URZ11578.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1S8LMY2; -.
DR STRING; 84029.CROST_03980; -.
DR KEGG; caun:CLAUR_008060; -.
DR KEGG; crw:CROST_022950; -.
DR Proteomes; UP000190175; Chromosome.
DR Proteomes; UP000190951; 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; 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 5..182
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 209 AA; 23710 MW; AAD645A1B3ABDD06 CRC64;
MSKKGLLIVI SGPSGAGKGT ICKALMKEQQ FWLSVSATTR SPRKGEVEGK SYYFLTVDDF
KSKIAKDGFL EYAQVYDNYY GTPKKNVCEK IDKGENVILE IDIQGALKVK ENYPEGVFIF
ILPPSMEELK KRIIGRGSET EKSLMTRFKS AYKEINYVSK YNYAVINDTV DSAVQKINSI
IIAEKCRVDR IKDNIIDSKE GKIHEQFYD
//