KGUA_CLOPE
ID KGUA_CLOPE Reviewed; 216 AA.
AC Q8XJK8;
DT 10-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 3.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Guanylate kinase;
DE EC=2.7.4.8;
DE AltName: Full=GMP kinase;
GN Name=gmk; OrderedLocusNames=CPE1748;
OS Clostridium perfringens (strain 13 / Type A).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=195102;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=13 / Type A;
RX PubMed=11792842; DOI=10.1073/pnas.022493799;
RA Shimizu T., Ohtani K., Hirakawa H., Ohshima K., Yamashita A., Shiba T.,
RA Ogasawara N., Hattori M., Kuhara S., Hayashi H.;
RT "Complete genome sequence of Clostridium perfringens, an anaerobic flesh-
RT eater.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:996-1001(2002).
CC -!- FUNCTION: Essential for recycling GMP and indirectly, cGMP.
CC {ECO:0000250}.
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the guanylate kinase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB81454.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BA000016; BAB81454.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_003478299.1; NC_003366.1.
DR AlphaFoldDB; Q8XJK8; -.
DR SMR; Q8XJK8; -.
DR STRING; 195102.gene:10491012; -.
DR PRIDE; Q8XJK8; -.
DR EnsemblBacteria; BAB81454; BAB81454; BAB81454.
DR KEGG; cpe:CPE1748; -.
DR HOGENOM; CLU_001715_1_2_9; -.
DR OMA; EWAVVHG; -.
DR Proteomes; UP000000818; 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..216
FT /note="Guanylate kinase"
FT /id="PRO_0000170525"
FT DOMAIN 11..189
FT /note="Guanylate kinase-like"
FT BINDING 18..25
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 216 AA; 24605 MW; DD7E7AF5E6F7875A CRC64;
MMNKIHKDNR GVLIVISGPS GAGKGTICKA LLEKHDDIFI SISATTRNPR VGEVDGVNYH
FLTKEEFKQR IAEDDFLEHA EVYGNYYGTP KSSVEKMLDE GKNVILEIDI QGALKVKEKA
TDGVFIFILP PSMEELKQRI IKRGSETPES LMTRFKSAYK EINYVSKYNY AVVNDNVEDA
VKKIEAILLA EKCRVDRLKE NLLESKEDEM HEQLYD