ID KGUA_PSEAE Reviewed; 203 AA. AC Q9HTM2; DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2001, sequence version 1. DT 27-MAR-2024, entry version 117. DE RecName: Full=Guanylate kinase; DE EC=2.7.4.8; DE AltName: Full=GMP kinase; GN Name=gmk; OrderedLocusNames=PA5336; OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=208964; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / RC 1C / PRS 101 / PAO1; RX PubMed=10984043; DOI=10.1038/35023079; RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P., RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M., RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y., RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M., RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J., RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.; RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic RT pathogen."; RL Nature 406:959-964(2000). 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 --------------------------------------------------------------------------- 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; AE004091; AAG08721.1; -; Genomic_DNA. DR PIR; F82978; F82978. DR RefSeq; NP_254023.1; NC_002516.2. DR RefSeq; WP_003098317.1; NZ_QZGE01000020.1. DR PDB; 7U5F; X-ray; 2.00 A; A/B/C/D=1-203. DR PDB; 8EGL; X-ray; 2.35 A; A/B/C/D/E/F/G/H/I/J/K/L=1-203. DR PDBsum; 7U5F; -. DR PDBsum; 8EGL; -. DR AlphaFoldDB; Q9HTM2; -. DR SMR; Q9HTM2; -. DR STRING; 208964.PA5336; -. DR PaxDb; 208964-PA5336; -. DR DNASU; 878047; -. DR GeneID; 878047; -. DR KEGG; pae:PA5336; -. DR PATRIC; fig|208964.12.peg.5591; -. DR PseudoCAP; PA5336; -. DR HOGENOM; CLU_001715_1_0_6; -. DR InParanoid; Q9HTM2; -. DR OrthoDB; 9808150at2; -. DR PhylomeDB; Q9HTM2; -. DR BioCyc; PAER208964:G1FZ6-5458-MONOMER; -. DR Proteomes; UP000002438; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0004385; F:guanylate kinase activity; IBA:GO_Central. 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 1: Evidence at protein level; KW 3D-structure; ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; KW Reference proteome; Transferase. FT CHAIN 1..203 FT /note="Guanylate kinase" FT /id="PRO_0000170587" FT DOMAIN 3..181 FT /note="Guanylate kinase-like" FT BINDING 10..17 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250" FT STRAND 5..9 FT /evidence="ECO:0007829|PDB:7U5F" FT HELIX 18..25 FT /evidence="ECO:0007829|PDB:7U5F" FT STRAND 30..32 FT /evidence="ECO:0007829|PDB:7U5F" FT TURN 47..49 FT /evidence="ECO:0007829|PDB:7U5F" FT HELIX 56..64 FT /evidence="ECO:0007829|PDB:7U5F" FT STRAND 68..74 FT /evidence="ECO:0007829|PDB:7U5F" FT STRAND 77..82 FT /evidence="ECO:0007829|PDB:7U5F" FT HELIX 83..91 FT /evidence="ECO:0007829|PDB:7U5F" FT STRAND 95..99 FT /evidence="ECO:0007829|PDB:7U5F" FT HELIX 102..111 FT /evidence="ECO:0007829|PDB:7U5F" FT STRAND 116..121 FT /evidence="ECO:0007829|PDB:7U5F" FT HELIX 125..131 FT /evidence="ECO:0007829|PDB:7U5F" FT HELIX 140..152 FT /evidence="ECO:0007829|PDB:7U5F" FT HELIX 154..159 FT /evidence="ECO:0007829|PDB:7U5F" FT STRAND 160..165 FT /evidence="ECO:0007829|PDB:7U5F" FT HELIX 169..184 FT /evidence="ECO:0007829|PDB:7U5F" FT HELIX 187..193 FT /evidence="ECO:0007829|PDB:7U5F" FT HELIX 195..202 FT /evidence="ECO:0007829|PDB:7U5F" SQ SEQUENCE 203 AA; 23102 MW; DE35644BBE88623A CRC64; MSGTLYIVSA PSGAGKTSLV KALLDAAPEV RVSVSHTTRG MRPGEVDGVN YHFTSREEFL AMLERNEFLE HAEVFGNLYG TSQRWVEKTL AEGLDLILEI DWQGAQQVRR LMPEAQSIFI LPPSQEALRQ RLTNRGQDSD EVIERRMREA VSEMSHYVEY DHLVINDDFA HALDDLKAIF RARQLRQDAQ QQRHAELLGR LLA //