ID Q87QL7_VIBPA Unreviewed; 434 AA.
AC Q87QL7;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 102.
DE RecName: Full=Guanosine-inosine kinase {ECO:0000256|HAMAP-Rule:MF_02246};
DE EC=2.7.1.73 {ECO:0000256|HAMAP-Rule:MF_02246};
GN Name=gsk {ECO:0000256|HAMAP-Rule:MF_02246};
GN OrderedLocusNames=VP1132 {ECO:0000313|EMBL:BAC59395.1};
OS Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=223926 {ECO:0000313|EMBL:BAC59395.1, ECO:0000313|Proteomes:UP000002493};
RN [1] {ECO:0000313|EMBL:BAC59395.1, ECO:0000313|Proteomes:UP000002493}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RIMD 2210633 {ECO:0000313|Proteomes:UP000002493};
RX PubMed=12620739; DOI=10.1016/S0140-6736(03)12659-1;
RA Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT distinct from that of V. cholerae.";
RL Lancet 361:743-749(2003).
CC -!- FUNCTION: Catalyzes the phosphorylation of guanosine and inosine to GMP
CC and IMP, respectively. {ECO:0000256|HAMAP-Rule:MF_02246}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + guanosine = ADP + GMP + H(+); Xref=Rhea:RHEA:27710,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16750, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:58115, ChEBI:CHEBI:456216; EC=2.7.1.73;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_02246};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + inosine = ADP + H(+) + IMP; Xref=Rhea:RHEA:21140,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17596, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:58053, ChEBI:CHEBI:456216; EC=2.7.1.73;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_02246};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_02246};
CC -!- PATHWAY: Purine metabolism; GMP biosynthesis via salvage pathway.
CC {ECO:0000256|HAMAP-Rule:MF_02246}.
CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via salvage pathway; IMP
CC from inosine: step 1/1. {ECO:0000256|HAMAP-Rule:MF_02246}.
CC -!- SIMILARITY: Belongs to the carbohydrate kinase PfkB family.
CC {ECO:0000256|HAMAP-Rule:MF_02246}.
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; BA000031; BAC59395.1; -; Genomic_DNA.
DR RefSeq; NP_797511.1; NC_004603.1.
DR RefSeq; WP_005459989.1; NC_004603.1.
DR AlphaFoldDB; Q87QL7; -.
DR GeneID; 1188637; -.
DR KEGG; vpa:VP1132; -.
DR PATRIC; fig|223926.6.peg.1073; -.
DR eggNOG; COG0524; Bacteria.
DR HOGENOM; CLU_060237_0_0_6; -.
DR UniPathway; UPA00591; UER00647.
DR UniPathway; UPA00909; -.
DR Proteomes; UP000002493; Chromosome 1.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0106366; F:guanosine kinase activity; IEA:InterPro.
DR GO; GO:0008906; F:inosine kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0032263; P:GMP salvage; IEA:UniProtKB-UniRule.
DR GO; GO:0032264; P:IMP salvage; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0006166; P:purine ribonucleoside salvage; IEA:UniProtKB-KW.
DR Gene3D; 3.40.1190.20; -; 1.
DR HAMAP; MF_02246; Gua_Ino_kinase; 1.
DR InterPro; IPR046405; IngK.
DR InterPro; IPR011611; PfkB_dom.
DR InterPro; IPR029056; Ribokinase-like.
DR PANTHER; PTHR43320:SF3; CARBOHYDRATE KINASE PFKB DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43320; SUGAR KINASE; 1.
DR Pfam; PF00294; PfkB; 1.
DR SUPFAM; SSF53613; Ribokinase-like; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_02246};
KW Kinase {ECO:0000256|HAMAP-Rule:MF_02246, ECO:0000313|EMBL:BAC59395.1};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_02246};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_02246};
KW Purine salvage {ECO:0000256|HAMAP-Rule:MF_02246};
KW Reference proteome {ECO:0000313|Proteomes:UP000002493};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_02246}.
FT DOMAIN 77..292
FT /note="Carbohydrate kinase PfkB"
FT /evidence="ECO:0000259|Pfam:PF00294"
FT BINDING 40..45
FT /ligand="GMP"
FT /ligand_id="ChEBI:CHEBI:58115"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02246"
FT BINDING 93..97
FT /ligand="GMP"
FT /ligand_id="ChEBI:CHEBI:58115"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02246"
FT BINDING 198
FT /ligand="GMP"
FT /ligand_id="ChEBI:CHEBI:58115"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02246"
FT BINDING 284..289
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02246"
FT BINDING 357
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02246"
FT BINDING 402
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02246"
SQ SEQUENCE 434 AA; 48478 MW; 6F968DB4CCC57B5B CRC64;
MKFPGQRKSK HYFPVHARDP LVSQAQESKK MTRTHIIGID QTLVDIEAKV TSDVIEKYGL
SKGHSLVIDD VKAEELYQQL KEENLITNEY AGGTIGNTLH NYSVLADDRS TLLGVMSQDI
KIGSYGYRYL CNTSSRMDLN YLQGVDGAIG RCFALITEDG ERTFAISEGQ MNQLHPDSIP
EKIFKNASAL VLTSYLVRCK EGDPMPEATM KAIEFAKKND VPVVLTLGTK FVIQDDPKYW
QDFIREHVSV VAMNEDEAEA LTGETDPLAA SDKTLEWADM VLCTAGPVGL FMAGYTEDSA
KRETTLPLLP GSIAEFNRYE FSRPAKKDAC QNPIRVYSHI SPYMGGPEKI KNTNGAGDAA
LSAVLHDMAA NKYHKENVPN SSKHSNEYLT YSSFSQVCKY ANRASYEVLV QHSPRLSRGL
PEREDSLEEA YWER
//
