ID Q9KLE5_VIBCH Unreviewed; 434 AA.
AC Q9KLE5;
DT 01-OCT-2000, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2000, sequence version 1.
DT 27-MAR-2024, entry version 109.
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=VC_A0801 {ECO:0000313|EMBL:AAF96699.1};
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277 {ECO:0000313|EMBL:AAF96699.1, ECO:0000313|Proteomes:UP000000584};
RN [1] {ECO:0000313|EMBL:AAF96699.1, ECO:0000313|Proteomes:UP000000584}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961
RC {ECO:0000313|Proteomes:UP000000584};
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D., Ermolaeva M.D.,
RA Vamathevan J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.,
RA Utterback T., Fleishmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
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 -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_02246}.
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DR EMBL; AE003853; AAF96699.1; -; Genomic_DNA.
DR PIR; H82414; H82414.
DR RefSeq; NP_233187.1; NC_002506.1.
DR RefSeq; WP_000671603.1; NZ_LT906615.1.
DR AlphaFoldDB; Q9KLE5; -.
DR STRING; 243277.VC_A0801; -.
DR DNASU; 2612659; -.
DR EnsemblBacteria; AAF96699; AAF96699; VC_A0801.
DR KEGG; vch:VC_A0801; -.
DR PATRIC; fig|243277.26.peg.3422; -.
DR eggNOG; COG0524; Bacteria.
DR HOGENOM; CLU_060237_0_0_6; -.
DR UniPathway; UPA00591; UER00647.
DR UniPathway; UPA00909; -.
DR Proteomes; UP000000584; Chromosome 2.
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; IBA:GO_Central.
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:AAF96699.1};
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:UP000000584};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_02246}.
FT DOMAIN 140..293
FT /note="Carbohydrate kinase PfkB"
FT /evidence="ECO:0000259|Pfam:PF00294"
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; 48731 MW; 4CABAA6557AEA9CF CRC64;
MKFPGQRKSK HYFPTHARDP LVNQIQQTPK LHRPTIVGVG QTIVDIEARV DDEFLTRYDL
SKGHSLVLEE SKADALYHEL VERGLITHQY PGDTIGNTLH NYSVLADSKS VLLGVMSKNI
EVGSYAYRYL CRTSARMNLN HLQTVDGPIG RCYTLISEDG ERTFAINEGH MNKLRPDSIP
EEVFDKASAL VVSSYLMRGK PEDPMPQAVQ RAIEIAKARS IPVVLTLGTK YVIEGNAEWW
QNYMKEHVTV VAMNEEEGAA LTGERDPLLA ADKALQWVDL VLCTAGPVGL YMAGYIDESA
KRETELPLLP GNIPEFNKYE FSRAMRKEDC RIPLKVYSHI GPYLGGPLEI KNTNGAGDGA
LSALLHDMAA NAYHQRNVPN SAKHDQPYLT YSSLSQVCKY ANRVSYEVLT QHSPRLSRAL
PEREDSLEEA YWDR
//
