INGK_EXIAC
ID INGK_EXIAC Reviewed; 303 AA.
AC O24767;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Guanosine-inosine kinase {ECO:0000303|PubMed:11129609};
DE EC=2.7.1.73 {ECO:0000269|PubMed:11129609, ECO:0000269|PubMed:9357959};
DE AltName: Full=ATP:guanosine 5'-phosphotransferase {ECO:0000303|PubMed:9357959};
DE AltName: Full=Guanosine kinase {ECO:0000303|PubMed:9357959};
DE Short=GKase {ECO:0000303|PubMed:9357959};
GN Name=gsk {ECO:0000303|PubMed:9371440};
OS Exiguobacterium acetylicum (Brevibacterium acetylicum).
OC Bacteria; Firmicutes; Bacilli; Bacillales;
OC Bacillales Family XII. Incertae Sedis; Exiguobacterium.
OX NCBI_TaxID=41170;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-28, AND INDUCTION.
RC STRAIN=ATCC 953 / DSM 20416 / JCM 1968 / KCTC 3255 / NCIMB 9889 / 1005;
RX PubMed=9371440; DOI=10.1128/jb.179.22.6959-6964.1997;
RA Usuda Y., Kawasaki H., Shimaoka M., Utagawa T.;
RT "Molecular cloning and transcriptional analysis of a guanosine kinase gene
RT of Brevibacterium acetylicum ATCC 953.";
RL J. Bacteriol. 179:6959-6964(1997).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, AND SUBUNIT.
RC STRAIN=ATCC 953 / DSM 20416 / JCM 1968 / KCTC 3255 / NCIMB 9889 / 1005;
RX PubMed=9357959; DOI=10.1016/s0167-4838(97)00080-0;
RA Usuda Y., Kawasaki H., Shimaoka M., Utagawa T.;
RT "Characterization of guanosine kinase from Brevibacterium acetylicum ATCC
RT 953.";
RL Biochim. Biophys. Acta 1341:200-206(1997).
RN [3]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=11129609; DOI=10.1271/bbb.64.2259;
RA Kawasaki H., Usuda Y., Shimaoka M., Utagawa T.;
RT "Phosphorylation of guanosine using guanosine-inosine kinase from
RT Exiguobacterium acetylicum coupled with ATP regeneration.";
RL Biosci. Biotechnol. Biochem. 64:2259-2261(2000).
CC -!- FUNCTION: Catalyzes the phosphorylation of guanosine and inosine to GMP
CC and IMP, respectively (PubMed:9357959, PubMed:11129609). Can also use
CC deoxyguanosine (PubMed:9357959). Shows a strong preference for
CC guanosine (PubMed:9357959). dATP, GTP and dGTP can serve as phosphate
CC donors (PubMed:9357959). {ECO:0000269|PubMed:11129609,
CC ECO:0000269|PubMed:9357959}.
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:0000269|PubMed:11129609, ECO:0000269|PubMed:9357959};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27711;
CC Evidence={ECO:0000269|PubMed:9357959};
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:0000269|PubMed:11129609, ECO:0000269|PubMed:9357959};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21141;
CC Evidence={ECO:0000269|PubMed:9357959};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:9357959};
CC Note=Manganese or cobalt, but not calcium, nickel or zinc can replace
CC Mg(2+) but results in reduced reaction rates.
CC {ECO:0000269|PubMed:9357959};
CC -!- ACTIVITY REGULATION: Kinase activity is stimulated by pyrimidine
CC nucleotides, especially CMP and CTP, and inhibited by AMP, ADP and GMP
CC (PubMed:9357959). Activity is stimulated by potassium or ammonium ions
CC (PubMed:9357959). {ECO:0000269|PubMed:9357959}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.022 mM for guanosine {ECO:0000269|PubMed:9357959};
CC KM=0.87 mM for inosine {ECO:0000269|PubMed:9357959};
CC KM=2.83 mM for deoxyguanosine {ECO:0000269|PubMed:9357959};
CC Vmax=217 umol/min/mg enzyme with guanosine as substrate
CC {ECO:0000269|PubMed:9357959};
CC Vmax=35.9 umol/min/mg enzyme with inosine as substrate
CC {ECO:0000269|PubMed:9357959};
CC Vmax=59.3 umol/min/mg enzyme with deoxyguanosine as substrate
CC {ECO:0000269|PubMed:9357959};
CC pH dependence:
CC Optimum pH is around 8.3. {ECO:0000269|PubMed:9357959};
CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via salvage pathway; IMP
CC from inosine: step 1/1. {ECO:0000305|PubMed:9357959}.
CC -!- PATHWAY: Purine metabolism; GMP biosynthesis via salvage pathway.
CC {ECO:0000305|PubMed:9357959}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:9357959}.
CC -!- INDUCTION: Specifically transcribed in the early exponential growth
CC phase. {ECO:0000269|PubMed:9371440}.
CC -!- SIMILARITY: Belongs to the carbohydrate kinase PfkB family.
CC {ECO:0000305}.
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DR EMBL; AB005149; BAA23613.1; -; Genomic_DNA.
DR RefSeq; WP_029340887.1; NZ_LFQN01000014.1.
DR AlphaFoldDB; O24767; -.
DR SMR; O24767; -.
DR PATRIC; fig|41170.3.peg.318; -.
DR UniPathway; UPA00591; UER00647.
DR UniPathway; UPA00909; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0106366; F:guanosine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0008906; F:inosine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0032263; P:GMP salvage; IEA:UniProtKB-UniPathway.
DR GO; GO:0032264; P:IMP salvage; IEA:UniProtKB-UniPathway.
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 InterPro; IPR002173; Carboh/pur_kinase_PfkB_CS.
DR InterPro; IPR011611; PfkB_dom.
DR InterPro; IPR029056; Ribokinase-like.
DR Pfam; PF00294; PfkB; 1.
DR SUPFAM; SSF53613; SSF53613; 1.
DR PROSITE; PS00584; PFKB_KINASES_2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Direct protein sequencing; Kinase; Magnesium;
KW Nucleotide-binding; Purine salvage; Transferase.
FT CHAIN 1..303
FT /note="Guanosine-inosine kinase"
FT /id="PRO_0000452717"
SQ SEQUENCE 303 AA; 32536 MW; 87630DB43A2829FA CRC64;
MNKIAVIGKV FVDIKGTSFA PLHKDAKNVG DITFSNGGTG RNVAQNLAVL GNEVRFISTV
TNDQIGVGVL DELKSYGANV DHVEMLEDHG MGMWLAVMDN EGDLQTSISK QPDAKLLEEA
ILRQSIYALD GVDAVAIDLD LSVTVLERLI HLCRKMELPL FGVCGHLSVI ERNRHLLQGF
TGFICSREEA EILSDLSIVT VEDAIHVANE LAKKGAPFTV VTMSELGAVY VDRRTATSGH
VGTKKVKVVD STGAGDSFFS AVLSELTQEK SAEEALKLGM KVAAEVIAST ENGLVPEMLD
ALQ
