ID A0A0J5L3I7_PLUGE Unreviewed; 433 AA.
AC A0A0J5L3I7;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 24-JAN-2024, entry version 26.
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 ORFNames=ABW06_08395 {ECO:0000313|EMBL:KMK14341.1};
OS Pluralibacter gergoviae (Enterobacter gergoviae).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Pluralibacter.
OX NCBI_TaxID=61647 {ECO:0000313|EMBL:KMK14341.1, ECO:0000313|Proteomes:UP000036196};
RN [1] {ECO:0000313|EMBL:KMK14341.1, ECO:0000313|Proteomes:UP000036196}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JS81F13 {ECO:0000313|EMBL:KMK14341.1,
RC ECO:0000313|Proteomes:UP000036196};
RA Greninger A.L., Miller S.;
RT "Genome sequences of Pluralibacter gergoviae.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00010688, 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KMK14341.1}.
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DR EMBL; LDZF01000007; KMK14341.1; -; Genomic_DNA.
DR RefSeq; WP_048278671.1; NZ_VWRP01000003.1.
DR AlphaFoldDB; A0A0J5L3I7; -.
DR STRING; 61647.LG71_22855; -.
DR PATRIC; fig|61647.15.peg.4984; -.
DR eggNOG; COG0524; Bacteria.
DR UniPathway; UPA00591; UER00647.
DR UniPathway; UPA00909; -.
DR Proteomes; UP000036196; Unassembled WGS sequence.
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; IPR002173; Carboh/pur_kinase_PfkB_CS.
DR InterPro; IPR046405; IngK.
DR InterPro; IPR011611; PfkB_dom.
DR InterPro; IPR029056; Ribokinase-like.
DR PANTHER; PTHR43320:SF3; PFKB DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43320; SUGAR KINASE; 1.
DR Pfam; PF00294; PfkB; 1.
DR SUPFAM; SSF53613; Ribokinase-like; 1.
DR PROSITE; PS00584; PFKB_KINASES_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_02246};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_02246};
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:UP000036196};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_02246}.
FT DOMAIN 147..293
FT /note="Carbohydrate kinase PfkB"
FT /evidence="ECO:0000259|Pfam:PF00294"
FT BINDING 39..44
FT /ligand="GMP"
FT /ligand_id="ChEBI:CHEBI:58115"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02246"
FT BINDING 197
FT /ligand="GMP"
FT /ligand_id="ChEBI:CHEBI:58115"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02246"
FT BINDING 283..288
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02246"
FT BINDING 356
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02246"
FT BINDING 401
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02246"
SQ SEQUENCE 433 AA; 47735 MW; DB00D3D79FA86D35 CRC64;
MKFPGKRKFK HYFPVDARDP LLSTAPEREA SPSWVVGIDQ TLVDIEAKVD DAFIARYGLS
VGHSLVIEDD VAEALYRELQ QGGLISHQFA GGSIGNTLHN YSVLADDRSV LLGVMCRNIE
IGGYAYRYLC NTSSRTDLDY LQGIDGAIGR CFTLIGDSGE RTFAISPGQM NQLRPESIPE
AVIAGASALV LTAYLLRSRP GEPMREATMQ AVAYAKKHGV PVVLTLGTTF IIADDPAWWQ
TFLKENVSIL AMNEDEAKAL TGIGDPLLAA DRALDWVDLV LCTAGPAGLY MAGFTEESAK
RETQHPLLPG AIAEFNQYEF SRAMRYRECD RPLRIYSHIA PYMGGPEKIM NTNGAGDAAL
AALLHDIAAN NYHRSTVPNS DKHALGWLTY SSLAQVCKYA NRVSYQVLNQ HSPRLTRGLP
EREDSLEEAY WER
//