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Database: UniProt
Entry: A0A0J5L3I7_PLUGE
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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
//
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