ID A0A0C5WXX3_9GAMM Unreviewed; 434 AA.
AC A0A0C5WXX3;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
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=H744_2c1231 {ECO:0000313|EMBL:AJR07910.1};
OS Photobacterium gaetbulicola Gung47.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=658445 {ECO:0000313|EMBL:AJR07910.1, ECO:0000313|Proteomes:UP000032303};
RN [1] {ECO:0000313|EMBL:AJR07910.1, ECO:0000313|Proteomes:UP000032303}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Gung47 {ECO:0000313|EMBL:AJR07910.1,
RC ECO:0000313|Proteomes:UP000032303};
RA Kim Y.-O.;
RT "Complete genome sequence of the lipase-producing bacterium Photobacterium
RT gaetbulicola Gung47.";
RL Submitted (MAY-2013) 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|HAMAP-Rule:MF_02246}.
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DR EMBL; CP005974; AJR07910.1; -; Genomic_DNA.
DR RefSeq; WP_044622772.1; NZ_CP005974.1.
DR AlphaFoldDB; A0A0C5WXX3; -.
DR STRING; 658445.H744_2c1231; -.
DR KEGG; pgb:H744_2c1231; -.
DR PATRIC; fig|658445.3.peg.3123; -.
DR HOGENOM; CLU_060237_0_0_6; -.
DR OrthoDB; 5288159at2; -.
DR UniPathway; UPA00591; UER00647.
DR UniPathway; UPA00909; -.
DR Proteomes; UP000032303; 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; 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:AJR07910.1};
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:UP000032303};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_02246}.
FT DOMAIN 134..293
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; 49079 MW; A30E940825B23FBF CRC64;
MKFPGQRKSK HYFPVHARDP LLSQAKQDKR LTRTHIVGID QTLVDIEACV EDEFLERYEL
SKGHSLVISD EKAEALYREL KDNDLISHEF AGGTIGNTLH NYSVLADDKS VLLGVMSKDI
EIGSYAYRYL CNTSSRMDMN YLQPVNGPIG RCFALISKDG ERTFAINEGR MNQLEPSSIP
EDVFKRASAL VLTAYLVRCK DGDPMPAATM KAIEYAKKHD VPVVLTLGTK FVIEDDPQWW
RDFLRDHVTV VAMNEDEAEA LTGESDPLMA SEKTLEWVDL VLCTAGPVGL YTAGYTEDEA
KRETSLPLLP GEIPEFNRYE FSRPMLKTEC QNPIKVYSHI APYMGGPERI KNTNGAGDGA
LSALLHDMSA NRYHKENVPK SSKHQFDFLT YSSFSQICLY SNRVSYEVLA QHSPRLSRGL
PEREDSLEEA YWER
//
