ID D4ZM46_SHEVD Unreviewed; 434 AA.
AC D4ZM46;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 27-MAR-2024, entry version 62.
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 ECO:0000313|EMBL:BAJ02745.1};
GN OrderedLocusNames=SVI_2774 {ECO:0000313|EMBL:BAJ02745.1};
OS Shewanella violacea (strain JCM 10179 / CIP 106290 / LMG 19151 / DSS12).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=637905 {ECO:0000313|EMBL:BAJ02745.1, ECO:0000313|Proteomes:UP000002350};
RN [1] {ECO:0000313|Proteomes:UP000002350}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10179 / CIP 106290 / LMG 19151 / DSS12
RC {ECO:0000313|Proteomes:UP000002350};
RX PubMed=20458400; DOI=10.1039/c000396d;
RA Aono E., Baba T., Ara T., Nishi T., Nakamichi T., Inamoto E., Toyonaga H.,
RA Hasegawa M., Takai Y., Okumura Y., Baba M., Tomita M., Kato C., Oshima T.,
RA Nakasone K., Mori H.;
RT "Complete genome sequence and comparative analysis of Shewanella violacea,
RT a psychrophilic and piezophilic bacterium from deep sea floor sediments.";
RL Mol. Biosyst. 6:1216-1226(2010).
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; AP011177; BAJ02745.1; -; Genomic_DNA.
DR RefSeq; WP_013052045.1; NC_014012.1.
DR AlphaFoldDB; D4ZM46; -.
DR STRING; 637905.SVI_2774; -.
DR KEGG; svo:SVI_2774; -.
DR eggNOG; COG0524; Bacteria.
DR HOGENOM; CLU_060237_0_0_6; -.
DR OrthoDB; 5288159at2; -.
DR UniPathway; UPA00591; UER00647.
DR UniPathway; UPA00909; -.
DR Proteomes; UP000002350; Chromosome.
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|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_02246};
KW Kinase {ECO:0000256|HAMAP-Rule:MF_02246, ECO:0000313|EMBL:BAJ02745.1};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_02246};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_02246}; Purine salvage {ECO:0000256|HAMAP-Rule:MF_02246};
KW Reference proteome {ECO:0000313|Proteomes:UP000002350};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_02246}.
FT DOMAIN 134..294
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; 48039 MW; B7332E7B0F16531E CRC64;
MKFPGQRKSK HYFPVQNRDP LLAQLTQQPL RFPTYITGID QTLVDIEAKV ADELLERYKL
PKGSSTLIDD ANAHALYSEL KQHNLISDEF AGGTIGNTVH NYSILADDRS VLFGVMSNNI
EVGSYAYRYL CNTSSKVDLN YLQPVDGAIG RCFTLISECG ERTFAISKGS MDKLTPEYID
KDLVQGASAL VLTAYLMRAS GDDQMTQAAL TAIEYAKEVG VPVVLTLGTR FLIEEDPSWW
RAFILENVTI LAMNEDEGEA LTGFKDPLLA SEAALELCDM VLTTAGPIGL YTAGYTEDAE
KRVTSNTLLP GSIPEFNRYE FSRPKLKSAC DEPIKVYAHI SPYMGGPEKI RNTNGAGDGA
LSALLHDLAS NTFHKANVPG SSKHKRDGLC YSSFSQICKY ANRVAYEVLA QHSPRLSRGL
PEREDSLEEV YWER
//
