GenomeNet

Database: UniProt
Entry: A0A1M5VFC3_9VIBR
LinkDB: A0A1M5VFC3_9VIBR
Original site: A0A1M5VFC3_9VIBR 
ID   A0A1M5VFC3_9VIBR        Unreviewed;       434 AA.
AC   A0A1M5VFC3;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
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_1 {ECO:0000313|EMBL:SHH73875.1};
GN   Synonyms=gsk {ECO:0000256|HAMAP-Rule:MF_02246};
GN   ORFNames=VA7868_00371 {ECO:0000313|EMBL:SHH73875.1};
OS   Vibrio aerogenes CECT 7868.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=1216006 {ECO:0000313|EMBL:SHH73875.1, ECO:0000313|Proteomes:UP000184608};
RN   [1] {ECO:0000313|EMBL:SHH73875.1, ECO:0000313|Proteomes:UP000184608}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT 7868 {ECO:0000313|EMBL:SHH73875.1,
RC   ECO:0000313|Proteomes:UP000184608};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) 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}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_02246}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; FQXZ01000005; SHH73875.1; -; Genomic_DNA.
DR   RefSeq; WP_073602144.1; NZ_FQXZ01000005.1.
DR   AlphaFoldDB; A0A1M5VFC3; -.
DR   STRING; 1216006.VA7868_00371; -.
DR   OrthoDB; 5288159at2; -.
DR   UniPathway; UPA00591; UER00647.
DR   UniPathway; UPA00909; -.
DR   Proteomes; UP000184608; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0106366; F:guanosine kinase activity; IEA:UniProtKB-EC.
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:SHH73875.1};
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:UP000184608};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_02246, ECO:0000313|EMBL:SHH73875.1}.
FT   DOMAIN          74..291
FT                   /note="Carbohydrate kinase PfkB"
FT                   /evidence="ECO:0000259|Pfam:PF00294"
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;  48462 MW;  043770C189A60E2E CRC64;
     MKFPGQRKSR HYFPVSERDT LIMPNTANHT LTLNHVIGMA QVIVDIEAKV PDALIEKYEL
     VIGQSLVIDD AKAEALYQEL SESQLITDQF AGGTIGNTLH NYSVLADARS TLLGVMSENI
     RIGSYGYQYL SNTSSRVDLN YLQGVDGPIG RCFTLISENG ERTFAINAGK MNFLRPESIP
     QEIFKTASAL VLSSYLLRCK AHEPISDAAM QSIEYAKKYQ VPIVLTLGTK YMIEQDVDFW
     QSFIKNHITV VAMNEEEAQA LTGIADPLLA ADKTLDWADM VLCTAGPVGL FMAGYTDDAA
     KRETRRPLLP GAIAEFNQYE FSRPMRKSDC TRPVRVYSHI SPYMGGPEKI KNTNGAGDAA
     LAAVLHDMAA NEFHQANVPN SVKHDYRCLT YSSFSQVCKY ANRVSYEVLV QHSPRLSRGL
     PEREDCLEES YWER
//
DBGET integrated database retrieval system