IOLC_MESH2
ID IOLC_MESH2 Reviewed; 338 AA.
AC Q601P9;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 2.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=5-dehydro-2-deoxygluconokinase {ECO:0000255|HAMAP-Rule:MF_01668};
DE EC=2.7.1.92 {ECO:0000255|HAMAP-Rule:MF_01668};
DE AltName: Full=2-deoxy-5-keto-D-gluconate kinase {ECO:0000255|HAMAP-Rule:MF_01668};
DE Short=DKG kinase {ECO:0000255|HAMAP-Rule:MF_01668};
GN Name=iolC {ECO:0000255|HAMAP-Rule:MF_01668}; OrderedLocusNames=mhp152;
OS Mesomycoplasma hyopneumoniae (strain 232) (Mycoplasma hyopneumoniae).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mesomycoplasma.
OX NCBI_TaxID=295358;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=232;
RX PubMed=15489423; DOI=10.1128/jb.186.21.7123-7133.2004;
RA Minion F.C., Lefkowitz E.J., Madsen M.L., Cleary B.J., Swartzell S.M.,
RA Mahairas G.G.;
RT "The genome sequence of Mycoplasma hyopneumoniae strain 232, the agent of
RT swine mycoplasmosis.";
RL J. Bacteriol. 186:7123-7133(2004).
CC -!- FUNCTION: Catalyzes the phosphorylation of 5-dehydro-2-deoxy-D-
CC gluconate (2-deoxy-5-keto-D-gluconate or DKG) to 6-phospho-5-dehydro-2-
CC deoxy-D-gluconate (DKGP). {ECO:0000255|HAMAP-Rule:MF_01668}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-dehydro-2-deoxy-D-gluconate + ATP = 6-phospho-5-dehydro-2-
CC deoxy-D-gluconate + ADP + H(+); Xref=Rhea:RHEA:13497,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16669, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:57949, ChEBI:CHEBI:456216; EC=2.7.1.92;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01668};
CC -!- PATHWAY: Polyol metabolism; myo-inositol degradation into acetyl-CoA;
CC acetyl-CoA from myo-inositol: step 5/7. {ECO:0000255|HAMAP-
CC Rule:MF_01668}.
CC -!- SIMILARITY: Belongs to the carbohydrate kinase PfkB family.
CC {ECO:0000255|HAMAP-Rule:MF_01668}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAV27744.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE017332; AAV27744.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_044284777.1; NC_006360.1.
DR AlphaFoldDB; Q601P9; -.
DR SMR; Q601P9; -.
DR STRING; 295358.mhp152; -.
DR EnsemblBacteria; AAV27744; AAV27744; mhp152.
DR KEGG; mhy:mhp152; -.
DR eggNOG; COG0524; Bacteria.
DR HOGENOM; CLU_027634_6_0_14; -.
DR UniPathway; UPA00076; UER00146.
DR Proteomes; UP000006822; Chromosome.
DR GO; GO:0047590; F:5-dehydro-2-deoxygluconokinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0019310; P:inositol catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 2.20.150.10; -; 1.
DR Gene3D; 3.40.1190.20; -; 1.
DR HAMAP; MF_01668; IolC; 1.
DR InterPro; IPR022841; DKG_kinase_firmi.
DR InterPro; IPR030830; Myo_inos_IolC.
DR InterPro; IPR023314; Myo_inos_IolC-like_sf.
DR InterPro; IPR011611; PfkB_dom.
DR InterPro; IPR029056; Ribokinase-like.
DR Pfam; PF00294; PfkB; 1.
DR SUPFAM; SSF53613; SSF53613; 1.
DR TIGRFAMs; TIGR04382; myo_inos_iolC_N; 1.
PE 3: Inferred from homology;
KW ATP-binding; Kinase; Nucleotide-binding; Transferase.
FT CHAIN 1..338
FT /note="5-dehydro-2-deoxygluconokinase"
FT /id="PRO_0000352305"
SQ SEQUENCE 338 AA; 38484 MW; DFC8447C99F11490 CRC64;
MKKEFDFILI GRITIDFNPM DYYNNLENSS LFKKYIGGSA ANIAIGLSRL KNKVGFFGSV
SDDQFGNFVL NVFEKEKIDI SHIKKTKDHK LGLTFTEMLS EEKSTILMYR DNVADLQIDV
SDIDLDYILR TKILVISGTS LAKSPSREAV LKALFLAKNN GIKVVFDIDY RPYSWKNLDE
VSLYYQIVAQ NSDLIIGSYE EIQLTSRFCL ENPENLIDDD YAKYWLKFVD LIIIKNGKKG
SKLYQKDKKL VAKVVPVKML KGYGGGDAYA SLFLDHYLKN ESDLENGLAL ATSAASIMVQ
SHSSFDLPDY QKILEFKDNA LKSDPDLVQK KEWNAFKK
