ID E7GU27_CLOSY Unreviewed; 338 AA.
AC E7GU27;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=5-dehydro-2-deoxygluconokinase {ECO:0000256|HAMAP-Rule:MF_01668};
DE EC=2.7.1.92 {ECO:0000256|HAMAP-Rule:MF_01668};
DE AltName: Full=2-deoxy-5-keto-D-gluconate kinase {ECO:0000256|HAMAP-Rule:MF_01668};
DE Short=DKG kinase {ECO:0000256|HAMAP-Rule:MF_01668};
GN Name=iolC {ECO:0000256|HAMAP-Rule:MF_01668};
GN ORFNames=HMPREF9474_04422 {ECO:0000313|EMBL:EGA91679.1};
OS [Clostridium] symbiosum WAL-14163.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=742740 {ECO:0000313|EMBL:EGA91679.1, ECO:0000313|Proteomes:UP000002970};
RN [1] {ECO:0000313|EMBL:EGA91679.1, ECO:0000313|Proteomes:UP000002970}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WAL-14163 {ECO:0000313|EMBL:EGA91679.1,
RC ECO:0000313|Proteomes:UP000002970};
RA Earl A., Ward D., Feldgarden M., Gevers D., Finegold S.M., Summanen P.H.,
RA Molitoris D.R., Vaisanen M.L., Daigneault M., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA Heilman E., Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P.,
RA Mehta T., Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M.,
RA Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S.,
RA White J., Yandava C., Nusbaum C., Birren B.;
RT "The Genome Sequence of Clostridium symbiosum strain WAL-14163.";
RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
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:0000256|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:0000256|HAMAP-Rule:MF_01668};
CC -!- PATHWAY: Polyol metabolism; myo-inositol degradation into acetyl-CoA;
CC acetyl-CoA from myo-inositol: step 5/7. {ECO:0000256|HAMAP-
CC Rule:MF_01668}.
CC -!- SIMILARITY: Belongs to the carbohydrate kinase PfkB family.
CC {ECO:0000256|ARBA:ARBA00010688, ECO:0000256|HAMAP-Rule:MF_01668}.
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:EGA91679.1}.
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DR EMBL; ADLQ01000104; EGA91679.1; -; Genomic_DNA.
DR RefSeq; WP_003504895.1; NZ_GL834322.1.
DR AlphaFoldDB; E7GU27; -.
DR STRING; 1512.GCA_900049235_04779; -.
DR GeneID; 57967309; -.
DR eggNOG; COG0524; Bacteria.
DR HOGENOM; CLU_027634_6_0_9; -.
DR UniPathway; UPA00076; UER00146.
DR Proteomes; UP000002970; Unassembled WGS sequence.
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 CDD; cd01166; KdgK; 1.
DR Gene3D; 3.40.1190.20; -; 1.
DR Gene3D; 2.20.150.10; putative 5-dehydro-2- deoxygluconokinase; 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 NCBIfam; TIGR04382; myo_inos_iolC_N; 1.
DR PANTHER; PTHR43085:SF49; 5-DEHYDRO-2-DEOXYGLUCONOKINASE; 1.
DR PANTHER; PTHR43085; HEXOKINASE FAMILY MEMBER; 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_01668};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_01668};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01668}; Reference proteome {ECO:0000313|Proteomes:UP000002970};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01668}.
FT DOMAIN 14..315
FT /note="Carbohydrate kinase PfkB"
FT /evidence="ECO:0000259|Pfam:PF00294"
SQ SEQUENCE 338 AA; 37025 MW; 40DBBBDAA76AE67D CRC64;
MKYITFDEDK PYDLILLGRV AIDFNPLDYN KPLYESETFK KYVGGSPANI AVGMARLGKK
IGFFAKVSDD QFGTFVERYF ENEGIDISHI SRCQNGEKLG LTFTEILSPT ESSILMYRGS
IADLQLSVED IDEEYIKSAK ALLISGTALA ASPSREAALK AVSLAKKNQV PVIFDIDYRA
YTWKNHDEIA IYYSAVASQA DIILGSREEY DLTENLIAPG RTDVETAKAW CAKGARIVVI
KHGREGSTAY AYDGNSFSIK PFPVKALKGF GGGDGYAAAF LYGLLEGKEL LDCLEMGSAE
AAMLVASHAC SADMPGAEAL YTFIRQCKDE YGEMVARA
//
