ID Q8X5M4_ECO57 Unreviewed; 309 AA.
AC Q8X5M4; A0A6M0JG87; Q7AA01;
DT 01-MAR-2002, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 4.
DT 27-MAR-2024, entry version 127.
DE RecName: Full=KDG kinase {ECO:0000256|ARBA:ARBA00044254};
GN Name=kdgK {ECO:0000313|EMBL:BAB37829.2};
GN ORFNames=ECs_4406 {ECO:0000313|EMBL:BAB37829.2};
OS Escherichia coli O157:H7.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334 {ECO:0000313|EMBL:BAB37829.2, ECO:0000313|Proteomes:UP000000558};
RN [1] {ECO:0000313|EMBL:BAB37829.2, ECO:0000313|Proteomes:UP000000558}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC
RC {ECO:0000313|Proteomes:UP000000558};
RX PubMed=11258796; DOI=.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
CC -!- PATHWAY: Carbohydrate acid metabolism; 2-dehydro-3-deoxy-D-gluconate
CC degradation; D-glyceraldehyde 3-phosphate and pyruvate from 2-dehydro-
CC 3-deoxy-D-gluconate: step 1/2. {ECO:0000256|ARBA:ARBA00043951}.
CC -!- SIMILARITY: Belongs to the carbohydrate kinase PfkB family.
CC {ECO:0000256|ARBA:ARBA00010688}.
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DR EMBL; BA000007; BAB37829.2; -; Genomic_DNA.
DR RefSeq; NP_312433.1; NC_002695.1.
DR RefSeq; WP_001301733.1; NZ_VOAI01000004.1.
DR AlphaFoldDB; Q8X5M4; -.
DR STRING; 155864.Z4940; -.
DR GeneID; 915730; -.
DR KEGG; ecs:ECs_4406; -.
DR PATRIC; fig|386585.9.peg.4605; -.
DR eggNOG; COG0524; Bacteria.
DR HOGENOM; CLU_027634_8_1_6; -.
DR OMA; MAMFYAN; -.
DR Proteomes; UP000000558; Chromosome.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0071704; P:organic substance metabolic process; IEA:UniProt.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd01166; KdgK; 1.
DR Gene3D; 3.40.1190.20; -; 1.
DR InterPro; IPR002173; Carboh/pur_kinase_PfkB_CS.
DR InterPro; IPR011611; PfkB_dom.
DR InterPro; IPR029056; Ribokinase-like.
DR PANTHER; PTHR43085:SF15; 2-DEHYDRO-3-DEOXYGLUCONOKINASE; 1.
DR PANTHER; PTHR43085; HEXOKINASE FAMILY MEMBER; 1.
DR Pfam; PF00294; PfkB; 1.
DR SUPFAM; SSF53613; Ribokinase-like; 1.
DR PROSITE; PS00584; PFKB_KINASES_2; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000000558};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 3..305
FT /note="Carbohydrate kinase PfkB"
FT /evidence="ECO:0000259|Pfam:PF00294"
SQ SEQUENCE 309 AA; 33947 MW; 52B925FCC2530E83 CRC64;
MSKKIAVIGE CMIELSEKGA DVKRGFGGDT LNTSVYIARQ VDPAALTVHY VTALGTDSFS
QQMLDAWHGE NVDTSLTQRM ENRLPGLYYI ETDSTGERTF YYWRNEAAAK FWLESDQSAA
ICEELANFDY LYLSGISLAI LSPTSREKLL SLLRECRANG GKVIFDNNYR PRLWASKEET
QQVYQQMLEC TDIAFLTLDD EDALWGQQPV EDVIARTHNA GVKEVVVKRG ADSCLVSIAG
EGLVDVPAVK LPKEKVIDTT AAGDSFSAGY LAVRLTGGSA ENAAKRGHLT ASTVIQYRGA
IIPREAMPA
//
