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Database: UniProt
Entry: I2B436_SHIBC
LinkDB: I2B436_SHIBC
Original site: I2B436_SHIBC 
ID   I2B436_SHIBC            Unreviewed;       310 AA.
AC   I2B436; K6WFN1;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   11-JUL-2012, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   RecName: Full=KDG kinase {ECO:0000256|ARBA:ARBA00044254};
GN   Name=kdgK {ECO:0000313|EMBL:AFJ45290.1};
GN   OrderedLocusNames=EBL_c01550 {ECO:0000313|EMBL:AFJ45290.1};
OS   Shimwellia blattae (strain ATCC 29907 / DSM 4481 / JCM 1650 / NBRC 105725 /
OS   CDC 9005-74) (Escherichia blattae).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shimwellia.
OX   NCBI_TaxID=630626 {ECO:0000313|EMBL:AFJ45290.1, ECO:0000313|Proteomes:UP000001955};
RN   [1] {ECO:0000313|EMBL:AFJ45290.1, ECO:0000313|Proteomes:UP000001955}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29907 / DSM 4481 / JCM 1650 / NBRC 105725 / CDC 9005-74
RC   {ECO:0000313|Proteomes:UP000001955};
RX   PubMed=22843577; DOI=10.1128/JB.00829-12;
RA   Brzuszkiewicz E., Waschkowitz T., Wiezer A., Daniel R.;
RT   "Complete genome sequence of the B12-producing Shimwellia blattae strain
RT   DSM 4481, isolated from a cockroach.";
RL   J. Bacteriol. 194:4436-4436(2012).
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; CP001560; AFJ45290.1; -; Genomic_DNA.
DR   RefSeq; WP_002440628.1; NZ_BAHA01000007.1.
DR   AlphaFoldDB; I2B436; -.
DR   STRING; 630626.EBL_c01550; -.
DR   KEGG; ebt:EBL_c01550; -.
DR   PATRIC; fig|630626.3.peg.160; -.
DR   eggNOG; COG0524; Bacteria.
DR   HOGENOM; CLU_027634_8_1_6; -.
DR   OrthoDB; 9776822at2; -.
DR   Proteomes; UP000001955; 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   Kinase {ECO:0000313|EMBL:AFJ45290.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001955};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          4..306
FT                   /note="Carbohydrate kinase PfkB"
FT                   /evidence="ECO:0000259|Pfam:PF00294"
SQ   SEQUENCE   310 AA;  33898 MW;  43D40482A2CC2B27 CRC64;
     MSTQKIAVIG ECMIELSEKG SSVSRGFGGD TLNTSVYIAR QVAPQALSVH YVTALGQDSF
     SQQMLDAWQA ENVDTSLTQR MENRLPGLYY IETDATGERT FYYWRNEAAA RYWLESADAD
     AICAQLATFD YLYLSGISLA ILSPQSREKL LGLLRQCRAN GGKVIFDNNY RPRLWASKEE
     TQQVYQQMLS CTDIAFLTLD DEDALWGEKP VDEVIARTQA AGVSEVVIKR GADSCLVAEK
     GQPLVEVPAV KLPKERVVDT TAAGDSFSAG YLSVRLTGGS TAAAAQRGHL TASTVIQYRG
     AIIPREAMPA
//
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