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Database: UniProt
Entry: K6ZF63_9ALTE
LinkDB: K6ZF63_9ALTE
Original site: K6ZF63_9ALTE 
ID   K6ZF63_9ALTE            Unreviewed;       305 AA.
AC   K6ZF63;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=KDG kinase {ECO:0000256|ARBA:ARBA00044254};
GN   Name=kdgK {ECO:0000313|EMBL:GAC22050.1};
GN   ORFNames=GARC_5115 {ECO:0000313|EMBL:GAC22050.1};
OS   Paraglaciecola arctica BSs20135.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadaceae; Paraglaciecola.
OX   NCBI_TaxID=493475 {ECO:0000313|EMBL:GAC22050.1, ECO:0000313|Proteomes:UP000006327};
RN   [1] {ECO:0000313|EMBL:GAC22050.1, ECO:0000313|Proteomes:UP000006327}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BSs20135 {ECO:0000313|EMBL:GAC22050.1,
RC   ECO:0000313|Proteomes:UP000006327};
RX   PubMed=25009843;
RA   Qin Q.-L., Xie B.-B., Yu Y., Shu Y.-L., Rong J.-C., Zhang Y.-J.,
RA   Zhao D.-L., Chen X.-L., Zhang X.-Y., Chen B., Zhou B.-C., Zhang Y.-Z.;
RT   "Comparative genomics of the marine bacterial genus Glaciecola reveals the
RT   high degree of genomic diversity and genomic characteristic for cold
RT   adaptation.";
RL   Environ. Microbiol. 16:1642-1653(2014).
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}.
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:GAC22050.1}.
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DR   EMBL; BAEO01000067; GAC22050.1; -; Genomic_DNA.
DR   AlphaFoldDB; K6ZF63; -.
DR   STRING; 493475.GARC_5115; -.
DR   eggNOG; COG0524; Bacteria.
DR   OrthoDB; 9776822at2; -.
DR   Proteomes; UP000006327; Unassembled WGS sequence.
DR   GO; GO:0008673; F:2-dehydro-3-deoxygluconokinase activity; IEA:UniProtKB-EC.
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   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Kinase {ECO:0000313|EMBL:GAC22050.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006327};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:GAC22050.1}.
FT   DOMAIN          1..293
FT                   /note="Carbohydrate kinase PfkB"
FT                   /evidence="ECO:0000259|Pfam:PF00294"
SQ   SEQUENCE   305 AA;  33332 MW;  CF2AF0D32E53FF43 CRC64;
     MKKVVVFGEC MLELVSKQGD TLHKGFAGDT YNTAIYLNRC AANVSVSYLT ALGNDLLSSE
     LLSKMDEEGI NTEYVLRSED RNLGLYMVHT DADGERTFTY WRQNSAATQS LNLLKGHKVE
     ADVFYFSAIS LAILDNDQKA KLFELMGELK GTGCKISFDP NYRPKLWTSK IEAQKWTDAA
     YAVSDLVFPG GDDHAELYGH MNAEAILQHL AQYEIEEIVV KNGASSVNIF IDNKLDSVPI
     EPVEKVVDTT AAGDGFNGGY LAARLTGSSH TDSARYGAKV AATVIGFPGA IIDKQALATH
     VNLIQ
//
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