ID   APLK_PECAS              Reviewed;         496 AA.
AC   Q6D5T8;
DT   16-JAN-2019, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Apulose kinase {ECO:0000303|PubMed:29867142};
DE            EC=2.7.1.- {ECO:0000269|PubMed:29867142};
GN   Name=aplK {ECO:0000303|PubMed:29867142};
GN   OrderedLocusNames=ECA1952 {ECO:0000312|EMBL:CAG74854.1};
OS   Pectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672) (Erwinia
OS   carotovora subsp. atroseptica).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Pectobacterium.
OX   NCBI_TaxID=218491;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCRI 1043 / ATCC BAA-672;
RX   PubMed=15263089; DOI=10.1073/pnas.0402424101;
RA   Bell K.S., Sebaihia M., Pritchard L., Holden M.T.G., Hyman L.J.,
RA   Holeva M.C., Thomson N.R., Bentley S.D., Churcher L.J.C., Mungall K.,
RA   Atkin R., Bason N., Brooks K., Chillingworth T., Clark K., Doggett J.,
RA   Fraser A., Hance Z., Hauser H., Jagels K., Moule S., Norbertczak H.,
RA   Ormond D., Price C., Quail M.A., Sanders M., Walker D., Whitehead S.,
RA   Salmond G.P.C., Birch P.R.J., Parkhill J., Toth I.K.;
RT   "Genome sequence of the enterobacterial phytopathogen Erwinia carotovora
RT   subsp. atroseptica and characterization of virulence factors.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:11105-11110(2004).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX   PubMed=29867142; DOI=10.1038/s41589-018-0067-7;
RA   Carter M.S., Zhang X., Huang H., Bouvier J.T., Francisco B.S.,
RA   Vetting M.W., Al-Obaidi N., Bonanno J.B., Ghosh A., Zallot R.G.,
RA   Andersen H.M., Almo S.C., Gerlt J.A.;
RT   "Functional assignment of multiple catabolic pathways for D-apiose.";
RL   Nat. Chem. Biol. 14:696-705(2018).
CC   -!- FUNCTION: Involved in catabolism of D-apiose. Catalyzes phosphorylation
CC       of apulose to form apulose 4-phosphate. {ECO:0000269|PubMed:29867142}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=apulose + ATP = ADP + apulose 4-phosphate + H(+);
CC         Xref=Rhea:RHEA:57020, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:141348, ChEBI:CHEBI:141351, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000269|PubMed:29867142};
CC   -!- PATHWAY: Carbohydrate metabolism. {ECO:0000269|PubMed:29867142}.
CC   -!- SIMILARITY: Belongs to the FGGY kinase family. {ECO:0000305}.
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DR   EMBL; BX950851; CAG74854.1; -; Genomic_DNA.
DR   RefSeq; WP_011093516.1; NC_004547.2.
DR   AlphaFoldDB; Q6D5T8; -.
DR   SMR; Q6D5T8; -.
DR   STRING; 218491.ECA1952; -.
DR   EnsemblBacteria; CAG74854; CAG74854; ECA1952.
DR   KEGG; eca:ECA1952; -.
DR   PATRIC; fig|218491.5.peg.1985; -.
DR   eggNOG; COG0554; Bacteria.
DR   HOGENOM; CLU_009281_2_3_6; -.
DR   OMA; DAVAWMA; -.
DR   OrthoDB; 233605at2; -.
DR   BioCyc; MetaCyc:MON-20955; -.
DR   BRENDA; 2.7.1.233; 9330.
DR   Proteomes; UP000007966; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016773; F:phosphotransferase activity, alcohol group as acceptor; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd07791; FGGY_GK2_bacteria; 1.
DR   InterPro; IPR042016; Apulose_kinase.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR000577; Carb_kinase_FGGY.
DR   InterPro; IPR018485; Carb_kinase_FGGY_C.
DR   InterPro; IPR018484; Carb_kinase_FGGY_N.
DR   Pfam; PF02782; FGGY_C; 1.
DR   Pfam; PF00370; FGGY_N; 1.
DR   PIRSF; PIRSF000538; GlpK; 1.
DR   SUPFAM; SSF53067; SSF53067; 2.
PE   1: Evidence at protein level;
KW   ATP-binding; Carbohydrate metabolism; Kinase; Nucleotide-binding;
KW   Reference proteome; Transferase.
FT   CHAIN           1..496
FT                   /note="Apulose kinase"
FT                   /id="PRO_0000446024"
FT   BINDING         13..15
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P0A6F3"
FT   BINDING         267
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P0A6F3"
FT   BINDING         308
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P0A6F3"
FT   BINDING         408..412
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P0A6F3"
SQ   SEQUENCE   496 AA;  53214 MW;  27ADBA2193D79EE8 CRC64;
     MYTPVILAID EGTTNAKAIA VDERGRILAK AAVALQVTHP QPGRSEQDAM AIWRAVCQAA
     EVCLSSLHRA QVVGVAISNQ RESVLIWDRQ TGKPMTPLVS WQDRRAEKFC QALQGSAEAR
     LIESRTGLQV DPLFPAAKLH AMLAELPNGV ARAMQGELCI GTVDCWLNWQ FSGGRAFSTD
     YSNAARTQLF NIHRGCWDED LLALFGIPSV CLPAVTPSSA LHGHTGVTGI SGLAACVPIV
     ALIGDSHAAL YGQGITQSGE IKATYGTGSS LMTTINTPHL HATGLSTTIA WHDGELRYAL
     EGNITHTGSG FAWIGQMLGV PSVTQLTELA LSAESNQGVF FVPALSGLGA PYWDVQARGL
     LCGLCDATTP AIIARAGLEA IAYQVADVFF AMEQVSQAAL PALRVDGGAT QNRWLMQFQA
     DLLQRPLIRN HNAEVSALGA AYLGGKMLGW WEHNEQIAAL PREVEVIEPS ATNHAILESY
     QQWRTAVARA RLRPEA