ID   FRLD_BACSU              Reviewed;         284 AA.
AC   O32153;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=Fructosamine kinase FrlD;
DE            EC=2.7.1.-;
GN   Name=frlD; Synonyms=yurL; OrderedLocusNames=BSU32570;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [2]
RP   FUNCTION, SUBSTRATE SPECIFICITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=15556630; DOI=10.1016/j.febslet.2004.10.049;
RA   Wiame E., Duquenne A., Delpierre G., Van Schaftingen E.;
RT   "Identification of enzymes acting on alpha-glycated amino acids in Bacillus
RT   subtilis.";
RL   FEBS Lett. 577:469-472(2004).
CC   -!- FUNCTION: Catalyzes the phosphorylation of a range of fructosamines to
CC       fructosamine 6-phosphates. {ECO:0000269|PubMed:15556630}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.1 mM for fructosevaline (at 30 degrees Celsius and pH 7.1)
CC         {ECO:0000269|PubMed:15556630};
CC         KM=0.6 mM for fructoseglycine (at 30 degrees Celsius and pH 7.1)
CC         {ECO:0000269|PubMed:15556630};
CC         KM=6 mM for fructoseglycylglycine (at 30 degrees Celsius and pH 7.1)
CC         {ECO:0000269|PubMed:15556630};
CC         KM=14 mM for fructoselysine (at 30 degrees Celsius and pH 7.1)
CC         {ECO:0000269|PubMed:15556630};
CC         KM=47 mM for 1-deoxy-1-morpholinofructose (DMF)(at 30 degrees Celsius
CC         and pH 7.1) {ECO:0000269|PubMed:15556630};
CC         Vmax=3 umol/min/mg enzyme with fructosevaline as substrate (at 30
CC         degrees Celsius and pH 7.1) {ECO:0000269|PubMed:15556630};
CC         Vmax=5 umol/min/mg enzyme with 1-deoxy-1-morpholinofructose (DMF) as
CC         substrate (at 30 degrees Celsius and pH 7.1)
CC         {ECO:0000269|PubMed:15556630};
CC         Vmax=7 umol/min/mg enzyme with fructoselysine as substrate (at 30
CC         degrees Celsius and pH 7.1) {ECO:0000269|PubMed:15556630};
CC         Vmax=10 umol/min/mg enzyme with fructoseglycine as substrate (at 30
CC         degrees Celsius and pH 7.1) {ECO:0000269|PubMed:15556630};
CC         Vmax=10 umol/min/mg enzyme with fructoseglycylglycine as substrate
CC         (at 30 degrees Celsius and pH 7.1) {ECO:0000269|PubMed:15556630};
CC   -!- SIMILARITY: Belongs to the carbohydrate kinase PfkB family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AL009126; CAB15247.1; -; Genomic_DNA.
DR   PIR; C70018; C70018.
DR   RefSeq; NP_391137.1; NC_000964.3.
DR   RefSeq; WP_003228626.1; NZ_JNCM01000033.1.
DR   AlphaFoldDB; O32153; -.
DR   SMR; O32153; -.
DR   IntAct; O32153; 1.
DR   STRING; 224308.BSU32570; -.
DR   PaxDb; O32153; -.
DR   PRIDE; O32153; -.
DR   EnsemblBacteria; CAB15247; CAB15247; BSU_32570.
DR   GeneID; 936704; -.
DR   KEGG; bsu:BSU32570; -.
DR   PATRIC; fig|224308.179.peg.3527; -.
DR   eggNOG; COG0524; Bacteria.
DR   InParanoid; O32153; -.
DR   OMA; DYGFVSC; -.
DR   PhylomeDB; O32153; -.
DR   BioCyc; BSUB:BSU32570-MON; -.
DR   BRENDA; 2.7.1.218; 658.
DR   SABIO-RK; O32153; -.
DR   Proteomes; UP000001570; 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   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   Pfam; PF00294; PfkB; 1.
DR   SUPFAM; SSF53613; SSF53613; 1.
DR   PROSITE; PS00584; PFKB_KINASES_2; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Carbohydrate metabolism; Kinase; Nucleotide-binding;
KW   Reference proteome; Transferase.
FT   CHAIN           1..284
FT                   /note="Fructosamine kinase FrlD"
FT                   /id="PRO_0000080142"
SQ   SEQUENCE   284 AA;  30986 MW;  3AE3D0F6A33BD430 CRC64;
     MKLIAVGDNV VDYYQDQETF YPGGNALNVA VLAKRLGHES SYIGIVGNDE AAAHLLNVLK
     LEQVNADYIR QAHGENGMAI VTLDEQGDRI FVRSNKGGIQ SRLRLAFQEK DVSFISGHDL
     LHTSVYSRLE NDLPQLCGLV PVSFDFSTNR EDDYLRRVCP YVTYAFFSGS DLSESECGEL
     AKTAHGYGAK MVCMTRGGQG AILSAGDRVY HQPIVEADII DTLGAGDSFI AGFLTAFCVK
     QDITYALRQA AETAAKTCGV YGAFGYGYPY RLEDGGSSEK TRIL