SCRK_BACSU
ID SCRK_BACSU Reviewed; 299 AA.
AC O05510;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Putative fructokinase;
DE EC=2.7.1.4;
DE AltName: Full=Glucomannan utilization protein E;
GN Name=gmuE; Synonyms=ydhR; OrderedLocusNames=BSU05860;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / JH642;
RX PubMed=9202461; DOI=10.1099/00221287-143-6-1861;
RA Sadaie Y., Yata K., Fujita M., Sagai H., Itaya M., Kasahara Y.,
RA Ogasawara N.;
RT "Nucleotide sequence and analysis of the phoB-rrnE-groESL region of the
RT Bacillus subtilis chromosome.";
RL Microbiology 143:1861-1866(1997).
RN [2]
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 [3]
RP INDUCTION, AND FUNCTION IN GLUCOMANNAN UTILIZATION.
RC STRAIN=168;
RX PubMed=18177310; DOI=10.1111/j.1574-6968.2007.01018.x;
RA Sadaie Y., Nakadate H., Fukui R., Yee L.M., Asai K.;
RT "Glucomannan utilization operon of Bacillus subtilis.";
RL FEMS Microbiol. Lett. 279:103-109(2008).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH ADP AND ZINC IONS.
RG Midwest center for structural genomics (MCSG);
RT "Structure of a putative fructokinase from Bacillus subtilis.";
RL Submitted (FEB-2009) to the PDB data bank.
CC -!- FUNCTION: Seems to be involved in the degradation of glucomannan.
CC {ECO:0000269|PubMed:18177310}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + D-fructose = ADP + D-fructose 6-phosphate + H(+);
CC Xref=Rhea:RHEA:16125, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:37721, ChEBI:CHEBI:61527, ChEBI:CHEBI:456216; EC=2.7.1.4;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305};
CC -!- ACTIVITY REGULATION: Inhibited by zinc ions. {ECO:0000305}.
CC -!- INDUCTION: Up-regulated by konjac glucomannan and by cellobiose and
CC mannobiose, the possible degradation products of glucomannan. Repressed
CC by glucose via the carbon catabolite repression system. Also repressed
CC by GmuR. {ECO:0000269|PubMed:18177310}.
CC -!- SIMILARITY: Belongs to the ROK (NagC/XylR) family. {ECO:0000305}.
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DR EMBL; D88802; BAA19710.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB12405.1; -; Genomic_DNA.
DR PIR; F69785; F69785.
DR RefSeq; NP_388467.1; NC_000964.3.
DR RefSeq; WP_003234095.1; NZ_JNCM01000031.1.
DR PDB; 1XC3; X-ray; 2.10 A; A=1-299.
DR PDB; 3LM9; X-ray; 2.45 A; A=1-299.
DR PDB; 3OHR; X-ray; 1.66 A; A=1-299.
DR PDBsum; 1XC3; -.
DR PDBsum; 3LM9; -.
DR PDBsum; 3OHR; -.
DR AlphaFoldDB; O05510; -.
DR SMR; O05510; -.
DR STRING; 224308.BSU05860; -.
DR PaxDb; O05510; -.
DR PRIDE; O05510; -.
DR DNASU; 938016; -.
DR EnsemblBacteria; CAB12405; CAB12405; BSU_05860.
DR GeneID; 938016; -.
DR KEGG; bsu:BSU05860; -.
DR PATRIC; fig|224308.179.peg.630; -.
DR eggNOG; COG1940; Bacteria.
DR InParanoid; O05510; -.
DR OMA; GHIYIRR; -.
DR PhylomeDB; O05510; -.
DR BioCyc; BSUB:BSU05860-MON; -.
DR BRENDA; 2.7.1.4; 658.
DR EvolutionaryTrace; O05510; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008865; F:fructokinase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR000600; ROK.
DR Pfam; PF00480; ROK; 1.
DR SUPFAM; SSF53067; SSF53067; 1.
DR PROSITE; PS01125; ROK; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Carbohydrate metabolism; Kinase; Magnesium;
KW Metal-binding; Nucleotide-binding; Polysaccharide degradation;
KW Reference proteome; Transferase; Zinc.
FT CHAIN 1..299
FT /note="Putative fructokinase"
FT /id="PRO_0000095681"
FT BINDING 130
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 153
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 168
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 171
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 174
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 182
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 230..234
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT STRAND 2..7
FT /evidence="ECO:0007829|PDB:3OHR"
FT STRAND 12..17
FT /evidence="ECO:0007829|PDB:3OHR"
FT STRAND 23..28
FT /evidence="ECO:0007829|PDB:3OHR"
FT HELIX 34..39
FT /evidence="ECO:0007829|PDB:3OHR"
FT HELIX 42..45
FT /evidence="ECO:0007829|PDB:3OHR"
FT STRAND 51..57
FT /evidence="ECO:0007829|PDB:3OHR"
FT STRAND 59..61
FT /evidence="ECO:0007829|PDB:3OHR"
FT TURN 68..71
FT /evidence="ECO:0007829|PDB:3OHR"
FT TURN 79..81
FT /evidence="ECO:0007829|PDB:1XC3"
FT HELIX 86..90
FT /evidence="ECO:0007829|PDB:3OHR"
FT STRAND 98..102
FT /evidence="ECO:0007829|PDB:3OHR"
FT HELIX 103..114
FT /evidence="ECO:0007829|PDB:3OHR"
FT TURN 116..119
FT /evidence="ECO:0007829|PDB:1XC3"
FT STRAND 123..138
FT /evidence="ECO:0007829|PDB:3OHR"
FT STRAND 145..147
FT /evidence="ECO:0007829|PDB:3OHR"
FT HELIX 151..153
FT /evidence="ECO:0007829|PDB:3OHR"
FT TURN 169..171
FT /evidence="ECO:0007829|PDB:3OHR"
FT STRAND 172..174
FT /evidence="ECO:0007829|PDB:3OHR"
FT HELIX 175..179
FT /evidence="ECO:0007829|PDB:3OHR"
FT HELIX 181..188
FT /evidence="ECO:0007829|PDB:3OHR"
FT HELIX 192..195
FT /evidence="ECO:0007829|PDB:3OHR"
FT HELIX 199..219
FT /evidence="ECO:0007829|PDB:3OHR"
FT STRAND 225..230
FT /evidence="ECO:0007829|PDB:3OHR"
FT HELIX 231..233
FT /evidence="ECO:0007829|PDB:3OHR"
FT HELIX 237..249
FT /evidence="ECO:0007829|PDB:3OHR"
FT HELIX 256..258
FT /evidence="ECO:0007829|PDB:3OHR"
FT TURN 259..261
FT /evidence="ECO:0007829|PDB:3OHR"
FT HELIX 262..264
FT /evidence="ECO:0007829|PDB:3OHR"
FT HELIX 272..274
FT /evidence="ECO:0007829|PDB:3OHR"
FT HELIX 275..292
FT /evidence="ECO:0007829|PDB:3OHR"
SQ SEQUENCE 299 AA; 32440 MW; E384CECFDDF056BE CRC64;
MLGGIEAGGT KFVCAVGRED GTIIDRIEFP TKMPDETIEK VIQYFSQFSL QAIGIGSFGP
VDNDKTSQTY GTITATPKAG WRHYPFLQTV KNEMKIPVGF STDVNAAALG EFLFGEAKGL
DSCLYITIGT GIGAGAIVEG RLLQGLSHPE MGHIYIRRHP DDVYQGKCPY HGDCFEGLAS
GPAIEARWGK KAADLSDIAQ VWELEGYYIA QALAQYILIL APKKIILGGG VMQQKQVFSY
IYQYVPKIMN SYLDFSELSD DISDYIVPPR LGSNAGIIGT LVLAHQALQA EAASGEVRS
