SQUV_ECOLI
ID SQUV_ECOLI Reviewed; 298 AA.
AC P32143; Q2M8I0;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Sulfofructose kinase {ECO:0000255|HAMAP-Rule:MF_00999};
DE Short=SF kinase {ECO:0000255|HAMAP-Rule:MF_00999};
DE EC=2.7.1.184 {ECO:0000255|HAMAP-Rule:MF_00999};
GN Name=yihV; OrderedLocusNames=b3883, JW5568;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8346018; DOI=10.1093/nar/21.15.3391;
RA Plunkett G. III, Burland V., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome. III. DNA sequence of the region
RT from 87.2 to 89.2 minutes.";
RL Nucleic Acids Res. 21:3391-3398(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12;
RX PubMed=24463506; DOI=10.1038/nature12947;
RA Denger K., Weiss M., Felux A.K., Schneider A., Mayer C., Spiteller D.,
RA Huhn T., Cook A.M., Schleheck D.;
RT "Sulphoglycolysis in Escherichia coli K-12 closes a gap in the
RT biogeochemical sulphur cycle.";
RL Nature 507:114-117(2014).
CC -!- FUNCTION: Phosphorylates 6-deoxy-6-sulfo-D-fructose (SF) to 6-deoxy-6-
CC sulfo-D-fructose 1-phosphate (SFP). {ECO:0000255|HAMAP-Rule:MF_00999,
CC ECO:0000269|PubMed:24463506}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=6-deoxy-6-sulfo-D-fructose + ATP = 6-deoxy-6-sulfo-D-fructose
CC 1-phosphate + ADP + H(+); Xref=Rhea:RHEA:40443, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:77133, ChEBI:CHEBI:77134,
CC ChEBI:CHEBI:456216; EC=2.7.1.184; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00999, ECO:0000269|PubMed:24463506};
CC -!- INDUCTION: Induced during growth with sulfoquinovose.
CC {ECO:0000269|PubMed:24463506}.
CC -!- DISRUPTION PHENOTYPE: Mutant fails to grow on sulfoquinovose as a sole
CC carbon source. {ECO:0000269|PubMed:24463506}.
CC -!- SIMILARITY: Belongs to the carbohydrate kinase PfkB family.
CC {ECO:0000255|HAMAP-Rule:MF_00999}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB03016.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; L19201; AAB03016.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAD13445.2; -; Genomic_DNA.
DR EMBL; AP009048; BAE77426.1; -; Genomic_DNA.
DR PIR; S40827; S40827.
DR RefSeq; NP_418319.2; NC_000913.3.
DR RefSeq; WP_000621656.1; NZ_STEB01000017.1.
DR PDB; 7AG6; X-ray; 2.08 A; A/B=1-298.
DR PDB; 7AGH; X-ray; 2.93 A; A/B/C/D=1-298.
DR PDB; 7AGK; X-ray; 2.97 A; A/B/C/D=1-298.
DR PDBsum; 7AG6; -.
DR PDBsum; 7AGH; -.
DR PDBsum; 7AGK; -.
DR AlphaFoldDB; P32143; -.
DR SMR; P32143; -.
DR BioGRID; 4260966; 8.
DR STRING; 511145.b3883; -.
DR PaxDb; P32143; -.
DR PRIDE; P32143; -.
DR EnsemblBacteria; AAD13445; AAD13445; b3883.
DR EnsemblBacteria; BAE77426; BAE77426; BAE77426.
DR GeneID; 66672211; -.
DR GeneID; 948382; -.
DR KEGG; ecj:JW5568; -.
DR KEGG; eco:b3883; -.
DR PATRIC; fig|1411691.4.peg.2828; -.
DR EchoBASE; EB1794; -.
DR eggNOG; COG0524; Bacteria.
DR HOGENOM; CLU_027634_2_2_6; -.
DR InParanoid; P32143; -.
DR OMA; CSGMPPE; -.
DR PhylomeDB; P32143; -.
DR BioCyc; EcoCyc:EG11848-MON; -.
DR BioCyc; MetaCyc:EG11848-MON; -.
DR PRO; PR:P32143; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0061594; F:6-deoxy-6-sulfofructose kinase activity; IDA:EcoCyc.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:1902777; P:6-sulfoquinovose(1-) catabolic process; IMP:EcoCyc.
DR GO; GO:0061720; P:6-sulfoquinovose(1-) catabolic process to glycerone phosphate and 3-sulfolactaldehyde; IMP:EcoCyc.
DR GO; GO:0046835; P:carbohydrate phosphorylation; IDA:EcoCyc.
DR Gene3D; 3.40.1190.20; -; 1.
DR HAMAP; MF_00999; SF_kinase; 1.
DR InterPro; IPR002173; Carboh/pur_kinase_PfkB_CS.
DR InterPro; IPR011611; PfkB_dom.
DR InterPro; IPR002139; Ribo/fructo_kinase.
DR InterPro; IPR029056; Ribokinase-like.
DR InterPro; IPR030877; SF_kinase.
DR Pfam; PF00294; PfkB; 1.
DR PRINTS; PR00990; RIBOKINASE.
DR SUPFAM; SSF53613; SSF53613; 1.
DR PROSITE; PS00584; PFKB_KINASES_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Kinase; Nucleotide-binding; Reference proteome;
KW Transferase.
FT CHAIN 1..298
FT /note="Sulfofructose kinase"
FT /id="PRO_0000080149"
FT STRAND 3..8
FT /evidence="ECO:0007829|PDB:7AG6"
FT STRAND 11..17
FT /evidence="ECO:0007829|PDB:7AG6"
FT STRAND 24..29
FT /evidence="ECO:0007829|PDB:7AG6"
FT STRAND 31..38
FT /evidence="ECO:0007829|PDB:7AG6"
FT HELIX 40..50
FT /evidence="ECO:0007829|PDB:7AG6"
FT STRAND 54..58
FT /evidence="ECO:0007829|PDB:7AG6"
FT STRAND 60..64
FT /evidence="ECO:0007829|PDB:7AGH"
FT HELIX 65..76
FT /evidence="ECO:0007829|PDB:7AG6"
FT STRAND 85..87
FT /evidence="ECO:0007829|PDB:7AGH"
FT STRAND 93..99
FT /evidence="ECO:0007829|PDB:7AG6"
FT STRAND 105..110
FT /evidence="ECO:0007829|PDB:7AG6"
FT HELIX 120..124
FT /evidence="ECO:0007829|PDB:7AG6"
FT HELIX 127..129
FT /evidence="ECO:0007829|PDB:7AG6"
FT STRAND 131..136
FT /evidence="ECO:0007829|PDB:7AG6"
FT HELIX 140..153
FT /evidence="ECO:0007829|PDB:7AG6"
FT STRAND 156..161
FT /evidence="ECO:0007829|PDB:7AG6"
FT HELIX 169..173
FT /evidence="ECO:0007829|PDB:7AG6"
FT STRAND 176..181
FT /evidence="ECO:0007829|PDB:7AG6"
FT HELIX 182..189
FT /evidence="ECO:0007829|PDB:7AG6"
FT HELIX 194..202
FT /evidence="ECO:0007829|PDB:7AG6"
FT STRAND 206..212
FT /evidence="ECO:0007829|PDB:7AG6"
FT HELIX 214..216
FT /evidence="ECO:0007829|PDB:7AG6"
FT STRAND 218..222
FT /evidence="ECO:0007829|PDB:7AG6"
FT STRAND 225..229
FT /evidence="ECO:0007829|PDB:7AG6"
FT HELIX 242..257
FT /evidence="ECO:0007829|PDB:7AG6"
FT HELIX 260..274
FT /evidence="ECO:0007829|PDB:7AG6"
FT TURN 279..283
FT /evidence="ECO:0007829|PDB:7AG6"
FT HELIX 287..295
FT /evidence="ECO:0007829|PDB:7AG6"
SQ SEQUENCE 298 AA; 31728 MW; 24D347B04542909E CRC64;
MIRVACVGIT VMDRIYYVEG LPTESGKYVA RNYTEVGGGP AATAAVAAAR LGAQVDFIGR
VGDDDTGNSL LAELESWGVN TRYTKRYNQA KSSQSAIMVD TKGERIIINY PSPDLLPDAE
WLEEIDFSQW DVVLADVRWH DGAKKAFTLA RQAGVMTVLD GDITPQDISE LVALSDHAAF
SEPGLARLTG VKEMASALKQ AQTLTNGHVY VTQGSAGCDW LENGGRQHQP AFKVDVVDTT
GAGDVFHGAL AVALATSGDL AESVRFASGV AALKCTRPGG RAGIPDCDQT RSFLSLFV
