FUCI_ECOLI
ID FUCI_ECOLI Reviewed; 591 AA.
AC P69922; P11552; Q2MA32;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=L-fucose isomerase {ECO:0000303|PubMed:4928018};
DE Short=FucIase {ECO:0000303|PubMed:9367760};
DE Short=FucIso {ECO:0000303|PubMed:8564401};
DE EC=5.3.1.25 {ECO:0000269|PubMed:4632320, ECO:0000269|PubMed:8564401, ECO:0000269|PubMed:9367760, ECO:0000305|PubMed:13319278, ECO:0000305|PubMed:4928018};
DE AltName: Full=6-deoxy-L-galactose isomerase;
DE AltName: Full=D-arabinose isomerase {ECO:0000303|PubMed:4632320};
DE EC=5.3.1.3 {ECO:0000269|PubMed:4632320, ECO:0000305|PubMed:13319278, ECO:0000305|PubMed:4928018};
GN Name=fucI {ECO:0000303|PubMed:2664711}; OrderedLocusNames=b2802, JW2773;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=2664711; DOI=10.1093/nar/17.12.4883;
RA Lu Z., Lin E.C.C.;
RT "The nucleotide sequence of Escherichia coli genes for L-fucose
RT dissimilation.";
RL Nucleic Acids Res. 17:4883-4884(1989).
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 PROTEIN SEQUENCE OF 1-9.
RX PubMed=8052131; DOI=10.1111/j.1365-2958.1994.tb01066.x;
RA Gunn F.J., Tate C.G., Henderson P.J.F.;
RT "Identification of a novel sugar-H+ symport protein, FucP, for transport of
RT L-fucose into Escherichia coli.";
RL Mol. Microbiol. 12:799-809(1994).
RN [5]
RP FUNCTION.
RX PubMed=13319278; DOI=10.1016/s0021-9258(18)65716-3;
RA Green M., Cohen S.S.;
RT "Enzymatic conversion of L-fucose to L-fuculose.";
RL J. Biol. Chem. 219:557-568(1956).
RN [6]
RP FUNCTION, AND INDUCTION.
RX PubMed=4928018; DOI=10.1128/jb.106.1.90-96.1971;
RA LeBlanc D.J., Mortlock R.P.;
RT "Metabolism of D-arabinose: a new pathway in Escherichia coli.";
RL J. Bacteriol. 106:90-96(1971).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND INDUCTION.
RC STRAIN=K12;
RX PubMed=4632320; DOI=10.1128/jb.113.2.687-696.1973;
RA Boulter J.R., Gielow W.O.;
RT "Properties of D-arabinose isomerase purified from two strains of
RT Escherichia coli.";
RL J. Bacteriol. 113:687-696(1973).
RN [8]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=8564401; DOI=10.1016/0968-0896(95)00119-2;
RA Garcia-Junceda E., Shen G.J., Alajarin R., Wong C.H.;
RT "Cloning and overexpression of rhamnose isomerase and fucose isomerase.";
RL Bioorg. Med. Chem. 3:1349-1355(1995).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RC STRAIN=K12;
RX PubMed=22133443; DOI=10.1016/j.enzmictec.2011.09.009;
RA Usvalampi A., Turunen O., Valjakka J., Pastinen O., Leisola M.,
RA Nyyssoelae A.;
RT "Production of L-xylose from L-xylulose using Escherichia coli L-fucose
RT isomerase.";
RL Enzyme Microb. Technol. 50:71-76(2012).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF COMPLEX WITH L-FUCITOL AND
RP MANGANESE, ACTIVE SITES, FUNCTION, CATALYTIC ACTIVITY, REACTION MECHANISM,
RP COFACTOR, AND SUBUNIT.
RX PubMed=9367760; DOI=10.1006/jmbi.1997.1280;
RA Seemann J.E., Schulz G.E.;
RT "Structure and mechanism of L-fucose isomerase from Escherichia coli.";
RL J. Mol. Biol. 273:256-268(1997).
CC -!- FUNCTION: Converts the aldose L-fucose into the corresponding ketose L-
CC fuculose (PubMed:13319278, PubMed:4928018, PubMed:4632320,
CC PubMed:8564401, PubMed:9367760). Also converts D-arabinose into D-
CC ribulose (PubMed:13319278, PubMed:4928018, PubMed:4632320). In
CC addition, catalyzes the isomerization of L-xylulose to L-xylose
CC (PubMed:22133443). {ECO:0000269|PubMed:13319278,
CC ECO:0000269|PubMed:22133443, ECO:0000269|PubMed:4632320,
CC ECO:0000269|PubMed:4928018, ECO:0000269|PubMed:8564401,
CC ECO:0000269|PubMed:9367760}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-fucose = L-fuculose; Xref=Rhea:RHEA:17233, ChEBI:CHEBI:2181,
CC ChEBI:CHEBI:17617; EC=5.3.1.25; Evidence={ECO:0000269|PubMed:4632320,
CC ECO:0000269|PubMed:8564401, ECO:0000269|PubMed:9367760,
CC ECO:0000305|PubMed:13319278, ECO:0000305|PubMed:4928018};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-arabinose = D-ribulose; Xref=Rhea:RHEA:13849,
CC ChEBI:CHEBI:17173, ChEBI:CHEBI:46994; EC=5.3.1.3;
CC Evidence={ECO:0000269|PubMed:4632320, ECO:0000305|PubMed:13319278,
CC ECO:0000305|PubMed:4928018};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-xylopyranose = L-xylulose; Xref=Rhea:RHEA:71251,
CC ChEBI:CHEBI:17399, ChEBI:CHEBI:59275;
CC Evidence={ECO:0000269|PubMed:22133443};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:4632320, ECO:0000269|PubMed:9367760};
CC Note=Can also use Co(2+). {ECO:0000269|PubMed:4632320};
CC -!- ACTIVITY REGULATION: Inhibited by ribitol, L-arabitol and dulcitol
CC (PubMed:4632320). Isomerization of L-xylulose to L-xylose is inhibited
CC by xylitol (PubMed:22133443). {ECO:0000269|PubMed:22133443,
CC ECO:0000269|PubMed:4632320}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=45 mM for L-fucose {ECO:0000269|PubMed:4632320};
CC KM=280 mM for D-arabinose {ECO:0000269|PubMed:4632320};
CC KM=41 mM for L-xylulose {ECO:0000269|PubMed:22133443};
CC Vmax=0.231 umol/min/mg enzyme with L-xylulose as substrate
CC {ECO:0000269|PubMed:22133443};
CC Note=kcat is 0.125 sec(-1) with L-xylulose as substrate.
CC {ECO:0000269|PubMed:22133443};
CC pH dependence:
CC Optimum pH is 7.6-10.6 with L-fucose or D-arabinose as substrate.
CC {ECO:0000269|PubMed:4632320};
CC Temperature dependence:
CC Optimum temperature is 50 degrees Celsius with L-xylulose as
CC substrate. {ECO:0000269|PubMed:22133443};
CC -!- PATHWAY: Carbohydrate degradation; L-fucose degradation; L-lactaldehyde
CC and glycerone phosphate from L-fucose: step 1/3.
CC {ECO:0000305|PubMed:8564401}.
CC -!- SUBUNIT: Homohexamer. {ECO:0000269|PubMed:9367760}.
CC -!- INTERACTION:
CC P69922; P69922: fucI; NbExp=2; IntAct=EBI-908978, EBI-908978;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- INDUCTION: By L-fucose. {ECO:0000269|PubMed:4632320,
CC ECO:0000269|PubMed:4928018}.
CC -!- SIMILARITY: Belongs to the L-fucose isomerase family. {ECO:0000305}.
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DR EMBL; X15025; CAA33127.1; -; Genomic_DNA.
DR EMBL; U29581; AAB40452.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75844.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76874.1; -; Genomic_DNA.
DR PIR; JS0185; ISECFI.
DR RefSeq; NP_417282.1; NC_000913.3.
DR RefSeq; WP_000724153.1; NZ_LN832404.1.
DR PDB; 1FUI; X-ray; 2.50 A; A/B/C/D/E/F=1-591.
DR PDBsum; 1FUI; -.
DR AlphaFoldDB; P69922; -.
DR SMR; P69922; -.
DR BioGRID; 4259466; 8.
DR BioGRID; 850555; 1.
DR IntAct; P69922; 2.
DR STRING; 511145.b2802; -.
DR jPOST; P69922; -.
DR PaxDb; P69922; -.
DR PRIDE; P69922; -.
DR EnsemblBacteria; AAC75844; AAC75844; b2802.
DR EnsemblBacteria; BAE76874; BAE76874; BAE76874.
DR GeneID; 946195; -.
DR KEGG; ecj:JW2773; -.
DR KEGG; eco:b2802; -.
DR PATRIC; fig|1411691.4.peg.3931; -.
DR EchoBASE; EB0345; -.
DR eggNOG; COG2407; Bacteria.
DR HOGENOM; CLU_033326_1_0_6; -.
DR InParanoid; P69922; -.
DR OMA; QDYRACA; -.
DR PhylomeDB; P69922; -.
DR BioCyc; EcoCyc:FUCISOM-MON; -.
DR BioCyc; MetaCyc:FUCISOM-MON; -.
DR BRENDA; 5.3.1.25; 2026.
DR UniPathway; UPA00563; UER00624.
DR EvolutionaryTrace; P69922; -.
DR PRO; PR:P69922; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; HDA:UniProtKB.
DR GO; GO:0008790; F:arabinose isomerase activity; IDA:EcoCyc.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0008736; F:L-fucose isomerase activity; IDA:EcoCyc.
DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0019571; P:D-arabinose catabolic process; IMP:EcoCyc.
DR GO; GO:0042355; P:L-fucose catabolic process; IMP:EcoCyc.
DR Gene3D; 3.20.14.10; -; 1.
DR Gene3D; 3.40.275.10; -; 1.
DR Gene3D; 3.40.50.1070; -; 1.
DR HAMAP; MF_01254; Fucose_iso; 1.
DR InterPro; IPR004216; Fuc/Ara_isomerase_C.
DR InterPro; IPR038393; Fuc_iso_dom3_sf.
DR InterPro; IPR015888; Fuc_isomerase_C.
DR InterPro; IPR038391; Fucose_iso_dom1_sf.
DR InterPro; IPR012888; Fucose_iso_N1.
DR InterPro; IPR005763; Fucose_isomerase.
DR InterPro; IPR038392; Fucose_isomerase_dom2_sf.
DR InterPro; IPR009015; Fucose_isomerase_N/cen_sf.
DR InterPro; IPR012889; Fucose_isomerase_N2.
DR Pfam; PF02952; Fucose_iso_C; 1.
DR Pfam; PF07881; Fucose_iso_N1; 1.
DR Pfam; PF07882; Fucose_iso_N2; 1.
DR SUPFAM; SSF50443; SSF50443; 1.
DR SUPFAM; SSF53743; SSF53743; 1.
DR TIGRFAMs; TIGR01089; fucI; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Cytoplasm;
KW Direct protein sequencing; Fucose metabolism; Isomerase; Manganese;
KW Metal-binding; Reference proteome.
FT CHAIN 1..591
FT /note="L-fucose isomerase"
FT /id="PRO_0000204145"
FT ACT_SITE 337
FT /note="Proton acceptor"
FT /evidence="ECO:0000269|PubMed:9367760"
FT ACT_SITE 361
FT /note="Proton acceptor"
FT /evidence="ECO:0000269|PubMed:9367760"
FT BINDING 337
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:9367760,
FT ECO:0007744|PDB:1FUI"
FT BINDING 361
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:9367760,
FT ECO:0007744|PDB:1FUI"
FT BINDING 528
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:9367760,
FT ECO:0007744|PDB:1FUI"
FT CONFLICT 8
FT /note="K -> P (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 8..14
FT /evidence="ECO:0007829|PDB:1FUI"
FT TURN 19..21
FT /evidence="ECO:0007829|PDB:1FUI"
FT HELIX 22..44
FT /evidence="ECO:0007829|PDB:1FUI"
FT STRAND 55..57
FT /evidence="ECO:0007829|PDB:1FUI"
FT HELIX 65..76
FT /evidence="ECO:0007829|PDB:1FUI"
FT TURN 77..79
FT /evidence="ECO:0007829|PDB:1FUI"
FT STRAND 80..89
FT /evidence="ECO:0007829|PDB:1FUI"
FT HELIX 93..96
FT /evidence="ECO:0007829|PDB:1FUI"
FT STRAND 101..103
FT /evidence="ECO:0007829|PDB:1FUI"
FT STRAND 105..109
FT /evidence="ECO:0007829|PDB:1FUI"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:1FUI"
FT HELIX 117..130
FT /evidence="ECO:0007829|PDB:1FUI"
FT STRAND 136..138
FT /evidence="ECO:0007829|PDB:1FUI"
FT HELIX 153..172
FT /evidence="ECO:0007829|PDB:1FUI"
FT STRAND 176..182
FT /evidence="ECO:0007829|PDB:1FUI"
FT HELIX 188..190
FT /evidence="ECO:0007829|PDB:1FUI"
FT HELIX 194..201
FT /evidence="ECO:0007829|PDB:1FUI"
FT STRAND 204..208
FT /evidence="ECO:0007829|PDB:1FUI"
FT HELIX 211..218
FT /evidence="ECO:0007829|PDB:1FUI"
FT HELIX 224..237
FT /evidence="ECO:0007829|PDB:1FUI"
FT HELIX 247..249
FT /evidence="ECO:0007829|PDB:1FUI"
FT HELIX 253..275
FT /evidence="ECO:0007829|PDB:1FUI"
FT HELIX 279..282
FT /evidence="ECO:0007829|PDB:1FUI"
FT HELIX 286..289
FT /evidence="ECO:0007829|PDB:1FUI"
FT STRAND 294..299
FT /evidence="ECO:0007829|PDB:1FUI"
FT TURN 302..308
FT /evidence="ECO:0007829|PDB:1FUI"
FT HELIX 313..320
FT /evidence="ECO:0007829|PDB:1FUI"
FT STRAND 321..324
FT /evidence="ECO:0007829|PDB:1FUI"
FT STRAND 334..336
FT /evidence="ECO:0007829|PDB:1FUI"
FT HELIX 340..353
FT /evidence="ECO:0007829|PDB:1FUI"
FT STRAND 358..366
FT /evidence="ECO:0007829|PDB:1FUI"
FT HELIX 368..375
FT /evidence="ECO:0007829|PDB:1FUI"
FT HELIX 381..385
FT /evidence="ECO:0007829|PDB:1FUI"
FT STRAND 387..390
FT /evidence="ECO:0007829|PDB:1FUI"
FT HELIX 398..401
FT /evidence="ECO:0007829|PDB:1FUI"
FT HELIX 416..418
FT /evidence="ECO:0007829|PDB:1FUI"
FT HELIX 421..429
FT /evidence="ECO:0007829|PDB:1FUI"
FT STRAND 432..435
FT /evidence="ECO:0007829|PDB:1FUI"
FT TURN 438..440
FT /evidence="ECO:0007829|PDB:1FUI"
FT STRAND 446..449
FT /evidence="ECO:0007829|PDB:1FUI"
FT STRAND 457..466
FT /evidence="ECO:0007829|PDB:1FUI"
FT TURN 467..469
FT /evidence="ECO:0007829|PDB:1FUI"
FT STRAND 470..480
FT /evidence="ECO:0007829|PDB:1FUI"
FT HELIX 485..494
FT /evidence="ECO:0007829|PDB:1FUI"
FT STRAND 501..506
FT /evidence="ECO:0007829|PDB:1FUI"
FT HELIX 512..514
FT /evidence="ECO:0007829|PDB:1FUI"
FT HELIX 517..522
FT /evidence="ECO:0007829|PDB:1FUI"
FT STRAND 525..534
FT /evidence="ECO:0007829|PDB:1FUI"
FT HELIX 537..547
FT /evidence="ECO:0007829|PDB:1FUI"
FT STRAND 551..553
FT /evidence="ECO:0007829|PDB:1FUI"
FT HELIX 558..560
FT /evidence="ECO:0007829|PDB:1FUI"
FT HELIX 566..569
FT /evidence="ECO:0007829|PDB:1FUI"
FT HELIX 574..585
FT /evidence="ECO:0007829|PDB:1FUI"
SQ SEQUENCE 591 AA; 64977 MW; E6245DEEDF34EF9B CRC64;
MKKISLPKIG IRPVIDGRRM GVRESLEEQT MNMAKATAAL LTEKLRHACG AAVECVISDT
CIAGMAEAAA CEEKFSSQNV GLTITVTPCW CYGSETIDMD PTRPKAIWGF NGTERPGAVY
LAAALAAHSQ KGIPAFSIYG HDVQDADDTS IPADVEEKLL RFARAGLAVA SMKGKSYLSL
GGVSMGIAGS IVDHNFFESW LGMKVQAVDM TELRRRIDQK IYDEAELEMA LAWADKNFRY
GEDENNKQYQ RNAEQSRAVL RESLLMAMCI RDMMQGNSKL ADIGRVEESL GYNAIAAGFQ
GQRHWTDQYP NGDTAEAILN SSFDWNGVRE PFVVATENDS LNGVAMLMGH QLTGTAQVFA
DVRTYWSPEA IERVTGHKLD GLAEHGIIHL INSGSAALDG SCKQRDSEGN PTMKPHWEIS
QQEADACLAA TEWCPAIHEY FRGGGYSSRF LTEGGVPFTM TRVNIIKGLG PVLQIAEGWS
VELPKDVHDI LNKRTNSTWP TTWFAPRLTG KGPFTDVYSV MANWGANHGV LTIGHVGADF
ITLASMLRIP VCMHNVEETK VYRPSAWAAH GMDIEGQDYR ACQNYGPLYK R
