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   27-MAR-2024, entry version 135.
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};
GN   OrderedLocusNames=b2802, JW2773;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadota; 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; 511145-b2802; -.
DR   EnsemblBacteria; AAC75844; AAC75844; b2802.
DR   GeneID; 75172886; -.
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; NHGAISY; -.
DR   OrthoDB; 9760430at2; -.
DR   PhylomeDB; P69922; -.
DR   BioCyc; EcoCyc:FUCISOM-MONOMER; -.
DR   BioCyc; MetaCyc:FUCISOM-MONOMER; -.
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   CDD; cd03556; L-fucose_isomerase; 1.
DR   Gene3D; 3.40.50.1070; -; 1.
DR   Gene3D; 3.20.14.10; L-fucose/L-arabinose isomerase, C-terminal; 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   NCBIfam; TIGR01089; fucI; 1.
DR   PANTHER; PTHR37840; L-FUCOSE ISOMERASE; 1.
DR   PANTHER; PTHR37840:SF1; L-FUCOSE ISOMERASE; 1.
DR   Pfam; PF02952; Fucose_iso_C; 1.
DR   Pfam; PF07881; Fucose_iso_N1; 1.
DR   Pfam; PF07882; Fucose_iso_N2; 1.
DR   SUPFAM; SSF50443; FucI/AraA C-terminal domain-like; 1.
DR   SUPFAM; SSF53743; FucI/AraA N-terminal and middle domains; 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
//