FUCI_STRPN
ID FUCI_STRPN Reviewed; 588 AA.
AC Q97N97;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=L-fucose isomerase {ECO:0000255|HAMAP-Rule:MF_01254};
DE EC=5.3.1.25 {ECO:0000255|HAMAP-Rule:MF_01254};
DE AltName: Full=6-deoxy-L-galactose isomerase {ECO:0000255|HAMAP-Rule:MF_01254};
DE AltName: Full=FucIase;
GN Name=fucI {ECO:0000255|HAMAP-Rule:MF_01254}; OrderedLocusNames=SP_2158;
OS Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=170187;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-334 / TIGR4;
RX PubMed=11463916; DOI=10.1126/science.1061217;
RA Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D.,
RA Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J.,
RA Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D.,
RA Umayam L.A., White O., Salzberg S.L., Lewis M.R., Radune D.,
RA Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L.,
RA McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., Hickey E.K.,
RA Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., Dougherty B.A.,
RA Morrison D.A., Hollingshead S.K., Fraser C.M.;
RT "Complete genome sequence of a virulent isolate of Streptococcus
RT pneumoniae.";
RL Science 293:498-506(2001).
CC -!- FUNCTION: Converts the aldose L-fucose into the corresponding ketose L-
CC fuculose. {ECO:0000255|HAMAP-Rule:MF_01254}.
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:0000255|HAMAP-
CC Rule:MF_01254};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01254};
CC -!- PATHWAY: Carbohydrate degradation; L-fucose degradation; L-lactaldehyde
CC and glycerone phosphate from L-fucose: step 1/3. {ECO:0000255|HAMAP-
CC Rule:MF_01254}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01254}.
CC -!- SIMILARITY: Belongs to the L-fucose isomerase family.
CC {ECO:0000255|HAMAP-Rule:MF_01254}.
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DR EMBL; AE005672; AAK76212.1; -; Genomic_DNA.
DR PIR; C95252; C95252.
DR RefSeq; WP_000614266.1; NZ_AKVY01000001.1.
DR PDB; 4C20; X-ray; 2.41 A; A/B=2-588.
DR PDB; 4C21; X-ray; 2.55 A; A/B=1-588.
DR PDB; 4C22; X-ray; 2.70 A; A/B=2-588.
DR PDBsum; 4C20; -.
DR PDBsum; 4C21; -.
DR PDBsum; 4C22; -.
DR AlphaFoldDB; Q97N97; -.
DR SMR; Q97N97; -.
DR STRING; 170187.SP_2158; -.
DR EnsemblBacteria; AAK76212; AAK76212; SP_2158.
DR KEGG; spn:SP_2158; -.
DR eggNOG; COG2407; Bacteria.
DR OMA; QDYRACA; -.
DR PhylomeDB; Q97N97; -.
DR BioCyc; SPNE170187:G1FZB-2252-MON; -.
DR UniPathway; UPA00563; UER00624.
DR Proteomes; UP000000585; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008736; F:L-fucose isomerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0042355; P:L-fucose catabolic process; IEA:UniProtKB-UniRule.
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; Fucose metabolism;
KW Isomerase; Manganese; Metal-binding.
FT CHAIN 1..588
FT /note="L-fucose isomerase"
FT /id="PRO_0000204152"
FT ACT_SITE 335
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01254"
FT ACT_SITE 359
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01254"
FT BINDING 335
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01254"
FT BINDING 359
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01254"
FT BINDING 525
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01254"
FT STRAND 6..12
FT /evidence="ECO:0007829|PDB:4C20"
FT TURN 17..19
FT /evidence="ECO:0007829|PDB:4C20"
FT HELIX 20..42
FT /evidence="ECO:0007829|PDB:4C20"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:4C20"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:4C20"
FT HELIX 63..74
FT /evidence="ECO:0007829|PDB:4C20"
FT TURN 75..77
FT /evidence="ECO:0007829|PDB:4C20"
FT STRAND 78..87
FT /evidence="ECO:0007829|PDB:4C20"
FT HELIX 91..94
FT /evidence="ECO:0007829|PDB:4C20"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:4C20"
FT STRAND 103..107
FT /evidence="ECO:0007829|PDB:4C20"
FT STRAND 111..113
FT /evidence="ECO:0007829|PDB:4C20"
FT HELIX 115..129
FT /evidence="ECO:0007829|PDB:4C20"
FT STRAND 134..136
FT /evidence="ECO:0007829|PDB:4C20"
FT HELIX 151..170
FT /evidence="ECO:0007829|PDB:4C20"
FT STRAND 174..180
FT /evidence="ECO:0007829|PDB:4C20"
FT HELIX 186..188
FT /evidence="ECO:0007829|PDB:4C20"
FT HELIX 192..199
FT /evidence="ECO:0007829|PDB:4C20"
FT STRAND 202..206
FT /evidence="ECO:0007829|PDB:4C20"
FT HELIX 209..216
FT /evidence="ECO:0007829|PDB:4C20"
FT HELIX 222..235
FT /evidence="ECO:0007829|PDB:4C20"
FT HELIX 245..247
FT /evidence="ECO:0007829|PDB:4C20"
FT HELIX 251..273
FT /evidence="ECO:0007829|PDB:4C20"
FT HELIX 276..280
FT /evidence="ECO:0007829|PDB:4C20"
FT HELIX 286..288
FT /evidence="ECO:0007829|PDB:4C20"
FT STRAND 292..297
FT /evidence="ECO:0007829|PDB:4C20"
FT TURN 300..306
FT /evidence="ECO:0007829|PDB:4C20"
FT HELIX 311..318
FT /evidence="ECO:0007829|PDB:4C20"
FT STRAND 319..322
FT /evidence="ECO:0007829|PDB:4C20"
FT STRAND 331..334
FT /evidence="ECO:0007829|PDB:4C20"
FT HELIX 338..351
FT /evidence="ECO:0007829|PDB:4C20"
FT STRAND 356..364
FT /evidence="ECO:0007829|PDB:4C20"
FT HELIX 366..373
FT /evidence="ECO:0007829|PDB:4C20"
FT HELIX 379..381
FT /evidence="ECO:0007829|PDB:4C20"
FT STRAND 385..388
FT /evidence="ECO:0007829|PDB:4C20"
FT HELIX 396..399
FT /evidence="ECO:0007829|PDB:4C20"
FT STRAND 402..404
FT /evidence="ECO:0007829|PDB:4C20"
FT STRAND 407..409
FT /evidence="ECO:0007829|PDB:4C20"
FT HELIX 413..415
FT /evidence="ECO:0007829|PDB:4C20"
FT HELIX 418..426
FT /evidence="ECO:0007829|PDB:4C20"
FT TURN 435..437
FT /evidence="ECO:0007829|PDB:4C20"
FT STRAND 454..463
FT /evidence="ECO:0007829|PDB:4C20"
FT TURN 464..466
FT /evidence="ECO:0007829|PDB:4C20"
FT STRAND 467..477
FT /evidence="ECO:0007829|PDB:4C20"
FT HELIX 482..490
FT /evidence="ECO:0007829|PDB:4C20"
FT STRAND 498..503
FT /evidence="ECO:0007829|PDB:4C20"
FT HELIX 514..519
FT /evidence="ECO:0007829|PDB:4C20"
FT STRAND 523..531
FT /evidence="ECO:0007829|PDB:4C20"
FT HELIX 534..544
FT /evidence="ECO:0007829|PDB:4C20"
FT STRAND 548..550
FT /evidence="ECO:0007829|PDB:4C20"
FT HELIX 555..557
FT /evidence="ECO:0007829|PDB:4C20"
FT HELIX 562..567
FT /evidence="ECO:0007829|PDB:4C20"
FT HELIX 572..583
FT /evidence="ECO:0007829|PDB:4C20"
SQ SEQUENCE 588 AA; 65895 MW; 06E678EDF801786A CRC64;
MIQHPRIGIR PTIDGRRQGV RESLEVQTMN MAKSVADLIS STLKYPDGEP VECVISPSTI
GRVPEAAASH ELFKKSNVCA TITVTPCWCY GSETMDMSPD IPHAIWGFNG TERPGAVYLA
AVLASHAQKG IPAFGIYGRD VQEASDTDIP EDVKEKLLRY ARAALATGLM RDTAYLSMGS
VSMGIGGSIV NPDFFQEYLG MRNESVDMTE FTRRMDRGIY DPEEFERALK WVKENVKEGF
DHNREDLVLS REEKDRQWEF VIKMFMIGRD LMVGNPRLAE LGFEEEAVGH HALVAGFQGQ
RQWTDHFPNG DFMETFLNTQ FDWNGIRKPF VFATENDSLN GVSMLFNYLL TNTPQIFADV
RTYWSPEAVK RVTGHTLEGR AAAGFLHLIN SGSCTLDGTG QATRDGKPIM KPFWELEESE
VQAMLENTDF PPANREYFRG GGFSTRFLTK GDMPVTMVRL NLLKGVGPVL QIAEGYTLEL
PEDVHHTLDN RTDPGWPTTW FAPRLTGKGA FKSVYDVMNN WGANHGAITY GHIGADLITL
ASMLRIPVNM HNVPEEDIFR PKNWSLFGTE DLESADYRAC QLLGPLHK
