FUCI_HAEIN
ID FUCI_HAEIN Reviewed; 589 AA.
AC P44779;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 2.
DT 03-AUG-2022, entry version 124.
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=HI_0614;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC22273.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; L42023; AAC22273.1; ALT_INIT; Genomic_DNA.
DR PIR; F64081; F64081.
DR RefSeq; NP_438772.2; NC_000907.1.
DR RefSeq; WP_010869020.1; NC_000907.1.
DR AlphaFoldDB; P44779; -.
DR SMR; P44779; -.
DR STRING; 71421.HI_0614; -.
DR EnsemblBacteria; AAC22273; AAC22273; HI_0614.
DR KEGG; hin:HI_0614; -.
DR PATRIC; fig|71421.8.peg.638; -.
DR eggNOG; COG2407; Bacteria.
DR HOGENOM; CLU_033326_1_0_6; -.
DR PhylomeDB; P44779; -.
DR BioCyc; HINF71421:G1GJ1-635-MON; -.
DR UniPathway; UPA00563; UER00624.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008790; F:arabinose isomerase activity; IBA:GO_Central.
DR GO; GO:0008736; F:L-fucose isomerase activity; IBA:GO_Central.
DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0019571; P:D-arabinose catabolic process; IBA:GO_Central.
DR GO; GO:0042355; P:L-fucose catabolic process; IBA:GO_Central.
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 3: Inferred from homology;
KW Carbohydrate metabolism; Cytoplasm; Fucose metabolism; Isomerase;
KW Manganese; Metal-binding; Reference proteome.
FT CHAIN 1..589
FT /note="L-fucose isomerase"
FT /id="PRO_0000204148"
FT ACT_SITE 340
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01254"
FT ACT_SITE 364
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01254"
FT BINDING 340
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01254"
FT BINDING 364
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01254"
FT BINDING 527
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01254"
SQ SEQUENCE 589 AA; 65401 MW; F2E8FF1C65FFFC90 CRC64;
MALATQSNRI KIGIRPTIDG RRMGVRESLE TQTIRMAQSV AQLLQTHIRH TDGTFVECVV
ADSTIGGVAE AAACADKFKR ENVGLTITVT PCWCYGSETI DMDPHMPKAI WGFNGTERPG
AVYLAAALAG HSQLGLPAFS IYGTEVQEAD DTNIPEDVKE KLLRFARAGL AVASIRGKSY
LSIGSVSMGI AGSIVNQAFF QEYLGMRNEY VDMMEIKRRL DRKIYDQEEV DLALSWVKQY
CKEGVDVNSL ENQRNAEERA ELWENVVKMT IITRDLMVGN PKLATLNYAE EALGHNAIAA
GFQGQRHWTD HLPNGDFMEA MLNSTYDWNG VRPPYILATE NDSLNAIGML FGHQLTGKAQ
IFADVRTYWS QDSVERVTGW RPESGFIHLI NSGSAALDGT GEHQDAQGNP TLKPAWDVTE
EEAKRCLENT RWCPAVHEYF RGGGLSSQFL TKGGIPFTIH RINLIKGLGP VLQIAEGWSI
DLPQDVHNKL NQRTNETWPT TWFVPRLTGK GAFTDVYSVM ANWGANHCVA THGHVGADLI
TLASMLRIPV CMHNVSEKNI FRPSAWNGFG QDKEGQDYRA CQNFGPLYK
