ID I0ANW3_IGNAJ Unreviewed; 326 AA.
AC I0ANW3;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=GDP-L-fucose synthase {ECO:0000256|HAMAP-Rule:MF_00956};
DE EC=1.1.1.271 {ECO:0000256|HAMAP-Rule:MF_00956};
DE AltName: Full=GDP-4-keto-6-deoxy-D-mannose-3,5-epimerase-4-reductase {ECO:0000256|HAMAP-Rule:MF_00956};
GN Name=fcl {ECO:0000256|HAMAP-Rule:MF_00956};
GN OrderedLocusNames=IALB_2967 {ECO:0000313|EMBL:AFH50670.1};
OS Ignavibacterium album (strain DSM 19864 / JCM 16511 / NBRC 101810 /
OS Mat9-16).
OC Bacteria; Ignavibacteriota; Ignavibacteria; Ignavibacteriales;
OC Ignavibacteriaceae; Ignavibacterium.
OX NCBI_TaxID=945713 {ECO:0000313|EMBL:AFH50670.1, ECO:0000313|Proteomes:UP000007394};
RN [1] {ECO:0000313|EMBL:AFH50670.1, ECO:0000313|Proteomes:UP000007394}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19864 / JCM 16511 / NBRC 101810 / Mat9-16
RC {ECO:0000313|Proteomes:UP000007394};
RX PubMed=22661972; DOI=10.3389/fmicb.2012.00185;
RA Liu Z., Frigaard N.-U., Vogl K., Iino T., Ohkuma M., Overmann J.,
RA Bryant D.A.;
RT "Complete genome of Ignavibacterium album, a metabolically versatile,
RT flagellated, facultative anaerobe from the phylum Chlorobi.";
RL Front. Microbiol. 3:185-185(2012).
CC -!- FUNCTION: Catalyzes the two-step NADP-dependent conversion of GDP-4-
CC dehydro-6-deoxy-D-mannose to GDP-fucose, involving an epimerase and a
CC reductase reaction. {ECO:0000256|HAMAP-Rule:MF_00956}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GDP-beta-L-fucose + NADP(+) = GDP-4-dehydro-alpha-D-rhamnose +
CC H(+) + NADPH; Xref=Rhea:RHEA:18885, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57273, ChEBI:CHEBI:57783, ChEBI:CHEBI:57964,
CC ChEBI:CHEBI:58349; EC=1.1.1.271; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_00956};
CC -!- PATHWAY: Nucleotide-sugar biosynthesis; GDP-L-fucose biosynthesis via
CC de novo pathway; GDP-L-fucose from GDP-alpha-D-mannose: step 2/2.
CC {ECO:0000256|HAMAP-Rule:MF_00956}.
CC -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC family. Fucose synthase subfamily. {ECO:0000256|ARBA:ARBA00005959,
CC ECO:0000256|HAMAP-Rule:MF_00956}.
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DR EMBL; CP003418; AFH50670.1; -; Genomic_DNA.
DR AlphaFoldDB; I0ANW3; -.
DR STRING; 945713.IALB_2967; -.
DR KEGG; ial:IALB_2967; -.
DR PATRIC; fig|945713.3.peg.2984; -.
DR eggNOG; COG0451; Bacteria.
DR HOGENOM; CLU_007383_18_0_10; -.
DR UniPathway; UPA00128; UER00191.
DR Proteomes; UP000007394; Chromosome.
DR GO; GO:0050577; F:GDP-L-fucose synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0070401; F:NADP+ binding; IEA:UniProtKB-UniRule.
DR GO; GO:0042351; P:'de novo' GDP-L-fucose biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd05239; GDP_FS_SDR_e; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.90.25.10; UDP-galactose 4-epimerase, domain 1; 1.
DR HAMAP; MF_00956; GDP_fucose_synth; 1.
DR InterPro; IPR001509; Epimerase_deHydtase.
DR InterPro; IPR028614; GDP_fucose/colitose_synth.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR43238; GDP-L-FUCOSE SYNTHASE; 1.
DR PANTHER; PTHR43238:SF1; GDP-L-FUCOSE SYNTHASE; 1.
DR Pfam; PF01370; Epimerase; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|HAMAP-Rule:MF_00956};
KW Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_00956};
KW NADP {ECO:0000256|HAMAP-Rule:MF_00956};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_00956}; Reference proteome {ECO:0000313|Proteomes:UP000007394}.
FT DOMAIN 14..245
FT /note="NAD-dependent epimerase/dehydratase"
FT /evidence="ECO:0000259|Pfam:PF01370"
FT ACT_SITE 144
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00956"
FT BINDING 18..24
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00956"
FT BINDING 113..116
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00956"
FT BINDING 148
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00956"
FT BINDING 171..174
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00956"
FT BINDING 187
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00956"
FT BINDING 195
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00956"
FT BINDING 210
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00956"
FT BINDING 217
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00956"
FT BINDING 284
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00956"
FT SITE 115
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00956"
FT SITE 117
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00956"
SQ SEQUENCE 326 AA; 37021 MW; 0683B665065AC799 CRC64;
MEFEAMAKYH NKKIYVAGHN GMVGSAIMRD LQKNGYENLI TKSFSELDLR RQSDVEKFFN
EQKPDVVIVA AAKVGGILAN NTYRAEFIYD NLMIETNLIH ASYLNKAEKL IFLGSSCIYP
KLAPQPLKEE YLLSGYLEYT NEPYAIAKIA GIKLCENYFK QYGCNFISAM PTNLYGPNDN
FDLQTSHVLP ALIRKFHEAK IHNTPTVTIW GTGKPLREFL FVDDLAEAII FMMENVEALE
LYNLGITHLN VGSGKDISIA ELASLIAKII GYNGRIEHDT SKPDGTPRKL MDVSRINSLG
WRYKTELEEG IKKTYDWFLN NFNSKV
//
