ID A0A076GWG7_9SYNE Unreviewed; 342 AA.
AC A0A076GWG7;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 34.
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 ORFNames=KR100_01855 {ECO:0000313|EMBL:AII41715.1};
OS Synechococcus sp. KORDI-100.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC Synechococcus.
OX NCBI_TaxID=1280380 {ECO:0000313|EMBL:AII41715.1, ECO:0000313|Proteomes:UP000028591};
RN [1] {ECO:0000313|EMBL:AII41715.1, ECO:0000313|Proteomes:UP000028591}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KORDI-100 {ECO:0000313|EMBL:AII41715.1,
RC ECO:0000313|Proteomes:UP000028591};
RA Choi D.H., Kwon K.-K., Lee J.-H., Noh J.H.;
RT "Genome sequence of Synechococcus sp. KORDI-100.";
RL Submitted (JUN-2013) to the EMBL/GenBank/DDBJ databases.
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; CP006269; AII41715.1; -; Genomic_DNA.
DR RefSeq; WP_038542708.1; NZ_CP006269.1.
DR AlphaFoldDB; A0A076GWG7; -.
DR STRING; 1280380.KR100_01855; -.
DR KEGG; synk:KR100_01855; -.
DR eggNOG; COG0451; Bacteria.
DR HOGENOM; CLU_007383_18_0_3; -.
DR OrthoDB; 9811425at2; -.
DR UniPathway; UPA00128; UER00191.
DR Proteomes; UP000028591; 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:UP000028591}.
FT DOMAIN 15..242
FT /note="NAD-dependent epimerase/dehydratase"
FT /evidence="ECO:0000259|Pfam:PF01370"
FT ACT_SITE 151
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00956"
FT BINDING 19..25
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00956"
FT BINDING 120..123
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00956"
FT BINDING 155
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00956"
FT BINDING 178..181
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00956"
FT BINDING 194
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00956"
FT BINDING 202
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 224
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00956"
FT BINDING 297
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00956"
FT SITE 122
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00956"
FT SITE 124
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00956"
SQ SEQUENCE 342 AA; 36868 MW; E52FB9CC637D34BB CRC64;
MKPETSLLIS ASDRILVAGA RGMAGSAVVR ALRRAGYGDE RCGGSLLTPT RQELDLLDLT
AVRTWFAKQQ PTVVVLTAAT VGGIEANRSR PADFLLQNLQ LETNVIETAW HQGARRLLFL
GSSCIYPKFA DQPIREEALL TGSLEPTNEW YAIAKIAGIK LAQALRLQHG FDAISLMPTN
LYGPGDNYHP TGSHVLPALI RRFQVAIERG VSTVTCWGSG TPLREFLHAD DLGEASVFAL
ERWNPDAEDA PCDEAGSPLA FLNVGTGIDL SIRELAEAVA HAVGYAGSIE WDTSKPDGTP
KKQLDVSRLA AMGWRAGISL SEGLPRAVAD FREQKAAGTL RN
//
