FCL_AZOC5
ID FCL_AZOC5 Reviewed; 312 AA.
AC P33217; A8IPA5;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=GDP-L-fucose synthase {ECO:0000255|HAMAP-Rule:MF_00956};
DE EC=1.1.1.271 {ECO:0000255|HAMAP-Rule:MF_00956};
DE AltName: Full=GDP-4-keto-6-deoxy-D-mannose-3,5-epimerase-4-reductase {ECO:0000255|HAMAP-Rule:MF_00956};
DE AltName: Full=Nodulation protein NolK;
GN Name=fcl {ECO:0000255|HAMAP-Rule:MF_00956}; Synonyms=nolK;
GN OrderedLocusNames=AZC_3850;
OS Azorhizobium caulinodans (strain ATCC 43989 / DSM 5975 / JCM 20966 / LMG
OS 6465 / NBRC 14845 / NCIMB 13405 / ORS 571).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Xanthobacteraceae; Azorhizobium.
OX NCBI_TaxID=438753;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RX PubMed=1472718; DOI=10.1094/mpmi-5-405;
RA Goethals K., Mergaert P., Gao M., Geelen D., van Montagu M., Holsters M.;
RT "Identification of a new inducible nodulation gene in Azorhizobium
RT caulinodans.";
RL Mol. Plant Microbe Interact. 5:405-411(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43989 / DSM 5975 / JCM 20966 / LMG 6465 / NBRC 14845 / NCIMB
RC 13405 / ORS 571;
RA Lee K.B., Backer P.D., Aono T., Liu C.T., Suzuki S., Suzuki T., Kaneko T.,
RA Yamada M., Tabata S., Kupfer D.M., Najar F.Z., Wiley G.B., Roe B.,
RA Binnewies T., Ussery D., Vereecke D., Gevers D., Holsters M., Oyaizu H.;
RT "Complete genome sequence of the nitrogen-fixing bacterium Azorhizobium
RT caulinodans ORS571.";
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PATHWAY.
RC STRAIN=ATCC 43989 / DSM 5975 / JCM 20966 / LMG 6465 / NBRC 14845 / NCIMB
RC 13405 / ORS 571;
RX PubMed=9202168; DOI=10.1016/s0014-5793(97)00461-4;
RA Mergaert P., Van Montagu M., Holsters M.;
RT "The nodulation gene nolK of Azorhizobium caulinodans is involved in the
RT formation of GDP-fucose from GDP-mannose.";
RL FEBS Lett. 409:312-316(1997).
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:0000255|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:0000255|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:0000255|HAMAP-Rule:MF_00956, ECO:0000269|PubMed:9202168}.
CC -!- INDUCTION: By flavanone naringenin. {ECO:0000269|PubMed:1472718}.
CC -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC family. Fucose synthase subfamily. {ECO:0000255|HAMAP-Rule:MF_00956}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB24744.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAF89848.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; S51942; AAB24744.1; ALT_INIT; Genomic_DNA.
DR EMBL; AP009384; BAF89848.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; P33217; -.
DR SMR; P33217; -.
DR STRING; 438753.AZC_3850; -.
DR EnsemblBacteria; BAF89848; BAF89848; AZC_3850.
DR KEGG; azc:AZC_3850; -.
DR eggNOG; COG0451; Bacteria.
DR HOGENOM; CLU_007383_18_0_5; -.
DR UniPathway; UPA00128; UER00191.
DR Proteomes; UP000000270; 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 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 Pfam; PF01370; Epimerase; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 2: Evidence at transcript level;
KW Isomerase; Multifunctional enzyme; NADP; Nodulation; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..312
FT /note="GDP-L-fucose synthase"
FT /id="PRO_0000174359"
FT ACT_SITE 136
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00956"
FT BINDING 11..17
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00956"
FT BINDING 140
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00956"
FT BINDING 179
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00956"
FT BINDING 187
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00956"
FT BINDING 202
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00956"
FT BINDING 209
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00956"
FT SITE 107
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00956"
FT SITE 109
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00956"
SQ SEQUENCE 312 AA; 34301 MW; BC2FCB01C87C097C CRC64;
MGKGKKLLIT GGRGMVGRNL IACAARSGWE IIAPTSVDLD LRNAEAVEQY IRRQLPDVVV
HAAGVVGGIH ANIADPIHFL ADNAAMALNV VMSSFRSEVV TLINLSSSCM YPACIEGPLK
ECDILRGPFE VTNEGYALAK TVGLKICEYI DKLPNFNYKT LIACNLYGVG DNFDPRRSHL
LPAIIEKIHK ASQCGSESVS IWGDGTARRE FMFAYDFAKI IIKALEVPEL IPSSMNVGVG
KDLSVLEYYS LVARVIGWSG EFVYDLNRPV GMRSKLMDIT HLTALGWVPE RSLEGGIRST
YQYYITGNEV YE
