(data stored in ACNUC7421 zone)

SWISSPROT: C6B1M8_RHILS

ID   C6B1M8_RHILS            Unreviewed;       306 AA.
AC   C6B1M8;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   07-JUN-2017, entry version 54.
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=Rleg_0438 {ECO:0000313|EMBL:ACS54747.1};
OS   Rhizobium leguminosarum bv. trifolii (strain WSM1325).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=395491 {ECO:0000313|EMBL:ACS54747.1, ECO:0000313|Proteomes:UP000002256};
RN   [1] {ECO:0000313|EMBL:ACS54747.1, ECO:0000313|Proteomes:UP000002256}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WSM1325 {ECO:0000313|EMBL:ACS54747.1,
RC   ECO:0000313|Proteomes:UP000002256};
RX   PubMed=21304718;
RA   Reeve W., O'Hara G., Chain P., Ardley J., Brau L., Nandesena K.,
RA   Tiwari R., Copeland A., Nolan M., Han C., Brettin T., Land M.,
RA   Ovchinikova G., Ivanova N., Mavromatis K., Markowitz V., Kyrpides N.,
RA   Melino V., Denton M., Yates R., Howieson J.;
RT   "Complete genome sequence of Rhizobium leguminosarum bv. trifolii
RT   strain WSM1325, an effective microsymbiont of annual Mediterranean
RT   clovers.";
RL   Stand. Genomic Sci. 2:347-356(2010).
CC   -!- FUNCTION: Catalyzes the two-step NADP-dependent conversion of GDP-
CC       4-dehydro-6-deoxy-D-mannose to GDP-fucose, involving an epimerase
CC       and a reductase reaction. {ECO:0000256|HAMAP-Rule:MF_00956}.
CC   -!- CATALYTIC ACTIVITY: GDP-beta-L-fucose + NADP(+) = GDP-4-dehydro-
CC       alpha-D-rhamnose + NADPH. {ECO:0000256|HAMAP-Rule:MF_00956}.
CC   -!- PATHWAY: Nucleotide-sugar biosynthesis; GDP-L-fucose biosynthesis
CC       via de novo pathway; GDP-L-fucose from GDP-alpha-D-mannose: step
CC       2/2. {ECO:0000256|HAMAP-Rule:MF_00956}.
CC   -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC       family. Fucose synthase subfamily. {ECO:0000256|HAMAP-
CC       Rule:MF_00956}.
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DR   EMBL; CP001622; ACS54747.1; -; Genomic_DNA.
DR   RefSeq; WP_012756135.1; NC_012850.1.
DR   ProteinModelPortal; C6B1M8; -.
DR   EnsemblBacteria; ACS54747; ACS54747; Rleg_0438.
DR   KEGG; rlg:Rleg_0438; -.
DR   HOGENOM; HOG000168011; -.
DR   KO; K02377; -.
DR   OMA; RQYGTKF; -.
DR   OrthoDB; POG091H0LVE; -.
DR   UniPathway; UPA00128; UER00191.
DR   Proteomes; UP000002256; Chromosome.
DR   GO; GO:0050577; F:GDP-L-fucose synthase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0070401; F:NADP+ binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0042351; P:'de novo' GDP-L-fucose biosynthetic process; IEA:UniProtKB-HAMAP.
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; IPR016040; NAD(P)-bd_dom.
DR   Pfam; PF01370; Epimerase; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   3: Inferred from homology;
DR   PRODOM; C6B1M8.
DR   SWISS-2DPAGE; C6B1M8.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002256};
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|HAMAP-Rule:MF_00956}.
FT   DOMAIN        7    238       Epimerase. {ECO:0000259|Pfam:PF01370}.
FT   NP_BIND      11     17       NADP. {ECO:0000256|HAMAP-Rule:MF_00956}.
FT   NP_BIND     106    109       NADP. {ECO:0000256|HAMAP-Rule:MF_00956}.
FT   NP_BIND     164    167       NADP. {ECO:0000256|HAMAP-Rule:MF_00956}.
FT   ACT_SITE    137    137       Proton donor/acceptor.
FT                                {ECO:0000256|HAMAP-Rule:MF_00956}.
FT   BINDING     141    141       NADP. {ECO:0000256|HAMAP-Rule:MF_00956}.
FT   BINDING     180    180       NADP. {ECO:0000256|HAMAP-Rule:MF_00956}.
FT   BINDING     188    188       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00956}.
FT   BINDING     203    203       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00956}.
FT   BINDING     210    210       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00956}.
FT   BINDING     270    270       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00956}.
FT   SITE        108    108       Important for catalytic activity.
FT                                {ECO:0000256|HAMAP-Rule:MF_00956}.
FT   SITE        110    110       Important for catalytic activity.
FT                                {ECO:0000256|HAMAP-Rule:MF_00956}.
SQ   SEQUENCE   306 AA;  34077 MW;  CB3EFC0E3FC48E63 CRC64;
     MNRDVKIYVA GHRGMVGSAI VRRLKAGGYT NIVTRSHAEL DLVNQAAVAE FMKAERPDYI
     FMAAARVGGI HANNVYRAEF LYQNLMIETN VVHAAWQAGV ERMLFLGSSC IYPRDCPQPI
     REEYLLTGPL EQTNEAYAIA KIAGVKLCES YNRQYGTRYV SGMPTNLYGP NDNYDLDSSH
     VMPALIRKVH EAKIRGDRQL VVWGSGRPMR EFLYVDDMAD ACVFLMEKEV SEGLINIGTG
     EDITIRELAE TIMRVVGFTG EIVYDQTKPD GTPRKLMSVD RLSALGWKAT TSLGDGIARA
     YADFAS
//

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