(data stored in SCRATCH zone)

SWISSPROT: A5GQG2_SYNR3

ID   A5GQG2_SYNR3            Unreviewed;       332 AA.
AC   A5GQG2;
DT   12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   12-JUN-2007, sequence version 1.
DT   08-MAY-2019, entry version 66.
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=wcaG {ECO:0000313|EMBL:CAK27121.1};
GN   Synonyms=fcl {ECO:0000256|HAMAP-Rule:MF_00956};
GN   OrderedLocusNames=SynRCC307_0218 {ECO:0000313|EMBL:CAK27121.1};
OS   Synechococcus sp. (strain RCC307).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=316278 {ECO:0000313|EMBL:CAK27121.1, ECO:0000313|Proteomes:UP000001115};
RN   [1] {ECO:0000313|EMBL:CAK27121.1, ECO:0000313|Proteomes:UP000001115}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCC307 {ECO:0000313|Proteomes:UP000001115};
RA   Genoscope;
RL   Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
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:
CC       Reaction=GDP-beta-L-fucose + NADP(+) = GDP-4-dehydro-alpha-D-
CC         rhamnose + H(+) + NADPH; Xref=Rhea:RHEA:18885,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:57964, ChEBI:CHEBI:58349; EC=1.1.1.271;
CC         Evidence={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; CT978603; CAK27121.1; -; Genomic_DNA.
DR   STRING; 316278.SynRCC307_0218; -.
DR   EnsemblBacteria; CAK27121; CAK27121; SynRCC307_0218.
DR   KEGG; syr:SynRCC307_0218; -.
DR   eggNOG; ENOG4105C30; Bacteria.
DR   eggNOG; COG0451; LUCA.
DR   HOGENOM; HOG000168011; -.
DR   KO; K02377; -.
DR   OMA; IHCAGRV; -.
DR   BioCyc; SSP316278:G1GJL-214-MONOMER; -.
DR   UniPathway; UPA00128; UER00191.
DR   Proteomes; UP000001115; 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   3: Inferred from homology;
DR   PRODOM; A5GQG2.
DR   SWISS-2DPAGE; A5GQG2.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001115};
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,
KW   ECO:0000313|EMBL:CAK27121.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001115}.
FT   DOMAIN       12    231       Epimerase. {ECO:0000259|Pfam:PF01370}.
FT   NP_BIND      14     20       NADP. {ECO:0000256|HAMAP-Rule:MF_00956}.
FT   NP_BIND     109    112       NADP. {ECO:0000256|HAMAP-Rule:MF_00956}.
FT   NP_BIND     167    170       NADP. {ECO:0000256|HAMAP-Rule:MF_00956}.
FT   ACT_SITE    140    140       Proton donor/acceptor.
FT                                {ECO:0000256|HAMAP-Rule:MF_00956}.
FT   BINDING     144    144       NADP. {ECO:0000256|HAMAP-Rule:MF_00956}.
FT   BINDING     183    183       NADP. {ECO:0000256|HAMAP-Rule:MF_00956}.
FT   BINDING     191    191       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00956}.
FT   BINDING     206    206       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00956}.
FT   BINDING     213    213       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00956}.
FT   BINDING     286    286       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00956}.
FT   SITE        111    111       Important for catalytic activity.
FT                                {ECO:0000256|HAMAP-Rule:MF_00956}.
FT   SITE        113    113       Important for catalytic activity.
FT                                {ECO:0000256|HAMAP-Rule:MF_00956}.
SQ   SEQUENCE   332 AA;  36246 MW;  CA535E5A4E96FFF1 CRC64;
     MTLIQPTDRF AIFGARGMAG SAISRALGRQ GYQDQLLPSR QQLDLLDGGS VDQWMATNKP
     DVVVLAAAKV GGILANNTYP ADFLLENLKI QTHVIESAWR HGVRRLLFLG SSCIYPKLAK
     QPIREESLLK GDLEPTNEWY AIAKIAGIKL CESLRKQYGF DAISLMPTNL YGPGDNYHPQ
     NSHVLPALIR RFHEAVQADA TSVTCWGSGS PLREFLHVDD LGDACVFALE RWSALAANAP
     KDQSGDALAF LNVGTGVDCT IKQLAEQVAA ATGFVGEIQW DTSKPDGTPK KQLDVSRLQA
     MGWSARIPLN QGIPMAFQDF KQAEAAQLVR SK
//

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