(data stored in ACNUC7421 zone)

SWISSPROT: Q144V3_PARXL

ID   Q144V3_PARXL            Unreviewed;       319 AA.
AC   Q144V3;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   08-MAY-2019, entry version 82.
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=Bxe_A3862 {ECO:0000313|EMBL:ABE29136.1};
OS   Paraburkholderia xenovorans (strain LB400).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=266265 {ECO:0000313|EMBL:ABE29136.1, ECO:0000313|Proteomes:UP000001817};
RN   [1] {ECO:0000313|EMBL:ABE29136.1, ECO:0000313|Proteomes:UP000001817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LB400 {ECO:0000313|EMBL:ABE29136.1,
RC   ECO:0000313|Proteomes:UP000001817};
RX   PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA   Chain P.S., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA   Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M.,
RA   Lao V., Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A.,
RA   Marx C.J., Parnell J.J., Ramette A., Richardson P., Seeger M.,
RA   Smith D., Spilker T., Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B.,
RA   Tiedje J.M.;
RT   "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp
RT   genome shaped for versatility.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006).
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}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00956}.
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DR   EMBL; CP000270; ABE29136.1; -; Genomic_DNA.
DR   RefSeq; WP_007179058.1; NZ_CP008760.1.
DR   STRING; 266265.Bxe_A3862; -.
DR   EnsemblBacteria; ABE29136; ABE29136; Bxe_A3862.
DR   GeneID; 4002485; -.
DR   KEGG; bxb:DR64_1538; -.
DR   KEGG; bxe:Bxe_A3862; -.
DR   eggNOG; ENOG4105C30; Bacteria.
DR   eggNOG; COG0451; LUCA.
DR   HOGENOM; HOG000168011; -.
DR   KO; K02377; -.
DR   OMA; NDSYPAE; -.
DR   OrthoDB; 1558163at2; -.
DR   BioCyc; BXEN266265:BXE_RS02955-MONOMER; -.
DR   UniPathway; UPA00128; UER00191.
DR   Proteomes; UP000001817; Chromosome 1.
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; Q144V3.
DR   SWISS-2DPAGE; Q144V3.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001817};
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:ABE29136.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001817}.
FT   DOMAIN        7    238       Epimerase. {ECO:0000259|Pfam:PF01370}.
FT   NP_BIND      11     17       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   319 AA;  35022 MW;  2BEB27CD279646D2 CRC64;
     MNKQARIFVA GHRGMVGSAL VRRLAADGYQ NVITRSRQEL DLTDQGAVNR FFESERIDVV
     LLAAARVGGI LANATRPGEF IYENLVIETN VIHAAYRARV ERLVFFGSSC IYPKQCPQPI
     REEYLLTSPL EPTNDAYAIA KIAGVKLCEA YNREYNTQYV ALMPTNLYGP NDNYDLNSSH
     VLPALLRKAH EAKLNGDATL SVWGSGTPRR EFLHVDDLAA ATLFVLEHNV TEGLFNVGVG
     KDLSIRELAE CICKVAGFDG ELMFDASKPD GTPRKLLDVS RLAQMGWQAS IALEDGIAST
     YRDFVESHAG STPAAAVEV
//

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