GDP-L-fucose synthase - Escherichia coli (strain K12)

Contribute

Send feedback

Read comments (?) or add your own

P32055 (FCL_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 116. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

text xml rdf/xml gff fasta

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
GDP-L-fucose synthase
EC=1.1.1.271

Alternative name(s):
GDP-4-keto-6-deoxy-D-mannose-3,5-epimerase-4-reductase

Gene names

Name:	fcl
Synonyms:	wcaG, yefB
Ordered Locus Names:	b2052, JW2037

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	321 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Two step NADP-dependent conversion of GDP-4-dehydro-6-deoxy-D-mannose to GDP-fucose, involving an epimerase and a reductase reaction.
Catalytic activity	GDP-beta-L-fucose + NADP⁺ = GDP-4-dehydro-6-deoxy-alpha-D-mannose + NADPH.
Pathway	Nucleotide-sugar biosynthesis; GDP-L-fucose biosynthesis via de novo pathway; GDP-L-fucose from GDP-alpha-D-mannose: step 2/2. Exopolysaccharide biosynthesis; colanic acid biosynthesis.
Subunit structure	Homodimer.
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the fucose synthase family.

Ontologies

Keywords
Biological process	Lipopolysaccharide biosynthesis
Cellular component	Cytoplasm
Ligand	NADP
Molecular function	Isomerase Oxidoreductase
Technical term	3D-structure Complete proteome Multifunctional enzyme Reference proteome
Gene Ontology (GO)
Biological_process	'de novo' GDP-L-fucose biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway colanic acid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway lipopolysaccharide biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	GDP-L-fucose synthase activity Inferred from direct assay PubMed 10480878. Source: EcoCyc coenzyme binding Inferred from electronic annotation. Source: InterPro isomerase activity Inferred from electronic annotation. Source: UniProtKB-KW nucleotide binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 321

321

GDP-L-fucose synthase

PRO_0000174358

Experimental info

Sequence conflict

255 – 256

EL → DV Ref.1

Sequence conflict

255 – 256

EL → DV Ref.2

Secondary structure

321

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P32055 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: 97077193D79684C7
Show »

FASTA

321

36,141

        10         20         30         40         50         60 
MSKQRVFIAG HRGMVGSAIR RQLEQRGDVE LVLRTRDELN LLDSRAVHDF FASERIDQVY 

        70         80         90        100        110        120 
LAAAKVGGIV ANNTYPADFI YQNMMIESNI IHAAHQNDVN KLLFLGSSCI YPKLAKQPMA 

       130        140        150        160        170        180 
ESELLQGTLE PTNEPYAIAK IAGIKLCESY NRQYGRDYRS VMPTNLYGPH DNFHPSNSHV 

       190        200        210        220        230        240 
IPALLRRFHE ATAQNAPDVV VWGSGTPMRE FLHVDDMAAA SIHVMELAHE VWLENTQPML 

       250        260        270        280        290        300 
SHINVGTGVD CTIRELAQTI AKVVGYKGRV VFDASKPDGT PRKLLDVTRL HQLGWYHEIS 

       310        320 
LEAGLASTYQ WFLENQDRFR G

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Evidence for effect of random genetic drift on G+C content after lateral transfer of fucose pathway genes to Escherichia coli K-12." Aoyama K., Haase A.M., Reeves P.R. Mol. Biol. Evol. 11:829-838(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[2]	"Organization of the Escherichia coli K-12 gene cluster responsible for production of the extracellular polysaccharide colanic acid." Stevenson G., Andrianopoulos K., Hobbs M., Reeves P.R. J. Bacteriol. 178:4885-4893(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[3]	"A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 40.1-50.0 min region on the linkage map." Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S. Horiuchi T. DNA Res. 3:379-392(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[5]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]	"Identification of the fucose synthetase gene in the colanic acid gene cluster of Escherichia coli K-12." Andrianopoulos K., Wang L., Reeves P.R. J. Bacteriol. 180:998-1001(1998) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION.
[7]	"GDP-fucose synthetase from Escherichia coli: structure of a unique member of the short-chain dehydrogenase/reductase family that catalyzes two distinct reactions at the same active site." Somers W.S., Stahl M.L., Sullivan F.X. Structure 6:1601-1612(1998) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS). Strain: K12.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U38473 Genomic DNA. Translation: AAC77843.1.
U00096 Genomic DNA. Translation: AAC75113.1.
AP009048 Genomic DNA. Translation: BAA15908.1.

PIR

C64971.

RefSeq

NP_416556.1. NC_000913.2.
YP_490294.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1BSV	X-ray	2.20	A	1-321	[»]
1BWS	X-ray	2.20	A	1-321	[»]
1E6U	X-ray	1.45	A	3-321	[»]
1E7Q	X-ray	1.60	A	3-321	[»]
1E7R	X-ray	1.60	A	1-321	[»]
1E7S	X-ray	1.50	A	1-321	[»]
1FXS	X-ray	2.30	A	1-321	[»]
1GFS	X-ray	2.20	A	1-321	[»]

ProteinModelPortal

P32055.

SMR

P32055. Positions 3-319.

ModBase

Search...

Protein-protein interaction databases

IntAct

P32055. 2 interactions.

STRING

511145.b2052.

Proteomic databases

PaxDb

P32055.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC75113; AAC75113; b2052.
BAA15908; BAA15908; BAA15908.

GeneID

12930697.
946563.

KEGG

ecj:Y75_p2015.
eco:b2052.

PATRIC

32119437. VBIEscCol129921_2129.

Organism-specific databases

EchoBASE

EB1736.

EcoGene

EG11788. fcl.

Phylogenomic databases

eggNOG

COG0451.

HOGENOM

HOG000168011.

K02377.

OMA

ASVHVMN.

ProtClustDB

CLSK880275.

Enzyme and pathway databases

BioCyc

EcoCyc:FCL-MONOMER.
ECOL316407:JW2037-MONOMER.
MetaCyc:FCL-MONOMER.

UniPathway

UPA00128; UER00191.
UPA00980.

Gene expression databases

Genevestigator

P32055.

Family and domain databases

Gene3D

3.40.50.720. 2 hits.

InterPro

IPR001509. Epimerase_deHydtase.
IPR016040. NAD(P)-bd_dom.
[Graphical view]

Pfam

PF01370. Epimerase. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P32055.

Entry information

Entry name

FCL_ECOLI

Accession

Primary (citable) accession number: P32055
Secondary accession number(s): P76382

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	November 1, 1997
Last modified:	May 1, 2013
This is version 116 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents