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Protein

CDP-paratose 2-epimerase

Gene

rfbE

Organism
Salmonella typhi
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Catalyzes the isomeration of CDP-paratose to CDP-tyvelose.

Catalytic activityi

CDP-3,6-dideoxy-D-glucose = CDP-3,6-dideoxy-D-mannose.

Cofactori

NAD+Note: Binds 1 NAD+ per subunit.

Pathwayi: CDP-3,6-dideoxy-D-mannose biosynthesis

This protein is involved in step 5 of the subpathway that synthesizes CDP-3,6-dideoxy-D-mannose from CTP and alpha-D-glucose 1-phosphate.
Proteins known to be involved in the 5 steps of the subpathway in this organism are:
  1. Glucose-1-phosphate cytidylyltransferase (rfbF)
  2. no protein annotated in this organism
  3. no protein annotated in this organism
  4. CDP-paratose synthase (rfbS)
  5. CDP-paratose 2-epimerase (rfbE)
This subpathway is part of the pathway CDP-3,6-dideoxy-D-mannose biosynthesis, which is itself part of Nucleotide-sugar biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes CDP-3,6-dideoxy-D-mannose from CTP and alpha-D-glucose 1-phosphate, the pathway CDP-3,6-dideoxy-D-mannose biosynthesis and in Nucleotide-sugar biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei124Substrate1 Publication1
Active sitei164Proton acceptor1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionIsomerase
Biological processLipopolysaccharide biosynthesis

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-13795
UniPathwayiUPA00055; UER00515

Names & Taxonomyi

Protein namesi
Recommended name:
CDP-paratose 2-epimerase (EC:5.1.3.10)
Alternative name(s):
CDP-tyvelose 2-epimerase
Gene namesi
Name:rfbE
Ordered Locus Names:STY2298, t0784
OrganismiSalmonella typhi
Taxonomic identifieri90370 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeSalmonella
Proteomesi
  • UP000002670 Componenti: Chromosome
  • UP000000541 Componenti: Chromosome

Pathology & Biotechi

Chemistry databases

DrugBankiDB04555 Cytidine-5'-Diphosphate

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001832601 – 338CDP-paratose 2-epimeraseAdd BLAST338

Proteomic databases

PRIDEiP14169

Interactioni

Subunit structurei

Homotetramer.1 Publication

Protein-protein interaction databases

STRINGi220341.STY2298

Structurei

Secondary structure

1338
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 6Combined sources5
Turni7 – 9Combined sources3
Helixi11 – 22Combined sources12
Beta strandi26 – 31Combined sources6
Helixi38 – 46Combined sources9
Beta strandi52 – 55Combined sources4
Helixi61 – 71Combined sources11
Beta strandi74 – 78Combined sources5
Helixi85 – 90Combined sources6
Helixi92 – 113Combined sources22
Beta strandi118 – 124Combined sources7
Helixi125 – 128Combined sources4
Beta strandi136 – 138Combined sources3
Beta strandi143 – 145Combined sources3
Helixi162 – 182Combined sources21
Beta strandi185 – 191Combined sources7
Helixi207 – 219Combined sources13
Beta strandi226 – 232Combined sources7
Beta strandi235 – 237Combined sources3
Helixi241 – 253Combined sources13
Helixi255 – 258Combined sources4
Beta strandi262 – 267Combined sources6
Helixi269 – 271Combined sources3
Beta strandi272 – 274Combined sources3
Helixi275 – 286Combined sources12
Beta strandi292 – 295Combined sources4
Beta strandi303 – 305Combined sources3
Helixi310 – 316Combined sources7
Helixi324 – 337Combined sources14

3D structure databases

ProteinModelPortaliP14169
SMRiP14169
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP14169

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4108IAJ Bacteria
COG0451 LUCA
HOGENOMiHOG000167994
KOiK12454
OMAiRAGDQRY

Family and domain databases

InterProiView protein in InterPro
IPR016040 NAD(P)-bd_dom
IPR036291 NAD(P)-bd_dom_sf
PfamiView protein in Pfam
PF16363 GDP_Man_Dehyd, 1 hit
SUPFAMiSSF51735 SSF51735, 1 hit

Sequencei

Sequence statusi: Complete.

P14169-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKLLITGGCG FLGSNLASFA LSQGIDLIVF DNLSRKGATD NLHWLSSLGN
60 70 80 90 100
FEFVHGDIRN KNDVTRLITK YMPDSCFHLA GQVAMTTSID NPCMDFEINV
110 120 130 140 150
GGTLNLLEAV RQYNSNCNII YSSTNKVYGD LEQYKYNETE TRYTCVDKPN
160 170 180 190 200
GYDESTQLDF HSPYGCSKGA ADQYMLDYAR IFGLNTVVFR HSSMYGGRQF
210 220 230 240 250
ATYDQGWVGW FCQKAVEIKN GINKPFTISG NGKQVRDVLH AEDMISLYFT
260 270 280 290 300
ALANVSKIRG NAFNIGGTIV NSLSLLELFK LLEDYCNIDM RFTNLPVRES
310 320 330
DQRVFVADIK KITNAIDWSP KVSAKDGVQK MYDWTSSI
Length:338
Mass (Da):37,958
Last modified:February 1, 1996 - v2
Checksum:i031175EDCF533888
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M29682 Genomic DNA Translation: AAB49384.1
AL513382 Genomic DNA Translation: CAD02451.1
AE014613 Genomic DNA Translation: AAO68475.1
PIRiB33604
RefSeqiNP_456637.1, NC_003198.1
WP_000770936.1, NZ_QAVU01000001.1

Genome annotation databases

EnsemblBacteriaiAAO68475; AAO68475; t0784
CAD02451; CAD02451; CAD02451
GeneIDi1248633
KEGGistt:t0784
sty:STY2298
PATRICifig|220341.7.peg.2318

Similar proteinsi

Entry informationi

Entry nameiRFBE_SALTI
AccessioniPrimary (citable) accession number: P14169
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: February 1, 1996
Last modified: July 18, 2018
This is version 132 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

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