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Protein

dTDP-4-dehydrorhamnose 3,5-epimerase

Gene

rfbC

Organism
Sulfolobus tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
Status
Unreviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the epimerization of the C3' and C5'positions of dTDP-6-deoxy-D-xylo-4-hexulose, forming dTDP-6-deoxy-L-lyxo-4-hexulose.UniRule annotation

Catalytic activityi

dTDP-4-dehydro-6-deoxy-alpha-D-glucose = dTDP-4-dehydro-beta-L-rhamnose.UniRule annotation

Pathwayi: dTDP-L-rhamnose biosynthesis

This protein is involved in the pathway dTDP-L-rhamnose biosynthesis, which is part of Carbohydrate biosynthesis.UniRule annotation
View all proteins of this organism that are known to be involved in the pathway dTDP-L-rhamnose biosynthesis and in Carbohydrate biosynthesis.

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionIsomeraseUniRule annotationImported

Enzyme and pathway databases

UniPathwayiUPA00124.

Names & Taxonomyi

Protein namesi
Recommended name:
dTDP-4-dehydrorhamnose 3,5-epimeraseUniRule annotation (EC:5.1.3.13UniRule annotation)
Alternative name(s):
Thymidine diphospho-4-keto-rhamnose 3,5-epimeraseUniRule annotation
Gene namesi
Name:rfbCImported
Synonyms:rmlCImported, ST1969Imported
Ordered Locus Names:STK_19690Imported
OrganismiSulfolobus tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)Imported
Taxonomic identifieri273063 [NCBI]
Taxonomic lineageiArchaeaCrenarchaeotaThermoproteiSulfolobalesSulfolobaceaeSulfolobus
Proteomesi
  • UP000001015 Componenti: Chromosome

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi144 ↔ 166Combined sources

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi273063.ST1969.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1WLTX-ray1.90A/B1-176[»]
2B9UX-ray2.07A/B/C/D/E/F/G/H/I/J/K/L1-176[»]
ProteinModelPortaliQ96Z62.
SMRiQ96Z62.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ96Z62.

Family & Domainsi

Sequence similaritiesi

Belongs to the dTDP-4-dehydrorhamnose 3,5-epimerase family.UniRule annotation

Phylogenomic databases

eggNOGiarCOG04188. Archaea.
COG1898. LUCA.
HOGENOMiHOG000227724.
KOiK01790.
OMAiRSILWND.
OrthoDBiPOG093Z0GEM.

Family and domain databases

Gene3Di2.60.120.10. 1 hit.
InterProiView protein in InterPro
IPR000888. dTDP_sugar_isom.
IPR014710. RmlC-like_jellyroll.
IPR011051. RmlC_Cupin_sf.
PANTHERiPTHR21047. PTHR21047. 1 hit.
PfamiView protein in Pfam
PF00908. dTDP_sugar_isom. 1 hit.
ProDomiView protein in ProDom or Entries sharing at least one domain
PD001462. dTDP_sugar_isom. 1 hit.
SUPFAMiSSF51182. SSF51182. 1 hit.
TIGRFAMsiTIGR01221. rmlC. 1 hit.

Sequencei

Sequence statusi: Complete.

Q96Z62-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPFEFENLGM GIILIKPKVF PDKRGFFLEV FKSEDFTKMR IPNVIQTNMS
60 70 80 90 100
FSRKGVVRGL HYQRTPKEQG KIIFVPKGRI LDVAVDVRKS SPTFGKYVKA
110 120 130 140 150
ELNEENHYML WIPPGFAHGF QALEDSIVIY FITHNEYSPP HERCISYSYI
160 170
DWPIKEVIIS DKDLQCPSLE KAEVFD
Length:176
Mass (Da):20,478
Last modified:December 1, 2001 - v1
Checksum:iAAC82724A028BD05
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000023 Genomic DNA. Translation: BAB67064.1.
RefSeqiWP_010980040.1. NC_003106.2.

Genome annotation databases

EnsemblBacteriaiBAB67064; BAB67064; STK_19690.
GeneIDi1460029.
KEGGisto:STK_19690.
PATRICifig|273063.9.peg.2244.

Entry informationi

Entry nameiQ96Z62_SULTO
AccessioniPrimary (citable) accession number: Q96Z62
Entry historyiIntegrated into UniProtKB/TrEMBL: December 1, 2001
Last sequence update: December 1, 2001
Last modified: November 22, 2017
This is version 99 of the entry and version 1 of the sequence. See complete history.
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources, Complete proteome, Reference proteomeImported