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Protein

dTDP-4-dehydrorhamnose 3,5-epimerase

Gene

rmlC

Organism
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum)
Status
Reviewed-Annotation score: Annotation score: 4 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.1 Publication

Catalytic activityi

dTDP-4-dehydro-6-deoxy-alpha-D-glucose = dTDP-4-dehydro-beta-L-rhamnose.1 Publication

Pathwayi: dTDP-L-rhamnose biosynthesis

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei26 – 261SubstrateBy similarity
Binding sitei31 – 311SubstrateBy similarity
Binding sitei61 – 611Substrate1 Publication
Binding sitei64 – 641SubstrateBy similarity
Binding sitei73 – 731SubstrateBy similarity
Binding sitei84 – 841SubstrateBy similarity
Binding sitei120 – 1201SubstrateBy similarity
Binding sitei172 – 1721SubstrateBy similarity

GO - Molecular functioni

  • dTDP-4-dehydrorhamnose 3,5-epimerase activity Source: UniProtKB

GO - Biological processi

  • dTDP-rhamnose biosynthetic process Source: UniProtKB-UniPathway
  • extracellular polysaccharide biosynthetic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Enzyme and pathway databases

BioCyciMTHE187420:GJNM-1794-MONOMER.
UniPathwayiUPA00124.

Names & Taxonomyi

Protein namesi
Recommended name:
dTDP-4-dehydrorhamnose 3,5-epimerase (EC:5.1.3.13)
Alternative name(s):
Thymidine diphospho-4-keto-rhamnose 3,5-epimerase
dTDP-4-keto-6-deoxyglucose 3,5-epimerase
dTDP-6-deoxy-D-xylo-4-hexulose 3,5-epimerase
dTDP-L-rhamnose synthase
Gene namesi
Name:rmlC
Ordered Locus Names:MTH_1790
OrganismiMethanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum)
Taxonomic identifieri187420 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanobacteriaMethanobacterialesMethanobacteriaceaeMethanothermobacter
Proteomesi
  • UP000005223 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 185185dTDP-4-dehydrorhamnose 3,5-epimerasePRO_0000395351Add
BLAST

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

STRINGi187420.MTH1790.

Structurei

Secondary structure

1
185
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 85Combined sources
Beta strandi15 – 195Combined sources
Beta strandi21 – 244Combined sources
Beta strandi27 – 304Combined sources
Helixi35 – 406Combined sources
Beta strandi49 – 568Combined sources
Beta strandi59 – 6911Combined sources
Beta strandi73 – 8816Combined sources
Turni94 – 974Combined sources
Beta strandi99 – 1057Combined sources
Turni106 – 1083Combined sources
Beta strandi111 – 1144Combined sources
Beta strandi118 – 1247Combined sources
Beta strandi126 – 13712Combined sources
Helixi141 – 1433Combined sources
Beta strandi144 – 1463Combined sources
Turni152 – 1543Combined sources
Helixi160 – 1623Combined sources
Helixi170 – 1734Combined sources
Turni178 – 1803Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EP0X-ray1.50A1-185[»]
1EPZX-ray1.75A1-185[»]
ProteinModelPortaliO27818.
SMRiO27818. Positions 3-185.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO27818.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni49 – 513Substrate binding

Sequence similaritiesi

Phylogenomic databases

eggNOGiarCOG04188. Archaea.
COG1898. LUCA.
KOiK01790.
OMAiAGFSINF.

Family and domain databases

Gene3Di2.60.120.10. 1 hit.
InterProiIPR000888. dTDP_sugar_isom.
IPR014710. RmlC-like_jellyroll.
IPR011051. RmlC_Cupin.
[Graphical view]
PANTHERiPTHR21047. PTHR21047. 1 hit.
PfamiPF00908. dTDP_sugar_isom. 1 hit.
[Graphical view]
ProDomiPD001462. dTDP_sugar_isom. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF51182. SSF51182. 1 hit.
TIGRFAMsiTIGR01221. rmlC. 1 hit.

Sequencei

Sequence statusi: Complete.

O27818-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAEFRFIKTS LDGAIIIEPE VYTDERGYFM ETFNEAIFQE NGLEVRFVQD
60 70 80 90 100
NESMSVRGVL RGLHFQREKP QGKLVRVIRG EIFDVAVDLR KNSDTYGEWT
110 120 130 140 150
GVRLSDENRR EFFIPEGFAH GFLALSDECI VNYKCTELYH PEYDSGIPWD
160 170 180
DPDIGIDWPL EMVDDLIISE KDRNWKPLRE NPVYL
Length:185
Mass (Da):21,678
Last modified:January 1, 1998 - v1
Checksum:iE321B0D881834139
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000666 Genomic DNA. Translation: AAB86256.1.
PIRiB69106.
RefSeqiWP_010877392.1. NC_000916.1.

Genome annotation databases

EnsemblBacteriaiAAB86256; AAB86256; MTH_1790.
GeneIDi1470875.
KEGGimth:MTH1790.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000666 Genomic DNA. Translation: AAB86256.1.
PIRiB69106.
RefSeqiWP_010877392.1. NC_000916.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EP0X-ray1.50A1-185[»]
1EPZX-ray1.75A1-185[»]
ProteinModelPortaliO27818.
SMRiO27818. Positions 3-185.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi187420.MTH1790.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAB86256; AAB86256; MTH_1790.
GeneIDi1470875.
KEGGimth:MTH1790.

Phylogenomic databases

eggNOGiarCOG04188. Archaea.
COG1898. LUCA.
KOiK01790.
OMAiAGFSINF.

Enzyme and pathway databases

UniPathwayiUPA00124.
BioCyciMTHE187420:GJNM-1794-MONOMER.

Miscellaneous databases

EvolutionaryTraceiO27818.

Family and domain databases

Gene3Di2.60.120.10. 1 hit.
InterProiIPR000888. dTDP_sugar_isom.
IPR014710. RmlC-like_jellyroll.
IPR011051. RmlC_Cupin.
[Graphical view]
PANTHERiPTHR21047. PTHR21047. 1 hit.
PfamiPF00908. dTDP_sugar_isom. 1 hit.
[Graphical view]
ProDomiPD001462. dTDP_sugar_isom. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF51182. SSF51182. 1 hit.
TIGRFAMsiTIGR01221. rmlC. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H.
  2. "Crystal structure of dTDP-4-keto-6-deoxy-D-hexulose 3,5-epimerase from Methanobacterium thermoautotrophicum complexed with dTDP."
    Christendat D., Saridakis V., Dharamsi A., Bochkarev A., Pai E.F., Arrowsmith C.H., Edwards A.M.
    J. Biol. Chem. 275:24608-24612(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEX WITH SUBSTRATE, FUNCTION IN DTDP-RHAMNOSE BIOSYNTHESIS, CATALYTIC ACTIVITY, SUBUNIT.

Entry informationi

Entry nameiRMLC_METTH
AccessioniPrimary (citable) accession number: O27818
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 13, 2010
Last sequence update: January 1, 1998
Last modified: December 9, 2015
This is version 99 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.