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Protein

GDP-6-deoxy-D-mannose reductase

Gene

rmd

Organism
Aneurinibacillus thermoaerophilus
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Reductase that catalyzes the conversion of GDP-6-deoxy-D-mannose to GDP-4-dehydro-6-deoxy-D-mannose (GDP-D-rhamnose).2 Publications

Catalytic activityi

GDP-alpha-D-rhamnose + NAD(P)+ = GDP-4-dehydro-alpha-D-rhamnose + NAD(P)H.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei32 – 321NADP
Binding sitei140 – 1401NADP
Binding sitei169 – 1691Substrate1 Publication
Binding sitei183 – 1831Substrate1 Publication
Binding sitei209 – 2091Substrate1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi11 – 122NADP
Nucleotide bindingi47 – 482NADP
Nucleotide bindingi71 – 733NADP

GO - Molecular functioni

  • GDP-4-dehydro-6-deoxy-D-mannose reductase activity Source: UniProtKB

GO - Biological processi

  • oxidation-reduction process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NAD, NADP

Names & Taxonomyi

Protein namesi
Recommended name:
GDP-6-deoxy-D-mannose reductase (EC:1.1.1.281)
Gene namesi
Name:rmd
OrganismiAneurinibacillus thermoaerophilus
Taxonomic identifieri143495 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesPaenibacillaceaeAneurinibacillus groupAneurinibacillus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 309309GDP-6-deoxy-D-mannose reductasePRO_0000419037Add
BLAST

Structurei

Secondary structure

1
309
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 65Combined sources
Turni7 – 93Combined sources
Helixi11 – 2212Combined sources
Beta strandi26 – 327Combined sources
Beta strandi41 – 455Combined sources
Helixi51 – 6111Combined sources
Beta strandi64 – 685Combined sources
Helixi75 – 784Combined sources
Helixi82 – 10322Combined sources
Beta strandi108 – 1147Combined sources
Helixi115 – 1173Combined sources
Helixi123 – 1253Combined sources
Helixi139 – 15820Combined sources
Beta strandi161 – 1677Combined sources
Beta strandi169 – 1713Combined sources
Helixi180 – 19213Combined sources
Beta strandi198 – 2036Combined sources
Beta strandi208 – 2136Combined sources
Helixi214 – 22714Combined sources
Beta strandi233 – 2375Combined sources
Beta strandi241 – 2433Combined sources
Helixi244 – 25411Combined sources
Beta strandi255 – 2573Combined sources
Beta strandi260 – 2634Combined sources
Helixi265 – 2673Combined sources
Helixi281 – 2877Combined sources
Helixi295 – 30713Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2PK3X-ray1.82A/B1-309[»]
ProteinModelPortaliQ6T1X6.
SMRiQ6T1X6. Positions 1-309.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ6T1X6.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni114 – 1152Substrate binding
Regioni269 – 2724Substrate binding

Sequence similaritiesi

Phylogenomic databases

KOiK15856.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF16363. GDP_Man_Dehyd. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.

Sequencei

Sequence statusi: Complete.

Q6T1X6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRALITGVAG FVGKYLANHL TEQNVEVFGT SRNNEAKLPN VEMISLDIMD
60 70 80 90 100
SQRVKKVISD IKPDYIFHLA AKSSVKDSWL NKKGTFSTNV FGTLHVLDAV
110 120 130 140 150
RDSNLDCRIL TIGSSEEYGM ILPEESPVSE ENQLRPMSPY GVSKASVGML
160 170 180 190 200
ARQYVKAYGM DIIHTRTFNH IGPGQSLGFV TQDFAKQIVD IEMEKQEPII
210 220 230 240 250
KVGNLEAVRD FTDVRDIVQA YWLLSQYGKT GDVYNVCSGI GTRIQDVLDL
260 270 280 290 300
LLAMANVKID TELNPLQLRP SEVPTLIGSN KRLKDSTGWK PRIPLEKSLF

EILQSYRQA
Length:309
Mass (Da):34,556
Last modified:July 5, 2004 - v1
Checksum:i737FFC9390B14868
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY442352 Genomic DNA. Translation: AAS55712.1.

Genome annotation databases

KEGGiag:AAS55712.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY442352 Genomic DNA. Translation: AAS55712.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2PK3X-ray1.82A/B1-309[»]
ProteinModelPortaliQ6T1X6.
SMRiQ6T1X6. Positions 1-309.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGiag:AAS55712.

Phylogenomic databases

KOiK15856.

Miscellaneous databases

EvolutionaryTraceiQ6T1X6.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF16363. GDP_Man_Dehyd. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Identification of two GDP-6-deoxy-D-lyxo-4-hexulose reductases synthesizing GDP-D-rhamnose in Aneurinibacillus thermoaerophilus L420-91T."
    Kneidinger B., Graninger M., Adam G., Puchberger M., Kosma P., Zayni S., Messner P.
    J. Biol. Chem. 276:5577-5583(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY.
    Strain: L420-91T.
  2. "The structural basis for catalytic function of GMD and RMD, two closely related enzymes from the GDP-D-rhamnose biosynthesis pathway."
    King J.D., Poon K.K.H., Webb N.A., Anderson E.M., McNally D.J., Brisson J.-R., Messner P., Garavito R.M., Lam J.S.
    FEBS J. 276:2686-2700(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.82 ANGSTROMS) IN COMPLEX WITH SUBSTRATE AND NADP ANALOG, FUNCTION, CATALYTIC ACTIVITY.

Entry informationi

Entry nameiRMD_ANETH
AccessioniPrimary (citable) accession number: Q6T1X6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 5, 2012
Last sequence update: July 5, 2004
Last modified: December 9, 2015
This is version 51 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

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.