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P55294 (RMLB_NEIMB) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
dTDP-glucose 4,6-dehydratase
EC=4.2.1.46
Gene names
Name:rfbB1
Ordered Locus Names:NMB0063
AND
Name:rfbB2
Ordered Locus Names:NMB0079
OrganismNeisseria meningitidis serogroup B
Taxonomic identifier491 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Neisseriales › Neisseriaceae › Neisseria

Protein attributes

Sequence length355 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the dehydration of dTDP-D-glucose to form dTDP-6-deoxy-D-xylo-4-hexulose via a three-step process involving oxidation, dehydration and reduction By similarity.

Catalytic activity

dTDP-glucose = dTDP-4-dehydro-6-deoxy-D-glucose + H2O.

Cofactor

Binds 1 NAD ion per monomer By similarity.

Pathway

Carbohydrate biosynthesis; dTDP-L-rhamnose biosynthesis.

Bacterial outer membrane biogenesis; LPS O-antigen biosynthesis.

Subunit structure

Homodimer By similarity.

Sequence similarities

Belongs to the sugar epimerase family. dTDP-glucose dehydratase subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 355355dTDP-glucose 4,6-dehydratase
PRO_0000183242

Regions

Nucleotide binding8 – 147NAD Potential
Nucleotide binding33 – 364NAD By similarity
Nucleotide binding59 – 602NAD By similarity
Nucleotide binding160 – 1645NAD By similarity
Region134 – 1363Substrate binding By similarity
Region199 – 2002Substrate binding By similarity
Region215 – 2173Substrate binding By similarity
Region294 – 2974Substrate binding By similarity

Sites

Active site1351Proton donor By similarity
Active site1361Proton acceptor By similarity
Active site1601Proton acceptor By similarity
Binding site811NAD; via carbonyl oxygen By similarity
Binding site851Substrate; via carbonyl oxygen By similarity
Binding site1001NAD By similarity
Binding site1891Substrate By similarity
Binding site1901NAD; via amide nitrogen By similarity
Binding site2241Substrate By similarity
Binding site2591Substrate By similarity

Experimental info

Sequence conflict1 – 33MRK → MQTANKKT in AAA63157. Ref.1
Sequence conflict26 – 283RDA → QDS in AAA63157. Ref.1
Sequence conflict321V → L in AAA63157. Ref.1
Sequence conflict46 – 472EV → DI in AAA63157. Ref.1
Sequence conflict731Y → H in AAA63157. Ref.1
Sequence conflict1421G → H in AAA63157. Ref.1
Sequence conflict1521A → T in AAA63157. Ref.1
Sequence conflict2681A → T in AAA63157. Ref.1
Sequence conflict2741A → V in AAA63157. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P55294 [UniParc].

Last modified January 11, 2001. Version 2.
Checksum: 631AA0EDA02B6F41

FASTA35539,865
        10         20         30         40         50         60 
MRKILVTGGA GFIGSAVVRH IIRNTRDAVV NVDKLTYAGN LESLTEVADN PRYAFEQVDI 

        70         80         90        100        110        120 
CDRAELDRVF AQYRPDAVMH LAAESHVDRS IGSAGEFIQT NIVGTFNLLE AARAYWQQMP 

       130        140        150        160        170        180 
SEQHEAFRFH HISTDEVYGD LGGTDDLFTE TAPYAPSSPY SASKASSDHL VRAWLRTYGL 

       190        200        210        220        230        240 
PTIVTNCSNN YGPYHFPEKL IPLMILNALD GKPLPVYGDG MQIRDWLFVE DHARALYQVV 

       250        260        270        280        290        300 
TEGVVGETYN IGGHNEKANI EVVKTICALL EELAPEKPAG VARYEDLITF VQDRPGHDVR 

       310        320        330        340        350 
YAVDAAKIRR DLGWLPLETF ESGLRKTVQW YLDNKTWWQN VLNGSYRLER LGTGK

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		L09188 Genomic DNA. Translation: AAA63157.1.
AE002098 Genomic DNA. Translation: AAF40531.1.
AE002098 Genomic DNA. Translation: AAF40543.1.
PIRG81242.
S42431.
RefSeqNP_273127.1. NC_003112.2.
NP_273142.1. NC_003112.2.

3D structure databases

ProteinModelPortalP55294.
SMRP55294. Positions 1-350.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBNEIT00000009034; EBNEIP00000008654; EBNEIG00000009034.
EBNEIT00000009474; EBNEIP00000009094; EBNEIG00000009474.
GeneID902170.
902183.
GenomeReviewsGene locus NMB0063 in contig AE002098_GR.
Gene locus NMB0079 in contig AE002098_GR.
KEGGnme:NMB0063.
nme:NMB0079.
PATRIC20355131. VBINeiMen85645_0099.
TIGRNMB0063.
NMB0079.

Phylogenomic databases

GeneTreeEBGT00050000020552.
HOGENOMHBG755066.
OMAHEAFRFH.
ProtClustDBCLSK877380.

Enzyme and pathway databases

BioCycNMEN122586:NMB_0063-MONOMER.
NMEN122586:NMB_0079-MONOMER.

Family and domain databases

InterProIPR005888. dTDP_Gluc_deHydtase.
IPR001509. Epimerase_deHydtase.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
KOK01710.
PANTHERPTHR10366:SF41. PTHR10366:SF41. 1 hit.
PfamPF01370. Epimerase. 1 hit.
[Graphical view]
TIGRFAMsTIGR01181. DTDP_gluc_dehyt. 1 hit.
ProtoNetSearch...

Entry information

Entry nameRMLB_NEIMB
AccessionPrimary (citable) accession number: P55294
Secondary accession number(s): Q9JS14
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 11, 2001
Last modified: January 25, 2012
This is version 76 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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