L-rhamnose mutarotase - Escherichia coli (strain K12)

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Reviewed, UniProtKB/Swiss-Prot P32156 (RHAM_ECOLI)

Last modified November 24, 2009. Version 70. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    L-rhamnose mutarotase
    EC=5.1.3.n3
Alternative name(s):
    Rhamnose 1-epimerase
    Type-3 mutarotase

Gene names

Name:	rhaM
Synonyms:	yiiL
Ordered Locus Names:	b3901, JW3872

Organism

Escherichia coli (strain K12) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

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Protein attributes

Sequence length	104 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	Involved in the anomeric conversion of L-rhamnose. Ref.4
Catalytic activity	Alpha-L-rhamnose = beta-L-rhamnose. HAMAP MF_01663
Pathway	Carbohydrate metabolism; L-rhamnose metabolism. HAMAP MF_01663
Subunit structure	Homodimer. Ref.5
Subcellular location	Cytoplasm Potential.
Sequence similarities	Belongs to the rhamnose mutarotase family.

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Ontologies

Keywords
Biological process	Carbohydrate metabolism Rhamnose metabolism
Cellular component	Cytoplasm
Molecular function	Isomerase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	rhamnose metabolic process Inferred from electronic annotation. Source: HAMAP
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	protein binding Inferred from physical interaction. Source: IntAct racemase and epimerase activity, acting on carbohydrates and derivatives Inferred from electronic annotation. Source: EC
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct	Notes
gloA	P0AC81	1	EBI-1134000,EBI-551143

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 104

104

L-rhamnose mutarotase HAMAP MF_01663

PRO_0000169687

Regions

Region

76 – 77

Substrate binding HAMAP MF_01663

Sites

Active site

Proton donor Probable

Binding site

Substrate HAMAP MF_01663

Binding site

Substrate HAMAP MF_01663

Experimental info

Mutagenesis

Y → F: Loss of mutarotase activity. Ref.5

Secondary structure

104

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P32156-1 [UniParc].

Last modified October 1, 1993. Version 1.
Checksum: 6A276C08E0EEC7E2
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FASTA

104

12,265

        10         20         30         40         50         60 
MIRKAFVMQV NPDAHEEYQR RHNPIWPELE AVLKSHGAHN YAIYLDKARN LLFAMVEIES 

        70         80         90        100 
EERWNAVAST DVCQRWWKYM TDVMPANPDN SPVSSELQEV FYLP

« Hide

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Analysis of the Escherichia coli genome. III. DNA sequence of the region from 87.2 to 89.2 minutes." Plunkett G. III, Burland V., Daniels D.L., Blattner F.R. Nucleic Acids Res. 21:3391-3398(1993) [PubMed: 8346018] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[2]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[3]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]	"NMR application probes a novel and ubiquitous family of enzymes that alter monosaccharide configuration." Ryu K.-S., Kim C., Kim I., Yoo S., Choi B.-S., Park C. J. Biol. Chem. 279:25544-25548(2004) [PubMed: 15060078] [Abstract] Cited for: FUNCTION AS A MUTAROTASE.
[5]	"Structural insights into the monosaccharide specificity of Escherichia coli rhamnose mutarotase." Ryu K.-S., Kim J.-I., Cho S.-J., Park D., Park C., Cheong H.-K., Lee J.-O., Choi B.-S. J. Mol. Biol. 349:153-162(2005) [PubMed: 15876375] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH L-RHAMNOSE, SUBUNIT, MUTAGENESIS OF TYR-18, REACTION MECHANISM.

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Cross-references

Sequence databases

L19201 Genomic DNA. Translation: AAB03034.1.
U00096 Genomic DNA. Translation: AAC76883.1.
AP009048 Genomic DNA. Translation: BAE77408.1.

PIR

S40845.

RefSeq

AP_003907.1.
NP_418337.1.

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1X8D	X-ray	1.80	A/B/C/D	1-104	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P32156. 2 interactions.

STRING

P32156.

Genome annotation databases

GeneID

948402.

GenomeReviews

Gene locus JW3872 in contig AP009048_GR.
Gene locus b3901 in contig U00096_GR.

KEGG

ecj:JW3872.
eco:b3901.

Organism-specific databases

EchoBASE

EB1811.

EcoGene

EG11865. rhaM.

CMR

Search...

Phylogenomic databases

HOGENOM

P32156.

OMA

DHGAHHY

Enzyme and pathway databases

BioCyc

EcoCyc:EG11865-MON.
ECOL168927:B3901-MON.
MetaCyc:EG11865-MON.

Gene expression databases

Genevestigator

P32156.

Family and domain databases

HAMAP

MF_01663.
[Tree]

InterPro

IPR013448. L-rhamnose_1-epimerase.
IPR008000. Rhamnose_mutarotase.
[Graphical view]

Pfam

PF05336. DUF718. 1 hit.
[Graphical view]

TIGRFAMs

TIGR02625. YiiL_rotase. 1 hit.

ProtoNet

Search...

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Entry information

Entry name

RHAM_ECOLI

Accession

Primary (citable) accession number: P32156
Secondary accession number(s): Q2M8J8

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	October 1, 1993
Last modified:	November 24, 2009
This is version 70 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents