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Q9KCL9 (RHAA_BACHD) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
L-rhamnose isomerase

EC=5.3.1.14
Gene names
Name:rhaA
Ordered Locus Names:BH1552
OrganismBacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125) [Complete proteome] [HAMAP]
Taxonomic identifier272558 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length418 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

L-rhamnopyranose = L-rhamnulose. HAMAP-Rule MF_00541

Cofactor

Binds 1 manganese ion per subunit By similarity. HAMAP-Rule MF_00541

Pathway

Carbohydrate degradation; L-rhamnose degradation; glycerone phosphate from L-rhamnose: step 1/3. HAMAP-Rule MF_00541

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00541.

Sequence similarities

Belongs to the rhamnose isomerase family.

Ontologies

Keywords
   Biological processRhamnose metabolism
   Cellular componentCytoplasm
   LigandManganese
Metal-binding
   Molecular functionIsomerase
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological_processrhamnose catabolic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionL-rhamnose isomerase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

manganese ion binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 418418L-rhamnose isomerase HAMAP-Rule MF_00541
PRO_0000090549

Sites

Metal binding2611Manganese By similarity
Metal binding2931Manganese By similarity
Metal binding2951Manganese By similarity

Secondary structure

............................................................................. 418
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9KCL9 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 10165258A259864F

FASTA41848,178
        10         20         30         40         50         60 
MSMKSQFERA KIEYGQWGID VEEALERLKQ VPISIHCWQG DDVGGFELSK GELSGGIDVT 

        70         80         90        100        110        120 
GDYPGKATTP EELRMDLEKA LSLIPGKHRV NLHAIYAETD GKVVERDQLE PRHFEKWVRW 

       130        140        150        160        170        180 
AKRHGLGLDF NPTLFSHEKA KDGLTLAHPD QAIRQFWIDH CIASRKIGEY FGKELETPCL 

       190        200        210        220        230        240 
TNIWIPDGYK DTPSDRLTPR KRLKESLDQI FAAEINEAYN LDAVESKLFG IGSESYVVGS 

       250        260        270        280        290        300 
HEFYLSYALK NDKLCLLDTG HYHPTETVSN KISAMLLFHD KLALHVSRPV RWDSDHVVTF 

       310        320        330        340        350        360 
DDELREIALE IVRNDALDRV LIGLDFFDAS INRIAAWTIG TRNVIKALLF AMLIPHKQLK 

       370        380        390        400        410 
EWQETGDYTR RLAVLEEFKT YPLGAIWNEY CERMNVPIKE EWLKEIAIYE KEVLLQRH 

« Hide

References

[1]"Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans and genomic sequence comparison with Bacillus subtilis."
Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F., Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.
Nucleic Acids Res. 28:4317-4331(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000004 Genomic DNA. Translation: BAB05271.1.
PIRH83843.
RefSeqNP_242418.1. NC_002570.2.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3P14X-ray2.51A/B/C/D1-418[»]
3UU0X-ray2.70A/B/C/D1-418[»]
3UVAX-ray2.69A/B/C/D1-418[»]
3UXIX-ray2.73A/B/C/D1-418[»]
ProteinModelPortalQ9KCL9.
SMRQ9KCL9. Positions 2-417.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272558.BH1552.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAB05271; BAB05271; BAB05271.
GeneID891271.
KEGGbha:BH1552.
PATRIC18940208. VBIBacHal18977_1617.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG4806.
HOGENOMHOG000269679.
KOK01813.
OMAIPVSMHC.
OrthoDBEOG6KMB74.

Enzyme and pathway databases

BioCycBHAL272558:GJC5-1636-MONOMER.
UniPathwayUPA00541; UER00601.

Family and domain databases

Gene3D3.20.20.150. 1 hit.
HAMAPMF_00541. RhaA.
InterProIPR009308. Rhamnose_isomerase.
IPR013022. Xyl_isomerase-like_TIM-brl.
[Graphical view]
PfamPF06134. RhaA. 1 hit.
[Graphical view]
SUPFAMSSF51658. SSF51658. 1 hit.
TIGRFAMsTIGR01748. rhaA. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ9KCL9.

Entry information

Entry nameRHAA_BACHD
AccessionPrimary (citable) accession number: Q9KCL9
Entry history
Integrated into UniProtKB/Swiss-Prot: December 19, 2001
Last sequence update: October 1, 2000
Last modified: May 14, 2014
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways