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Reviewed, UniProtKB/Swiss-Prot Q983U5 (FUMC_RHILO)

Last modified November 3, 2009. Version 43. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Fumarate hydratase class II
      Short name=Fumarase C
    EC=4.2.1.2
Gene names
Name: fumC
Ordered Locus Names: mll8172
OrganismRhizobium loti (Mesorhizobium loti) [Complete proteome] [HAMAP]
Taxonomic identifier381 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesPhyllobacteriaceaeMesorhizobium

Protein attributes

Sequence length465 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Catalytic activity

(S)-malate = fumarate + H2O. HAMAP MF_00743

Pathway

Carbohydrate metabolism; tricarboxylic acid cycle. HAMAP MF_00743

Subunit structure

Homotetramer By similarity.

Subcellular location

Cytoplasm By similarity.

Miscellaneous

There are 2 substrate binding sites: the catalytic A site, and the non-catalytic B site that may play a role in the transfer of substrate or product between the active site and the solvent. Alternatively, the B site may bind allosteric effectors By similarity.

Sequence similarities

Belongs to the class-II fumarase/aspartase family. Fumarase subfamily.

Ontologies

Keywords
   Biological processTricarboxylic acid cycle
   Cellular componentCytoplasm
   Molecular functionLyase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processfumarate metabolic process

Inferred from electronic annotation. Source: InterPro

tricarboxylic acid cycle

Inferred from electronic annotation. Source: HAMAP

   Cellular componenttricarboxylic acid cycle enzyme complex

Inferred from electronic annotation. Source: InterPro

   Molecular functionfumarate hydratase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 465465Fumarate hydratase class II HAMAP MF_00743
PRO_0000161304

Regions

Region131 – 1344B site By similarity
Region141 – 1433Substrate binding By similarity

Sites

Binding site1021Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q983U5-1 [UniParc].

Last modified October 1, 2001. Version 1.
Checksum: 85407C084D9221F9

FASTA46549,592
        10         20         30         40         50         60 
MTVAKTRTET DTFGPIEVAA DRYWGAQAQR SLGNFKIGWE KQPASIVRAL GVVKRAAAEV 

        70         80         90        100        110        120 
NMEMKRLDPV VGKAIVDAAQ EVIDGKLNDH FPLVVWQTGS GTQSNMNANE VISNRAIEML 

       130        140        150        160        170        180 
GGVMGSKKPV HPNDHVNMSQ SSNDTYPTAM HIACAEQVVH HLIPALHHLH KALDAKARAF 

       190        200        210        220        230        240 
NHIIKIGRTH TQDATPLTLG QEFSGYAAQV ASSIKRIEMT LPGLQELAQG GTAVGTGLNA 

       250        260        270        280        290        300 
PVGFAEKVAD RIAAITGIAF VTAPNKFEAL AAHDSMVFSH GAINAAAAAL FKIANDIRFL 

       310        320        330        340        350        360 
GSGPRSGLGE LSLPENEPGS SIMPGKVNPT QCEAMTQVCV QVFGNNAALT FAGSQGHFEL 

       370        380        390        400        410        420 
NVYNPLMAYN FLQSVQLLSD ASVSFTDNCV VGIEAREDNI KAALDRSLML VTALAPTIGY 

       430        440        450        460 
DNAAKIAKTA HKNGTTLREE ALATGLVSEV DYDRLVRPED MTHPG 

« Hide

References

[1]"Complete genome structure of the nitrogen-fixing symbiotic bacterium Mesorhizobium loti."
Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S., Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y., Nakayama S. expand/collapse author list , Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M., Tabata S.
DNA Res. 7:331-338(2000) [PubMed: 11214968] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MAFF303099.

Cross-references

Sequence databases

BA000012 Genomic DNA. Translation: BAB53785.1.
RefSeqNP_108324.1.

3D structure databases

HSSPHSSP built from PDB template 1YFM based on UniProtKB P08417.
ModBaseSearch...

Genome annotation databases

GeneID1230976.
GenomeReviewsGene locus mll8172 in contig BA000012_GR.
KEGGmlo:mll8172.
NMPDRfig|266835.1.peg.6423.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ983U5.
OMAGSQGHFE.

Enzyme and pathway databases

BRENDA4.2.1.2. 3315.

Family and domain databases

HAMAPMF_00743.
[Tree]
InterProIPR003031. D_crystallin.
IPR005677. Fum_hydII.
IPR018951. Fumarase_C_C.
IPR000362. Fumarate_lyase.
IPR020557. Fumarate_lyase_CS.
[Graphical view]
PfamPF10415. FumaraseC_C. 1 hit.
PF00206. Lyase_1. 1 hit.
[Graphical view]
PRINTSPR00145. ARGSUCLYASE.
PR00149. FUMRATELYASE.
TIGRFAMsTIGR00979. fumC_II. 1 hit.
PROSITEPS00163. FUMARATE_LYASES. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFUMC_RHILO
AccessionPrimary (citable) accession number: Q983U5
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: October 1, 2001
Last modified: November 3, 2009
This is version 43 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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