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Reviewed, UniProtKB/Swiss-Prot P28894 (FUMC1_BRAJA)

Last modified February 9, 2010. Version 73. 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 1
      Short name=Fumarase C 1
    EC=4.2.1.2
Gene names
Name: fumC1
Synonyms: fumC
Ordered Locus Names: blr6519
OrganismBradyrhizobium japonicum [Complete proteome] [HAMAP]
Taxonomic identifier375 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBradyrhizobiaceaeBradyrhizobium

Protein attributes

Sequence length473 AA.
Sequence statusComplete.
Protein existenceInferred from homology.

General annotation (Comments)

Catalytic activity

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

Pathway

Carbohydrate metabolism; tricarboxylic acid cycle; (S)-malate from fumarate: step 1/1. HAMAP MF_00743

Subunit structure

Homotetramer By similarity. HAMAP MF_00743

Subcellular location

Cytoplasm HAMAP MF_00743.

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. HAMAP MF_00743

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 – 473473Fumarate hydratase class II 1 HAMAP MF_00743
PRO_0000161259

Regions

Region139 – 1424B site By similarity
Region149 – 1513Substrate binding By similarity

Sites

Binding site1101Substrate By similarity

Experimental info

Sequence conflict91 – 944IDGS → STAD in AAA26211. Ref.1
Sequence conflict91 – 944IDGS → STAD in AAA26212. Ref.1
Sequence conflict2201S → R in AAA26211. Ref.1
Sequence conflict2201S → R in AAA26212. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P28894-1 [UniParc].

Last modified December 15, 2003. Version 3.
Checksum: CDB35CFA32062957

FASTA47350,924
        10         20         30         40         50         60 
MAKSARTKTA RPATRTETDS FGPIEVPSDR YWGAQTERSR QNFRIGTDRM PISLVHALGI 

        70         80         90        100        110        120 
VKLAAAQSNR ELGLLDQRRA SAIIRAAREV IDGSLDDHFP LVVWQTGSGT QTNMNLNEVI 

       130        140        150        160        170        180 
ANRANELLGG ELGAKKPVHP NDHVNMSQSS NDSFPTAMHI AAASRITADL VPALGELLRA 

       190        200        210        220        230        240 
LRKKEKEFAK IVKIGRTHTQ DATPLTLGQE FSGYAAQVES GIARLKVAVK ELYPLAQGGT 

       250        260        270        280        290        300 
AVGTGLNAKP RFARLFAKHV AGITKLPFTS AANKFEALAS NDAYVLAHGA ISSVATGLFK 

       310        320        330        340        350        360 
IANDIRLLGS GPRSGLGELI LPENEPGSSI MPGKVNPTQC EAMTMVCCQV FGNHTAITVA 

       370        380        390        400        410        420 
GSQGHFELNV YKPVLAYNML HSIRLMADAA RSFTEHCVSG IRADEKRISE LMQRSLMLVT 

       430        440        450        460        470 
ALAPKIGYDN AAKVAKTAHA NGTTLKEEAL RLGFVTADEF DRLVQPEKMT KPG 

« Hide

References

« Hide 'large scale' references
[1]"Cloning, sequencing, and mutational analysis of the Bradyrhizobium japonicum fumC-like gene: evidence for the existence of two different fumarases."
Acuna G., Ebeling S., Hennecke H.
J. Gen. Microbiol. 137:991-1000(1991) [PubMed: 1856685] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: USDA 110spc4.
[2]"Complete genomic sequence of nitrogen-fixing symbiotic bacterium Bradyrhizobium japonicum USDA110."
Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S., Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M., Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.
DNA Res. 9:189-197(2002) [PubMed: 12597275] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: USDA 110.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M79457 Genomic DNA. Translation: AAA26211.1. Different initiation.
M79457 Genomic DNA. Translation: AAA26212.1.
BA000040 Genomic DNA. Translation: BAC51784.1. Different initiation.
RefSeqNP_773159.2.

3D structure databases

SMRP28894. Positions 15-472.
ModBaseSearch...

Genome annotation databases

GeneID1054478.
GenomeReviewsGene locus blr6519 in contig BA000040_GR.
KEGGbja:blr6519.
NMPDRfig|224911.1.peg.6519.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG284369.
OMARIEKDTM.
PhylomeDBP28894.

Enzyme and pathway databases

BioCycBJAP224911:BLR6519-MONOMER.
BRENDA4.2.1.2. 280.

Family and domain databases

HAMAPMF_00743. FumaraseC.
[Tree]
InterProIPR005677. Fum_hydII.
IPR018951. Fumarase_C_C.
IPR000362. Fumarate_lyase.
IPR020557. Fumarate_lyase_CS.
IPR008948. L-Aspartase-like.
[Graphical view]
PfamPF10415. FumaraseC_C. 1 hit.
PF00206. Lyase_1. 1 hit.
[Graphical view]
PRINTSPR00149. FUMRATELYASE.
TIGRFAMsTIGR00979. fumC_II. 1 hit.
PROSITEPS00163. FUMARATE_LYASES. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFUMC1_BRAJA
AccessionPrimary (citable) accession number: P28894
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: December 15, 2003
Last modified: February 9, 2010
This is version 73 of the entry and version 3 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