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P28894 (FUMC1_BRADU) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 101. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
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 diazoefficiens (strain JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110) [Reference proteome] [HAMAP]
Taxonomic identifier224911 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBradyrhizobiaceaeBradyrhizobium

Protein attributes

Sequence length473 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the reversible addition of water to fumarate to give L-malate By similarity. HAMAP-Rule MF_00743

Catalytic activity

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

Pathway

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

Subunit structure

Homotetramer By similarity. HAMAP-Rule MF_00743

Subcellular location

Cytoplasm HAMAP-Rule 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.

Sequence similarities

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

Sequence caution

The sequence AAA26211.1 differs from that shown. Reason: Erroneous initiation.

The sequence BAC51784.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processTricarboxylic acid cycle
   Cellular componentCytoplasm
   Molecular functionLyase
   Technical termAllosteric enzyme
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processfumarate metabolic process

Inferred from electronic annotation. Source: InterPro

tricarboxylic acid cycle

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componenttricarboxylic acid cycle enzyme complex

Inferred from electronic annotation. Source: InterPro

   Molecular_functionfumarate hydratase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 473473Fumarate hydratase class II 1 HAMAP-Rule MF_00743
PRO_0000161259

Regions

Region108 – 1103Substrate binding By similarity
Region139 – 1424B site By similarity
Region149 – 1513Substrate binding By similarity
Region197 – 1982Substrate binding By similarity
Region334 – 3363Substrate binding By similarity

Sites

Active site1981Proton donor/acceptor By similarity
Active site3281 By similarity
Binding site3291Substrate By similarity
Site3411Important for catalytic activity 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 [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: JCM 10833 / IAM 13628 / NBRC 14792 / 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. NC_004463.1.

3D structure databases

ProteinModelPortalP28894.
SMRP28894. Positions 15-472.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING224911.blr6519.

Proteomic databases

PRIDEP28894.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAC51784; BAC51784; BAC51784.
GeneID1054478.
KEGGbja:blr6519.
PATRIC21196868. VBIBraJap65052_6668.

Phylogenomic databases

eggNOGCOG0114.
HOGENOMHOG000061736.
KOK01679.
OMAIGHHTAI.
OrthoDBEOG6V1M4M.
ProtClustDBPRK00485.

Enzyme and pathway databases

BioCycBJAP224911:GJEJ-6569-MONOMER.
UniPathwayUPA00223; UER01007.

Family and domain databases

Gene3D1.10.275.10. 1 hit.
HAMAPMF_00743. FumaraseC.
InterProIPR005677. Fum_hydII.
IPR024083. Fumarase/histidase_N.
IPR018951. Fumarase_C_C.
IPR020557. Fumarate_lyase_CS.
IPR000362. Fumarate_lyase_fam.
IPR022761. Fumarate_lyase_N.
IPR008948. L-Aspartase-like.
[Graphical view]
PANTHERPTHR11444. PTHR11444. 1 hit.
PfamPF10415. FumaraseC_C. 1 hit.
PF00206. Lyase_1. 1 hit.
[Graphical view]
PRINTSPR00149. FUMRATELYASE.
SUPFAMSSF48557. SSF48557. 1 hit.
TIGRFAMsTIGR00979. fumC_II. 1 hit.
PROSITEPS00163. FUMARATE_LYASES. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFUMC1_BRADU
AccessionPrimary (citable) accession number: P28894
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: December 15, 2003
Last modified: March 19, 2014
This is version 101 of the entry and version 3 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

PATHWAY comments

Index of metabolic and biosynthesis pathways