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P55250 (FUMH_RHIOR) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 80. 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, mitochondrial

Short name=Fumarase
EC=4.2.1.2
Gene names
Name:FUMR
OrganismRhizopus oryzae (Mucormycosis agent) (Rhizopus arrhizus var. delemar)
Taxonomic identifier64495 [NCBI]
Taxonomic lineageEukaryotaFungiFungi incertae sedisEarly diverging fungal lineagesMucoromycotinaMucoralesMucorineaeRhizopodaceaeRhizopus

Protein attributes

Sequence length494 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

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

Subcellular location

Mitochondrion. 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.

Ontologies

Keywords
   Biological processTricarboxylic acid cycle
   Cellular componentCytoplasm
Mitochondrion
   DomainTransit peptide
   Molecular functionLyase
Gene Ontology (GO)
   Biological_processfumarate metabolic process

Inferred from electronic annotation. Source: InterPro

tricarboxylic acid cycle

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentmitochondrion

Inferred from electronic annotation. Source: UniProtKB-SubCell

tricarboxylic acid cycle enzyme complex

Inferred from electronic annotation. Source: InterPro

   Molecular_functionfumarate hydratase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 1515Mitochondrion Potential
Chain16 – 494479Fumarate hydratase, mitochondrial HAMAP-Rule MF_00743
PRO_0000010331

Regions

Region159 – 1624B site By similarity
Region169 – 1713Substrate binding By similarity

Sites

Binding site1301Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
P55250 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 8FDB9D323A9146EE

FASTA49453,157
        10         20         30         40         50         60 
MLRASATRFL SQAKNMNNSP RLFSSASAAL QKFRAERDTF GDLQVPADRY WGAQTQRSLQ 

        70         80         90        100        110        120 
NFDIGGPTER MPEPLIRAFG VLKKAAATVN MTYGLDPKVG EAIQKAADEV IDGSLIDHFP 

       130        140        150        160        170        180 
LVVWQTGSGT QTKMNVNEVI SNRAIELLGG ELGSKAPVHP NDHVNMSQSS NDTFPTAMHV 

       190        200        210        220        230        240 
AAVVEIHGRL IPALTTLRDA LQAKSAEFEH IIKIGRTHLQ DATPLTLGQE FSGYTQQLTY 

       250        260        270        280        290        300 
GIARVQGTLE RLYNLAQGGT AVGTGLNTRK GFDAKVAEAI ASITGLPFKT APNKFEALAA 

       310        320        330        340        350        360 
HDALVEAHGA LNTVACSLMK IANDIRYLGS GPRCGLGELS LPENEPGSSI MPGKVNPTQC 

       370        380        390        400        410        420 
EAMTMVCAQV MGNNTAISVA GSNGQFELNV FKPVMIKNLI QSIRLISDAS ISFTKNCVVG 

       430        440        450        460        470        480 
IEANEKKISS IMNESLMLVT ALNPHIGYDK AAKCAKKAHK EGTTLKEAAL SLGYLTSEEF 

       490 
DQWVRPEDMI SAKD 

« Hide

References

[1]"The fumR gene encoding fumarase in the filamentous fungus Rhizopus oryzae: cloning, structure and expression."
Friedberg D., Peleg Y., Monsonego A., Maissi S., Battat E., Rokem J.S., Goldberg I.
Gene 163:139-144(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 10260 / CBS 329.47 / DSM 905 / NRRL 1526.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X78576 Genomic DNA. Translation: CAA55314.1.

3D structure databases

ProteinModelPortalP55250.
SMRP55250. Positions 33-493.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

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 nameFUMH_RHIOR
AccessionPrimary (citable) accession number: P55250
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: March 19, 2014
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways