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Reviewed, UniProtKB/Swiss-Prot Q82SM5 (FUMC_NITEU)

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: NE2286
OrganismNitrosomonas europaea [Complete proteome] [HAMAP]
Taxonomic identifier915 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaNitrosomonadalesNitrosomonadaceaeNitrosomonas

Protein attributes

Sequence length462 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 – 462462Fumarate hydratase class II HAMAP MF_00743
PRO_0000161292

Regions

Region129 – 1324B site By similarity
Region139 – 1413Substrate binding By similarity

Sites

Binding site1001Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q82SM5-1 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: D20178003603A48A

FASTA46249,530
        10         20         30         40         50         60 
MDQYREEHDA IGTVQVPASA LWGAQTQRSL NNFNISGERM PSALIHALAL VKRAAASVNH 

        70         80         90        100        110        120 
DLGLLDENIA RAIITAADEV LAGEHAGEFP LVVWQTGSGT QTNMNMNEVL ANRASEILGG 

       130        140        150        160        170        180 
TRGKGRKVHP NDHVNKGQSS NDVFPTAMHI AAVEAIRNRL IPALEALRKT LSSKSAAFSD 

       190        200        210        220        230        240 
IVKIGRTHLQ DATPLTLGQE FSGYVSQLDH GLAHLESALP HLLELALGGT AVGTGLNTHP 

       250        260        270        280        290        300 
EFARRVAAEI ARLSGYPFIT AANKFEALAA HDALVHAHGV LKTLAAILIK IANDVRWLAS 

       310        320        330        340        350        360 
GPRCGIGEIL IPENEPGSSI MPGKVNPTQS EAVVMLACQV MGNDVAINLG GAMGNFELNT 

       370        380        390        400        410        420 
MKPLIIHNFL QSTRLLADGA ESFNTHCAAG ITANTVRIKQ HLQESLMLVT ALNPHIGYDK 

       430        440        450        460 
AAEIAKKAHH EMLTLKEAAI RLGYVTAEQF DVWVDPQKMT EV 

« Hide

References

[1]"Complete genome sequence of the ammonia-oxidizing bacterium and obligate chemolithoautotroph Nitrosomonas europaea."
Chain P., Lamerdin J.E., Larimer F.W., Regala W., Lao V., Land M.L., Hauser L., Hooper A.B., Klotz M.G., Norton J., Sayavedra-Soto L.A., Arciero D.M., Hommes N.G., Whittaker M.M., Arp D.J.
J. Bacteriol. 185:2759-2773(2003) [PubMed: 12700255] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 19718 / IFO 14298.

Cross-references

Sequence databases

AL954747 Genomic DNA. Translation: CAD86198.1.
RefSeqNP_842286.1.

3D structure databases

HSSPHSSP built from PDB template 1FUR based on UniProtKB P05042.
SMRQ82SM5. Positions 5-459.
ModBaseSearch...

Genome annotation databases

GeneID1083253.
GenomeReviewsGene locus NE2286 in contig AL954747_GR.
KEGGneu:NE2286.
NMPDRfig|228410.1.peg.2185.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ82SM5.
OMAGSQGHFE.

Enzyme and pathway databases

BioCycNEUR228410:NE2286-MON.
BRENDA4.2.1.2. 444.

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_NITEU
AccessionPrimary (citable) accession number: Q82SM5
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: June 1, 2003
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