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Reviewed, UniProtKB/Swiss-Prot Q8FQP8 (FUMC_COREF)

Last modified September 22, 2009. Version 39. 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: CE1071
OrganismCorynebacterium efficiens [Complete proteome] [HAMAP]
Taxonomic identifier152794 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium

Protein attributes

Sequence length473 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 processtricarboxylic acid cycle

Inferred from electronic annotation. Source: HAMAP

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   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 HAMAP MF_00743
PRO_0000161271

Regions

Region128 – 1314B site By similarity
Region138 – 1403Substrate binding By similarity

Sites

Binding site1061Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8FQP8-1 [UniParc].

Last modified December 15, 2003. Version 2.
Checksum: C4CC4FFA6F3EA1A3

FASTA47350,073
        10         20         30         40         50         60 
MSDFMTEQEF RIEHDTMGEV KVPAQALWRA QTQRAVENFP ISGRGLESAQ IRAMGLLKAA 

        70         80         90        100        110        120 
CAQVNKDSGA LDAAKADAII AAGKEIATGK HDAEFPIDVF QTGSGTSSNM NTNEVIASIA 

       130        140        150        160        170        180 
KANGTEVHPN DDVNMGQSSN DTFPTATHVA ATEAAVNDLI PGLKVLHESL AKKANEWDSV 

       190        200        210        220        230        240 
VKSGRTHLMD AVPVTLGQEF GGYARQIQLG IERIEATLPR LGELAIGGTA VGTGINTSAD 

       250        260        270        280        290        300 
FGGKVVAELV ELTGVTQLQE AANHFEAQAN RDALVEFSGA MRVVAVSLYK IANDIRLMGS 

       310        320        330        340        350        360 
GPLTGLGEIQ LPDLQPGSSI MPGKVNPVLC ETATQVSAQV IGNDAAVAFA GSQGQFELNV 

       370        380        390        400        410        420 
FIPVMARNVL ESARLLANTA RVFATRLVDG IVPNEEHMKQ LAESSPSIVT PLNSAIGYEA 

       430        440        450        460        470 
AAKVAKAALA EGKTIRQTVI DMGFVDGEKL TEEELDKRLD VLAMANTDRK QKF 

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References

[1]"Comparative complete genome sequence analysis of the amino acid replacements responsible for the thermostability of Corynebacterium efficiens."
Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E., Sugimoto S., Matsui K., Yamagishi A., Kikuchi H., Ikeo K., Gojobori T.
Genome Res. 13:1572-1579(2003) [PubMed: 12840036] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395.

Cross-references

Sequence databases

BA000035 Genomic DNA. Translation: BAC17881.1. Different initiation.
RefSeqNP_737681.2.

3D structure databases

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

Genome annotation databases

GeneID1033250.
GenomeReviewsGene locus CE1071 in contig BA000035_GR.
KEGGcef:CE1071.
NMPDRfig|196164.1.peg.1071.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ8FQP8.

Enzyme and pathway databases

BioCycCEFF196164:CE1071-MON.
BRENDA4.2.1.2. 277326.

Family and domain databases

HAMAPMF_00743.
[Tree]
InterProIPR003031. D_crystallin.
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.
PROSITEPS00163. FUMARATE_LYASES. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFUMC_COREF
AccessionPrimary (citable) accession number: Q8FQP8
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: December 15, 2003
Last modified: September 22, 2009
This is version 39 of the entry and version 2 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