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P95331 (FUMC_MYXXD) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 90. 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

Short name=Fumarase C
EC=4.2.1.2
Gene names
Name:fumC
Synonyms:fhy
Ordered Locus Names:MXAN_6439
OrganismMyxococcus xanthus (strain DK 1622) [Complete proteome] [HAMAP]
Taxonomic identifier246197 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaMyxococcalesCystobacterineaeMyxococcaceaeMyxococcus

Protein attributes

Sequence length466 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 By similarity 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
   Molecular functionLyase
   Technical termAllosteric enzyme
Complete 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 – 466466Fumarate hydratase class II HAMAP-Rule MF_00743
PRO_0000161290

Regions

Region100 – 1023Substrate binding By similarity
Region131 – 1344B site By similarity
Region141 – 1433Substrate binding By similarity
Region189 – 1902Substrate binding By similarity
Region326 – 3283Substrate binding By similarity

Sites

Active site1901Proton donor/acceptor By similarity
Active site3201 By similarity
Binding site3211Substrate By similarity
Site3331Important for catalytic activity By similarity

Sequences

Sequence LengthMass (Da)Tools
P95331 [UniParc].

Last modified June 1, 1998. Version 2.
Checksum: 9496DDD6C1690C55

FASTA46649,913
        10         20         30         40         50         60 
MSTKNVRTEK DTFGPIDVPA DRLWGAQTQR SLQNFAISTE RMPLALIRAL VLVKKAAARV 

        70         80         90        100        110        120 
NVENGSLAKE KGEAIIRAAD EVLAGQHDAE FPLSVWQTGS GTQTNMNTNE VLANRASELL 

       130        140        150        160        170        180 
GGERGERRKV HPNDDVNKGQ SSNDVFPTAM SVAAVAAITE HVLPELKALR DVLAQKARAF 

       190        200        210        220        230        240 
HDVVKVGRTH LQDATPLTLG QEVGGFVAQL DHAKGHLERT LPHLLELALG GTAVGTGLNA 

       250        260        270        280        290        300 
PKGYAERVAQ ELAQLTGHPF VTAPNKFEAL AANDALVQAH GALKGLAAVL FKVANDVRWL 

       310        320        330        340        350        360 
SSGPRSGLAE ITIPENEPGS SIMPGKVNPT QSEALTMLCA QVMGNDVAVT VGGASGNFQL 

       370        380        390        400        410        420 
NVFKPLIAHN LLQSCRLLAD GMRSFRLHCA VGIEPNRPRI QENLERSLML VTALNPHIGY 

       430        440        450        460 
DNAAKIAKTA HRDGTTLKET AVALGLVTPE QFDQWVRPED MTGHKG 

« Hide

References

« Hide 'large scale' references
[1]"Myxococcus xanthus fumarate hydratase, major proteosome subunit, and acyl-CoA oxidase genes."
Salmi D., Creighton C., Youderian P.
Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Evolution of sensory complexity recorded in a myxobacterial genome."
Goldman B.S., Nierman W.C., Kaiser D., Slater S.C., Durkin A.S., Eisen J., Ronning C.M., Barbazuk W.B., Blanchard M., Field C., Halling C., Hinkle G., Iartchuk O., Kim H.S., Mackenzie C., Madupu R., Miller N., Shvartsbeyn A. expand/collapse author list , Sullivan S.A., Vaudin M., Wiegand R., Kaplan H.B.
Proc. Natl. Acad. Sci. U.S.A. 103:15200-15205(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DK 1622.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF013216 Genomic DNA. Translation: AAB97818.1.
CP000113 Genomic DNA. Translation: ABF86177.1.
RefSeqYP_634563.1. NC_008095.1.

3D structure databases

ProteinModelPortalP95331.
SMRP95331. Positions 6-461.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING246197.MXAN_6439.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABF86177; ABF86177; MXAN_6439.
GeneID4105200.
KEGGmxa:MXAN_6439.
PATRIC22655381. VBIMyxXan43560_6334.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0114.
HOGENOMHOG000061737.
KOK01679.
OMAMESFNIH.
OrthoDBEOG6V1M4M.

Enzyme and pathway databases

BioCycMXAN246197:GIWU-6388-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 nameFUMC_MYXXD
AccessionPrimary (citable) accession number: P95331
Secondary accession number(s): Q1CYG0
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: June 1, 1998
Last modified: May 14, 2014
This is version 90 of the entry and version 2 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