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P39461 (FUMC_SULSO) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 97. 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
Ordered Locus Names:SSO1077
OrganismSulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) [Reference proteome] [HAMAP]
Taxonomic identifier273057 [NCBI]
Taxonomic lineageArchaeaCrenarchaeotaThermoproteiSulfolobalesSulfolobaceaeSulfolobus

Protein attributes

Sequence length438 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May function as an auxiliary aerobic enzyme in the citric acid cycle. Ref.4

Catalytic activity

(S)-malate = fumarate + H2O. Ref.4

Pathway

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

Subunit structure

Homotetramer. Ref.4

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.

Biophysicochemical properties

Kinetic parameters:

KM=0.125 mM for malate (at pH 7.5 and at 70 degrees Celsius) Ref.4

KM=0.3 mM for malate (at pH 7.5 and at 70 degrees Celsius)

pH dependence:

Optimum pH is 8.0.

Temperature dependence:

Optimum temperature is 85 degrees Celsius. Active from 40 to 90 degrees Celsius.

Sequence caution

The sequence AAK41339.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Biological processTricarboxylic acid cycle
   Cellular componentCytoplasm
   Molecular functionLyase
   Technical termComplete proteome
Direct protein sequencing
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 – 438438Fumarate hydratase class II HAMAP-Rule MF_00743
PRO_0000161334

Regions

Region76 – 783Substrate binding By similarity
Region101 – 1044B site By similarity
Region111 – 1133Substrate binding By similarity
Region159 – 1602Substrate binding By similarity
Region297 – 2993Substrate binding By similarity

Sites

Active site1601Proton donor/acceptor By similarity
Active site2911 By similarity
Binding site2921Substrate By similarity
Site3041Important for catalytic activity By similarity

Sequences

Sequence LengthMass (Da)Tools
P39461 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: 8D2A9CF37817EA6C

FASTA43847,911
        10         20         30         40         50         60 
MKYTDTAPKL FMNTGTKFPR RIIWSMGVLK KSCAKVNADL GLLDKKIADS IIKASDDLID 

        70         80         90        100        110        120 
GKLDDKIVLD VFQTGSGTGL NMNVNEVIAE VASSYSNLKV HPNDHVNFGQ SSNDTVPTAI 

       130        140        150        160        170        180 
RIAAVAEVTN RLLPALQQII SSLNKKAEEY KDVIKAGRTH LRDALPVTLG QELSAYADAF 

       190        200        210        220        230        240 
QHEHEQVMNI LEYVKELPIG GTATGTGLNS HPEFQERVIN EINRITGLGF KPANRFRAMR 

       250        260        270        280        290        300 
LLTDLLLLSG ALRNIAVDLY RLGQDIRLMF SGPLTGLNEI DLPTQEEIAG SSIMPGKTNP 

       310        320        330        340        350        360 
VTVEATLLIS AQVVGLDHAN QFASMLGEFE LSMGIPLVGY NIVTQVNFIS EALEKMSRLV 

       370        380        390        400        410        420 
IDGMVANVEK MKRYAESSPS LITIVSPVIG YDKATEIGKK LNKGMSIREA LRELGYSDNE 

       430 
INKILDLSKL VKPGFTAK 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning, nucleotide sequence and expression of a Sulfolobus solfataricus gene encoding a class II fumarase."
Colombo S., Grisa M., Tortora P., Vanoni M.
FEBS Lett. 337:93-98(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-14.
Strain: DSM 5833 / MT-4.
[2]Erratum
Colombo S., Grisa M., Tortora P., Vanoni M.
FEBS Lett. 340:151-153(1994) [PubMed] [Europe PMC] [Abstract]
[3]"The complete genome of the crenarchaeon Sulfolobus solfataricus P2."
She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J., Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G., Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J., Medina N., Peng X. expand/collapse author list , Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C., Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T., Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.
Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 35092 / DSM 1617 / JCM 11322 / P2.
[4]"Purification and properties of a thermostable fumarate hydratase from the archaeobacterium Sulfolobus solfataricus."
Puchegger S., Redl B., Stoeffler G.
J. Gen. Microbiol. 136:1537-1541(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
Strain: ATCC 35091 / DSM 1616 / IFO 15331 / JCM 8930 / P1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X75402 Genomic DNA. Translation: CAA53156.1.
AE006641 Genomic DNA. Translation: AAK41339.1. Different initiation.
PIRD90260.
S40448.
RefSeqNP_342549.1. NC_002754.1.

3D structure databases

ProteinModelPortalP39461.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING273057.SSO1077.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAK41339; AAK41339; SSO1077.
GeneID1454118.
KEGGsso:SSO1077.

Phylogenomic databases

eggNOGCOG0114.
HOGENOMHOG000061736.
KOK01679.
OMAGLNMNIN.
ProtClustDBPRK00485.

Enzyme and pathway databases

BioCycSSOL273057:GCH2-1024-MONOMER.
BRENDA4.2.1.2. 6163.
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.
IPR001611. Leu-rich_rpt.
[Graphical view]
PANTHERPTHR11444. PTHR11444. 1 hit.
PfamPF10415. FumaraseC_C. 1 hit.
PF00206. Lyase_1. 1 hit.
[Graphical view]
PRINTSPR00149. FUMRATELYASE.
SUPFAMSSF48557. SSF48557. 1 hit.
PROSITEPS00163. FUMARATE_LYASES. 1 hit.
PS51450. LRR. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFUMC_SULSO
AccessionPrimary (citable) accession number: P39461
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: March 19, 2014
This is version 97 of the entry and version 1 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