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Reviewed, UniProtKB/Swiss-Prot Q81SA0 (FUMC_BACAN)

Last modified November 3, 2009. Version 48. 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: BA_1767, GBAA_1767, BAS1637
OrganismBacillus anthracis [Complete proteome] [HAMAP]
Taxonomic identifier1392 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillusBacillus cereus group

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_0000161252

Regions

Region127 – 1304B site By similarity
Region137 – 1393Substrate binding By similarity

Sites

Binding site991Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q81SA0-1 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 0FB897C31FAC981D

FASTA46250,345
        10         20         30         40         50         60 
MEYRIERDTL GEIKVPADKL WAAQTQRSKE NFPIGTEQMP LEIVKAFAIL KKSAALSNQK 

        70         80         90        100        110        120 
LGKLSEEKAE AIVVAADEII AGKWNEHFPL VVWQTGSGTQ SNMNVNEVIA NRGNQILKEK 

       130        140        150        160        170        180 
GSDVHIHPND DVNMSQSSND TFPTALHVAC VLAVENHVLP AITKLKETLA EKVTAFEHII 

       190        200        210        220        230        240 
KIGRTHLQDA TPLTLGQEIS GWHRMLEKTE RMIAESNTYM KELAIGGTAV GTGINAHPKF 

       250        260        270        280        290        300 
GEMVSEEISQ FTGKQFISAP NKFHALTSHD EVVYTHGALK ALAADLMKIA NDVRWLASGP 

       310        320        330        340        350        360 
RSGLGEIIIP ANEPGSSIMP GKVNPTQSEA LTMVVAQVMG NDATIGFAAS QGNFELNVFK 

       370        380        390        400        410        420 
PVIAYNFLQS AHLLADAIVS FNDNCAVGIE ADEEIIKENV NRSLMLVTAL NPHIGYENAA 

       430        440        450        460 
KIAKHAHKEG LTLKEAALQS GLLTEEQFNE IVDPKKMIAP KE 

« Hide

References

[1]"The genome sequence of Bacillus anthracis Ames and comparison to closely related bacteria."
Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T., Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R., Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M., Kolonay J.F., Beanan M.J., Dodson R.J. expand/collapse author list , Brinkac L.M., Gwinn M.L., DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C., Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y., Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M., Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E., White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M., Hanna P.C., Kolstoe A.-B., Fraser C.M.
Nature 423:81-86(2003) [PubMed: 12721629] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Ames / isolate Porton.
[2]"Bacillus anthracis comparative genomics."
Ravel J., Rasko D.A., Shumway M.F., Jiang L., Cer R.Z., Federova N.B., Wilson M., Stanley S., Decker S., Read T.D., Salzberg S.L., Fraser C.M.
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Ames ancestor.
[3]"Complete genome sequence of Bacillus anthracis Sterne."
Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K., Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R., Richardson P., Rubin E., Tice H.
Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Sterne.

Cross-references

Sequence databases

AE016879 Genomic DNA. Translation: AAP25681.1.
AE017334 Genomic DNA. Translation: AAT30883.1.
AE017225 Genomic DNA. Translation: AAT53954.1.
RefSeqNP_844195.1.
YP_018408.1.
YP_027903.1.

3D structure databases

HSSPHSSP built from PDB template 1FUR based on UniProtKB P05042.
ModBaseSearch...

Genome annotation databases

GeneID1086574.
2818045.
2851297.
GenomeReviewsGene locus BA_1767 in contig AE016879_GR.
Gene locus BAS1637 in contig AE017225_GR.
Gene locus GBAA_1767 in contig AE017334_GR.
KEGGban:BA1767.
bar:GBAA1767.
bat:BAS1637.
TIGRBA_1767.
GBAA_1767.

Phylogenomic databases

HOGENOMQ81SA0.
OMAGSQGHFE.

Enzyme and pathway databases

BioCycBANT260799:BAS1637-MON.
BANT261594:GBAA1767-MON.
BRENDA4.2.1.2. 267517.

Family and domain databases

HAMAPMF_00743.
[Tree]
InterProIPR005677. 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]
PRINTSPR00149. FUMRATELYASE.
TIGRFAMsTIGR00979. fumC_II. 1 hit.
PROSITEPS00163. FUMARATE_LYASES. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFUMC_BACAN
AccessionPrimary (citable) accession number: Q81SA0
Secondary accession number(s): Q6I0I3, Q6KUE7
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: June 1, 2003
Last modified: November 3, 2009
This is version 48 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