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P07343 (FUMC_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 117. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:citG
Ordered Locus Names:BSU33040
OrganismBacillus subtilis (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length462 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.

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.

Ontologies

Keywords
   Biological processTricarboxylic acid cycle
   Cellular componentCytoplasm
   Molecular functionLyase
   Technical termAllosteric enzyme
Complete proteome
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 – 462462Fumarate hydratase class II HAMAP-Rule MF_00743
PRO_0000161255

Regions

Region97 – 993Substrate binding By similarity
Region127 – 1304B site By similarity
Region137 – 1393Substrate binding By similarity
Region185 – 1862Substrate binding By similarity
Region322 – 3243Substrate binding By similarity

Sites

Active site1861Proton donor/acceptor By similarity
Active site3161 By similarity
Binding site3171Substrate By similarity
Site3291Important for catalytic activity By similarity

Experimental info

Sequence conflict661A → V in CAA25849. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P07343 [UniParc].

Last modified May 30, 2000. Version 2.
Checksum: 8D797D18FEA82C06

FASTA46250,532
        10         20         30         40         50         60 
MEYRIERDTM GEVKVPADKF WGAQTQRSKE NFKIGSEKMP MRVVKAFAIL KRSTALANKR 

        70         80         90        100        110        120 
LGNLDAEKAE AIAAVCDDVL KGKYDDNFPL VVWQTGSGTQ SNMNMNEVVA NRATALLKEK 

       130        140        150        160        170        180 
NSDQTIHPND DVNRSQSSND TFPTAMHVAA VLAVYEQLVP ALDQLRNTLD EKAKAYNDIV 

       190        200        210        220        230        240 
KIGRTHLQDA TPLTLGQEIS GWVHMLDRSK EMILEATDKM RALAIGGTAV GTGINAHPEF 

       250        260        270        280        290        300 
GELVSEEITK LTGQTFSSSP NKFHALTSHD EITYAHGALK ALAADLMKIA NDVRWLASGP 

       310        320        330        340        350        360 
RCGIGEIVIP ENEPGSSIMP GKVNPTQSEA LTMIAAQIMG NDATIGFAAS QGNFELNVFK 

       370        380        390        400        410        420 
PVIIYNFLQS VQLLSDGMNS FHDKCAVGIE PNKETIQENL SNSLMLVTAL NPHIGYENAA 

       430        440        450        460 
KIAKLAHKEG LTLKEAALKL ELLTEEQFNE MVKPEDMVKP KA 

« Hide

References

« Hide 'large scale' references
[1]"Complete nucleotide sequence of the fumarase gene (citG) of Bacillus subtilis 168."
Miles J.S., Guest J.R.
Nucleic Acids Res. 13:131-140(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168.
[2]"The yvsA-yvqA (293 degrees - 289 degrees) region of the Bacillus subtilis chromosome containing genes involved in metal ion uptake and a putative sigma factor."
Wipat A., Brignell C.S., Guy J.B., Rose M., Emmerson P.T., Harwood C.R.
Microbiology 144:1593-1600(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168.
[3]"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. expand/collapse author list , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.
[4]"The nucleotide sequence of a spore germination gene (gerA) of Bacillus subtilis 168."
Feavers I.M., Miles J.S., Moir A.
Gene 38:95-102(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-50.
Strain: 168.
[5]"Role of sigma H in expression of the fumarase gene (citG) in vegetative cells of Bacillus subtilis 168."
Price V.A., Feavers I.M., Moir A.
J. Bacteriol. 171:5933-5939(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-50.
Strain: 168.
[6]"Sequencing of regions downstream of addA (98 degrees) and citG (289 degrees) in Bacillus subtilis."
Medina N., Vannier F., Roche B., Autret S., Levine A., Seror S.J.
Microbiology 143:3305-3308(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 224-462.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X01701 Genomic DNA. Translation: CAA25849.1.
AJ223978 Genomic DNA. Translation: CAA11749.1.
AL009126 Genomic DNA. Translation: CAB15294.1.
M11918 Genomic DNA. Translation: AAA22464.1.
Z93941 Genomic DNA. Translation: CAB07973.1.
PIRUFBSC8. A23033.
RefSeqNP_391184.1. NC_000964.3.

3D structure databases

ProteinModelPortalP07343.
SMRP07343. Positions 4-457.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP07343. 2 interactions.
MINTMINT-8365703.
STRING224308.BSU33040.

Proteomic databases

PaxDbP07343.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB15294; CAB15294; BSU33040.
GeneID938591.
KEGGbsu:BSU33040.
PATRIC18978594. VBIBacSub10457_3460.

Organism-specific databases

GenoListBSU33040. [Micado]

Phylogenomic databases

eggNOGCOG0114.
HOGENOMHOG000061736.
KOK01679.
OMAMESFNIH.
OrthoDBEOG6V1M4M.
PhylomeDBP07343.

Enzyme and pathway databases

BioCycBSUB:BSU33040-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_BACSU
AccessionPrimary (citable) accession number: P07343
Secondary accession number(s): O32194
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: May 30, 2000
Last modified: July 9, 2014
This is version 117 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

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList