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Protein

Fumarate hydratase class II

Gene

fumC

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

Functioni

Catalyzes the reversible addition of water to fumarate to give L-malate.By similarity

Catalytic activityi

(S)-malate = fumarate + H2O.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei186 – 1861Proton donor/acceptorBy similarity
Active sitei316 – 3161By similarity
Binding sitei317 – 3171SubstrateUniRule annotation
Sitei329 – 3291Important for catalytic activityBy similarity

GO - Molecular functioni

  1. fumarate hydratase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. fumarate metabolic process Source: InterPro
  2. tricarboxylic acid cycle Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Tricarboxylic acid cycle

Enzyme and pathway databases

BioCyciBSUB:BSU33040-MONOMER.
UniPathwayiUPA00223; UER01007.

Names & Taxonomyi

Protein namesi
Recommended name:
Fumarate hydratase class IIUniRule annotation (EC:4.2.1.2UniRule annotation)
Short name:
Fumarase CUniRule annotation
Gene namesi
Name:fumCUniRule annotation
Synonyms:citG
Ordered Locus Names:BSU33040
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001570 Componenti: Chromosome

Organism-specific databases

GenoListiBSU33040. [Micado]

Subcellular locationi

GO - Cellular componenti

  1. tricarboxylic acid cycle enzyme complex Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 462462Fumarate hydratase class IIPRO_0000161255Add
BLAST

Proteomic databases

PaxDbiP07343.

Interactioni

Subunit structurei

Homotetramer.

Protein-protein interaction databases

IntActiP07343. 2 interactions.
MINTiMINT-8365703.
STRINGi224308.BSU33040.

Structurei

3D structure databases

ProteinModelPortaliP07343.
SMRiP07343. Positions 4-457.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni97 – 993Substrate bindingUniRule annotation
Regioni127 – 1304B siteUniRule annotation
Regioni137 – 1393Substrate bindingUniRule annotation
Regioni185 – 1862Substrate bindingUniRule annotation
Regioni322 – 3243Substrate bindingUniRule annotation

Sequence similaritiesi

Belongs to the class-II fumarase/aspartase family. Fumarase subfamily.UniRule annotation

Phylogenomic databases

eggNOGiCOG0114.
HOGENOMiHOG000061736.
InParanoidiP07343.
KOiK01679.
OMAiNTPKGYD.
OrthoDBiEOG6V1M4M.
PhylomeDBiP07343.

Family and domain databases

Gene3Di1.10.275.10. 1 hit.
HAMAPiMF_00743. FumaraseC.
InterProiIPR005677. 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]
PANTHERiPTHR11444. PTHR11444. 1 hit.
PfamiPF10415. FumaraseC_C. 1 hit.
PF00206. Lyase_1. 1 hit.
[Graphical view]
PRINTSiPR00149. FUMRATELYASE.
SUPFAMiSSF48557. SSF48557. 1 hit.
TIGRFAMsiTIGR00979. fumC_II. 1 hit.
PROSITEiPS00163. FUMARATE_LYASES. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P07343-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEYRIERDTM GEVKVPADKF WGAQTQRSKE NFKIGSEKMP MRVVKAFAIL
60 70 80 90 100
KRSTALANKR LGNLDAEKAE AIAAVCDDVL KGKYDDNFPL VVWQTGSGTQ
110 120 130 140 150
SNMNMNEVVA NRATALLKEK NSDQTIHPND DVNRSQSSND TFPTAMHVAA
160 170 180 190 200
VLAVYEQLVP ALDQLRNTLD EKAKAYNDIV KIGRTHLQDA TPLTLGQEIS
210 220 230 240 250
GWVHMLDRSK EMILEATDKM RALAIGGTAV GTGINAHPEF GELVSEEITK
260 270 280 290 300
LTGQTFSSSP NKFHALTSHD EITYAHGALK ALAADLMKIA NDVRWLASGP
310 320 330 340 350
RCGIGEIVIP ENEPGSSIMP GKVNPTQSEA LTMIAAQIMG NDATIGFAAS
360 370 380 390 400
QGNFELNVFK PVIIYNFLQS VQLLSDGMNS FHDKCAVGIE PNKETIQENL
410 420 430 440 450
SNSLMLVTAL NPHIGYENAA KIAKLAHKEG LTLKEAALKL ELLTEEQFNE
460
MVKPEDMVKP KA
Length:462
Mass (Da):50,532
Last modified:May 30, 2000 - v2
Checksum:i8D797D18FEA82C06
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti66 – 661A → V in CAA25849 (PubMed:3923430).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiA23033. UFBSC8.
RefSeqiNP_391184.1. NC_000964.3.

Genome annotation databases

EnsemblBacteriaiCAB15294; CAB15294; BSU33040.
GeneIDi938591.
KEGGibsu:BSU33040.
PATRICi18978594. VBIBacSub10457_3460.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiA23033. UFBSC8.
RefSeqiNP_391184.1. NC_000964.3.

3D structure databases

ProteinModelPortaliP07343.
SMRiP07343. Positions 4-457.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP07343. 2 interactions.
MINTiMINT-8365703.
STRINGi224308.BSU33040.

Proteomic databases

PaxDbiP07343.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB15294; CAB15294; BSU33040.
GeneIDi938591.
KEGGibsu:BSU33040.
PATRICi18978594. VBIBacSub10457_3460.

Organism-specific databases

GenoListiBSU33040. [Micado]

Phylogenomic databases

eggNOGiCOG0114.
HOGENOMiHOG000061736.
InParanoidiP07343.
KOiK01679.
OMAiNTPKGYD.
OrthoDBiEOG6V1M4M.
PhylomeDBiP07343.

Enzyme and pathway databases

UniPathwayiUPA00223; UER01007.
BioCyciBSUB:BSU33040-MONOMER.

Family and domain databases

Gene3Di1.10.275.10. 1 hit.
HAMAPiMF_00743. FumaraseC.
InterProiIPR005677. 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]
PANTHERiPTHR11444. PTHR11444. 1 hit.
PfamiPF10415. FumaraseC_C. 1 hit.
PF00206. Lyase_1. 1 hit.
[Graphical view]
PRINTSiPR00149. FUMRATELYASE.
SUPFAMiSSF48557. SSF48557. 1 hit.
TIGRFAMsiTIGR00979. fumC_II. 1 hit.
PROSITEiPS00163. FUMARATE_LYASES. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiFUMC_BACSU
AccessioniPrimary (citable) accession number: P07343
Secondary accession number(s): O32194
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: May 30, 2000
Last modified: January 7, 2015
This is version 120 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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).By similarity

Keywords - Technical termi

Allosteric enzyme, Complete proteome, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.