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Protein

Fumarate hydratase class II

Gene

fumC

Organism
Rickettsia prowazekii (strain Madrid E)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

(S)-malate = fumarate + H2O.

Pathway: tricarboxylic acid cycle

This protein is involved in step 1 of the subpathway that synthesizes (S)-malate from fumarate.
Proteins known to be involved in this subpathway in this organism are:
  1. Fumarate hydratase class II (fumC)
This subpathway is part of the pathway tricarboxylic acid cycle, which is itself part of Carbohydrate metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes (S)-malate from fumarate, the pathway tricarboxylic acid cycle and in Carbohydrate metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei188 – 1881Proton donor/acceptorBy similarity
Active sitei318 – 3181By similarity
Binding sitei319 – 3191Substrate
Sitei331 – 3311Important for catalytic activityBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Tricarboxylic acid cycle

Enzyme and pathway databases

UniPathwayiUPA00223; UER01007.

Names & Taxonomyi

Protein namesi
Recommended name:
Fumarate hydratase class II (EC:4.2.1.2)
Short name:
Fumarase C
Gene namesi
Name:fumC
Ordered Locus Names:RP665
OrganismiRickettsia prowazekii (strain Madrid E)
Taxonomic identifieri272947 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRickettsialesRickettsiaceaeRickettsieaeRickettsiatyphus group
ProteomesiUP000002480 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 461461Fumarate hydratase class IIPRO_0000161307Add
BLAST

Interactioni

Subunit structurei

Homotetramer.1 Publication

Protein-protein interaction databases

STRINGi272947.RP665.

Structurei

Secondary structure

1
461
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 96Combined sources
Beta strandi12 – 176Combined sources
Helixi24 – 329Combined sources
Helixi42 – 6120Combined sources
Helixi67 – 8216Combined sources
Turni83 – 875Combined sources
Beta strandi92 – 954Combined sources
Helixi100 – 11920Combined sources
Beta strandi124 – 1285Combined sources
Helixi130 – 1345Combined sources
Turni135 – 1373Combined sources
Helixi140 – 15819Combined sources
Helixi160 – 17516Combined sources
Helixi178 – 1803Combined sources
Beta strandi182 – 1876Combined sources
Beta strandi190 – 1967Combined sources
Helixi197 – 21923Combined sources
Turni220 – 2234Combined sources
Turni230 – 2323Combined sources
Helixi242 – 25413Combined sources
Helixi264 – 2696Combined sources
Helixi272 – 29827Combined sources
Beta strandi302 – 3054Combined sources
Beta strandi319 – 3213Combined sources
Helixi328 – 35124Combined sources
Helixi362 – 38625Combined sources
Turni387 – 3904Combined sources
Helixi395 – 40410Combined sources
Helixi406 – 4083Combined sources
Helixi409 – 4168Combined sources
Helixi418 – 43114Combined sources
Helixi435 – 4417Combined sources
Helixi447 – 4548Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3GTDX-ray2.40A/B1-461[»]
ProteinModelPortaliQ9ZCQ4.
SMRiQ9ZCQ4. Positions 4-460.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9ZCQ4.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni98 – 1003Substrate binding
Regioni129 – 1324B siteBy similarity
Regioni139 – 1413Substrate bindingCurated
Regioni187 – 1882Substrate bindingBy similarity
Regioni324 – 3263Substrate binding

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0114.
HOGENOMiHOG000061736.
KOiK01679.
OMAiNNFPISG.
OrthoDBiEOG6V1M4M.

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.

Q9ZCQ4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKNYRIESDS FGEIQIEEKF YWGAQTQRSL NNFKISKQKM PKILIRALAI
60 70 80 90 100
LKKCAAQVNY EFGDLEYKIA TSIDKAIDRI LAGEFEDNFP LVVWQTGSGT
110 120 130 140 150
QTNMNMNEVI ASIANEELTG KKGGKFPVHP NDHVNKGQSS NDSFPTAMHI
160 170 180 190 200
ATVLATKQQL IPALNNLLTY LQDKSKDWDK IIKIGRTHLQ DATPLTLKQE
210 220 230 240 250
FSGYITQIEY ALERIEDALK KVYLLAQGGT AVGTGINSKI GFDIKFAQKV
260 270 280 290 300
AEFTQQPFKT APNKFESLAA HDALVEFSGT LNTIAVSLMK IANDIRLLGS
310 320 330 340 350
GPRCGLGELH LPENEPGSSI MPGKVNPTQV EALTMVCTQV MGNHVTVTIA
360 370 380 390 400
GSNGHLELNV FKPVIIYNIL QSIELLSDSV NSFVTHCVKG LEPNIARINT
410 420 430 440 450
LRDKSLMLVT VLNPHIGYDN AAKIAKEAHK YGITLKEAAK KLNFLSEEEF
460
DKIVVPEKMI S
Length:461
Mass (Da):51,008
Last modified:May 1, 1999 - v1
Checksum:iC9929CC94E7E617D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ235272 Genomic DNA. Translation: CAA15103.1.
PIRiE71672.
RefSeqiNP_221027.1. NC_000963.1.
WP_004596191.1. NC_000963.1.

Genome annotation databases

EnsemblBacteriaiCAA15103; CAA15103; CAA15103.
GeneIDi883633.
KEGGirpr:RP665.
PATRICi17902157. VBIRicPro72556_0685.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ235272 Genomic DNA. Translation: CAA15103.1.
PIRiE71672.
RefSeqiNP_221027.1. NC_000963.1.
WP_004596191.1. NC_000963.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3GTDX-ray2.40A/B1-461[»]
ProteinModelPortaliQ9ZCQ4.
SMRiQ9ZCQ4. Positions 4-460.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi272947.RP665.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAA15103; CAA15103; CAA15103.
GeneIDi883633.
KEGGirpr:RP665.
PATRICi17902157. VBIRicPro72556_0685.

Phylogenomic databases

eggNOGiCOG0114.
HOGENOMiHOG000061736.
KOiK01679.
OMAiNNFPISG.
OrthoDBiEOG6V1M4M.

Enzyme and pathway databases

UniPathwayiUPA00223; UER01007.

Miscellaneous databases

EvolutionaryTraceiQ9ZCQ4.

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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Madrid E.
  2. "Structure of fumarate hydratase from Rickettsia prowazekii, the agent of typhus and suspected relative of the mitochondria."
    Phan I., Subramanian S., Olsen C., Edwards T.E., Guo W., Zhang Y., Van Voorhis W.C., Stewart L.J., Myler P.J.
    Acta Crystallogr. F 67:1123-1128(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS, SUBUNIT.

Entry informationi

Entry nameiFUMC_RICPR
AccessioniPrimary (citable) accession number: Q9ZCQ4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: May 1, 1999
Last modified: May 27, 2015
This is version 87 of the entry and version 1 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

3D-structure, Allosteric enzyme, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Rickettsia prowazekii
    Rickettsia prowazekii (strain Madrid E): entries and gene names
  4. 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.