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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.

Pathwayi: 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)DescriptionActionsGraphical viewLength
Active sitei188Proton donor/acceptorBy similarity1
Active sitei318By similarity1
Binding sitei319Substrate1
Sitei331Important for catalytic activityBy similarity1

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
Proteomesi
  • UP000002480 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001613071 – 461Fumarate hydratase class IIAdd BLAST461

Interactioni

Subunit structurei

Homotetramer.1 Publication

Protein-protein interaction databases

STRINGi272947.RP665.

Structurei

Secondary structure

1461
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 9Combined sources6
Beta strandi12 – 17Combined sources6
Helixi24 – 32Combined sources9
Helixi42 – 61Combined sources20
Helixi67 – 82Combined sources16
Turni83 – 87Combined sources5
Beta strandi92 – 95Combined sources4
Helixi100 – 119Combined sources20
Beta strandi124 – 128Combined sources5
Helixi130 – 134Combined sources5
Turni135 – 137Combined sources3
Helixi140 – 158Combined sources19
Helixi160 – 175Combined sources16
Helixi178 – 180Combined sources3
Beta strandi182 – 187Combined sources6
Beta strandi190 – 196Combined sources7
Helixi197 – 219Combined sources23
Turni220 – 223Combined sources4
Turni230 – 232Combined sources3
Helixi242 – 254Combined sources13
Helixi264 – 269Combined sources6
Helixi272 – 298Combined sources27
Beta strandi302 – 305Combined sources4
Beta strandi319 – 321Combined sources3
Helixi328 – 351Combined sources24
Helixi362 – 386Combined sources25
Turni387 – 390Combined sources4
Helixi395 – 404Combined sources10
Helixi406 – 408Combined sources3
Helixi409 – 416Combined sources8
Helixi418 – 431Combined sources14
Helixi435 – 441Combined sources7
Helixi447 – 454Combined sources8

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ9ZCQ4.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni98 – 100Substrate binding3
Regioni129 – 132B siteBy similarity4
Regioni139 – 141Substrate bindingCurated3
Regioni187 – 188Substrate bindingBy similarity2
Regioni324 – 326Substrate binding3

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105C9Q. Bacteria.
COG0114. LUCA.
HOGENOMiHOG000061736.
KOiK01679.
OMAiFAYLKKA.

Family and domain databases

Gene3Di1.10.275.10. 1 hit.
HAMAPiMF_00743. FumaraseC. 1 hit.
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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3GTDX-ray2.40A/B1-461[»]
ProteinModelPortaliQ9ZCQ4.
SMRiQ9ZCQ4.
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

eggNOGiENOG4105C9Q. Bacteria.
COG0114. LUCA.
HOGENOMiHOG000061736.
KOiK01679.
OMAiFAYLKKA.

Enzyme and pathway databases

UniPathwayiUPA00223; UER01007.

Miscellaneous databases

EvolutionaryTraceiQ9ZCQ4.

Family and domain databases

Gene3Di1.10.275.10. 1 hit.
HAMAPiMF_00743. FumaraseC. 1 hit.
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...

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: November 2, 2016
This is version 94 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

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 one 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.