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Protein

Probable fumarate hydratase, mitochondrial

Gene

fum-1

Organism
Caenorhabditis elegans
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

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. Probable fumarate hydratase, mitochondrial (fum-1)
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
Binding sitei138SubstrateBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Tricarboxylic acid cycle

Enzyme and pathway databases

ReactomeiR-CEL-71403. Citric acid cycle (TCA cycle).
UniPathwayiUPA00223; UER01007.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable fumarate hydratase, mitochondrial (EC:4.2.1.2)
Short name:
Fumarase
Gene namesi
Name:fum-1
ORF Names:H14A12.2
OrganismiCaenorhabditis elegans
Taxonomic identifieri6239 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
Proteomesi
  • UP000001940 Componenti: Chromosome III

Organism-specific databases

WormBaseiH14A12.2a; CE11580; WBGene00001503; fum-1.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: GO_Central
  • mitochondrion Source: WormBase
  • tricarboxylic acid cycle enzyme complex Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_0000010328? – 501Probable fumarate hydratase, mitochondrial
Transit peptidei1 – ?MitochondrionSequence analysis

Proteomic databases

EPDiO17214.
PaxDbiO17214.
PeptideAtlasiO17214.
PRIDEiO17214.

2D gel databases

World-2DPAGE0020:O17214.

Expressioni

Gene expression databases

BgeeiWBGene00001503.
ExpressionAtlasiO17214. differential.

Interactioni

Protein-protein interaction databases

BioGridi41267. 6 interactors.
DIPiDIP-25418N.
IntActiO17214. 3 interactors.
MINTiMINT-1047829.
STRINGi6239.H14A12.2a.

Structurei

3D structure databases

ProteinModelPortaliO17214.
SMRiO17214.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni167 – 170B siteBy similarity4
Regioni177 – 179Substrate bindingBy similarity3

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG1317. Eukaryota.
COG0114. LUCA.
GeneTreeiENSGT00390000002779.
HOGENOMiHOG000061736.
InParanoidiO17214.
KOiK01679.
OMAiGREVNSR.
OrthoDBiEOG091G05UL.
PhylomeDBiO17214.

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.

Sequence processingi: The displayed sequence is further processed into a mature form.

O17214-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSAVSMLQGE MLARGGAVIA RGASLATARN FSRTTVPMAK IRKERDTFGE
60 70 80 90 100
LEVPADKYYG AQTARSQMNF KIGGPEERMP IPVIHAFGIL KKAAALVNTE
110 120 130 140 150
FGLDKKLADA ISQAADEVVD GKLDEHFPLV TWQTGSGTQS NMNVNEVISN
160 170 180 190 200
RAIEILGGEL GSKKPVHPND HVNMSQSSND TFPTAMHIAV GREVNSRLLP
210 220 230 240 250
ALKKLRTALH NKAEEFKDII KIGRTHTQDA VPLTLGQEFS AYVTQLDNSI
260 270 280 290 300
ARVESTLPRL YQLAAGGTAV GTGLNTRKGF AEKVAATVSE LTGLPFVTAP
310 320 330 340 350
NKFEALAAHD ALVEVHGALN TVAVSFMKIG NDIRFLGSGP RCGLGELSLP
360 370 380 390 400
ENEPGSSIMP GKVNPTQCEA ITMVAAQVMG NQVAVSVGGS NGHFELNVFK
410 420 430 440 450
PLIVRNVLQS TRLLADSAVS FTDHCVDGIV ANKDNIAKIM RESLMLVTAL
460 470 480 490 500
NPHIGYDNAA KIAKTAHKNG TTLVQEAVKL GILTEEQFAQ WVKPENMLGP

K
Length:501
Mass (Da):53,647
Last modified:January 1, 1998 - v1
Checksum:iDA578BE105509C1D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FO081548 Genomic DNA. Translation: CCD72341.1.
PIRiC88508.
RefSeqiNP_498642.1. NM_066241.7.
UniGeneiCel.17823.

Genome annotation databases

EnsemblMetazoaiH14A12.2a; H14A12.2a; WBGene00001503.
GeneIDi176059.
KEGGicel:CELE_H14A12.2.
UCSCiH14A12.2a. c. elegans.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FO081548 Genomic DNA. Translation: CCD72341.1.
PIRiC88508.
RefSeqiNP_498642.1. NM_066241.7.
UniGeneiCel.17823.

3D structure databases

ProteinModelPortaliO17214.
SMRiO17214.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi41267. 6 interactors.
DIPiDIP-25418N.
IntActiO17214. 3 interactors.
MINTiMINT-1047829.
STRINGi6239.H14A12.2a.

2D gel databases

World-2DPAGE0020:O17214.

Proteomic databases

EPDiO17214.
PaxDbiO17214.
PeptideAtlasiO17214.
PRIDEiO17214.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiH14A12.2a; H14A12.2a; WBGene00001503.
GeneIDi176059.
KEGGicel:CELE_H14A12.2.
UCSCiH14A12.2a. c. elegans.

Organism-specific databases

CTDi176059.
WormBaseiH14A12.2a; CE11580; WBGene00001503; fum-1.

Phylogenomic databases

eggNOGiKOG1317. Eukaryota.
COG0114. LUCA.
GeneTreeiENSGT00390000002779.
HOGENOMiHOG000061736.
InParanoidiO17214.
KOiK01679.
OMAiGREVNSR.
OrthoDBiEOG091G05UL.
PhylomeDBiO17214.

Enzyme and pathway databases

UniPathwayiUPA00223; UER01007.
ReactomeiR-CEL-71403. Citric acid cycle (TCA cycle).

Miscellaneous databases

PROiO17214.

Gene expression databases

BgeeiWBGene00001503.
ExpressionAtlasiO17214. differential.

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 nameiFUMH_CAEEL
AccessioniPrimary (citable) accession number: O17214
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: January 1, 1998
Last modified: November 30, 2016
This is version 128 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

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

Complete proteome, Reference proteome

Documents

  1. Caenorhabditis elegans
    Caenorhabditis elegans: entries, gene names and cross-references to WormBase
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. 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.