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Protein

Fumarate hydratase class II

Gene

fumC

Organism
Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)
Status
Reviewed-Annotation score: Annotation score: 3 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 sitei190 – 1901Proton donor/acceptorBy similarity
Active sitei320 – 3201By similarity
Binding sitei321 – 3211SubstrateUniRule annotation
Sitei333 – 3331Important 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

BioCyciDRAD243230:GH46-2682-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
Ordered Locus Names:DR_2627
OrganismiDeinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)
Taxonomic identifieri243230 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciDeinococcalesDeinococcaceaeDeinococcus
ProteomesiUP000002524 Componenti: Chromosome I

Subcellular locationi

  1. Cytoplasm UniRule annotation

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 – 464464Fumarate hydratase class IIPRO_0000161274Add
BLAST

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Protein-protein interaction databases

STRINGi243230.DR_2627.

Structurei

3D structure databases

ProteinModelPortaliQ9RR70.
SMRiQ9RR70. Positions 5-459.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni100 – 1023Substrate bindingUniRule annotation
Regioni131 – 1344B siteUniRule annotation
Regioni141 – 1433Substrate bindingUniRule annotation
Regioni189 – 1902Substrate bindingUniRule annotation
Regioni326 – 3283Substrate bindingUniRule annotation

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0114.
HOGENOMiHOG000061736.
InParanoidiQ9RR70.
KOiK01679.
OMAiNTPKGYD.
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.

Q9RR70-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTKTRQETDT MGKMDVDASR YWGAQTERSI HNFPIGRDTF VWGRPVIRAL
60 70 80 90 100
GILKKGAAQA NAELGELPAD VADLIVKAAD EVIAGKLDEH FPLVVFQTGS
110 120 130 140 150
GTQSNMNANE VISNRAIELA GGEMGSKKPV HPNDHVNRGQ SSNDTFPTAM
160 170 180 190 200
HIAVVLELNE RLYGAVGKLR DTLHAKAEQY KDLVKVGRTH LQDATPITLG
210 220 230 240 250
QEIGGWVAQL DYALSEVKHA GEGLLDLAIG GTAVGTGLNA HPKFGDLAAK
260 270 280 290 300
KYEEETGYHF RSAENKFAAL SAHDALVQTS AALRTLAGAL MKMANDVRWL
310 320 330 340 350
ASGPRNGIGE ITIPENEPGS SIMPGKVNPT QSEAMTMVAT RVFGNDATVA
360 370 380 390 400
FAGSQGNFQL NVFKPVMVHA VLESIRLISD ACLAFNDHCA VGIQPNEAKI
410 420 430 440 450
KENLDKNLMQ VTALNRHIGY DKAAAIAKKA HKEGTSLKDA ALALGYVTED
460
EFAQWVVPLG MTHN
Length:464
Mass (Da):49,876
Last modified:May 1, 2000 - v1
Checksum:i6CE8DC9A8D90A07E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000513 Genomic DNA. Translation: AAF12164.1.
PIRiB75250.
RefSeqiNP_296346.1. NC_001263.1.

Genome annotation databases

EnsemblBacteriaiAAF12164; AAF12164; DR_2627.
GeneIDi1797634.
KEGGidra:DR_2627.
PATRICi21633009. VBIDeiRad64572_2875.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000513 Genomic DNA. Translation: AAF12164.1.
PIRiB75250.
RefSeqiNP_296346.1. NC_001263.1.

3D structure databases

ProteinModelPortaliQ9RR70.
SMRiQ9RR70. Positions 5-459.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi243230.DR_2627.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAF12164; AAF12164; DR_2627.
GeneIDi1797634.
KEGGidra:DR_2627.
PATRICi21633009. VBIDeiRad64572_2875.

Phylogenomic databases

eggNOGiCOG0114.
HOGENOMiHOG000061736.
InParanoidiQ9RR70.
KOiK01679.
OMAiNTPKGYD.
OrthoDBiEOG6V1M4M.

Enzyme and pathway databases

UniPathwayiUPA00223; UER01007.
BioCyciDRAD243230:GH46-2682-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

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422.

Entry informationi

Entry nameiFUMC_DEIRA
AccessioniPrimary (citable) accession number: Q9RR70
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: May 1, 2000
Last modified: January 7, 2015
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

Allosteric enzyme, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. 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.