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Protein

Fumarate hydratase class II

Gene

fumC

Organism
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
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 sitei182 – 1821Proton donor/acceptorBy similarity
Active sitei312 – 3121By similarity
Binding sitei313 – 3131SubstrateUniRule annotation
Sitei325 – 3251Important 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

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:SCO5042
ORF Names:SCK7.15c
OrganismiStreptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Taxonomic identifieri100226 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomycesStreptomyces albidoflavus group
ProteomesiUP000001973: Chromosome

Subcellular locationi

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 – 461461Fumarate hydratase class IIPRO_0000161322Add
BLAST

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Protein-protein interaction databases

STRINGi100226.SCO5042.

Structurei

3D structure databases

ProteinModelPortaliQ9FBN6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni98 – 1003Substrate bindingUniRule annotation
Regioni123 – 1264B siteUniRule annotation
Regioni133 – 1353Substrate bindingUniRule annotation
Regioni181 – 1822Substrate bindingUniRule annotation
Regioni318 – 3203Substrate bindingUniRule annotation

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0114.
HOGENOMiHOG000061737.
InParanoidiQ9FBN6.
KOiK01679.
OMAiNNFPISG.
OrthoDBiEOG6V1M4M.
PhylomeDBiQ9FBN6.

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.
PROSITEiPS00163. FUMARATE_LYASES. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9FBN6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSEYRIEHDS MGEVRVPADA KWRAQTQRAV ENFPVSGQRI ERAHIEALAR
60 70 80 90 100
IKSAAAKVNA ELGVLDEDVA GAIQEAAGEV AEGKWDEHFP VDVFQTGSGT
110 120 130 140 150
SSNMNTNEVV ATLATERLGR DVHPNDHVNA SQSSNDVFPS SIHIAATAAV
160 170 180 190 200
TRDLIPALDH LAGALERKAG EFADVVKSGR THLMDATPVT LGQEFGGYAA
210 220 230 240 250
QVRYGIERLQ ASLPRLAELP LGGTAVGTGI NTPPGFSAAV IEEVARATGL
260 270 280 290 300
PLTEARDHFE AQGARDGIVE TSGQLRTIGV GLTKIANDLR WMASGPRTGL
310 320 330 340 350
AEISLPDLQP GSSIMPGKVN PVIPEAVLMV AAQVTGNDAT VAAAGAAGNF
360 370 380 390 400
ELNVMLPVIA KNVLESVRLL ANVSRLLADR TVDGIVAHPE RAREYAESSP
410 420 430 440 450
SVVTPLNKYL GYEEAAKVAK RALAERKTIR QTVLEGGYVE RGDLTREQLD
460
QALDVLRMTR P
Length:461
Mass (Da):49,068
Last modified:March 1, 2001 - v1
Checksum:i0853F809C265A62D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL939122 Genomic DNA. Translation: CAC05887.1.
RefSeqiNP_629194.1. NC_003888.3.
WP_011030018.1. NC_003888.3.

Genome annotation databases

EnsemblBacteriaiCAC05887; CAC05887; CAC05887.
GeneIDi1100483.
KEGGisco:SCO5042.
PATRICi23739922. VBIStrCoe124346_5121.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL939122 Genomic DNA. Translation: CAC05887.1.
RefSeqiNP_629194.1. NC_003888.3.
WP_011030018.1. NC_003888.3.

3D structure databases

ProteinModelPortaliQ9FBN6.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi100226.SCO5042.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAC05887; CAC05887; CAC05887.
GeneIDi1100483.
KEGGisco:SCO5042.
PATRICi23739922. VBIStrCoe124346_5121.

Phylogenomic databases

eggNOGiCOG0114.
HOGENOMiHOG000061737.
InParanoidiQ9FBN6.
KOiK01679.
OMAiNNFPISG.
OrthoDBiEOG6V1M4M.
PhylomeDBiQ9FBN6.

Enzyme and pathway databases

UniPathwayiUPA00223; UER01007.

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.
PROSITEiPS00163. FUMARATE_LYASES. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC BAA-471 / A3(2) / M145.

Entry informationi

Entry nameiFUMC_STRCO
AccessioniPrimary (citable) accession number: Q9FBN6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: March 1, 2001
Last modified: March 4, 2015
This is version 86 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.