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Q8DIP7

- FUMC_THEEB

UniProt

Q8DIP7 - FUMC_THEEB

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Protein
Fumarate hydratase class II
Gene
fumC, tll1534
Organism
Thermosynechococcus elongatus (strain BP-1)
Status
Reviewed - 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.UniRule annotation

Catalytic activityi

(S)-malate = fumarate + H2O.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei189 – 1891Proton donor/acceptor By similarity
Active sitei319 – 3191 By similarity
Binding sitei320 – 3201Substrate By similarity
Sitei332 – 3321Important for catalytic activity By 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 II (EC:4.2.1.2)
Short name:
Fumarase C
Gene namesi
Name:fumC
Ordered Locus Names:tll1534
OrganismiThermosynechococcus elongatus (strain BP-1)
Taxonomic identifieri197221 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesThermosynechococcus
ProteomesiUP000000440: Chromosome

Subcellular locationi

Cytoplasm By similarity 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 – 467467Fumarate hydratase class IIUniRule annotation
PRO_0000161323Add
BLAST

Interactioni

Subunit structurei

Homotetramer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi197221.tll1534.

Structurei

3D structure databases

ProteinModelPortaliQ8DIP7.
SMRiQ8DIP7. Positions 6-461.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni99 – 1013Substrate binding By similarity
Regioni130 – 1334B site By similarity
Regioni140 – 1423Substrate binding By similarity
Regioni188 – 1892Substrate binding By similarity
Regioni325 – 3273Substrate binding By similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0114.
HOGENOMiHOG000061736.
KOiK01679.
OMAiMESFNIH.
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.

Q8DIP7-1 [UniParc]FASTAAdd to Basket

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MTTDTRLEYD SLGAVEVPAD CYWGAQTARS LKHFAIGSQR MPLAVIHAMA    50
RLKKAAAIAN RDLGVLDPEK AKWIIQAADE VIAGQWDDQF PLAIWQTGSG 100
TQTNMNVNEV IANRAIELAG GVKGSKSPIH PNDHVNCSQS SNDTFPTAMH 150
VATVLALQER LLPTLRHLLT VLQEKAAAFA EIIKIGRTHL MDAVPLTLGQ 200
EFSGYASQIA AAQAHIEYAL QHLYPLAIGA TAVGTGLNAP AGFGDRVAAE 250
LAQMTGYPFR KAENPFAALA AHDPLVMLSG ALKTLAAALM KIANDIRWLG 300
SGPRCGLGEL RLPANEPGSS IMPGKVNPTQ CEALTMVCVQ VMGNDAAVGI 350
AGSQGNFELN VYKPLIIYNV LQSIALLSDA AQSFTDHCLV GVEPNRQQIQ 400
AYVERSLMLV TALNPHIGYD KAAAVAKKAY SEGKTLKEAA VELGYLTAEE 450
FDRWVRLELM LGEKGTS 467
Length:467
Mass (Da):50,030
Last modified:March 1, 2003 - v1
Checksum:i79F600152E5C0D66
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BA000039 Genomic DNA. Translation: BAC09086.1.
RefSeqiNP_682324.1. NC_004113.1.

Genome annotation databases

EnsemblBacteriaiBAC09086; BAC09086; BAC09086.
GeneIDi1011091.
KEGGitel:tll1534.
PATRICi23928428. VBITheElo119873_1609.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BA000039 Genomic DNA. Translation: BAC09086.1 .
RefSeqi NP_682324.1. NC_004113.1.

3D structure databases

ProteinModelPortali Q8DIP7.
SMRi Q8DIP7. Positions 6-461.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 197221.tll1534.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAC09086 ; BAC09086 ; BAC09086 .
GeneIDi 1011091.
KEGGi tel:tll1534.
PATRICi 23928428. VBITheElo119873_1609.

Phylogenomic databases

eggNOGi COG0114.
HOGENOMi HOG000061736.
KOi K01679.
OMAi MESFNIH.
OrthoDBi EOG6V1M4M.

Enzyme and pathway databases

UniPathwayi UPA00223 ; UER01007 .

Family and domain databases

Gene3Di 1.10.275.10. 1 hit.
HAMAPi MF_00743. FumaraseC.
InterProi IPR005677. 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 ]
PANTHERi PTHR11444. PTHR11444. 1 hit.
Pfami PF10415. FumaraseC_C. 1 hit.
PF00206. Lyase_1. 1 hit.
[Graphical view ]
PRINTSi PR00149. FUMRATELYASE.
SUPFAMi SSF48557. SSF48557. 1 hit.
TIGRFAMsi TIGR00979. fumC_II. 1 hit.
PROSITEi PS00163. FUMARATE_LYASES. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: BP-1.

Entry informationi

Entry nameiFUMC_THEEB
AccessioniPrimary (citable) accession number: Q8DIP7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: March 1, 2003
Last modified: May 14, 2014
This is version 76 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.

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

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