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Q983U5

- FUMC_RHILO

UniProt

Q983U5 - FUMC_RHILO

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Protein

Fumarate hydratase class II

Gene
fumC, mll8172
Organism
Rhizobium loti (strain MAFF303099) (Mesorhizobium loti)
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 sitei190 – 1901Proton donor/acceptor By similarity
Active sitei320 – 3201 By similarity
Binding sitei321 – 3211Substrate By similarity
Sitei333 – 3331Important 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

BioCyciMLOT266835:GJ9L-6478-MONOMER.
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:mll8172
OrganismiRhizobium loti (strain MAFF303099) (Mesorhizobium loti)
Taxonomic identifieri266835 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesPhyllobacteriaceaeMesorhizobium
ProteomesiUP000000552: 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 – 465465Fumarate hydratase class IIUniRule annotationPRO_0000161304Add
BLAST

Interactioni

Subunit structurei

Homotetramer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi266835.mll8172.

Structurei

3D structure databases

ProteinModelPortaliQ983U5.
SMRiQ983U5. Positions 7-464.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni100 – 1023Substrate binding By similarity
Regioni131 – 1344B site By similarity
Regioni141 – 1433Substrate binding By similarity
Regioni189 – 1902Substrate binding By similarity
Regioni326 – 3283Substrate 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.

Q983U5-1 [UniParc]FASTAAdd to Basket

« Hide

MTVAKTRTET DTFGPIEVAA DRYWGAQAQR SLGNFKIGWE KQPASIVRAL    50
GVVKRAAAEV NMEMKRLDPV VGKAIVDAAQ EVIDGKLNDH FPLVVWQTGS 100
GTQSNMNANE VISNRAIEML GGVMGSKKPV HPNDHVNMSQ SSNDTYPTAM 150
HIACAEQVVH HLIPALHHLH KALDAKARAF NHIIKIGRTH TQDATPLTLG 200
QEFSGYAAQV ASSIKRIEMT LPGLQELAQG GTAVGTGLNA PVGFAEKVAD 250
RIAAITGIAF VTAPNKFEAL AAHDSMVFSH GAINAAAAAL FKIANDIRFL 300
GSGPRSGLGE LSLPENEPGS SIMPGKVNPT QCEAMTQVCV QVFGNNAALT 350
FAGSQGHFEL NVYNPLMAYN FLQSVQLLSD ASVSFTDNCV VGIEAREDNI 400
KAALDRSLML VTALAPTIGY DNAAKIAKTA HKNGTTLREE ALATGLVSEV 450
DYDRLVRPED MTHPG 465
Length:465
Mass (Da):49,592
Last modified:October 1, 2001 - v1
Checksum:i85407C084D9221F9
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BA000012 Genomic DNA. Translation: BAB53785.1.
RefSeqiNP_108324.1. NC_002678.2.
WP_010915411.1. NC_002678.2.

Genome annotation databases

EnsemblBacteriaiBAB53785; BAB53785; BAB53785.
GeneIDi1230976.
KEGGimlo:mll8172.
PATRICi22487309. VBIMesLot2464_6528.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BA000012 Genomic DNA. Translation: BAB53785.1 .
RefSeqi NP_108324.1. NC_002678.2.
WP_010915411.1. NC_002678.2.

3D structure databases

ProteinModelPortali Q983U5.
SMRi Q983U5. Positions 7-464.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 266835.mll8172.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAB53785 ; BAB53785 ; BAB53785 .
GeneIDi 1230976.
KEGGi mlo:mll8172.
PATRICi 22487309. VBIMesLot2464_6528.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00223 ; UER01007 .
BioCyci MLOT266835:GJ9L-6478-MONOMER.

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: MAFF303099.

Entry informationi

Entry nameiFUMC_RHILO
AccessioniPrimary (citable) accession number: Q983U5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: October 1, 2001
Last modified: September 3, 2014
This is version 73 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

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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