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Q8UEY7

- FUMC_AGRT5

UniProt

Q8UEY7 - FUMC_AGRT5

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Protein

Fumarate hydratase class II

Gene
fumC, Atu1616, AGR_C_2979
Organism
Agrobacterium tumefaciens (strain C58 / ATCC 33970)
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 sitei188 – 1881Proton donor/acceptor By similarity
Active sitei318 – 3181 By similarity
Binding sitei319 – 3191Substrate By similarity
Sitei331 – 3311Important 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:Atu1616
ORF Names:AGR_C_2979
OrganismiAgrobacterium tumefaciens (strain C58 / ATCC 33970)
Taxonomic identifieri176299 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhizobiaceaeRhizobium/Agrobacterium groupAgrobacteriumAgrobacterium tumefaciens complex
ProteomesiUP000000813: Chromosome circular

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 – 463463Fumarate hydratase class IIUniRule annotationPRO_0000161251Add
BLAST

Interactioni

Subunit structurei

Homotetramer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi176299.Atu1616.

Structurei

3D structure databases

ProteinModelPortaliQ8UEY7.
SMRiQ8UEY7. Positions 5-463.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni98 – 1003Substrate binding By similarity
Regioni129 – 1324B site By similarity
Regioni139 – 1413Substrate binding By similarity
Regioni187 – 1882Substrate binding By similarity
Regioni324 – 3263Substrate 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.

Q8UEY7-1 [UniParc]FASTAAdd to Basket

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MTATRTETDT FGPIEVQADR YWGAQAQRSL GNFKIGWEKQ PASVVRALGI    50
VKQAAARANM ALAGLDPKVG DAIIAAAQEV IDGKLTEHFP LVVWQTGSGT 100
QSNMNANEVI SNRAIEMLGG EMGTKKPVHP NDHVNMSQSS NDTYPTAMHI 150
ACVEEIVHHL LPALKHLHTA LEAKVKQFEK IIKIGRTHTQ DATPLTLGQE 200
FSGYAAQVAS AIANIELTLP ALSKLAQGGT AVGTGLNAPV GFAEKVAEEI 250
SEITGLSFVT APNKFEALAS HDSMVFSHGA INAAAAALFK IANDIRFLGS 300
GPRAGLGELS LPENEPGSSI MPGKVNPTQS EALTQVCAHI FGNNAALSFA 350
GSQGHFELNV YNPMMAYNFL QSVQLLGDAA VSFTDNCVVG IEAREDNIRK 400
GVENSLMLVT ALNGKLGYDI CAKIAKTAHK NGTTLREEAV GGGYLTNEEF 450
DQYVRPENMI GPK 463
Length:463
Mass (Da):49,244
Last modified:December 15, 2003 - v2
Checksum:iCDC3B0A32C5CC41C
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE007869 Genomic DNA. Translation: AAK87395.2.
PIRiAD2775.
B97555.
RefSeqiNP_354610.2. NC_003062.2.

Genome annotation databases

EnsemblBacteriaiAAK87395; AAK87395; Atu1616.
GeneIDi1133654.
KEGGiatu:Atu1616.
PATRICi20813009. VBIAgrTum91616_1635.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE007869 Genomic DNA. Translation: AAK87395.2 .
PIRi AD2775.
B97555.
RefSeqi NP_354610.2. NC_003062.2.

3D structure databases

ProteinModelPortali Q8UEY7.
SMRi Q8UEY7. Positions 5-463.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 176299.Atu1616.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAK87395 ; AAK87395 ; Atu1616 .
GeneIDi 1133654.
KEGGi atu:Atu1616.
PATRICi 20813009. VBIAgrTum91616_1635.

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: C58 / ATCC 33970.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C58 / ATCC 33970.

Entry informationi

Entry nameiFUMC_AGRT5
AccessioniPrimary (citable) accession number: Q8UEY7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: December 15, 2003
Last modified: May 14, 2014
This is version 80 of the entry and version 2 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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