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Q92PB6

- FUMC_RHIME

UniProt

Q92PB6 - FUMC_RHIME

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Protein
Fumarate hydratase class II
Gene
fumC, R01859, SMc00149
Organism
Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium meliloti)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at protein leveli

Functioni

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
Complete GO annotation...

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

BioCyciRETL1328306-WGS:GSTH-2397-MONOMER.
SMEL266834:GJF6-1907-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:R01859
ORF Names:SMc00149
OrganismiRhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium meliloti)
Taxonomic identifieri266834 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhizobiaceaeSinorhizobium/Ensifer groupSinorhizobium
ProteomesiUP000001976: 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 – 463463Fumarate hydratase class IIUniRule annotation
PRO_0000161305Add
BLAST

Proteomic databases

ProMEXiQ92PB6.

Interactioni

Subunit structurei

Homotetramer.1 Publication

Protein-protein interaction databases

STRINGi266834.SMc00149.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 96
Beta strandi12 – 176
Helixi24 – 329
Helixi42 – 6120
Helixi67 – 8115
Helixi86 – 883
Beta strandi92 – 954
Helixi100 – 11718
Turni122 – 1254
Helixi130 – 1345
Turni135 – 1373
Helixi140 – 15819
Helixi160 – 17819
Beta strandi182 – 1876
Beta strandi190 – 1967
Helixi197 – 21721
Helixi219 – 2224
Turni230 – 2323
Helixi242 – 25413
Helixi264 – 2696
Helixi272 – 29827
Beta strandi302 – 3054
Helixi328 – 35225
Helixi362 – 38625
Helixi388 – 3903
Helixi395 – 40410
Helixi407 – 4115
Helixi413 – 4164
Helixi418 – 43114
Helixi435 – 4406
Turni441 – 4433
Helixi447 – 4537
Helixi456 – 4583
Beta strandi459 – 4613

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4HGVX-ray2.09A/B/C/D1-463[»]
ProteinModelPortaliQ92PB6.
SMRiQ92PB6. Positions 5-462.

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.
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.

Q92PB6-1 [UniParc]FASTAAdd to Basket

« Hide

MTSTRTETDT FGPIEVASDR YWGAQAQRSL GNFKIGWEKQ PLAIVRALGI    50
VKQAAARANM ALGRLDPAIG DAIVKAAQEV IDGKLDEHFP LVVWQTGSGT 100
QSNMNANEVV SNRAIELLGG VMGSKKPVHP NDHVNMSQSS NDTYPTAMHI 150
ACAERVIHDL LPALKHLHKA LEEKVKAFDH IIKIGRTHTQ DATPLTLGQE 200
FSGYAAQVAS SIKRIEMTLP GLCELAQGGT AVGTGLNAPV GFAEKVAEEI 250
AAITGIGFTS APNKFEALAA HDSMVFSHGA INATAAALFK IANDIRFLGS 300
GPRSGLGELS LPENEPGSSI MPGKVNPTQC EALTQVCVQV FGNHAALTFA 350
GSQGHFELNV YNPLMAYNFL QSVQLLADAA ISFTDNCVVG IEAREDNIKA 400
ALDRSLMLVT ALAPKIGYDN AAKIAKTAHK NGTTLREEAV GGGYVTDEEF 450
DAVVRPETMI GPA 463
Length:463
Mass (Da):49,133
Last modified:December 15, 2003 - v2
Checksum:iA500EDE8A6789C5F
GO

Sequence cautioni

The sequence CAC46438.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AL591688 Genomic DNA. Translation: CAC46438.1. Different initiation.
RefSeqiNP_385965.3. NC_003047.1.

Genome annotation databases

EnsemblBacteriaiCAC46438; CAC46438; SMc00149.
GeneIDi1233524.
KEGGisme:SMc00149.
PATRICi23633127. VBISinMel96828_3302.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AL591688 Genomic DNA. Translation: CAC46438.1 . Different initiation.
RefSeqi NP_385965.3. NC_003047.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4HGV X-ray 2.09 A/B/C/D 1-463 [» ]
ProteinModelPortali Q92PB6.
SMRi Q92PB6. Positions 5-462.
ModBasei Search...

Protein-protein interaction databases

STRINGi 266834.SMc00149.

Proteomic databases

ProMEXi Q92PB6.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAC46438 ; CAC46438 ; SMc00149 .
GeneIDi 1233524.
KEGGi sme:SMc00149.
PATRICi 23633127. VBISinMel96828_3302.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00223 ; UER01007 .
BioCyci RETL1328306-WGS:GSTH-2397-MONOMER.
SMEL266834:GJF6-1907-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

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 1021.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 1021.
  3. Cited for: X-RAY CRYSTALLOGRAPHY (2.09 ANGSTROMS), SUBUNIT.

Entry informationi

Entry nameiFUMC_RHIME
AccessioniPrimary (citable) accession number: Q92PB6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: December 15, 2003
Last modified: July 9, 2014
This is version 81 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

3D-structure, Complete proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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