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Q92PB6

- FUMC_RHIME

UniProt

Q92PB6 - FUMC_RHIME

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Protein

Fumarate hydratase class II

Gene

fumC

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.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei188 – 1881Proton donor/acceptorBy similarity
Active sitei318 – 3181By similarity
Binding sitei319 – 3191SubstrateBy similarity
Sitei331 – 3311Important 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

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

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 IIPRO_0000161305Add
BLAST

Interactioni

Subunit structurei

Homotetramer.1 Publication

Protein-protein interaction databases

STRINGi266834.SMc00149.

Structurei

Secondary structure

1
463
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 96Combined sources
Beta strandi12 – 176Combined sources
Helixi24 – 329Combined sources
Helixi42 – 6120Combined sources
Helixi67 – 8115Combined sources
Helixi86 – 883Combined sources
Beta strandi92 – 954Combined sources
Helixi100 – 11718Combined sources
Turni122 – 1254Combined sources
Helixi130 – 1345Combined sources
Turni135 – 1373Combined sources
Helixi140 – 15819Combined sources
Helixi160 – 17819Combined sources
Beta strandi182 – 1876Combined sources
Beta strandi190 – 1967Combined sources
Helixi197 – 21721Combined sources
Helixi219 – 2224Combined sources
Turni230 – 2323Combined sources
Helixi242 – 25413Combined sources
Helixi264 – 2696Combined sources
Helixi272 – 29827Combined sources
Beta strandi302 – 3054Combined sources
Helixi328 – 35225Combined sources
Helixi362 – 38625Combined sources
Helixi388 – 3903Combined sources
Helixi395 – 40410Combined sources
Helixi407 – 4115Combined sources
Helixi413 – 4164Combined sources
Helixi418 – 43114Combined sources
Helixi435 – 4406Combined sources
Turni441 – 4433Combined sources
Helixi447 – 4537Combined sources
Helixi456 – 4583Combined sources
Beta strandi459 – 4613Combined sources

3D structure databases

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

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni98 – 1003Substrate bindingBy similarity
Regioni129 – 1324B siteBy similarity
Regioni139 – 1413Substrate bindingBy similarity
Regioni187 – 1882Substrate bindingBy similarity
Regioni324 – 3263Substrate bindingBy 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

        10         20         30         40         50
MTSTRTETDT FGPIEVASDR YWGAQAQRSL GNFKIGWEKQ PLAIVRALGI
60 70 80 90 100
VKQAAARANM ALGRLDPAIG DAIVKAAQEV IDGKLDEHFP LVVWQTGSGT
110 120 130 140 150
QSNMNANEVV SNRAIELLGG VMGSKKPVHP NDHVNMSQSS NDTYPTAMHI
160 170 180 190 200
ACAERVIHDL LPALKHLHKA LEEKVKAFDH IIKIGRTHTQ DATPLTLGQE
210 220 230 240 250
FSGYAAQVAS SIKRIEMTLP GLCELAQGGT AVGTGLNAPV GFAEKVAEEI
260 270 280 290 300
AAITGIGFTS APNKFEALAA HDSMVFSHGA INATAAALFK IANDIRFLGS
310 320 330 340 350
GPRSGLGELS LPENEPGSSI MPGKVNPTQC EALTQVCVQV FGNHAALTFA
360 370 380 390 400
GSQGHFELNV YNPLMAYNFL QSVQLLADAA ISFTDNCVVG IEAREDNIKA
410 420 430 440 450
ALDRSLMLVT ALAPKIGYDN AAKIAKTAHK NGTTLREEAV GGGYVTDEEF
460
DAVVRPETMI GPA
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.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
Links Updated
AL591688 Genomic DNA. Translation: CAC46438.1 . Different initiation.
RefSeqi NP_385965.3. NC_003047.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 266834.SMc00149.

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: November 26, 2014
This is version 83 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).By similarity

Keywords - Technical termi

3D-structure, Complete proteome, Reference 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