Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Fumarate hydratase class II

Gene

fumC

Organism
Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium meliloti)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

(S)-malate = fumarate + H2O.

Pathwayi: tricarboxylic acid cycle

This protein is involved in step 1 of the subpathway that synthesizes (S)-malate from fumarate.
Proteins known to be involved in this subpathway in this organism are:
  1. Fumarate hydratase class II (fumC)
This subpathway is part of the pathway tricarboxylic acid cycle, which is itself part of Carbohydrate metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes (S)-malate from fumarate, the pathway tricarboxylic acid cycle and in Carbohydrate metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei188Proton donor/acceptorBy similarity1
Active sitei318By similarity1
Binding sitei319SubstrateBy similarity1
Sitei331Important for catalytic activityBy similarity1

GO - Molecular functioni

GO - Biological processi

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:R01859
ORF Names:SMc00149
OrganismiRhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium meliloti)
Taxonomic identifieri266834 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhizobiaceaeSinorhizobium/Ensifer groupSinorhizobium
Proteomesi
  • UP000001976 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001613051 – 463Fumarate hydratase class IIAdd BLAST463

Interactioni

Subunit structurei

Homotetramer.1 Publication

Protein-protein interaction databases

STRINGi266834.SMc00149.

Structurei

Secondary structure

1463
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 9Combined sources6
Beta strandi12 – 17Combined sources6
Helixi24 – 32Combined sources9
Helixi42 – 61Combined sources20
Helixi67 – 81Combined sources15
Helixi86 – 88Combined sources3
Beta strandi92 – 95Combined sources4
Helixi100 – 117Combined sources18
Turni122 – 125Combined sources4
Helixi130 – 134Combined sources5
Turni135 – 137Combined sources3
Helixi140 – 158Combined sources19
Helixi160 – 178Combined sources19
Beta strandi182 – 187Combined sources6
Beta strandi190 – 196Combined sources7
Helixi197 – 217Combined sources21
Helixi219 – 222Combined sources4
Turni230 – 232Combined sources3
Helixi242 – 254Combined sources13
Helixi264 – 269Combined sources6
Helixi272 – 298Combined sources27
Beta strandi302 – 305Combined sources4
Helixi328 – 352Combined sources25
Helixi362 – 386Combined sources25
Helixi388 – 390Combined sources3
Helixi395 – 404Combined sources10
Helixi407 – 411Combined sources5
Helixi413 – 416Combined sources4
Helixi418 – 431Combined sources14
Helixi435 – 440Combined sources6
Turni441 – 443Combined sources3
Helixi447 – 453Combined sources7
Helixi456 – 458Combined sources3
Beta strandi459 – 461Combined sources3

3D structure databases

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

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni98 – 100Substrate bindingBy similarity3
Regioni129 – 132B siteBy similarity4
Regioni139 – 141Substrate bindingBy similarity3
Regioni187 – 188Substrate bindingBy similarity2
Regioni324 – 326Substrate bindingBy similarity3

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105C9Q. Bacteria.
COG0114. LUCA.
HOGENOMiHOG000061736.
KOiK01679.

Family and domain databases

Gene3Di1.10.275.10. 1 hit.
HAMAPiMF_00743. FumaraseC. 1 hit.
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 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.
WP_010969522.1. 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.
RefSeqiNP_385965.3. NC_003047.1.
WP_010969522.1. NC_003047.1.

3D structure databases

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

Protein-protein interaction databases

STRINGi266834.SMc00149.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Phylogenomic databases

eggNOGiENOG4105C9Q. Bacteria.
COG0114. LUCA.
HOGENOMiHOG000061736.
KOiK01679.

Enzyme and pathway databases

UniPathwayiUPA00223; UER01007.

Family and domain databases

Gene3Di1.10.275.10. 1 hit.
HAMAPiMF_00743. FumaraseC. 1 hit.
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]
ProtoNetiSearch...

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 30, 2016
This is version 96 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.