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Protein

Fumarate hydratase class II

Gene

fumC

Organism
Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
Status
Unreviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

(S)-malate = fumarate + H2O.UniRule annotation

Pathwayi: tricarboxylic acid cycle

This protein is involved in step 1 of the subpathway that synthesizes (S)-malate from fumarate.UniRule annotation
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
Binding sitei104SubstrateUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

LyaseUniRule annotationSAAS annotationImported

Keywords - Biological processi

Tricarboxylic acid cycleUniRule annotation

Enzyme and pathway databases

UniPathwayiUPA00223; UER01007.

Names & Taxonomyi

Protein namesi
Recommended name:
Fumarate hydratase class IIUniRule annotation (EC:4.2.1.2UniRule annotation)
Short name:
Fumarase CUniRule annotation
Gene namesi
Name:fumCUniRule annotationImported
Ordered Locus Names:MSMEG_5240Imported, MSMEI_5102Imported
OrganismiMycobacterium smegmatis (strain ATCC 700084 / mc(2)155)Imported
Taxonomic identifieri246196 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacterium
Proteomesi
  • UP000006158 Componenti: Chromosome
  • UP000000757 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

CytoplasmUniRule annotation

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Protein-protein interaction databases

STRINGi246196.MSMEG_5240.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3RD8X-ray2.20A1-468[»]
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini16 – 340Lyase_1InterPro annotationAdd BLAST325
Domaini406 – 462FumaraseC_CInterPro annotationAdd BLAST57

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni126 – 129B siteUniRule annotation4
Regioni136 – 138Substrate bindingUniRule annotation3

Sequence similaritiesi

Belongs to the class-II fumarase/aspartase family. Fumarase subfamily.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105C9Q. Bacteria.
COG0114. LUCA.
HOGENOMiHOG000061737.
KOiK01679.
OMAiFAYLKKA.
OrthoDBiPOG091H01XG.

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.
PROSITEiPS00163. FUMARATE_LYASES. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

A0R2U8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MADTDVEYRI EHDTMGEVRV PKDALWRAQT QRAVENFPIS FRGLERTQIR
60 70 80 90 100
ALGLLKAACA QVNKDLGLLD PEKADAIIAA AGEIAEGKHD DQFPIDVFQT
110 120 130 140 150
GSGTSSNMNT NEVIASIAAA NGVTVHPNDH VNMSQSSNDT FPTATHIAAT
160 170 180 190 200
EAAVRHLIPA LEVLHASLAA KAKQWRTVVK SGRTHLMDAV PVTLGQEFGG
210 220 230 240 250
YARQIEAGIE RVKATLPRLG ELAIGGTAVG TGLNAPEGFG AKVVEVLVNE
260 270 280 290 300
TGLAELRTAV DSFEAQAARD GLVEASGALR TIAVSLTKIA NDIRWMGSGP
310 320 330 340 350
LTGLAEIQLP DLQPGSSIMP GKVNPVLPEA VTQVACQVVG NDAAIAFGGA
360 370 380 390 400
SGAFELNVYI PMMARNLLES FTLLSNVSRL FAERCIDGLV ANEERLRELA
410 420 430 440 450
ESSPSIVTPL NSAIGYEEAA KVAKQALAEK KTIRQTVIDR GLIGDKLSLE
460
ELDRRLDVLA MARVKDGE
Length:468
Mass (Da):49,763
Last modified:January 9, 2007 - v1
Checksum:i859EF30B20531A37
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000480 Genomic DNA. Translation: ABK75151.1.
CP001663 Genomic DNA. Translation: AFP41546.1.
RefSeqiWP_011730408.1. NZ_CP009494.1.
YP_889486.1. NC_008596.1.

Genome annotation databases

EnsemblBacteriaiABK75151; ABK75151; MSMEG_5240.
AFP41546; AFP41546; MSMEI_5102.
GeneIDi4532307.
KEGGimsb:LJ00_25915.
msg:MSMEI_5102.
msm:MSMEG_5240.
PATRICi18082765. VBIMycSme59918_5111.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000480 Genomic DNA. Translation: ABK75151.1.
CP001663 Genomic DNA. Translation: AFP41546.1.
RefSeqiWP_011730408.1. NZ_CP009494.1.
YP_889486.1. NC_008596.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3RD8X-ray2.20A1-468[»]
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi246196.MSMEG_5240.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABK75151; ABK75151; MSMEG_5240.
AFP41546; AFP41546; MSMEI_5102.
GeneIDi4532307.
KEGGimsb:LJ00_25915.
msg:MSMEI_5102.
msm:MSMEG_5240.
PATRICi18082765. VBIMycSme59918_5111.

Phylogenomic databases

eggNOGiENOG4105C9Q. Bacteria.
COG0114. LUCA.
HOGENOMiHOG000061737.
KOiK01679.
OMAiFAYLKKA.
OrthoDBiPOG091H01XG.

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.
PROSITEiPS00163. FUMARATE_LYASES. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiA0R2U8_MYCS2
AccessioniPrimary (citable) accession number: A0R2U8
Entry historyi
Integrated into UniProtKB/TrEMBL: January 9, 2007
Last sequence update: January 9, 2007
Last modified: November 2, 2016
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

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.UniRule annotation

Keywords - Technical termi

3D-structureCombined sources, Complete proteome, Reference proteomeImported

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.