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Q71XE0

- FUMC_LISMF

UniProt

Q71XE0 - FUMC_LISMF

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Protein

Fumarate hydratase class II

Gene

fumC

Organism
Listeria monocytogenes serotype 4b (strain F2365)
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

Catalytic activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei181 – 1811Proton donor/acceptorBy similarity
Active sitei311 – 3111By similarity
Binding sitei312 – 3121SubstrateUniRule annotation
Sitei324 – 3241Important 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

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 annotation
Ordered Locus Names:LMOf2365_2258
OrganismiListeria monocytogenes serotype 4b (strain F2365)
Taxonomic identifieri265669 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesListeriaceaeListeria
ProteomesiUP000000563: Chromosome

Subcellular locationi

Cytoplasm 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 – 455455Fumarate hydratase class IIPRO_0000161285Add
BLAST

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Protein-protein interaction databases

STRINGi265669.LMOf2365_2258.

Structurei

3D structure databases

ProteinModelPortaliQ71XE0.
SMRiQ71XE0. Positions 3-452.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni96 – 983Substrate bindingUniRule annotation
Regioni122 – 1254B siteUniRule annotation
Regioni132 – 1343Substrate bindingUniRule annotation
Regioni180 – 1812Substrate bindingUniRule annotation
Regioni317 – 3193Substrate bindingUniRule annotation

Sequence similaritiesi

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

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.

Q71XE0-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MERIERDTLG EISVDATKYW GAQTERSKRN FAIGDNPMPI EIIYAFAQLK
60 70 80 90 100
KATAKVNAAE GKLSEEKAIA IGQVCDQIIQ GELDEHFPLV VWQTGSGTQS
110 120 130 140 150
NMNVNEVIAH VANLTLGEGQ IHPNDDVNMS QSSNDTFPTA MHIAAYGALV
160 170 180 190 200
TKLLPEITKM EAVLAEKKSK YMHLVKIGRT HLQDATPLTL GQEISGWEAC
210 220 230 240 250
LTNNKNYLET SMKAILPLAI GGTAVGTGLN ASRDFGDKVA EELMKQTGYP
260 270 280 290 300
FTSDSNKYFA LTSHSPINFV HGSIRSLASD LMKIANDIRL LASGPRSGIG
310 320 330 340 350
ELTIPVNEPG SSIMPGKVNP TQCEAMTMVA AQVMGNDVTI NVAASQGNFE
360 370 380 390 400
LNVYKPVIIF NFLESVKLLS DSMRSFRLHC LEGLTANEKV IETKVNDSLM
410 420 430 440 450
LVTALNPHIG YEKAAKIAKL AFDENTTLKE AAIKTGFVTE KQFDLWIDPL

KMTNL
Length:455
Mass (Da):49,635
Last modified:July 5, 2004 - v1
Checksum:iF471032E5D146F5C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE017262 Genomic DNA. Translation: AAT05025.1.
RefSeqiYP_014848.1. NC_002973.6.

Genome annotation databases

EnsemblBacteriaiAAT05025; AAT05025; LMOf2365_2258.
GeneIDi2799834.
KEGGilmf:LMOf2365_2258.
PATRICi20325839. VBILisMon105049_2273.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE017262 Genomic DNA. Translation: AAT05025.1 .
RefSeqi YP_014848.1. NC_002973.6.

3D structure databases

ProteinModelPortali Q71XE0.
SMRi Q71XE0. Positions 3-452.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 265669.LMOf2365_2258.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAT05025 ; AAT05025 ; LMOf2365_2258 .
GeneIDi 2799834.
KEGGi lmf:LMOf2365_2258.
PATRICi 20325839. VBILisMon105049_2273.

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: F2365.

Entry informationi

Entry nameiFUMC_LISMF
AccessioniPrimary (citable) accession number: Q71XE0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: July 5, 2004
Last modified: October 29, 2014
This is version 73 of the entry and version 1 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

Allosteric enzyme, Complete proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3