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Q929E8

- FUMC_LISIN

UniProt

Q929E8 - FUMC_LISIN

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Protein

Fumarate hydratase class II

Gene

fumC

Organism
Listeria innocua serovar 6a (strain CLIP 11262)
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
Synonyms:citG
Ordered Locus Names:lin2328
OrganismiListeria innocua serovar 6a (strain CLIP 11262)
Taxonomic identifieri272626 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesListeriaceaeListeria
ProteomesiUP000002513: Chromosome

Organism-specific databases

GenoListiLIN2328.

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_0000161284Add
BLAST

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Protein-protein interaction databases

STRINGi272626.lin2328.

Structurei

3D structure databases

ProteinModelPortaliQ929E8.
SMRiQ929E8. 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.

Q929E8 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MERIERDTLG EISVDATKYW GAQTERSRRN FAIGDNYMPK EIIYAFAQLK
60 70 80 90 100
KAAAKVNALE GKLSEAKSVA IGNVCDQIIQ GELDEHFPLV VWQTGSGTQS
110 120 130 140 150
NMNVNEVIAH VANLTLGEEK VHPNDDVNMS QSSNDTFPTA MHIAAYQALV
160 170 180 190 200
TKLLSEITKM EEVLTTKKNQ YMQLVKIGRT HLQDATPLTL GQEISGWEAC
210 220 230 240 250
LTNNKNYLES SMKAILPLAI GGTAVGTGLN ASKDFGDKVA EELRKQTGYP
260 270 280 290 300
FTSDSNKYFA LTSHSPINFV HGAIRSLASD LMKIANDIRL LASGPRSGIG
310 320 330 340 350
ELTLPANEPG SSIMPGKVNP TQCEAITMVA AQVMGNDTTI NIAASQGNFE
360 370 380 390 400
LNVYKPVIIF NFLESITLLS DSMRSFRIHC LEGLTANESV IEAKVNDSLM
410 420 430 440 450
LVTALNPHIG YEKAAKIAKL AFDENTTLKE AAIKTGFVTE KEFDLWIDPL

KMTNL
Length:455
Mass (Da):49,737
Last modified:December 1, 2001 - v1
Checksum:i800F577E7E5BEB38
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AL596171 Genomic DNA. Translation: CAC97556.1.
PIRiAD1723.
RefSeqiNP_471660.1. NC_003212.1.

Genome annotation databases

EnsemblBacteriaiCAC97556; CAC97556; CAC97556.
GeneIDi1131082.
KEGGilin:lin2328.
PATRICi20301493. VBILisInn102668_2379.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AL596171 Genomic DNA. Translation: CAC97556.1 .
PIRi AD1723.
RefSeqi NP_471660.1. NC_003212.1.

3D structure databases

ProteinModelPortali Q929E8.
SMRi Q929E8. Positions 3-452.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 272626.lin2328.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAC97556 ; CAC97556 ; CAC97556 .
GeneIDi 1131082.
KEGGi lin:lin2328.
PATRICi 20301493. VBILisInn102668_2379.

Organism-specific databases

GenoListi LIN2328.

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: CLIP 11262.

Entry informationi

Entry nameiFUMC_LISIN
AccessioniPrimary (citable) accession number: Q929E8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: December 1, 2001
Last modified: October 29, 2014
This is version 81 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