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Q87DC2 (FUMC_XYLFT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 74. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Fumarate hydratase class II

Short name=Fumarase C
EC=4.2.1.2
Gene names
Name:fumC
Ordered Locus Names:PD_0763
OrganismXylella fastidiosa (strain Temecula1 / ATCC 700964) [Complete proteome] [HAMAP]
Taxonomic identifier183190 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeXylella

Protein attributes

Sequence length473 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the reversible addition of water to fumarate to give L-malate By similarity. HAMAP-Rule MF_00743

Catalytic activity

(S)-malate = fumarate + H2O. HAMAP-Rule MF_00743

Pathway

Carbohydrate metabolism; tricarboxylic acid cycle; (S)-malate from fumarate: step 1/1. HAMAP-Rule MF_00743

Subunit structure

Homotetramer By similarity. HAMAP-Rule MF_00743

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00743.

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.

Sequence similarities

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

Ontologies

Keywords
   Biological processTricarboxylic acid cycle
   Cellular componentCytoplasm
   Molecular functionLyase
   Technical termAllosteric enzyme
Complete proteome
Gene Ontology (GO)
   Biological_processfumarate metabolic process

Inferred from electronic annotation. Source: InterPro

tricarboxylic acid cycle

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componenttricarboxylic acid cycle enzyme complex

Inferred from electronic annotation. Source: InterPro

   Molecular_functionfumarate hydratase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 473473Fumarate hydratase class II HAMAP-Rule MF_00743
PRO_0000161330

Regions

Region105 – 1073Substrate binding By similarity
Region130 – 1334B site By similarity
Region140 – 1423Substrate binding By similarity
Region188 – 1892Substrate binding By similarity
Region325 – 3273Substrate binding By similarity

Sites

Active site1891Proton donor/acceptor By similarity
Active site3191 By similarity
Binding site3201Substrate By similarity
Site3321Important for catalytic activity By similarity

Sequences

Sequence LengthMass (Da)Tools
Q87DC2 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 2524DE56009C298D

FASTA47350,411
        10         20         30         40         50         60 
MEMQMSNSDR YRIEHDSMGD LRVPIDALWG AQTQRAIENF PISGRSMPQG FIHALGFIKA 

        70         80         90        100        110        120 
AAAKVNAELG LLPKSMAKEI EAAALDVAAG RYDAEFPVDI YQTGSGTSSN MNANEVIATL 

       130        140        150        160        170        180 
AMRATKGPIH PNDHVNLGQS SNDVVPTAIR ISATLAVQGR LLPALKHLRK MINKRARGLG 

       190        200        210        220        230        240 
SVVKTGRTHL MDAMPLTFAQ EFGAWSAQIV SAEARLNDTL KRLHRLPLGG TAIGTGINTD 

       250        260        270        280        290        300 
PHFGRNAVKV LSALTGIHFE SANNKFEGLA AQDDLVELSG QFNTLAVALM KIANDLRWMN 

       310        320        330        340        350        360 
AGPLAGLGEI ELPALQPGSS IMPGKVNPVI PEAVVMVASQ VIGHHTAVTV AGQSGNFQLN 

       370        380        390        400        410        420 
VTLPLIAYNL LESATLLGNV VMLLADKVIV GLKVRQDRVQ EVLERNPILV TALNPIIGYE 

       430        440        450        460        470 
KAAVIAKRAY KEHRPVLEVA CEESNLNPVE LARLLDPAAL TEGGIHVVGG GGG 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE009442 Genomic DNA. Translation: AAO28632.1.
RefSeqNP_778983.2. NC_004556.1.

3D structure databases

ProteinModelPortalQ87DC2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING183190.PD0763.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAO28632; AAO28632; PD_0763.
GeneID1143485.
KEGGxft:PD0763.
PATRIC24149343. VBIXylFas71109_0986.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0114.
KOK01679.
OMAMFSGPMT.
OrthoDBEOG6V1M4M.

Enzyme and pathway databases

BioCycXFAS183190:GIX4-763-MONOMER.
UniPathwayUPA00223; UER01007.

Family and domain databases

Gene3D1.10.275.10. 1 hit.
HAMAPMF_00743. FumaraseC.
InterProIPR005677. 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]
PANTHERPTHR11444. PTHR11444. 1 hit.
PfamPF10415. FumaraseC_C. 1 hit.
PF00206. Lyase_1. 1 hit.
[Graphical view]
PRINTSPR00149. FUMRATELYASE.
SUPFAMSSF48557. SSF48557. 1 hit.
PROSITEPS00163. FUMARATE_LYASES. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFUMC_XYLFT
AccessionPrimary (citable) accession number: Q87DC2
Entry history
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: June 1, 2003
Last modified: May 14, 2014
This is version 74 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways