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Q9HQ29 (FUMC_HALSA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 79. 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:VNG_1356G
OrganismHalobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1) (Halobacterium halobium) [Reference proteome] [HAMAP]
Taxonomic identifier64091 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaHalobacteriaHalobacterialesHalobacteriaceaeHalobacterium

Protein attributes

Sequence length470 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
Reference 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 – 470470Fumarate hydratase class II HAMAP-Rule MF_00743
PRO_0000161332

Regions

Region99 – 1013Substrate binding By similarity
Region129 – 1324B site By similarity
Region139 – 1413Substrate binding By similarity
Region187 – 1882Substrate binding By similarity
Region324 – 3263Substrate binding By similarity

Sites

Active site1881Proton donor/acceptor By similarity
Active site3181 By similarity
Binding site3191Substrate By similarity
Site3311Important for catalytic activity By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9HQ29 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 31FF468F0B4FC261

FASTA47049,597
        10         20         30         40         50         60 
MSEDYRTEQD SLGEMQVPAD AYWGAQTQRA IENFPISGIA FGRRFVRALG VVKKAAAQAN 

        70         80         90        100        110        120 
RDLGLVDDER ADAIVAAADE VIAGEHDDQF PVDVFQTGSG TSSNMNANEV IANRAAELLG 

       130        140        150        160        170        180 
EEIGDRVVHP NDHVNYGQSS NDVIPTAMHV ASLDALVNDV KPGLETLAAE LDDKADAFDG 

       190        200        210        220        230        240 
VVKTGRTHLQ DATPVRLGQE FGGYRTQVEK GIDRIEAVAP RLSELALGGT AVGTGLNTHP 

       250        260        270        280        290        300 
EFPETAAGYI SEETGVTFRE ADNHFEAQAA HDAMNEAHGA LRTVAGSLNK IANDLRLLAS 

       310        320        330        340        350        360 
GPRNGLGEIE QPENQPGSSI MPGKINPVVA EAVNQVHKQV VGNDAAIAAG AAEGQIDLNL 

       370        380        390        400        410        420 
YKPVLAHNFL QSADMLANAS AAFGEKFVAK LEANEAACEA QVERSMALAT ALNPTIGYDK 

       430        440        450        460        470 
ASEVAKAALK EGKTVTEVVV EKGYLSEAEA ADVLDPEGMT HRGILSGDDT 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE004437 Genomic DNA. Translation: AAG19688.1.
PIRD84290.
RefSeqNP_280208.1. NC_002607.1.

3D structure databases

ProteinModelPortalQ9HQ29.
SMRQ9HQ29. Positions 5-459.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING64091.VNG1356G.

Proteomic databases

PaxDbQ9HQ29.
PRIDEQ9HQ29.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAG19688; AAG19688; VNG_1356G.
GeneID1447987.
KEGGhal:VNG1356G.

Phylogenomic databases

eggNOGCOG0114.
KOK01679.
OMALNVMLPI.
PhylomeDBQ9HQ29.

Enzyme and pathway databases

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_HALSA
AccessionPrimary (citable) accession number: Q9HQ29
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: March 1, 2001
Last modified: May 14, 2014
This is version 79 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