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P71384 (FUMC_HAEIN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 101. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:HI_1398
OrganismHaemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) [Reference proteome] [HAMAP]
Taxonomic identifier71421 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHaemophilus

Protein attributes

Sequence length464 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 – 464464Fumarate hydratase class II HAMAP-Rule MF_00743
PRO_0000161279

Regions

Region98 – 1003Substrate 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
P71384 [UniParc].

Last modified February 1, 1997. Version 1.
Checksum: AC836336DA7457CE

FASTA46450,482
        10         20         30         40         50         60 
MAFRIEKDTM GEVQVLADKY WAAQTERSRN NFKIGPAASM PHEIIEAFGY LKKAAAFANH 

        70         80         90        100        110        120 
DLGVLPLEKR DLIALACDEI LANKLDDQFP LVIWQTGSGT QSNMNVNEVV ANRAHVLNGG 

       130        140        150        160        170        180 
KLGEKSIIHP NDDVNKSQSS NDTFPTAMHI AAYKKVVEHT IPCVERLQKT FAAKSEAFKN 

       190        200        210        220        230        240 
VVKIGRTHLM DATPLTLGQE FSAYAAQLDF GLKALKNTLP HLSQLALGGT AVGTGLNTPK 

       250        260        270        280        290        300 
GYDLKVVDYI AKFTALPFVT ADNKFEALAA HDAIVETHGA LRQLAMSLFK IANDIRLLAS 

       310        320        330        340        350        360 
GPRSGIGEIL IPENEPGSSI MPGKVNPTQC EXMTMVCAQV FGNDTTIAFV GSQGHFQLNV 

       370        380        390        400        410        420 
FNPVMIANFL QSAQLLGDAC VSFDEHCAVG IEPNYPRIKQ QLENSLMLVT ALNTHIGYEN 

       430        440        450        460 
AAKIAKTAHK NGTTLREEAI NLGLVSAEDF DKWVRPEDMV GSLK 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L42023 Genomic DNA. Translation: AAC23045.1.
RefSeqNP_439551.1. NC_000907.1.

3D structure databases

ProteinModelPortalP71384.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING71421.HI1398.

Proteomic databases

PRIDEP71384.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC23045; AAC23045; HI_1398.
GeneID950314.
KEGGhin:HI1398.
PATRIC20191495. VBIHaeInf48452_1458.

Phylogenomic databases

eggNOGCOG0114.
KOK01679.
OMARIEKDTM.
OrthoDBEOG6V1M4M.
ProtClustDBPRK00485.

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.
TIGRFAMsTIGR00979. fumC_II. 1 hit.
PROSITEPS00163. FUMARATE_LYASES. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFUMC_HAEIN
AccessionPrimary (citable) accession number: P71384
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: February 1, 1997
Last modified: March 19, 2014
This is version 101 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

Haemophilus influenzae

Haemophilus influenzae (strain Rd): entries and gene names