Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q7U0N6 (FUMC_MYCBO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 64. 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
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
Synonyms:fum
Ordered Locus Names:Mb1128c
OrganismMycobacterium bovis (strain ATCC BAA-935 / AF2122/97) [Complete proteome] [HAMAP]
Taxonomic identifier233413 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex ›

Protein attributes

Sequence length474 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.

Subcellular location

Cytoplasm 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 termComplete proteome
Gene Ontology (GO)
   Biological_processfumarate metabolic process

Inferred from electronic annotation. Source: InterPro

tricarboxylic acid cycle

Inferred from electronic annotation. Source: HAMAP

   Cellular_componenttricarboxylic acid cycle enzyme complex

Inferred from electronic annotation. Source: InterPro

   Molecular_functionfumarate hydratase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 474474Fumarate hydratase class II HAMAP-Rule MF_00743
PRO_0000161288

Regions

Region104 – 1063Substrate binding By similarity
Region138 – 1403Substrate binding By similarity
Region186 – 1872Substrate binding By similarity
Region324 – 3263Substrate binding By similarity

Sites

Active site1871Proton donor/acceptor By similarity
Active site3181 By similarity
Binding site3191Substrate By similarity
Site3311Important for catalytic activity By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7U0N6 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: 4052F93F963D3DBB

FASTA47450,141
        10         20         30         40         50         60 
MAVDADSANY RIEHDTMGEV RVPAKALWRA QTQRAVENFP ISGRGLERTQ IRALGLLKGA 

        70         80         90        100        110        120 
CAQVNSDLGL LAPEKADAII AAAAEIADGQ HDDQFPIDVF QTGSGTSSNM NTNEVIASIA 

       130        140        150        160        170        180 
AKGGVTLHPN DDVNMSQSSN DTFPTATHIA ATEAAVAHLI PALQQLHDAL AAKALDWHTV 

       190        200        210        220        230        240 
VKSGRTHLMD AVPVTLGQEF SGYARQIEAG IERVRACLPR LGELAIGGTA VGTGLNAPDD 

       250        260        270        280        290        300 
FGVRVVAVLV AQTGLSELRT AANSFEAQAA RDGLVEASGA LRTIAVSLTK IANDIRWMGS 

       310        320        330        340        350        360 
GPLTGLAEIQ LPDLQPGSSI MPGKVNPVLP EAVTQVAAQV IGNDAAIAWG GANGAFELNV 

       370        380        390        400        410        420 
YIPMMARNIL ESFKLLTNVS RLFAQRCIAG LTANVEHLRR LAESSPSIVT PLNSAIGYEE 

       430        440        450        460        470 
AAAVAKQALK ERKTIRQTVI DRGLIGDRLS IEDLDRRLDV LAMAKAEQLD SDRL

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BX248337 Genomic DNA. Translation: CAD93989.1.
RefSeqNP_854784.1. NC_002945.3.

3D structure databases

ProteinModelPortalQ7U0N6.
SMRQ7U0N6. Positions 10-465.
ModBaseSearch...

Protein-protein interaction databases

STRING233413.Mb1128c.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAD93989; CAD93989; Mb1128c.
GeneID1090418.
KEGGmbo:Mb1128c.
PATRIC18004163. VBIMycBov88188_1234.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0114.
HOGENOMHOG000061736.
KOK01679.
OMAIIPTTIH.
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.
IPR000362. Fumarate_lyase.
IPR020557. Fumarate_lyase_CS.
IPR022761. Fumarate_lyase_N.
IPR008948. L-Aspartase-like.
[Graphical view]
PfamPF10415. FumaraseC_C. 1 hit.
PF00206. Lyase_1. 1 hit.
[Graphical view]
PRINTSPR00149. FUMRATELYASE.
SUPFAMSSF48557. L-Aspartase-like. 1 hit.
PROSITEPS00163. FUMARATE_LYASES. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFUMC_MYCBO
AccessionPrimary (citable) accession number: Q7U0N6
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: October 1, 2003
Last modified: May 1, 2013
This is version 64 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents