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B2HT54 (B2HT54_MYCMM) Unreviewed, UniProtKB/TrEMBL

Last modified February 19, 2014. Version 40. Feed History...

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

Names and origin

Protein namesRecommended name:
Fumarate hydratase class II HAMAP-Rule MF_00743

Short name=Fumarase C HAMAP-Rule MF_00743
EC=4.2.1.2 HAMAP-Rule MF_00743
Gene names
Name:fum EMBL ACC42775.1
Synonyms:fumC HAMAP-Rule MF_00743
Ordered Locus Names:MMAR_4368 EMBL ACC42775.1
OrganismMycobacterium marinum (strain ATCC BAA-535 / M) [Complete proteome] [HAMAP] EMBL ACC42775.1
Taxonomic identifier216594 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium

Protein attributes

Sequence length476 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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 SAAS SAAS005677.

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. HAMAP-Rule MF_00743

Sequence similarities

Belongs to the class-II fumarase/aspartase family. Fumarase subfamily. HAMAP-Rule MF_00743

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Region133 – 1364B site By similarity HAMAP-Rule MF_00743
Region143 – 1453Substrate binding By similarity HAMAP-Rule MF_00743

Sites

Binding site1111Substrate By similarity HAMAP-Rule MF_00743

Sequences

Sequence LengthMass (Da)Tools
B2HT54 [UniParc].

Last modified June 10, 2008. Version 1.
Checksum: EA3DEA92B5FFD49F

FASTA47650,192
        10         20         30         40         50         60 
MAHSAHDDAD NDTEYRIEHD TMGEVRVPAK ALWRAQTQRA VENFPISGRG LERAQIRALG 

        70         80         90        100        110        120 
LLKGACAQVN MDLGLLAPEK AEAIIAAAAE IADGQHDDQF PIDVFQTGSG TSSNMNTNEV 

       130        140        150        160        170        180 
IASIAGANGV AVHPNDDVNM SQSSNDTFPT ATHIAATEAA VSHLIPALEI LQDALATKAL 

       190        200        210        220        230        240 
EWQSVVKSGR THLMDAVPVT LGQEFSGYAR QIEAGIERVR ATLPRLGELA IGGTAVGTGL 

       250        260        270        280        290        300 
NAPEGFGVKV VSVLVSQTGL PQLRTAANSF EAQAARDGLV EASGALRTIA VSLTKIANDI 

       310        320        330        340        350        360 
RWMGSGPLTG LAEIQLPDLQ PGSSIMPGKV NPVLPEAVTQ VAAQVIGNDA AVAWGGANGA 

       370        380        390        400        410        420 
FELNVYIPMM ARNILESFTL LTNVSKLFAQ RCIAGLTANA EHLRELAESS PSIVTPLNSA 

       430        440        450        460        470 
IGYEEAAAVA KQALKERKTI RQTVIDRGLI GDKLSLEELD RRLDVLAMAK VEATDD 

« Hide

References

« Hide 'large scale' references
[1]"Insights from the complete genome sequence of Mycobacterium marinum on the evolution of Mycobacterium tuberculosis."
Stinear T.P., Seemann T., Harrison P.F., Jenkin G.A., Davies J.K., Johnson P.D., Abdellah Z., Arrowsmith C., Chillingworth T., Churcher C., Clarke K., Cronin A., Davis P., Goodhead I., Holroyd N., Jagels K., Lord A., Moule S. expand/collapse author list , Mungall K., Norbertczak H., Quail M.A., Rabbinowitsch E., Walker D., White B., Whitehead S., Small P.L., Brosch R., Ramakrishnan L., Fischbach M.A., Parkhill J., Cole S.T.
Genome Res. 18:729-741(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-535 / M.
[2]"Crystal structure of fumarase Fum from Mycobacterium marinum."
Edwards T.E., Gardberg A.S., Sankaran B.
Submitted (JAN-2011) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 1-474.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000854 Genomic DNA. Translation: ACC42775.1.
RefSeqYP_001852630.1. NC_010612.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3QBPX-ray1.85A/B/C/D1-474[»]
ProteinModelPortalB2HT54.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING216594.MMAR_4368.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACC42775; ACC42775; MMAR_4368.
GeneID6228650.
KEGGmmi:MMAR_4368.
PATRIC18070061. VBIMycMar75906_4696.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0114.
HOGENOMHOG000061737.
KOK01679.
OMARIEKDTM.
OrthoDBEOG6V1M4M.
ProtClustDBPRK00485.

Enzyme and pathway databases

BioCycMMAR216594:GJOB-4401-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...

Other

EvolutionaryTraceB2HT54.

Entry information

Entry nameB2HT54_MYCMM
AccessionPrimary (citable) accession number: B2HT54
Entry history
Integrated into UniProtKB/TrEMBL: June 10, 2008
Last sequence update: June 10, 2008
Last modified: February 19, 2014
This is version 40 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)