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B3QK62 (B3QK62_RHOPT) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 35. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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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:fumC HAMAP-Rule MF_00743
Ordered Locus Names:Rpal_1545
OrganismRhodopseudomonas palustris (strain TIE-1) [Complete proteome] [HAMAP] EMBL ACF00079.1
Taxonomic identifier395960 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Bradyrhizobiaceae › Rhodopseudomonas ›

Protein attributes

Sequence length485 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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.

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Region157 – 1593Substrate binding By similarity HAMAP-Rule MF_00743

Sites

Binding site1181Substrate By similarity HAMAP-Rule MF_00743

Sequences

Sequence LengthMass (Da)Tools
B3QK62 [UniParc].

Last modified September 2, 2008. Version 1.
Checksum: 603962A74ED3F8FF

FASTA48551,713
        10         20         30         40         50         60 
MASETVTPTL RDVPIGFAAK GERREFDSMG SVDVPADRYW GAQTQRSLQH FSIGGDRMPK 

        70         80         90        100        110        120 
AVYHAYGYVK KACALVNHAA GRLPAWKTDA IVRAADETIS GALDDHYPLF VWQTGSGTQS 

       130        140        150        160        170        180 
NMNVNEVVSN RAIQLLGGGL GTQQPVGPND DVNMGQSSND TFPTAMHIAA VTAIDDQVVP 

       190        200        210        220        230        240 
QLSKLIEIIE RKADGWMDVV KIGRTHLEDA VPLTVGQEWH GWAGQLRDAR DAIEASRVGL 

       250        260        270        280        290        300 
YQLAVGGTAV GTGLNAPKGF AVDVAAKIAE LTGKPFVTAP NKFAAQGSLD AMVRAHGALR 

       310        320        330        340        350        360 
DLAVALMKIA NDMRWLASGP RCGFGELLLP SNEPGSSIMP GKVNPTQCEA MVMICIQVMG 

       370        380        390        400        410        420 
NDSAVAFAGS QGNFELNAMR PVIINNFLHS ARILADGCEK FRTYSVEGTD LNRDRIAQYV 

       430        440        450        460        470        480 
EGSVMLVTAL SPVIGYQNAA HIAEDAIAKD LTLKQAALAS GKVDEVMFDR IVRPIDMVGS 


GLAGA

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References

[1]"Complete sequence of Rhodopseudomonas palustris TIE-1."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Lang D., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N. expand/collapse author list , Emerson D., Newman D.K., Roden E., Richardson P.
Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: TIE-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP001096 Genomic DNA. Translation: ACF00079.1.
RefSeqYP_001990554.1. NC_011004.1.

3D structure databases

ProteinModelPortalB3QK62.
SMRB3QK62. Positions 23-477.
ModBaseSearch...

Protein-protein interaction databases

STRING395960.Rpal_1545.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACF00079; ACF00079; Rpal_1545.
GeneID6409202.
KEGGrpt:Rpal_1545.
PATRIC23307509. VBIRhoPal88240_1572.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0114.
HOGENOMHOG000061736.
KOK01679.
OMAQCEAMVM.
ProtClustDBPRK00485.

Enzyme and pathway databases

BioCycRPAL395960:GHPC-1560-MONOMER.
UniPathwayUPA00223; UER01007.

Family and domain databases

Gene3D1.10.275.10. 1 hit.
HAMAPMF_00743. FumaraseC.
InterProIPR003031. D_crystallin.
IPR005677. 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]
PRINTSPR00145. ARGSUCLYASE.
PR00149. FUMRATELYASE.
SUPFAMSSF48557. L-Aspartase-like. 1 hit.
TIGRFAMsTIGR00979. fumC_II. 1 hit.
PROSITEPS00163. FUMARATE_LYASES. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameB3QK62_RHOPT
AccessionPrimary (citable) accession number: B3QK62
Entry history
Integrated into UniProtKB/TrEMBL: September 2, 2008
Last sequence update: September 2, 2008
Last modified: May 1, 2013
This is version 35 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info