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Q8F9L0 (FUMC_LEPIN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 60. 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
Synonyms:fum
Ordered Locus Names:LA_0185
OrganismLeptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain 56601)
Taxonomic identifier189518 [NCBI]
Taxonomic lineageBacteriaSpirochaetesSpirochaetalesLeptospiraceaeLeptospira

Protein attributes

Sequence length464 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

(S)-malate = fumarate + H2O. HAMAP MF_00743

Pathway

Carbohydrate metabolism; tricarboxylic acid cycle; (S)-malate from fumarate: step 1/1. HAMAP MF_00743

Subunit structure

Homotetramer By similarity. HAMAP MF_00743

Subcellular location

Cytoplasm By similarity HAMAP 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 MF_00743

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
Reference proteome
Gene Ontology (GO)
   Biological processfumarate metabolic process

Inferred from electronic annotation. Source: InterPro

tricarboxylic acid cycle

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componenttricarboxylic acid cycle enzyme complex

Inferred from electronic annotation. Source: InterPro

   Molecular functionfumarate hydratase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 464464Fumarate hydratase class II HAMAP MF_00743
PRO_0000161283

Regions

Region128 – 1314B site By similarity
Region138 – 1403Substrate binding By similarity

Sites

Binding site991Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8F9L0 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: AE316E36BAB02FA8

FASTA46450,397
        10         20         30         40         50         60 
MKTRIETDSM GEIAVDDSKY WGAQTERSLH HFHIGNDRFP REMIRALGIL KKSAAVVNAE 

        70         80         90        100        110        120 
LGLLSEDKKK LIVQAADEVI SGKLDEHFPL SVWQTGSGTQ TNMNSNEVIS NRAIEIAGGV 

       130        140        150        160        170        180 
KGSKKPIHPN DDVNKAQSSN DTFPTAMHIA AAEQLNQKLI PALIQLKETF KKKTDEFQNI 

       190        200        210        220        230        240 
IKIGRTHLQD ATPLTLGQEF SGYVQQLEYN IARVKAVLPS VYRLALGGTA VGTGLNTHPQ 

       250        260        270        280        290        300 
FAVKAAAQIA KETGLPFVSA ENKFEALAAH DSLVETSGVL KTIAASLMKI ANDIRWLSSG 

       310        320        330        340        350        360 
PRCGIGEISI PENEPGSSIM PGKVNPTQSE QMTMVAAQVI ANDVAVNIGG ASGNFELNVF 

       370        380        390        400        410        420 
KPLIIHNVLN SIRLLSDSCV SFEEHCARGI IPNKEKLNEH LNNSLMLVTA LNPHIGYDNA 

       430        440        450        460 
AKIAKNAHKK GTTLKESGIE LGLLTSEQFD QWVLPEKMIH PSVD 

« Hide

References

« Hide 'large scale' references
[1]"Unique physiological and pathogenic features of Leptospira interrogans revealed by whole-genome sequencing."
Ren S.-X., Fu G., Jiang X.-G., Zeng R., Miao Y.-G., Xu H., Zhang Y.-X., Xiong H., Lu G., Lu L.-F., Jiang H.-Q., Jia J., Tu Y.-F., Jiang J.-X., Gu W.-Y., Zhang Y.-Q., Cai Z., Sheng H.-H. expand/collapse author list , Yin H.-F., Zhang Y., Zhu G.-F., Wan M., Huang H.-L., Qian Z., Wang S.-Y., Ma W., Yao Z.-J., Shen Y., Qiang B.-Q., Xia Q.-C., Guo X.-K., Danchin A., Saint Girons I., Somerville R.L., Wen Y.-M., Shi M.-H., Chen Z., Xu J.-G., Zhao G.-P.
Nature 422:888-893(2003) [PubMed: 12712204] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 56601.
[2]"Physical and genetic maps of the Leptospira interrogans serovar icterohaemorrhagiae strain Ictero No.1 chromosome and sequencing of a 19-kb region of the genome containing the 5S rRNA gene."
Takahashi Y., Akase K., Hirano H., Fukunaga M.
Gene 215:37-45(1998) [PubMed: 9666070] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-459.
Strain: Ictero No.1 / Serogroup Icterohaemorrhagiae.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE010300 Genomic DNA. Translation: AAN47384.1.
AB010203 Genomic DNA. Translation: BAA24376.1.
PIRT00129.
RefSeqNP_710366.1. NC_004342.2.

3D structure databases

ProteinModelPortalQ8F9L0.
SMRQ8F9L0. Positions 4-459.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1149528.
GenomeReviewsGene locus LA_0185 in contig AE010300_GR.
KEGGlil:LA_0185.
PATRIC22381209. VBILepInt91350_0184.

Phylogenomic databases

HOGENOMHBG284369.
OMARIEKDTM.
PhylomeDBQ8F9L0.
ProtClustDBPRK00485.

Enzyme and pathway databases

BioCycLINT-130-01:LINT-130-01-000154-MONOMER.
LINT189518:LA0185-MONOMER.

Family and domain databases

HAMAPMF_00743. FumaraseC.
[Tree]
InterProIPR003031. D_crystallin.
IPR005677. Fum_hydII.
IPR018951. Fumarase_C_C.
IPR000362. Fumarate_lyase.
IPR020557. Fumarate_lyase_CS.
IPR008948. L-Aspartase-like.
IPR024083. L-Aspartase-like_N.
IPR022761. Lyase1_N.
[Graphical view]
Gene3DG3DSA:1.10.275.10. G3DSA:1.10.275.10. 1 hit.
KOK01679.
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 nameFUMC_LEPIN
AccessionPrimary (citable) accession number: Q8F9L0
Secondary accession number(s): O50640
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: March 1, 2003
Last modified: January 25, 2012
This is version 60 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