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Q8F9L0 (FUMC_LEPIN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 72. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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) [Reference proteome] [HAMAP]
Taxonomic identifier189518 [NCBI]
Taxonomic lineageBacteria › Spirochaetes › Spirochaetales › Leptospiraceae › Leptospira ›

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.

Subcellular location

Cytoplasm By similarity.

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.

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: 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 – 464464Fumarate hydratase class II HAMAP-Rule MF_00743
PRO_0000161283

Regions

Region97 – 993Substrate binding By similarity
Region128 – 1314B site By similarity
Region138 – 1403Substrate binding By similarity
Region186 – 1872Substrate binding By similarity
Region323 – 3253Substrate binding By similarity

Sites

Active site1871Proton donor/acceptor By similarity
Active site3171 By similarity
Binding site3181Substrate By similarity
Site3301Important for catalytic activity 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] [Europe PMC] [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] [Europe PMC] [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...

Proteomic databases

PaxDbQ8F9L0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAN47384; AAN47384; LA_0185.
GeneID1149528.
KEGGlil:LA_0185.
PATRIC22381209. VBILepInt91350_0184.

Phylogenomic databases

eggNOGCOG0114.
HOGENOMHOG000061736.
KOK01679.
OMAKDTMGEV.
ProtClustDBPRK00485.

Enzyme and pathway databases

BioCycLINT189518:GJBB-158-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 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: May 1, 2013
This is version 72 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

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