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Q8F9L0

- FUMC_LEPIN

UniProt

Q8F9L0 - FUMC_LEPIN

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Protein

Fumarate hydratase class II

Gene
fumC, fum, LA_0185
Organism
Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain 56601)
Status
Reviewed - Annotation score: 3 out of 5 - Protein inferred from homologyi

Functioni

Catalyzes the reversible addition of water to fumarate to give L-malate By similarity.UniRule annotation

Catalytic activityi

(S)-malate = fumarate + H2O.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei187 – 1871Proton donor/acceptor By similarity
Active sitei317 – 3171 By similarity
Binding sitei318 – 3181Substrate By similarity
Sitei330 – 3301Important for catalytic activity By similarity

GO - Molecular functioni

  1. fumarate hydratase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. fumarate metabolic process Source: InterPro
  2. tricarboxylic acid cycle Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Tricarboxylic acid cycle

Enzyme and pathway databases

BioCyciLINT189518:GJBB-158-MONOMER.
UniPathwayiUPA00223; UER01007.

Names & Taxonomyi

Protein namesi
Recommended name:
Fumarate hydratase class II (EC:4.2.1.2)
Short name:
Fumarase C
Gene namesi
Name:fumC
Synonyms:fum
Ordered Locus Names:LA_0185
OrganismiLeptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain 56601)
Taxonomic identifieri189518 [NCBI]
Taxonomic lineageiBacteriaSpirochaetesSpirochaetalesLeptospiraceaeLeptospira
ProteomesiUP000001408: Chromosome I

Subcellular locationi

Cytoplasm By similarity UniRule annotation

GO - Cellular componenti

  1. tricarboxylic acid cycle enzyme complex Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 464464Fumarate hydratase class IIUniRule annotationPRO_0000161283Add
BLAST

Proteomic databases

PaxDbiQ8F9L0.

Interactioni

Subunit structurei

Homotetramer By similarity.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliQ8F9L0.
SMRiQ8F9L0. Positions 4-459.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni97 – 993Substrate binding By similarity
Regioni128 – 1314B site By similarity
Regioni138 – 1403Substrate binding By similarity
Regioni186 – 1872Substrate binding By similarity
Regioni323 – 3253Substrate binding By similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0114.
HOGENOMiHOG000061736.
KOiK01679.
OMAiMESFNIH.
OrthoDBiEOG6V1M4M.

Family and domain databases

Gene3Di1.10.275.10. 1 hit.
HAMAPiMF_00743. FumaraseC.
InterProiIPR005677. 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]
PANTHERiPTHR11444. PTHR11444. 1 hit.
PfamiPF10415. FumaraseC_C. 1 hit.
PF00206. Lyase_1. 1 hit.
[Graphical view]
PRINTSiPR00149. FUMRATELYASE.
SUPFAMiSSF48557. SSF48557. 1 hit.
TIGRFAMsiTIGR00979. fumC_II. 1 hit.
PROSITEiPS00163. FUMARATE_LYASES. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8F9L0-1 [UniParc]FASTAAdd to Basket

« Hide

MKTRIETDSM GEIAVDDSKY WGAQTERSLH HFHIGNDRFP REMIRALGIL    50
KKSAAVVNAE LGLLSEDKKK LIVQAADEVI SGKLDEHFPL SVWQTGSGTQ 100
TNMNSNEVIS NRAIEIAGGV KGSKKPIHPN DDVNKAQSSN DTFPTAMHIA 150
AAEQLNQKLI PALIQLKETF KKKTDEFQNI IKIGRTHLQD ATPLTLGQEF 200
SGYVQQLEYN IARVKAVLPS VYRLALGGTA VGTGLNTHPQ FAVKAAAQIA 250
KETGLPFVSA ENKFEALAAH DSLVETSGVL KTIAASLMKI ANDIRWLSSG 300
PRCGIGEISI PENEPGSSIM PGKVNPTQSE QMTMVAAQVI ANDVAVNIGG 350
ASGNFELNVF KPLIIHNVLN SIRLLSDSCV SFEEHCARGI IPNKEKLNEH 400
LNNSLMLVTA LNPHIGYDNA AKIAKNAHKK GTTLKESGIE LGLLTSEQFD 450
QWVLPEKMIH PSVD 464
Length:464
Mass (Da):50,397
Last modified:March 1, 2003 - v1
Checksum:iAE316E36BAB02FA8
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE010300 Genomic DNA. Translation: AAN47384.1.
AB010203 Genomic DNA. Translation: BAA24376.1.
PIRiT00129.
RefSeqiNP_710366.1. NC_004342.2.

Genome annotation databases

EnsemblBacteriaiAAN47384; AAN47384; LA_0185.
GeneIDi1149528.
KEGGilil:LA_0185.
PATRICi22381209. VBILepInt91350_0184.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE010300 Genomic DNA. Translation: AAN47384.1 .
AB010203 Genomic DNA. Translation: BAA24376.1 .
PIRi T00129.
RefSeqi NP_710366.1. NC_004342.2.

3D structure databases

ProteinModelPortali Q8F9L0.
SMRi Q8F9L0. Positions 4-459.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PaxDbi Q8F9L0.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAN47384 ; AAN47384 ; LA_0185 .
GeneIDi 1149528.
KEGGi lil:LA_0185.
PATRICi 22381209. VBILepInt91350_0184.

Phylogenomic databases

eggNOGi COG0114.
HOGENOMi HOG000061736.
KOi K01679.
OMAi MESFNIH.
OrthoDBi EOG6V1M4M.

Enzyme and pathway databases

UniPathwayi UPA00223 ; UER01007 .
BioCyci LINT189518:GJBB-158-MONOMER.

Family and domain databases

Gene3Di 1.10.275.10. 1 hit.
HAMAPi MF_00743. FumaraseC.
InterProi IPR005677. 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 ]
PANTHERi PTHR11444. PTHR11444. 1 hit.
Pfami PF10415. FumaraseC_C. 1 hit.
PF00206. Lyase_1. 1 hit.
[Graphical view ]
PRINTSi PR00149. FUMRATELYASE.
SUPFAMi SSF48557. SSF48557. 1 hit.
TIGRFAMsi TIGR00979. fumC_II. 1 hit.
PROSITEi PS00163. FUMARATE_LYASES. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. 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.

Entry informationi

Entry nameiFUMC_LEPIN
AccessioniPrimary (citable) accession number: Q8F9L0
Secondary accession number(s): O50640
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: March 1, 2003
Last modified: May 14, 2014
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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.

Keywords - Technical termi

Allosteric enzyme, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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