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Q1RHL6

- FUMC_RICBR

UniProt

Q1RHL6 - FUMC_RICBR

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Protein

Fumarate hydratase class II

Gene

fumC

Organism
Rickettsia bellii (strain RML369-C)
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

Catalytic activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei188 – 1881Proton donor/acceptorBy similarity
Active sitei318 – 3181By similarity
Binding sitei319 – 3191SubstrateUniRule annotation
Sitei331 – 3311Important for catalytic activityBy 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

BioCyciRBEL336407:GJCY-1099-MONOMER.
UniPathwayiUPA00223; UER01007.

Names & Taxonomyi

Protein namesi
Recommended name:
Fumarate hydratase class IIUniRule annotation (EC:4.2.1.2UniRule annotation)
Short name:
Fumarase CUniRule annotation
Gene namesi
Name:fumCUniRule annotation
Ordered Locus Names:RBE_1067
OrganismiRickettsia bellii (strain RML369-C)
Taxonomic identifieri336407 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRickettsialesRickettsiaceaeRickettsieaeRickettsiabelli group
ProteomesiUP000001951: Chromosome

Subcellular locationi

Cytoplasm 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 – 463463Fumarate hydratase class IIPRO_0000277938Add
BLAST

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Protein-protein interaction databases

STRINGi336407.RBE_1067.

Structurei

3D structure databases

ProteinModelPortaliQ1RHL6.
SMRiQ1RHL6. Positions 3-460.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni98 – 1003Substrate bindingUniRule annotation
Regioni129 – 1324B siteUniRule annotation
Regioni139 – 1413Substrate bindingUniRule annotation
Regioni187 – 1882Substrate bindingUniRule annotation
Regioni324 – 3263Substrate bindingUniRule annotation

Sequence similaritiesi

Belongs to the class-II fumarase/aspartase family. Fumarase subfamily.UniRule annotation

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.

Q1RHL6 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTNYRTESDS FGEIQIEDKF YWGAQTQRSL ENFKIGKQRM PEILIRSLAI
60 70 80 90 100
LKKCAAKVNL EFGDLEPKIA ESIDKATSRI LNAEFSDNFP LVVWQTGSGT
110 120 130 140 150
QTNMNMNEVI ASIANEELTG MKGGKSPVHP NDHVNKGQSS NDSFPTAMHI
160 170 180 190 200
ATVLATREKL IPALNNLLTA LQNKSKDWDS IIKIGRTHLQ DATPLTLKQE
210 220 230 240 250
FSGYITQIEY ALERIEDALK KVYLLAQGGT AVGTGINSRK GFDIKFAEEV
260 270 280 290 300
AEFTKQPFKT APNKFESLAA HDALVEFSGT LNTIAVSLMK IANDIRLLGS
310 320 330 340 350
GPRCGLGELH LPENEPGSSI MPGKVNPTQV EALTMVCTQV MGNHVTVTIA
360 370 380 390 400
GSNGHLELNV FKPVIIYNIL QSIELLSDAA NSFVTHCVDG IEPNITHIND
410 420 430 440 450
LRDKSLMLVT ALNPHIGYDN AAKIAKEAHK HGITLKEAAK KLNLLSEEEF
460
NKIVVPEKMV RQS
Length:463
Mass (Da):50,903
Last modified:May 16, 2006 - v1
Checksum:i13988722F6B3A0BC
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000087 Genomic DNA. Translation: ABE05148.1.
RefSeqiYP_538237.1. NC_007940.1.

Genome annotation databases

EnsemblBacteriaiABE05148; ABE05148; RBE_1067.
GeneIDi3995904.
KEGGirbe:RBE_1067.
PATRICi17883701. VBIRicBel102610_1204.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000087 Genomic DNA. Translation: ABE05148.1 .
RefSeqi YP_538237.1. NC_007940.1.

3D structure databases

ProteinModelPortali Q1RHL6.
SMRi Q1RHL6. Positions 3-460.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 336407.RBE_1067.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABE05148 ; ABE05148 ; RBE_1067 .
GeneIDi 3995904.
KEGGi rbe:RBE_1067.
PATRICi 17883701. VBIRicBel102610_1204.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00223 ; UER01007 .
BioCyci RBEL336407:GJCY-1099-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

  1. "Genome sequence of Rickettsia bellii illuminates the role of amoebae in gene exchanges between intracellular pathogens."
    Ogata H., La Scola B., Audic S., Renesto P., Blanc G., Robert C., Fournier P.-E., Claverie J.-M., Raoult D.
    PLoS Genet. 2:733-744(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: RML369-C.

Entry informationi

Entry nameiFUMC_RICBR
AccessioniPrimary (citable) accession number: Q1RHL6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 20, 2007
Last sequence update: May 16, 2006
Last modified: October 1, 2014
This is version 59 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).By similarity

Keywords - Technical termi

Allosteric enzyme, Complete proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. Rickettsia bellii strain RML369-C
    Rickettsia bellii (strain RML369-C): entries and gene names
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3