Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9ZCQ4

- FUMC_RICPR

UniProt

Q9ZCQ4 - FUMC_RICPR

Protein

Fumarate hydratase class II

Gene

fumC

Organism
Rickettsia prowazekii (strain Madrid E)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 83 (01 Oct 2014)
      Sequence version 1 (01 May 1999)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

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

    Catalytic activityi

    (S)-malate = fumarate + H2O.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei188 – 1881Proton donor/acceptorBy similarity
    Active sitei318 – 3181By similarity
    Binding sitei319 – 3191Substrate
    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

    Keywords - Molecular functioni

    Lyase

    Keywords - Biological processi

    Tricarboxylic acid cycle

    Enzyme and pathway databases

    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
    Ordered Locus Names:RP665
    OrganismiRickettsia prowazekii (strain Madrid E)
    Taxonomic identifieri272947 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRickettsialesRickettsiaceaeRickettsieaeRickettsiatyphus group
    ProteomesiUP000002480: Chromosome

    Subcellular locationi

    Cytoplasm By similarity

    GO - Cellular componenti

    1. tricarboxylic acid cycle enzyme complex Source: InterPro

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 461461Fumarate hydratase class IIPRO_0000161307Add
    BLAST

    Interactioni

    Subunit structurei

    Homotetramer.1 Publication

    Protein-protein interaction databases

    STRINGi272947.RP665.

    Structurei

    Secondary structure

    1
    461
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi4 – 96
    Beta strandi12 – 176
    Helixi24 – 329
    Helixi42 – 6120
    Helixi67 – 8216
    Turni83 – 875
    Beta strandi92 – 954
    Helixi100 – 11920
    Beta strandi124 – 1285
    Helixi130 – 1345
    Turni135 – 1373
    Helixi140 – 15819
    Helixi160 – 17516
    Helixi178 – 1803
    Beta strandi182 – 1876
    Beta strandi190 – 1967
    Helixi197 – 21923
    Turni220 – 2234
    Turni230 – 2323
    Helixi242 – 25413
    Helixi264 – 2696
    Helixi272 – 29827
    Beta strandi302 – 3054
    Beta strandi319 – 3213
    Helixi328 – 35124
    Helixi362 – 38625
    Turni387 – 3904
    Helixi395 – 40410
    Helixi406 – 4083
    Helixi409 – 4168
    Helixi418 – 43114
    Helixi435 – 4417
    Helixi447 – 4548

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3GTDX-ray2.40A/B1-461[»]
    ProteinModelPortaliQ9ZCQ4.
    SMRiQ9ZCQ4. Positions 4-460.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9ZCQ4.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni98 – 1003Substrate binding
    Regioni129 – 1324B siteBy similarity
    Regioni139 – 1413Substrate bindingCurated
    Regioni187 – 1882Substrate bindingBy similarity
    Regioni324 – 3263Substrate binding

    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.

    Q9ZCQ4-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKNYRIESDS FGEIQIEEKF YWGAQTQRSL NNFKISKQKM PKILIRALAI    50
    LKKCAAQVNY EFGDLEYKIA TSIDKAIDRI LAGEFEDNFP LVVWQTGSGT 100
    QTNMNMNEVI ASIANEELTG KKGGKFPVHP NDHVNKGQSS NDSFPTAMHI 150
    ATVLATKQQL IPALNNLLTY LQDKSKDWDK IIKIGRTHLQ DATPLTLKQE 200
    FSGYITQIEY ALERIEDALK KVYLLAQGGT AVGTGINSKI GFDIKFAQKV 250
    AEFTQQPFKT APNKFESLAA HDALVEFSGT LNTIAVSLMK IANDIRLLGS 300
    GPRCGLGELH LPENEPGSSI MPGKVNPTQV EALTMVCTQV MGNHVTVTIA 350
    GSNGHLELNV FKPVIIYNIL QSIELLSDSV NSFVTHCVKG LEPNIARINT 400
    LRDKSLMLVT VLNPHIGYDN AAKIAKEAHK YGITLKEAAK KLNFLSEEEF 450
    DKIVVPEKMI S 461
    Length:461
    Mass (Da):51,008
    Last modified:May 1, 1999 - v1
    Checksum:iC9929CC94E7E617D
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ235272 Genomic DNA. Translation: CAA15103.1.
    PIRiE71672.
    RefSeqiNP_221027.1. NC_000963.1.

    Genome annotation databases

    EnsemblBacteriaiCAA15103; CAA15103; CAA15103.
    GeneIDi883633.
    KEGGirpr:RP665.
    PATRICi17902157. VBIRicPro72556_0685.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ235272 Genomic DNA. Translation: CAA15103.1 .
    PIRi E71672.
    RefSeqi NP_221027.1. NC_000963.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3GTD X-ray 2.40 A/B 1-461 [» ]
    ProteinModelPortali Q9ZCQ4.
    SMRi Q9ZCQ4. Positions 4-460.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 272947.RP665.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAA15103 ; CAA15103 ; CAA15103 .
    GeneIDi 883633.
    KEGGi rpr:RP665.
    PATRICi 17902157. VBIRicPro72556_0685.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00223 ; UER01007 .

    Miscellaneous databases

    EvolutionaryTracei Q9ZCQ4.

    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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Madrid E.
    2. "Structure of fumarate hydratase from Rickettsia prowazekii, the agent of typhus and suspected relative of the mitochondria."
      Phan I., Subramanian S., Olsen C., Edwards T.E., Guo W., Zhang Y., Van Voorhis W.C., Stewart L.J., Myler P.J.
      Acta Crystallogr. F 67:1123-1128(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS, SUBUNIT.

    Entry informationi

    Entry nameiFUMC_RICPR
    AccessioniPrimary (citable) accession number: Q9ZCQ4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 2003
    Last sequence update: May 1, 1999
    Last modified: October 1, 2014
    This is version 83 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

    3D-structure, Allosteric enzyme, Complete proteome, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. Rickettsia prowazekii
      Rickettsia prowazekii (strain Madrid E): entries and gene names
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3