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)

P71384

- FUMC_HAEIN

UniProt

P71384 - FUMC_HAEIN

Protein

Fumarate hydratase class II

Gene

fumC

Organism
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 104 (01 Oct 2014)
      Sequence version 1 (01 Feb 1997)
      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.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

    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 IIUniRule annotation (EC:4.2.1.2UniRule annotation)
    Short name:
    Fumarase CUniRule annotation
    Gene namesi
    Name:fumCUniRule annotation
    Ordered Locus Names:HI_1398
    OrganismiHaemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
    Taxonomic identifieri71421 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHaemophilus
    ProteomesiUP000000579: Chromosome

    Subcellular locationi

    Cytoplasm UniRule annotation

    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 – 464464Fumarate hydratase class IIPRO_0000161279Add
    BLAST

    Proteomic databases

    PRIDEiP71384.

    Interactioni

    Subunit structurei

    Homotetramer.UniRule annotation

    Protein-protein interaction databases

    STRINGi71421.HI1398.

    Structurei

    3D structure databases

    ProteinModelPortaliP71384.
    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.
    KOiK01679.
    OMAiNAHPEYH.
    OrthoDBiEOG6V1M4M.
    PhylomeDBiP71384.

    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.

    P71384-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAFRIEKDTM GEVQVLADKY WAAQTERSRN NFKIGPAASM PHEIIEAFGY    50
    LKKAAAFANH DLGVLPLEKR DLIALACDEI LANKLDDQFP LVIWQTGSGT 100
    QSNMNVNEVV ANRAHVLNGG KLGEKSIIHP NDDVNKSQSS NDTFPTAMHI 150
    AAYKKVVEHT IPCVERLQKT FAAKSEAFKN VVKIGRTHLM DATPLTLGQE 200
    FSAYAAQLDF GLKALKNTLP HLSQLALGGT AVGTGLNTPK GYDLKVVDYI 250
    AKFTALPFVT ADNKFEALAA HDAIVETHGA LRQLAMSLFK IANDIRLLAS 300
    GPRSGIGEIL IPENEPGSSI MPGKVNPTQC EXMTMVCAQV FGNDTTIAFV 350
    GSQGHFQLNV FNPVMIANFL QSAQLLGDAC VSFDEHCAVG IEPNYPRIKQ 400
    QLENSLMLVT ALNTHIGYEN AAKIAKTAHK NGTTLREEAI NLGLVSAEDF 450
    DKWVRPEDMV GSLK 464
    Length:464
    Mass (Da):50,482
    Last modified:February 1, 1997 - v1
    Checksum:iAC836336DA7457CE
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L42023 Genomic DNA. Translation: AAC23045.1.
    RefSeqiNP_439551.1. NC_000907.1.

    Genome annotation databases

    EnsemblBacteriaiAAC23045; AAC23045; HI_1398.
    GeneIDi950314.
    KEGGihin:HI1398.
    PATRICi20191495. VBIHaeInf48452_1458.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L42023 Genomic DNA. Translation: AAC23045.1 .
    RefSeqi NP_439551.1. NC_000907.1.

    3D structure databases

    ProteinModelPortali P71384.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 71421.HI1398.

    Proteomic databases

    PRIDEi P71384.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC23045 ; AAC23045 ; HI_1398 .
    GeneIDi 950314.
    KEGGi hin:HI1398.
    PATRICi 20191495. VBIHaeInf48452_1458.

    Phylogenomic databases

    eggNOGi COG0114.
    KOi K01679.
    OMAi NAHPEYH.
    OrthoDBi EOG6V1M4M.
    PhylomeDBi P71384.

    Enzyme and pathway databases

    UniPathwayi UPA00223 ; UER01007 .

    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: ATCC 51907 / DSM 11121 / KW20 / Rd.

    Entry informationi

    Entry nameiFUMC_HAEIN
    AccessioniPrimary (citable) accession number: P71384
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1999
    Last sequence update: February 1, 1997
    Last modified: October 1, 2014
    This is version 104 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, Reference proteome

    Documents

    1. Haemophilus influenzae
      Haemophilus influenzae (strain Rd): entries and gene names
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3