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)

Q8NRN8

- FUMC_CORGL

UniProt

Q8NRN8 - FUMC_CORGL

Protein

Fumarate hydratase class II

Gene

fumC

Organism
Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 77 (01 Oct 2014)
      Sequence version 1 (01 Oct 2002)
      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 sitei187 – 1871Proton 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

    BRENDAi4.2.1.2. 1648.
    SABIO-RKQ8NRN8.
    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
    Synonyms:fum
    Ordered Locus Names:Cgl1010, cg1145
    OrganismiCorynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025)
    Taxonomic identifieri196627 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium
    ProteomesiUP000000582: Chromosome, UP000001009: 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 – 473473Fumarate hydratase class IIPRO_0000161272Add
    BLAST

    2D gel databases

    World-2DPAGE0001:Q8NRN8.

    Interactioni

    Subunit structurei

    Homotetramer.UniRule annotation

    Protein-protein interaction databases

    STRINGi196627.cg1145.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8NRN8.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni104 – 1063Substrate bindingUniRule annotation
    Regioni128 – 1314B siteUniRule annotation
    Regioni138 – 1403Substrate bindingUniRule annotation
    Regioni186 – 1872Substrate bindingUniRule annotation
    Regioni324 – 3263Substrate bindingUniRule annotation

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0114.
    HOGENOMiHOG000061737.
    KOiK01679.
    OMAiENYRIES.
    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.
    PROSITEiPS00163. FUMARATE_LYASES. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q8NRN8-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSDFMTEQEF RIEHDTMGEV KVPAKALWQA QTQRAVENFP ISGRGLESAQ    50
    IRAMGLLKAA CAQVNKDSGA LDAEKADAII AAGKEIASGK HDAEFPIDVF 100
    QTGSGTSSNM NTNEVIASIA KANGVEVHPN DHVNMGQSSN DTFPTATHVA 150
    ATEAAVNDLI PGLKVLHESL AKKANEWSEV VKSGRTHLMD AVPVTLGQEF 200
    GGYARQIQLG IERVEATLPR LGELAIGGTA AGTGINTSAD FGGKVVAELI 250
    NLTDVKELKE AENHFEAQAA RDALVEFSGA MRVIAVSLYK IANDIRLMGS 300
    GPLTGLGEIR LPDLQPGSSI MPGKVNPVLC ETATQVSAQV IGNDAAVAFS 350
    GTQGQFELNV FIPVMARNVL ESARLLANTS RVFATRLVDG IEPNEAHMKE 400
    LAESSPSIVT PLNSAIGYEA AAKVAKTALA EGKTIRQTVI DLGLVDGEKL 450
    TEEELDKRLD VLAMAHTERE NKF 473
    Length:473
    Mass (Da):50,244
    Last modified:October 1, 2002 - v1
    Checksum:i315AF884777A39F0
    GO

    Sequence cautioni

    The sequence CAF19712.1 differs from that shown. Reason: Erroneous initiation.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BA000036 Genomic DNA. Translation: BAB98403.1.
    BX927151 Genomic DNA. Translation: CAF19712.1. Different initiation.
    RefSeqiNP_600233.1. NC_003450.3.
    YP_225298.1. NC_006958.1.

    Genome annotation databases

    EnsemblBacteriaiBAB98403; BAB98403; BAB98403.
    CAF19712; CAF19712; cg1145.
    GeneIDi1018996.
    KEGGicgb:cg1145.
    cgl:NCgl0967.
    PATRICi21494066. VBICorGlu203724_0990.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BA000036 Genomic DNA. Translation: BAB98403.1 .
    BX927151 Genomic DNA. Translation: CAF19712.1 . Different initiation.
    RefSeqi NP_600233.1. NC_003450.3.
    YP_225298.1. NC_006958.1.

    3D structure databases

    ProteinModelPortali Q8NRN8.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 196627.cg1145.

    2D gel databases

    World-2DPAGE 0001:Q8NRN8.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai BAB98403 ; BAB98403 ; BAB98403 .
    CAF19712 ; CAF19712 ; cg1145 .
    GeneIDi 1018996.
    KEGGi cgb:cg1145.
    cgl:NCgl0967.
    PATRICi 21494066. VBICorGlu203724_0990.

    Phylogenomic databases

    eggNOGi COG0114.
    HOGENOMi HOG000061737.
    KOi K01679.
    OMAi ENYRIES.
    OrthoDBi EOG6V1M4M.

    Enzyme and pathway databases

    UniPathwayi UPA00223 ; UER01007 .
    BRENDAi 4.2.1.2. 1648.
    SABIO-RK Q8NRN8.

    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.
    PROSITEi PS00163. FUMARATE_LYASES. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The Corynebacterium glutamicum genome: features and impacts on biotechnological processes."
      Ikeda M., Nakagawa S.
      Appl. Microbiol. Biotechnol. 62:99-109(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.

    Entry informationi

    Entry nameiFUMC_CORGL
    AccessioniPrimary (citable) accession number: Q8NRN8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 2003
    Last sequence update: October 1, 2002
    Last modified: October 1, 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.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