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)

Q7VA47

- FUMC_PROMA

UniProt

Q7VA47 - FUMC_PROMA

Protein

Fumarate hydratase class II

Gene

fumC

Organism
Prochlorococcus marinus (strain SARG / CCMP1375 / SS120)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 70 (01 Oct 2014)
      Sequence version 1 (01 Oct 2003)
      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 sitei189 – 1891Proton donor/acceptorBy similarity
    Active sitei319 – 3191By similarity
    Binding sitei320 – 3201SubstrateUniRule annotation
    Sitei332 – 3321Important 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

    BioCyciPMAR167539:GJN2-1656-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:Pro_1620
    OrganismiProchlorococcus marinus (strain SARG / CCMP1375 / SS120)
    Taxonomic identifieri167539 [NCBI]
    Taxonomic lineageiBacteriaCyanobacteriaProchloralesProchlorococcaceaeProchlorococcus
    ProteomesiUP000001420: 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 – 465465Fumarate hydratase class IIPRO_0000161296Add
    BLAST

    Interactioni

    Subunit structurei

    Homotetramer.UniRule annotation

    Protein-protein interaction databases

    STRINGi167539.Pro1620.

    Structurei

    3D structure databases

    ProteinModelPortaliQ7VA47.
    SMRiQ7VA47. Positions 4-462.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni99 – 1013Substrate bindingUniRule annotation
    Regioni130 – 1334B siteUniRule annotation
    Regioni140 – 1423Substrate bindingUniRule annotation
    Regioni188 – 1892Substrate bindingUniRule annotation
    Regioni325 – 3273Substrate bindingUniRule annotation

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0114.
    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.
    PROSITEiPS00163. FUMARATE_LYASES. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q7VA47-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAQSFRIEND SMGTIKVPDQ ALWGAQTQRS LINFAIGHNK MPMKLIYSIV    50
    QIKASAAIVN CRLGVLDKQR KNFILNACNE ISNGMHDEQF PLSVWQTGSG 100
    TQTNMNVNEV ISNIASHLNG NKLGSHEPLH PNDHVNRSQS TNDVFPAAIQ 150
    IATVQEILEN LLPELDQLIE TFDKKIIKWN RIIKTGRTHL QDAVPLTLGQ 200
    EASAWKEQLI ASRNRLNKSL NELYPLPLGG TAIGTGLNAP AKFDKEIALE 250
    IAKSTRSPFV SAQNKFAIMA SHDALVHTMS QLKLLAVSLF KIVNDLRLLS 300
    CGPRGGLGEL RLPENEPGSS IMPGKVNPTQ CEAMAMVCTQ IMALDSAVTM 350
    AGSGGHLQMN SYKPLIAFNL LESIDLLSSA CKSSRILMIE GIEPNLEKIQ 400
    NSLQNSLMLI TSLTPIIGYE KASKIAQCAH EKDITLKEAT KLLGYLNEDD 450
    FDRIVNPQSM TGMEN 465
    Length:465
    Mass (Da):51,045
    Last modified:October 1, 2003 - v1
    Checksum:iF2F17242168FDA54
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE017126 Genomic DNA. Translation: AAQ00664.1.
    RefSeqiNP_876011.1. NC_005042.1.

    Genome annotation databases

    EnsemblBacteriaiAAQ00664; AAQ00664; Pro_1620.
    GeneIDi1463002.
    KEGGipma:Pro_1620.
    PATRICi23030061. VBIProMar8617_1712.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE017126 Genomic DNA. Translation: AAQ00664.1 .
    RefSeqi NP_876011.1. NC_005042.1.

    3D structure databases

    ProteinModelPortali Q7VA47.
    SMRi Q7VA47. Positions 4-462.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 167539.Pro1620.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAQ00664 ; AAQ00664 ; Pro_1620 .
    GeneIDi 1463002.
    KEGGi pma:Pro_1620.
    PATRICi 23030061. VBIProMar8617_1712.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00223 ; UER01007 .
    BioCyci PMAR167539:GJN2-1656-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.
    PROSITEi PS00163. FUMARATE_LYASES. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: SARG / CCMP1375 / SS120.

    Entry informationi

    Entry nameiFUMC_PROMA
    AccessioniPrimary (citable) accession number: Q7VA47
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 2003
    Last sequence update: October 1, 2003
    Last modified: October 1, 2014
    This is version 70 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