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)

Q55674

- FUMC_SYNY3

UniProt

Q55674 - FUMC_SYNY3

Protein

Fumarate hydratase class II

Gene

fumC

Organism
Synechocystis sp. (strain PCC 6803 / Kazusa)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 98 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      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

    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:slr0018
    OrganismiSynechocystis sp. (strain PCC 6803 / Kazusa)
    Taxonomic identifieri1111708 [NCBI]
    Taxonomic lineageiBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechocystis
    ProteomesiUP000001425: 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 – 466466Fumarate hydratase class IIPRO_0000161325Add
    BLAST

    Proteomic databases

    PaxDbiQ55674.

    Interactioni

    Subunit structurei

    Homotetramer.UniRule annotation

    Protein-protein interaction databases

    IntActiQ55674. 1 interaction.
    STRINGi1148.slr0018.

    Structurei

    3D structure databases

    ProteinModelPortaliQ55674.
    SMRiQ55674. Positions 6-461.
    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.
    HOGENOMiHOG000061736.
    KOiK01679.
    OMAiAARHMKL.
    OrthoDBiEOG6V1M4M.
    PhylomeDBiQ55674.

    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.

    Q55674-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVNSHRLETD SMGSLEVQAD RLWGAQTQRS LMFFDIGSDV MPPDLIRAFA    50
    ILKKAAAITN QDLGKLPADK AELIITAADE IIAGQWLDHF PLRIWQTGSG 100
    TQTNMNVNEV IANRAIAICG GELGSKNPIH PNDHVNMSQS SNDTFPTAMH 150
    IAAVAGLQTK LIPSLQALRD SLNEKAECFA GITKIGRTHL MDAVPLTLGQ 200
    EFSGYVAQLD QGLTQINYCL PGLLELALGG TAVGTGLNSH PQFAKKVAEE 250
    IAQLTGYTFI SAPNKFAALA GHEAIAFASG VLKSIAASLM KIANDLRWMG 300
    SGPRCGLGEL ALPANEPGSS IMPGKVNPTQ CEAMTMVCVQ VMGNDATIGF 350
    AASQGNFELN VFKPVIIHNF LHSLHLLSDA CASFRQHLVV GLQVNESKVK 400
    DFLDTSLMLV TALNPHIGYD NAALVAKTAF AQGITLKQAA VDLGLLTPAQ 450
    FDAWVVPEQM IAPIAD 466
    Length:466
    Mass (Da):49,687
    Last modified:November 1, 1996 - v1
    Checksum:i7C46A68EA26233C7
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BA000022 Genomic DNA. Translation: BAA10200.1.
    PIRiS76348.
    RefSeqiNP_442130.1. NC_000911.1.
    YP_005652188.1. NC_017277.1.
    YP_007452007.1. NC_020286.1.

    Genome annotation databases

    EnsemblBacteriaiBAA10200; BAA10200; BAA10200.
    GeneIDi952663.
    KEGGisyn:slr0018.
    syy:SYNGTS_2235.
    syz:MYO_122590.
    PATRICi23841868. VBISynSp132158_2478.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BA000022 Genomic DNA. Translation: BAA10200.1 .
    PIRi S76348.
    RefSeqi NP_442130.1. NC_000911.1.
    YP_005652188.1. NC_017277.1.
    YP_007452007.1. NC_020286.1.

    3D structure databases

    ProteinModelPortali Q55674.
    SMRi Q55674. Positions 6-461.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q55674. 1 interaction.
    STRINGi 1148.slr0018.

    Proteomic databases

    PaxDbi Q55674.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai BAA10200 ; BAA10200 ; BAA10200 .
    GeneIDi 952663.
    KEGGi syn:slr0018.
    syy:SYNGTS_2235.
    syz:MYO_122590.
    PATRICi 23841868. VBISynSp132158_2478.

    Phylogenomic databases

    eggNOGi COG0114.
    HOGENOMi HOG000061736.
    KOi K01679.
    OMAi AARHMKL.
    OrthoDBi EOG6V1M4M.
    PhylomeDBi Q55674.

    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. "Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. I. Sequence features in the 1 Mb region from map positions 64% to 92% of the genome."
      Kaneko T., Tanaka A., Sato S., Kotani H., Sazuka T., Miyajima N., Sugiura M., Tabata S.
      DNA Res. 2:153-166(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 27184 / PCC 6803 / N-1.
    2. "Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions."
      Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y., Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T., Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.
      , Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
      DNA Res. 3:109-136(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: PCC 6803 / Kazusa.

    Entry informationi

    Entry nameiFUMC_SYNY3
    AccessioniPrimary (citable) accession number: Q55674
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 2003
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 98 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
    3. Synechocystis PCC 6803
      Synechocystis (strain PCC 6803): entries and gene names

    External Data

    Dasty 3