Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Malate synthase

Gene

aceB

Organism
Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the glyoxylate cycle which synthesizes precursors for carbohydrates from C2 compounds such as acetate. Catalyzes the Claisen condensation between acetyl-coenzyme A (acetyl-CoA) and glyoxylate to form the malyl-CoA intermediate that is subsequently hydrolyzed to produce malate and CoA.3 Publications

Catalytic activityi

Acetyl-CoA + H2O + glyoxylate = (S)-malate + CoA.1 Publication

Cofactori

Mg2+1 Publication

Kineticsi

AceB requires a high salt concentration for activity, the optimum being around 3.0 M KCl. Replacement of KCl by NaCl causes a decrease in activity (about 2-fold).

  1. KM=0.11 µM for glyoxylate (with 0.2 mM acetyl-CoA at pH 8 and 40 degrees Celsius)1 Publication
  2. KM=0.119 µM for acetyl-CoA (with 0.5 mM glyoxylate at pH 8 and 40 degrees Celsius)1 Publication

    pH dependencei

    Optimum pH is between 8 and 9.1 Publication

    Temperature dependencei

    Optimum temperature is between 45 and 65 degrees Celsius. The activity of the enzyme at 80 degrees Celsius is half of the maximum.1 Publication

    Pathwayi: glyoxylate cycle

    This protein is involved in step 2 of the subpathway that synthesizes (S)-malate from isocitrate.
    Proteins known to be involved in the 2 steps of the subpathway in this organism are:
    1. Isocitrate lyase (aceA)
    2. Malate synthase (aceB)
    This subpathway is part of the pathway glyoxylate cycle, which is itself part of Carbohydrate metabolism.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes (S)-malate from isocitrate, the pathway glyoxylate cycle and in Carbohydrate metabolism.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi52 – 521Magnesium1 Publication
    Binding sitei84 – 841Acetyl-CoA1 Publication
    Binding sitei84 – 841Glyoxylate1 Publication
    Metal bindingi158 – 1581Magnesium1 Publication
    Binding sitei158 – 1581Glyoxylate1 Publication
    Metal bindingi192 – 1921Magnesium1 Publication
    Binding sitei236 – 2361Acetyl-CoA
    Binding sitei259 – 2591Acetyl-CoA; via carbonyl oxygen
    Active sitei388 – 3881Proton acceptorSequence analysis

    GO - Molecular functioni

    • malate synthase activity Source: UniProtKB
    • metal ion binding Source: UniProtKB

    GO - Biological processi

    • glyoxylate cycle Source: UniProtKB
    • tricarboxylic acid cycle Source: UniProtKB-KW
    Complete GO annotation...

    Keywords - Molecular functioni

    Transferase

    Keywords - Biological processi

    Glyoxylate bypass, Tricarboxylic acid cycle

    Keywords - Ligandi

    Magnesium, Metal-binding

    Enzyme and pathway databases

    BioCyciHVOL309800:GCOK-1982-MONOMER.
    BRENDAi2.3.3.9. 2561.
    UniPathwayiUPA00703; UER00720.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Malate synthase (EC:2.3.3.9)
    Short name:
    MSH
    Gene namesi
    Name:aceB
    Synonyms:aceB1
    Ordered Locus Names:HVO_1983
    ORF Names:C498_05196
    OrganismiHaloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii)
    Taxonomic identifieri309800 [NCBI]
    Taxonomic lineageiArchaeaEuryarchaeotaHalobacteriaHaloferacalesHaloferacaceaeHaloferax
    Proteomesi
    • UP000011532 Componenti: Unassembled WGS sequence
    • UP000008243 Componenti: Chromosome

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 433433Malate synthasePRO_0000429586Add
    BLAST

    Interactioni

    Subunit structurei

    Homotrimer and homohexamer in equilibrium.3 Publications

    Protein-protein interaction databases

    STRINGi309800.HVO_1983.

    Structurei

    Secondary structure

    1
    433
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi13 – 197Combined sources
    Beta strandi23 – 253Combined sources
    Helixi29 – 368Combined sources
    Helixi39 – 413Combined sources
    Beta strandi44 – 518Combined sources
    Helixi56 – 583Combined sources
    Helixi59 – 7315Combined sources
    Helixi74 – 763Combined sources
    Beta strandi78 – 814Combined sources
    Helixi92 – 10514Combined sources
    Helixi108 – 1103Combined sources
    Helixi113 – 1153Combined sources
    Beta strandi118 – 1214Combined sources
    Helixi127 – 14317Combined sources
    Beta strandi151 – 1577Combined sources
    Helixi160 – 1656Combined sources
    Helixi166 – 1683Combined sources
    Helixi169 – 1746Combined sources
    Helixi180 – 1823Combined sources
    Beta strandi183 – 1886Combined sources
    Helixi190 – 1978Combined sources
    Helixi210 – 22314Combined sources
    Beta strandi226 – 2294Combined sources
    Helixi238 – 24912Combined sources
    Turni250 – 2523Combined sources
    Beta strandi255 – 2584Combined sources
    Helixi261 – 2699Combined sources
    Helixi329 – 3346Combined sources
    Helixi343 – 35816Combined sources
    Beta strandi364 – 3696Combined sources
    Beta strandi382 – 3876Combined sources
    Helixi389 – 3957Combined sources
    Helixi397 – 40812Combined sources
    Helixi410 – 4123Combined sources
    Helixi413 – 4208Combined sources
    Helixi422 – 4287Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3OYXX-ray2.51A1-433[»]
    3OYZX-ray1.95A1-433[»]
    3PUGX-ray2.70A1-433[»]
    ProteinModelPortaliD4GTL2.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni16 – 172Acetyl-CoA binding1 Publication
    Regioni191 – 1922Glyoxylate binding1 Publication

    Sequence similaritiesi

    Belongs to the HpcH/HpaI aldolase family.Curated

    Phylogenomic databases

    eggNOGiarCOG00760. Archaea.
    COG2301. LUCA.
    HOGENOMiHOG000094928.
    KOiK19282.
    OMAiEVDYTKD.

    Family and domain databases

    Gene3Di3.20.20.60. 1 hit.
    InterProiIPR005000. Aldolase/citrate-lyase_domain.
    IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
    [Graphical view]
    PfamiPF03328. HpcH_HpaI. 1 hit.
    [Graphical view]
    SUPFAMiSSF51621. SSF51621. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    D4GTL2-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MTERRHDREF VRTFFTSPTA VEGEDDSAKM LRRAAGLRGM QAPDVWVPDN
    60 70 80 90 100
    EDATAPSMRD EGAENIVEVI SEQGAEFPGE IHPRMVWHRD SPETRYQGFQ
    110 120 130 140 150
    HMLDITDPER GAVEHIHGFV IPEVGGIDDW KKADEFFTIV EHEHGLDEGS
    160 170 180 190 200
    LAMSVIIESG EAELAMGDLR DEMGKPTNNL ERLFLLVDGE VDYTKDMRAM
    210 220 230 240 250
    TPTGELPAWP ELRHNTSRGA SAAGCVAVDG PYDDIRDVEG YRERMTDNQA
    260 270 280 290 300
    KGMLGIWSLT PGQVVEANTS PLPPKTGSWL LDADGEEVEL ASEDGVEAYD
    310 320 330 340 350
    GDRLSLEATD GGYELRVGGD ARELTADELR EELLGLTSYV PSMDDIVDSM
    360 370 380 390 400
    EEFEAAKEAG RGAIAMTQSA TLRIGGTEID IEKDRMWDEA TYQAAMTPIS
    410 420 430
    LFQDVYENRP DQHEELEERY GAGVVERAME VGL
    Length:433
    Mass (Da):48,018
    Last modified:May 18, 2010 - v1
    Checksum:i67AAD93EF9E576D9
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti326 – 3261A → V in CAC48389 (PubMed:11513957).Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AJ250923 Genomic DNA. Translation: CAC48389.1.
    CP001956 Genomic DNA. Translation: ADE04727.1.
    AOHU01000038 Genomic DNA. Translation: ELY34497.1.
    RefSeqiWP_004041864.1. NZ_AOHU01000038.1.

    Genome annotation databases

    EnsemblBacteriaiADE04727; ADE04727; HVO_1983.
    ELY34497; ELY34497; C498_05196.
    GeneIDi8925725.
    KEGGihvo:HVO_1983.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AJ250923 Genomic DNA. Translation: CAC48389.1.
    CP001956 Genomic DNA. Translation: ADE04727.1.
    AOHU01000038 Genomic DNA. Translation: ELY34497.1.
    RefSeqiWP_004041864.1. NZ_AOHU01000038.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3OYXX-ray2.51A1-433[»]
    3OYZX-ray1.95A1-433[»]
    3PUGX-ray2.70A1-433[»]
    ProteinModelPortaliD4GTL2.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi309800.HVO_1983.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiADE04727; ADE04727; HVO_1983.
    ELY34497; ELY34497; C498_05196.
    GeneIDi8925725.
    KEGGihvo:HVO_1983.

    Phylogenomic databases

    eggNOGiarCOG00760. Archaea.
    COG2301. LUCA.
    HOGENOMiHOG000094928.
    KOiK19282.
    OMAiEVDYTKD.

    Enzyme and pathway databases

    UniPathwayiUPA00703; UER00720.
    BioCyciHVOL309800:GCOK-1982-MONOMER.
    BRENDAi2.3.3.9. 2561.

    Family and domain databases

    Gene3Di3.20.20.60. 1 hit.
    InterProiIPR005000. Aldolase/citrate-lyase_domain.
    IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
    [Graphical view]
    PfamiPF03328. HpcH_HpaI. 1 hit.
    [Graphical view]
    SUPFAMiSSF51621. SSF51621. 1 hit.
    ProtoNetiSearch...

    Entry informationi

    Entry nameiACEB_HALVD
    AccessioniPrimary (citable) accession number: D4GTL2
    Secondary accession number(s): Q977U4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 9, 2014
    Last sequence update: May 18, 2010
    Last modified: December 9, 2015
    This is version 40 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, 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. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.