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Protein

Glyceraldehyde dehydrogenase small chain

Gene

cutC

Organism
Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Component of the glyceraldehyde dehydrogenase which is involved the nonphosphorylated Entner-Doudoroff pathway. Catalyzes the oxidation of D-glyceraldehyde to yield glycerate. When the artificial electron acceptor 2,6-dichlorophenol-indophenol (Cl2Ind) is used, the enzyme shows a broad substrate range (glyceraldehyde-3-phosphate, formaldehyde, acetaldehyde, propionaldehyde and isobutyraldehyde), but is most active with D-glyceraldehyde. It is not known which acceptor is utilized in vivo.1 Publication

Catalytic activityi

D-glyceraldehyde + H2O + acceptor = D-glycerate + reduced acceptor.1 Publication

Cofactori

[2Fe-2S] cluster1 PublicationNote: Binds 2 [2Fe-2S] cluster per subunit.1 Publication

Kineticsi

  1. KM=30 µM for propionaldehyde (at 80 degrees Celsius and pH 6.7)1 Publication
  2. KM=90 µM for D,L-glyceraldehyde (at 80 degrees Celsius and pH 6.7)1 Publication

    pH dependencei

    Optimum pH is 6.7. At pH 6.7, glyceraldehyde is the predominant substrate, however at pH 7.5 the dehydrogenase exhibits activity preferentially towards the aliphatic aldehydes such as formaldehyde, acetaldehyde and propionaldehyde.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi48 – 481Iron-sulfur 1 (2Fe-2S)By similarity
    Metal bindingi53 – 531Iron-sulfur 1 (2Fe-2S)By similarity
    Metal bindingi56 – 561Iron-sulfur 1 (2Fe-2S)By similarity
    Metal bindingi68 – 681Iron-sulfur 1 (2Fe-2S)By similarity
    Metal bindingi107 – 1071Iron-sulfur 2 (2Fe-2S)By similarity
    Metal bindingi110 – 1101Iron-sulfur 2 (2Fe-2S)By similarity
    Metal bindingi142 – 1421Iron-sulfur 2 (2Fe-2S)By similarity
    Metal bindingi144 – 1441Iron-sulfur 2 (2Fe-2S)By similarity

    GO - Molecular functioni

    • 2 iron, 2 sulfur cluster binding Source: UniProtKB
    • electron carrier activity Source: InterPro
    • metal ion binding Source: UniProtKB-KW
    • oxidoreductase activity, acting on the aldehyde or oxo group of donors Source: UniProtKB
    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    2Fe-2S, Iron, Iron-sulfur, Metal-binding

    Enzyme and pathway databases

    BioCyciSACI330779:GH9J-2226-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glyceraldehyde dehydrogenase small chain (EC:1.2.99.8)
    Alternative name(s):
    Glyceraldehyde dehydrogenase subunit C
    Glyceraldehyde dehydrogenase subunit gamma
    Gene namesi
    Name:cutC
    Ordered Locus Names:Saci_2270
    OrganismiSulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)
    Taxonomic identifieri330779 [NCBI]
    Taxonomic lineageiArchaeaCrenarchaeotaThermoproteiSulfolobalesSulfolobaceaeSulfolobus
    Proteomesi
    • UP000001018 Componenti: Chromosome

    Subcellular locationi

    • Cytoplasm 1 Publication

    GO - Cellular componenti

    • cytoplasm Source: UniProtKB
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 163163Glyceraldehyde dehydrogenase small chainPRO_0000424273Add
    BLAST

    Interactioni

    Subunit structurei

    Heterotrimer composed of a large chain (CutA), a medium chain (CutB) and a small chain (CutC).1 Publication

    Protein-protein interaction databases

    STRINGi330779.Saci_2270.

    Structurei

    3D structure databases

    ProteinModelPortaliQ4J6M5.
    SMRiQ4J6M5. Positions 11-163.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini10 – 86772Fe-2S ferredoxin-typePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 2Fe-2S ferredoxin-type domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiarCOG01925. Archaea.
    COG2080. LUCA.
    HOGENOMiHOG000166647.
    KOiK18022.
    OMAiVHRKGHE.

    Family and domain databases

    Gene3Di1.10.150.120. 1 hit.
    3.10.20.30. 1 hit.
    InterProiIPR002888. 2Fe-2S-bd.
    IPR001041. 2Fe-2S_ferredoxin-type.
    IPR012675. Beta-grasp_dom.
    [Graphical view]
    PfamiPF00111. Fer2. 1 hit.
    PF01799. Fer2_2. 1 hit.
    [Graphical view]
    SUPFAMiSSF47741. SSF47741. 1 hit.
    SSF54292. SSF54292. 1 hit.
    PROSITEiPS51085. 2FE2S_FER_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q4J6M5-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MLVVKKGEGV KVRVRVNGVW YEKYVSPRTL LVDFIRDELG LTGTKVGCDT
    60 70 80 90 100
    TTCGACTVIM NGKSVKSCTV LAAQADGAEI TTIEGLSSDS KLHPIQEAFK
    110 120 130 140 150
    DNFALQCGFC TAGMIMQTYF FLKEHPNPTE EEVRDGIHGN ICRCTGYQNI
    160
    VKAVLDASKR LRS
    Length:163
    Mass (Da):17,856
    Last modified:August 2, 2005 - v1
    Checksum:iB81B889CA7553E2A
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    CP000077 Genomic DNA. Translation: AAY81556.1.
    RefSeqiWP_011279058.1. NC_007181.1.

    Genome annotation databases

    EnsemblBacteriaiAAY81556; AAY81556; Saci_2270.
    GeneIDi3474531.
    KEGGisai:Saci_2270.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    CP000077 Genomic DNA. Translation: AAY81556.1.
    RefSeqiWP_011279058.1. NC_007181.1.

    3D structure databases

    ProteinModelPortaliQ4J6M5.
    SMRiQ4J6M5. Positions 11-163.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi330779.Saci_2270.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAY81556; AAY81556; Saci_2270.
    GeneIDi3474531.
    KEGGisai:Saci_2270.

    Phylogenomic databases

    eggNOGiarCOG01925. Archaea.
    COG2080. LUCA.
    HOGENOMiHOG000166647.
    KOiK18022.
    OMAiVHRKGHE.

    Enzyme and pathway databases

    BioCyciSACI330779:GH9J-2226-MONOMER.

    Family and domain databases

    Gene3Di1.10.150.120. 1 hit.
    3.10.20.30. 1 hit.
    InterProiIPR002888. 2Fe-2S-bd.
    IPR001041. 2Fe-2S_ferredoxin-type.
    IPR012675. Beta-grasp_dom.
    [Graphical view]
    PfamiPF00111. Fer2. 1 hit.
    PF01799. Fer2_2. 1 hit.
    [Graphical view]
    SUPFAMiSSF47741. SSF47741. 1 hit.
    SSF54292. SSF54292. 1 hit.
    PROSITEiPS51085. 2FE2S_FER_2. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiCUTC_SULAC
    AccessioniPrimary (citable) accession number: Q4J6M5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 13, 2013
    Last sequence update: August 2, 2005
    Last modified: December 9, 2015
    This is version 79 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

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. 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.