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Protein

Succinate--CoA ligase [ADP-forming] subunit beta

Gene

sucC

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The beta subunit provides nucleotide specificity of the enzyme and binds the substrate succinate, while the binding sites for coenzyme A and phosphate are found in the alpha subunit. Can use either ATP or GTP, but prefers ATP. It can also function in the other direction for anabolic purposes, and this may be particularly important for providing succinyl-CoA during anaerobic growth when the oxidative route from 2-oxoglutarate is severely repressed.UniRule annotation1 Publication

Catalytic activityi

ATP + succinate + CoA = ADP + phosphate + succinyl-CoA.UniRule annotation1 Publication

Cofactori

Mg2+UniRule annotation1 PublicationNote: Binds 1 Mg2+ ion per subunit.UniRule annotation1 Publication

Enzyme regulationi

Exhibits two interesting properties: "substrate synergism", in which the enzyme is most active for the catalysis of its partial reactions only when all the substrate-binding sites are occupied, and "catalytic cooperativity" between alternating active sites in the tetramer, whereby the interaction of substrates (particularly ATP) at one site is needed to promote catalysis at the other.

Kineticsi

kcat is 2684 min(-1) with ATP as substrate and 1471 min(-1) with GTP as substrate.1 Publication

Manual assertion based on experiment ini

  1. KM=70 µM for ATP1 Publication
  2. KM=394 µM for GTP1 Publication

    pH dependencei

    Optimum pH is 7.4.1 Publication

    Pathwayi: tricarboxylic acid cycle

    This protein is involved in step 1 of the subpathway that synthesizes succinate from succinyl-CoA (ligase route).UniRule annotation1 Publication
    Proteins known to be involved in this subpathway in this organism are:
    1. Succinate--CoA ligase [ADP-forming] subunit alpha (sucD), Succinate--CoA ligase [ADP-forming] subunit beta (sucC)
    This subpathway is part of the pathway tricarboxylic acid 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 succinate from succinyl-CoA (ligase route), the pathway tricarboxylic acid cycle and in Carbohydrate metabolism.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei46ATPUniRule annotation1 Publication1
    Binding sitei99ATPUniRule annotation1 Publication1
    Binding sitei102ATP; via amide nitrogenUniRule annotation1 Publication1
    Binding sitei107ATPUniRule annotation1 Publication1
    Metal bindingi199MagnesiumUniRule annotation1 Publication1
    Metal bindingi213MagnesiumUniRule annotation1 Publication1
    Binding sitei264Substrate; shared with subunit alphaUniRule annotation1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi53 – 55ATPUniRule annotation1 Publication3

    GO - Molecular functioni

    • ATP binding Source: UniProtKB-HAMAP
    • magnesium ion binding Source: UniProtKB-HAMAP
    • manganese ion binding Source: UniProtKB-HAMAP
    • succinate-CoA ligase (ADP-forming) activity Source: EcoliWiki

    GO - Biological processi

    • tricarboxylic acid cycle Source: EcoliWiki
    Complete GO annotation...

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Tricarboxylic acid cycle

    Keywords - Ligandi

    ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciEcoCyc:SUCCCOASYN-BETA.
    ECOL316407:JW0717-MONOMER.
    MetaCyc:SUCCCOASYN-BETA.
    BRENDAi6.2.1.5. 2165.
    UniPathwayiUPA00223; UER00999.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Succinate--CoA ligase [ADP-forming] subunit betaUniRule annotation (EC:6.2.1.5UniRule annotation1 Publication)
    Alternative name(s):
    Succinyl-CoA synthetase subunit betaUniRule annotation
    Short name:
    SCS-betaUniRule annotation
    Gene namesi
    Name:sucCUniRule annotation
    Ordered Locus Names:b0728, JW0717
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG10981. sucC.

    Subcellular locationi

    GO - Cellular componenti

    • cytoplasm Source: UniProtKB
    • cytosol Source: EcoCyc
    • succinate-CoA ligase complex (ADP-forming) Source: EcoCyc
    Complete GO annotation...

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi197E → A: Prevents phosphorylation of the enzyme intermediate in both reaction directions. 1 Publication1
    Mutagenesisi197E → Q: Prevents phosphorylation of the enzyme intermediate by ATP. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00001028321 – 388Succinate--CoA ligase [ADP-forming] subunit betaAdd BLAST388

    Proteomic databases

    EPDiP0A836.
    PaxDbiP0A836.
    PRIDEiP0A836.

    2D gel databases

    SWISS-2DPAGEP0A836.

    Interactioni

    Subunit structurei

    Heterotetramer of two alpha and two beta subunits.UniRule annotation2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    sucDP0AGE93EBI-369117,EBI-369078

    Protein-protein interaction databases

    BioGridi4259946. 7 interactors.
    DIPiDIP-31852N.
    IntActiP0A836. 8 interactors.
    STRINGi511145.b0728.

    Structurei

    Secondary structure

    1388
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi5 – 14Combined sources10
    Beta strandi22 – 27Combined sources6
    Helixi28 – 38Combined sources11
    Beta strandi43 – 47Combined sources5
    Beta strandi50 – 52Combined sources3
    Turni54 – 58Combined sources5
    Beta strandi60 – 63Combined sources4
    Helixi66 – 76Combined sources11
    Beta strandi79 – 81Combined sources3
    Beta strandi96 – 100Combined sources5
    Beta strandi104 – 115Combined sources12
    Turni116 – 119Combined sources4
    Beta strandi120 – 127Combined sources8
    Helixi133 – 139Combined sources7
    Helixi141 – 143Combined sources3
    Beta strandi144 – 148Combined sources5
    Turni151 – 153Combined sources3
    Helixi157 – 166Combined sources10
    Helixi172 – 190Combined sources19
    Beta strandi193 – 204Combined sources12
    Beta strandi209 – 212Combined sources4
    Beta strandi215 – 218Combined sources4
    Helixi220 – 225Combined sources6
    Helixi227 – 232Combined sources6
    Helixi235 – 237Combined sources3
    Helixi240 – 247Combined sources8
    Beta strandi251 – 254Combined sources4
    Beta strandi256 – 265Combined sources10
    Helixi266 – 278Combined sources13
    Beta strandi285 – 288Combined sources4
    Helixi295 – 306Combined sources12
    Beta strandi308 – 310Combined sources3
    Beta strandi313 – 320Combined sources8
    Beta strandi321 – 323Combined sources3
    Helixi325 – 339Combined sources15
    Beta strandi345 – 351Combined sources7
    Helixi354 – 362Combined sources9
    Beta strandi366 – 370Combined sources5
    Helixi374 – 384Combined sources11
    Turni385 – 387Combined sources3

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1CQIX-ray3.30B/E1-385[»]
    1CQJX-ray2.90B/E1-385[»]
    1JKJX-ray2.35B/E1-388[»]
    1JLLX-ray2.69B/E1-388[»]
    1SCUX-ray2.50B/E1-388[»]
    2NU6X-ray2.55B/E1-388[»]
    2NU7X-ray2.20B/E1-388[»]
    2NU8X-ray2.15B/E1-388[»]
    2NU9X-ray2.90B/E/G/I1-388[»]
    2NUAX-ray2.95B/E1-388[»]
    2SCUX-ray2.30B/E1-388[»]
    ProteinModelPortaliP0A836.
    SMRiP0A836.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0A836.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Domaini9 – 244ATP-graspUniRule annotationAdd BLAST236

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni321 – 323Substrate binding; shared with subunit alphaUniRule annotation3

    Sequence similaritiesi

    Belongs to the succinate/malate CoA ligase beta subunit family.UniRule annotation
    Contains 1 ATP-grasp domain.UniRule annotation

    Phylogenomic databases

    eggNOGiENOG4105CMV. Bacteria.
    COG0045. LUCA.
    HOGENOMiHOG000007059.
    InParanoidiP0A836.
    KOiK01903.
    OMAiYIESGCD.
    PhylomeDBiP0A836.

    Family and domain databases

    Gene3Di3.30.1490.20. 1 hit.
    3.30.470.20. 1 hit.
    3.40.50.261. 1 hit.
    HAMAPiMF_00558. Succ_CoA_beta. 1 hit.
    InterProiIPR011761. ATP-grasp.
    IPR013650. ATP-grasp_succ-CoA_synth-type.
    IPR013815. ATP_grasp_subdomain_1.
    IPR013816. ATP_grasp_subdomain_2.
    IPR005811. CoA_ligase.
    IPR017866. Succ-CoA_synthase_bsu_CS.
    IPR005809. Succ_CoA_synthase_bsu.
    IPR016102. Succinyl-CoA_synth-like.
    [Graphical view]
    PANTHERiPTHR11815. PTHR11815. 1 hit.
    PfamiPF08442. ATP-grasp_2. 1 hit.
    PF00549. Ligase_CoA. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001554. SucCS_beta. 1 hit.
    SUPFAMiSSF52210. SSF52210. 1 hit.
    TIGRFAMsiTIGR01016. sucCoAbeta. 1 hit.
    PROSITEiPS50975. ATP_GRASP. 1 hit.
    PS01217. SUCCINYL_COA_LIG_3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P0A836-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MNLHEYQAKQ LFARYGLPAP VGYACTTPRE AEEAASKIGA GPWVVKCQVH
    60 70 80 90 100
    AGGRGKAGGV KVVNSKEDIR AFAENWLGKR LVTYQTDANG QPVNQILVEA
    110 120 130 140 150
    ATDIAKELYL GAVVDRSSRR VVFMASTEGG VEIEKVAEET PHLIHKVALD
    160 170 180 190 200
    PLTGPMPYQG RELAFKLGLE GKLVQQFTKI FMGLATIFLE RDLALIEINP
    210 220 230 240 250
    LVITKQGDLI CLDGKLGADG NALFRQPDLR EMRDQSQEDP REAQAAQWEL
    260 270 280 290 300
    NYVALDGNIG CMVNGAGLAM GTMDIVKLHG GEPANFLDVG GGATKERVTE
    310 320 330 340 350
    AFKIILSDDK VKAVLVNIFG GIVRCDLIAD GIIGAVAEVG VNVPVVVRLE
    360 370 380
    GNNAELGAKK LADSGLNIIA AKGLTDAAQQ VVAAVEGK
    Length:388
    Mass (Da):41,393
    Last modified:April 1, 1988 - v1
    Checksum:i09C429EC97A823CF
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    J01619 Genomic DNA. Translation: AAA23899.1.
    U00096 Genomic DNA. Translation: AAC73822.1.
    AP009048 Genomic DNA. Translation: BAA35394.1.
    PIRiA24090. SYECSB.
    RefSeqiNP_415256.1. NC_000913.3.
    WP_001048602.1. NZ_LN832404.1.

    Genome annotation databases

    EnsemblBacteriaiAAC73822; AAC73822; b0728.
    BAA35394; BAA35394; BAA35394.
    GeneIDi945312.
    KEGGiecj:JW0717.
    eco:b0728.
    PATRICi32116651. VBIEscCol129921_0758.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    J01619 Genomic DNA. Translation: AAA23899.1.
    U00096 Genomic DNA. Translation: AAC73822.1.
    AP009048 Genomic DNA. Translation: BAA35394.1.
    PIRiA24090. SYECSB.
    RefSeqiNP_415256.1. NC_000913.3.
    WP_001048602.1. NZ_LN832404.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1CQIX-ray3.30B/E1-385[»]
    1CQJX-ray2.90B/E1-385[»]
    1JKJX-ray2.35B/E1-388[»]
    1JLLX-ray2.69B/E1-388[»]
    1SCUX-ray2.50B/E1-388[»]
    2NU6X-ray2.55B/E1-388[»]
    2NU7X-ray2.20B/E1-388[»]
    2NU8X-ray2.15B/E1-388[»]
    2NU9X-ray2.90B/E/G/I1-388[»]
    2NUAX-ray2.95B/E1-388[»]
    2SCUX-ray2.30B/E1-388[»]
    ProteinModelPortaliP0A836.
    SMRiP0A836.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4259946. 7 interactors.
    DIPiDIP-31852N.
    IntActiP0A836. 8 interactors.
    STRINGi511145.b0728.

    2D gel databases

    SWISS-2DPAGEP0A836.

    Proteomic databases

    EPDiP0A836.
    PaxDbiP0A836.
    PRIDEiP0A836.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC73822; AAC73822; b0728.
    BAA35394; BAA35394; BAA35394.
    GeneIDi945312.
    KEGGiecj:JW0717.
    eco:b0728.
    PATRICi32116651. VBIEscCol129921_0758.

    Organism-specific databases

    EchoBASEiEB0974.
    EcoGeneiEG10981. sucC.

    Phylogenomic databases

    eggNOGiENOG4105CMV. Bacteria.
    COG0045. LUCA.
    HOGENOMiHOG000007059.
    InParanoidiP0A836.
    KOiK01903.
    OMAiYIESGCD.
    PhylomeDBiP0A836.

    Enzyme and pathway databases

    UniPathwayiUPA00223; UER00999.
    BioCyciEcoCyc:SUCCCOASYN-BETA.
    ECOL316407:JW0717-MONOMER.
    MetaCyc:SUCCCOASYN-BETA.
    BRENDAi6.2.1.5. 2165.

    Miscellaneous databases

    EvolutionaryTraceiP0A836.
    PROiP0A836.

    Family and domain databases

    Gene3Di3.30.1490.20. 1 hit.
    3.30.470.20. 1 hit.
    3.40.50.261. 1 hit.
    HAMAPiMF_00558. Succ_CoA_beta. 1 hit.
    InterProiIPR011761. ATP-grasp.
    IPR013650. ATP-grasp_succ-CoA_synth-type.
    IPR013815. ATP_grasp_subdomain_1.
    IPR013816. ATP_grasp_subdomain_2.
    IPR005811. CoA_ligase.
    IPR017866. Succ-CoA_synthase_bsu_CS.
    IPR005809. Succ_CoA_synthase_bsu.
    IPR016102. Succinyl-CoA_synth-like.
    [Graphical view]
    PANTHERiPTHR11815. PTHR11815. 1 hit.
    PfamiPF08442. ATP-grasp_2. 1 hit.
    PF00549. Ligase_CoA. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001554. SucCS_beta. 1 hit.
    SUPFAMiSSF52210. SSF52210. 1 hit.
    TIGRFAMsiTIGR01016. sucCoAbeta. 1 hit.
    PROSITEiPS50975. ATP_GRASP. 1 hit.
    PS01217. SUCCINYL_COA_LIG_3. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiSUCC_ECOLI
    AccessioniPrimary (citable) accession number: P0A836
    Secondary accession number(s): P07460
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1988
    Last sequence update: April 1, 1988
    Last modified: November 30, 2016
    This is version 105 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Succinyl-CoA synthetase (SCS) of E.coli catalyzes its reaction via three steps that involve phosphoryl enzyme and enzyme-bound succinyl phosphate as intermediates.

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. 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.