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Entry version 132 (12 Aug 2020)
Sequence version 1 (01 Apr 1988)
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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

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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

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.

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Mg2+UniRule annotation2 PublicationsNote: Binds 1 Mg2+ ion per subunit.UniRule annotation1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity 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.

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

kcat is 2684 min(-1) with ATP as substrate and 1471 min(-1) with GTP as substrate.1 Publication
  1. KM=70 µM for ATP1 Publication
  2. KM=394 µM for GTP1 Publication

    pH dependencei

    Optimum pH is 7.4.1 Publication

    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>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 alpha (sucD), Succinate--CoA ligase [ADP-forming] subunit beta (sucC), 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
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei46ATPUniRule annotation1 Publication1
    Binding sitei99ATPUniRule annotation1 Publication1
    Binding sitei102ATP; via amide nitrogenUniRule annotation1 Publication1
    Binding sitei107ATPUniRule annotation1 Publication1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi199MagnesiumUniRule annotation1 Publication1
    Metal bindingi213MagnesiumUniRule annotation1 Publication1
    Binding sitei264Substrate; shared with subunit alphaUniRule annotation1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi53 – 55ATPUniRule annotation1 Publication3

    <p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

    GO - Biological processi

    <p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

    Molecular functionLigase
    Biological processTricarboxylic acid cycle
    LigandATP-binding, Magnesium, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    EcoCyc:SUCCCOASYN-BETA
    ECOL316407:JW0717-MONOMER
    MetaCyc:SUCCCOASYN-BETA

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    6.2.1.5, 2165

    UniPathway: a resource for the exploration and annotation of metabolic pathways

    More...
    UniPathwayi
    UPA00223;UER00999

    <p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
    Recommended name:
    Succinate--CoA ligase [ADP-forming] subunit betaUniRule annotation (EC:6.2.1.5UniRule annotation2 Publications)
    Alternative name(s):
    Succinyl-CoA synthetase subunit betaUniRule annotation
    Short name:
    SCS-betaUniRule annotation
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
    Name:sucCUniRule annotation
    Ordered Locus Names:b0728, JW0717
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiEscherichia coli (strain K12)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri83333 [NCBI]
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
    • UP000000318 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    <p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

    GO - Cellular componenti

    <p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>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

    <p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001028321 – 388Succinate--CoA ligase [ADP-forming] subunit betaAdd BLAST388

    Proteomic databases

    jPOST - Japan Proteome Standard Repository/Database

    More...
    jPOSTi
    P0A836

    PaxDb, a database of protein abundance averages across all three domains of life

    More...
    PaxDbi
    P0A836

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P0A836

    2D gel databases

    Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital

    More...
    SWISS-2DPAGEi
    P0A836

    PTM databases

    CarbonylDB database of protein carbonylation sites

    More...
    CarbonylDBi
    P0A836

    <p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

    <p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

    Heterotetramer of two alpha and two beta subunits.

    UniRule annotation2 Publications

    <p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGRID)

    More...
    BioGRIDi
    4259946, 19 interactors

    ComplexPortal: manually curated resource of macromolecular complexes

    More...
    ComplexPortali
    CPX-1092, Succinyl-CoA synthetase

    Database of interacting proteins

    More...
    DIPi
    DIP-31852N

    Protein interaction database and analysis system

    More...
    IntActi
    P0A836, 30 interactors

    STRING: functional protein association networks

    More...
    STRINGi
    511145.b0728

    <p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

    Secondary structure

    1388
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    SWISS-MODEL Repository - a database of annotated 3D protein structure models

    More...
    SMRi
    P0A836

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    Protein Data Bank in Europe - Knowledge Base

    More...
    PDBe-KBi
    Search...

    Miscellaneous databases

    Relative evolutionary importance of amino acids within a protein sequence

    More...
    EvolutionaryTracei
    P0A836

    <p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini9 – 244ATP-graspUniRule annotationAdd BLAST236

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni321 – 323Substrate binding; shared with subunit alphaUniRule annotation3

    <p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

    Belongs to the succinate/malate CoA ligase beta subunit family.UniRule annotation

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    COG0045, Bacteria

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    CLU_037430_4_0_6

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    P0A836

    KEGG Orthology (KO)

    More...
    KOi
    K01903

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    P0A836

    Family and domain databases

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    3.30.1490.20, 1 hit
    3.40.50.261, 1 hit

    HAMAP database of protein families

    More...
    HAMAPi
    MF_00558, Succ_CoA_beta, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR011761, ATP-grasp
    IPR013650, ATP-grasp_succ-CoA_synth-type
    IPR013815, ATP_grasp_subdomain_1
    IPR005811, CoA_ligase
    IPR017866, Succ-CoA_synthase_bsu_CS
    IPR005809, Succ_CoA_synthase_bsu
    IPR016102, Succinyl-CoA_synth-like

    The PANTHER Classification System

    More...
    PANTHERi
    PTHR11815, PTHR11815, 1 hit

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF08442, ATP-grasp_2, 1 hit
    PF00549, Ligase_CoA, 1 hit

    PIRSF; a whole-protein classification database

    More...
    PIRSFi
    PIRSF001554, SucCS_beta, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF52210, SSF52210, 1 hit

    TIGRFAMs; a protein family database

    More...
    TIGRFAMsi
    TIGR01016, sucCoAbeta, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS50975, ATP_GRASP, 1 hit
    PS01217, SUCCINYL_COA_LIG_3, 1 hit

    <p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>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
    <p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i09C429EC97A823CF
    GO

    Sequence databases

    Select the link destinations:

    EMBL nucleotide sequence database

    More...
    EMBLi

    GenBank nucleotide sequence database

    More...
    GenBanki

    DNA Data Bank of Japan; a nucleotide sequence database

    More...
    DDBJi
    Links Updated
    J01619 Genomic DNA Translation: AAA23899.1
    U00096 Genomic DNA Translation: AAC73822.1
    AP009048 Genomic DNA Translation: BAA35394.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    A24090, SYECSB

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_415256.1, NC_000913.3
    WP_001048602.1, NZ_STEB01000035.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...
    EnsemblBacteriai
    AAC73822; AAC73822; b0728
    BAA35394; BAA35394; BAA35394

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    52076039
    945312

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    ecj:JW0717
    eco:b0728

    Pathosystems Resource Integration Center (PATRIC)

    More...
    PATRICi
    fig|1411691.4.peg.1545

    <p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

    <p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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_STEB01000035.1

    3D structure databases

    Select the link destinations:

    Protein Data Bank Europe

    More...
    PDBei

    Protein Data Bank RCSB

    More...
    RCSB PDBi

    Protein Data Bank Japan

    More...
    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[»]
    SMRiP0A836
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein-protein interaction databases

    BioGRIDi4259946, 19 interactors
    ComplexPortaliCPX-1092, Succinyl-CoA synthetase
    DIPiDIP-31852N
    IntActiP0A836, 30 interactors
    STRINGi511145.b0728

    PTM databases

    CarbonylDBiP0A836

    2D gel databases

    SWISS-2DPAGEiP0A836

    Proteomic databases

    jPOSTiP0A836
    PaxDbiP0A836
    PRIDEiP0A836

    Genome annotation databases

    EnsemblBacteriaiAAC73822; AAC73822; b0728
    BAA35394; BAA35394; BAA35394
    GeneIDi52076039
    945312
    KEGGiecj:JW0717
    eco:b0728
    PATRICifig|1411691.4.peg.1545

    Organism-specific databases

    EchoBASE - an integrated post-genomic database for E. coli

    More...
    EchoBASEi
    EB0974

    Phylogenomic databases

    eggNOGiCOG0045, Bacteria
    HOGENOMiCLU_037430_4_0_6
    InParanoidiP0A836
    KOiK01903
    PhylomeDBiP0A836

    Enzyme and pathway databases

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

    Miscellaneous databases

    EvolutionaryTraceiP0A836

    Protein Ontology

    More...
    PROi
    PR:P0A836

    Family and domain databases

    Gene3Di3.30.1490.20, 1 hit
    3.40.50.261, 1 hit
    HAMAPiMF_00558, Succ_CoA_beta, 1 hit
    InterProiView protein in InterPro
    IPR011761, ATP-grasp
    IPR013650, ATP-grasp_succ-CoA_synth-type
    IPR013815, ATP_grasp_subdomain_1
    IPR005811, CoA_ligase
    IPR017866, Succ-CoA_synthase_bsu_CS
    IPR005809, Succ_CoA_synthase_bsu
    IPR016102, Succinyl-CoA_synth-like
    PANTHERiPTHR11815, PTHR11815, 1 hit
    PfamiView protein in Pfam
    PF08442, ATP-grasp_2, 1 hit
    PF00549, Ligase_CoA, 1 hit
    PIRSFiPIRSF001554, SucCS_beta, 1 hit
    SUPFAMiSSF52210, SSF52210, 1 hit
    TIGRFAMsiTIGR01016, sucCoAbeta, 1 hit
    PROSITEiView protein in PROSITE
    PS50975, ATP_GRASP, 1 hit
    PS01217, SUCCINYL_COA_LIG_3, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins

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    ProtoNeti
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    MobiDB: a database of protein disorder and mobility annotations

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    MobiDBi
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    <p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

    <p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiSUCC_ECOLI
    <p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P0A836
    Secondary accession number(s): P07460
    <p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1988
    Last sequence update: April 1, 1988
    Last modified: August 12, 2020
    This is version 132 of the entry and version 1 of the sequence. See complete history.
    <p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    <p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

    Keywords - Technical termi

    3D-structure, 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
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