Skip Header

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

UniProtKB - P53590 (SUCB2_PIG)

Protein

Succinate--CoA ligase [GDP-forming] subunit beta, mitochondrial

Gene

SUCLG2

Organism
Sus scrofa (Pig)
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

GTP-specific succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of 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.UniRule annotation2 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 annotationNote: Binds 1 Mg2+ ion per subunit.UniRule annotation

<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

  1. KM=0.76 mM for succinate1 Publication
  1. Vmax=5.99 µmol/min/mg enzyme1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'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 beta, mitochondrial (SUCLA2), Succinate--CoA ligase [GDP-forming] subunit beta, mitochondrial (SUCLG2), Succinate--CoA ligase [ADP/GDP-forming] subunit alpha, mitochondrial (SUCLG1), Succinate--CoA ligase [GDP-forming] subunit beta, mitochondrial (SUCLG2), Succinate--CoA ligase [GDP-forming] subunit beta, mitochondrial (SUCLG2), Succinate--CoA ligase [ADP/GDP-forming] subunit alpha, mitochondrial (SUCLG1), Succinate--CoA ligase [GDP-forming] subunit beta, mitochondrial (SUCLG2), Succinate--CoA ligase [ADP/GDP-forming] subunit alpha, mitochondrial (SUCLG1), Succinate--CoA ligase [GDP-forming] subunit beta, mitochondrial (SUCLG2), Succinate--CoA ligase [ADP-forming] subunit beta, mitochondrial (SUCLA2), Succinate--CoA ligase [ADP/GDP-forming] subunit alpha, mitochondrial (SUCLG1), Succinate--CoA ligase [ADP-forming] subunit beta, mitochondrial (SUCLA2)
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 ‘Function’ 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 sitei58GTPUniRule annotation1 Publication1
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei80Important for substrate specificityUniRule annotation1
Binding sitei147GTP; via amide nitrogen and carbonyl oxygenUniRule annotation1 Publication1
Sitei148Important for substrate specificityUniRule annotation1
<p>This subsection of the ‘Function’ 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 bindingi244MagnesiumUniRule annotation1 Publication1
Metal bindingi258MagnesiumUniRule annotation1 Publication1
Binding sitei309Substrate; shared with subunit alphaUniRule annotation1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ 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 bindingi91 – 93GTPUniRule 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

View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

<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
LigandGTP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

SABIO-RK: Biochemical Reaction Kinetics Database

More...SABIO-RKi		P53590

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_and_taxonomy_section">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 [GDP-forming] subunit beta, mitochondrialUniRule annotation (EC:6.2.1.4UniRule annotation2 Publications)
Alternative name(s):
GTP-specific succinyl-CoA synthetase subunit betaUniRule annotation
Short name:
G-SCSUniRule annotation
Short name:
GTPSCSUniRule annotation
Succinyl-CoA synthetase beta-G chainUniRule annotation
Short name:
SCS-betaGUniRule annotation
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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:SUCLG2UniRule annotation
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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>OrganismiSus scrofa (Pig)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 identifieri9823 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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
  • UP000008227 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">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: Unplaced

<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

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Mitochondrion

<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 transit peptide.<p><a href='/help/transit' target='_top'>More...</a></p>Transit peptidei‹1 – 38MitochondrionAdd BLAST›38
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000003335839 – 433Succinate--CoA ligase [GDP-forming] subunit beta, mitochondrialUniRule annotationAdd BLAST395

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei74N6-acetyllysineBy similarity1
Modified residuei79N6-succinyllysineBy similarity1
Modified residuei133N6-acetyllysineBy similarity1
Modified residuei140N6-acetyllysineBy similarity1
Modified residuei162PhosphoserineBy similarity1
Modified residuei201N6-acetyllysineBy similarity1
Modified residuei228N6-acetyllysineBy similarity1
Modified residuei272N6-acetyllysineBy similarity1
Modified residuei292N6-acetyllysineBy similarity1
Modified residuei339N6-succinyllysineBy similarity1
Modified residuei348N6-acetyllysineBy similarity1
Modified residuei387N6-acetyllysineBy similarity1
Modified residuei424N6-acetyllysineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

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

More...PaxDbi		P53590

PeptideAtlas

More...PeptideAtlasi		P53590

PRoteomics IDEntifications database

More...PRIDEi		P53590

<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_section">'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_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Heterodimer of an alpha and a beta subunit. The beta subunit determines specificity for GTP.UniRule annotation4 Publications

Protein-protein interaction databases

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		P53590

Molecular INTeraction database

More...MINTi		P53590

STRING: functional protein association networks

More...STRINGi		9823.ENSSSCP00000012257

<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

1433
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...ProteinModelPortali		P53590

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

More...SMRi		P53590

Database of comparative protein structure models

More...ModBasei		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P53590

<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_and_domains_section">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>Domaini47 – 275ATP-graspUniRule annotationAdd BLAST229

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>Regioni366 – 368Substrate binding; shared with subunit alphaUniRule annotation1 Publication3

<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. GTP-specific subunit beta subfamily.UniRule annotation

Keywords - Domaini

Transit peptide

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG2799 Eukaryota
COG0045 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000007059

The HOVERGEN Database of Homologous Vertebrate Genes

More...HOVERGENi		HBG055555

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P53590

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
MF_03221 Succ_CoA_betaG_euk, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR013650 ATP-grasp_succ-CoA_synth-type
IPR013815 ATP_grasp_subdomain_1
IPR005811 CoA_ligase
IPR017866 Succ-CoA_synthase_bsu_CS
IPR034722 Succ_CoA_betaG_euk
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
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_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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: Fragment.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P53590-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
IPAAPVAAQA RKLLRDLAFR PPLLAARSQV VQLTPRRWLN LQEYQSKKLM 
        60         70         80         90        100
SDNGVKVQRF FVADTANEAL EAAKRLNAKE IVLKAQILAG GRGKGVFSSG 
       110        120        130        140        150
LKGGVHLTKD PEVVGQLAKQ MIGYNLATKQ TPKEGVKVNK VMVAEALDIS 
       160        170        180        190        200
RETYLAILMD RSCNGPVLVG SPQGGVDIEE VAASNPELIF KEQIDIIEGI 
       210        220        230        240        250
KDSQAQRMAE NLGFLGPLQN QAADQIKKLY NLFLKIDATQ VEVNPFGETP 
       260        270        280        290        300
EGQVVCFDAK INFDDNAEFR QKDIFAMDDK SENEPIENEA AKYDLKYIGL 
       310        320        330        340        350
DGNIACFVNG AGLAMATCDI IFLNGGKPAN FLDLGGGVKE SQVYQAFKLL 
       360        370        380        390        400
TADPKVEAIL VNIFGGIVNC AIIANGITKA CRELELKVPL VVRLEGTNVH 
       410        420        430 
EAQNILTNSG LPITSAVDLE DAAKKAVASV TKK
Length:433
Mass (Da):46,803
Last modified:May 27, 2002 - v2
<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:iAA04B72BC1B80E24
GO

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence AAA31120 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section is used for sequence fragments to indicate that the residue at the extremity of the sequence is not the actual terminal residue in the complete protein sequence.<p><a href='/help/non_ter' target='_top'>More...</a></p>Non-terminal residuei11

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
L06944 mRNA Translation: AAA31120.1 Different initiation.
Z81187 mRNA Translation: CAB03559.1

Protein sequence database of the Protein Information Resource

More...PIRi		A44529

UniGene gene-oriented nucleotide sequence clusters

More...UniGenei		Ssc.12108

<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
L06944 mRNA Translation: AAA31120.1 Different initiation.
Z81187 mRNA Translation: CAB03559.1
PIRiA44529
UniGeneiSsc.12108

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
1EUCX-ray2.10B39-433[»]
1EUDX-ray2.10B39-433[»]
2FP4X-ray2.08B40-433[»]
2FPGX-ray2.96B40-433[»]
2FPIX-ray2.70B40-433[»]
2FPPX-ray2.35B40-433[»]
4XX0X-ray2.10B40-433[»]
5CAEX-ray2.20B40-433[»]
ProteinModelPortaliP53590
SMRiP53590
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

CORUMiP53590
MINTiP53590
STRINGi9823.ENSSSCP00000012257

Proteomic databases

PaxDbiP53590
PeptideAtlasiP53590
PRIDEiP53590

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiKOG2799 Eukaryota
COG0045 LUCA
HOGENOMiHOG000007059
HOVERGENiHBG055555
InParanoidiP53590

Enzyme and pathway databases

UniPathwayi
UPA00223;UER00999

SABIO-RKiP53590

Miscellaneous databases

EvolutionaryTraceiP53590

Family and domain databases

Gene3Di3.30.1490.20, 1 hit
3.40.50.261, 1 hit
HAMAPiMF_00558 Succ_CoA_beta, 1 hit
MF_03221 Succ_CoA_betaG_euk, 1 hit
InterProiView protein in InterPro
IPR013650 ATP-grasp_succ-CoA_synth-type
IPR013815 ATP_grasp_subdomain_1
IPR005811 CoA_ligase
IPR017866 Succ-CoA_synthase_bsu_CS
IPR034722 Succ_CoA_betaG_euk
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
PS01217 SUCCINYL_COA_LIG_3, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

<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 nameiSUCB2_PIG
<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: P53590
Secondary accession number(s): Q95279
<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_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: May 27, 2002
Last modified: December 5, 2018
This is version 145 of the entry and version 2 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 programChordata 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, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again