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Protein

Succinate dehydrogenase flavoprotein subunit

Gene

sdhA

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

Two distinct, membrane-bound, FAD-containing enzymes are responsible for the catalysis of fumarate and succinate interconversion; the fumarate reductase is used in anaerobic growth, and the succinate dehydrogenase is used in aerobic growth.3 Publications1 Publication

<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

FAD3 PublicationsNote: Flavinylated by SdhE, about 5% flavinylation occurs in the absence of SdhE.1 Publication

<p>This subsection of the ‘Function’ 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

Inhibited by oxaloacetate.1 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 fumarate from succinate (bacterial route).1 Publication
Proteins known to be involved in this subpathway in this organism are:
  1. Succinate dehydrogenase iron-sulfur subunit (sdhB), Succinate dehydrogenase flavoprotein subunit (sdhA)
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 fumarate from succinate (bacterial 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 sitei221FAD3 Publications1
Binding sitei242Substrate1 Publication1
Binding sitei254Substrate1 Publication1
<p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei286Proton acceptor1 Publication1
Binding sitei354Substrate1 Publication1
Binding sitei388FAD3 Publications1
Binding sitei399Substrate1 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 bindingi14 – 19FAD3 Publications6
Nucleotide bindingi37 – 52FAD3 PublicationsAdd BLAST16
Nucleotide bindingi404 – 405FAD3 Publications2

<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

  • electron transfer activity Source: EcoCyc
  • flavin adenine dinucleotide binding Source: EcoliWiki
  • succinate dehydrogenase (ubiquinone) activity Source: UniProtKB-EC
  • succinate dehydrogenase activity Source: EcoliWiki

GO - Biological processi

  • aerobic respiration Source: EcoliWiki
  • anaerobic respiration Source: GO_Central
  • oxidation-reduction process Source: EcoliWiki
  • tricarboxylic acid cycle Source: EcoliWiki

<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 functionOxidoreductase
Biological processElectron transport, Transport, Tricarboxylic acid cycle
LigandFAD, Flavoprotein

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
EcoCyc:SDH-FLAVO
MetaCyc:SDH-FLAVO

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
1.3.5.1 2026

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

More...
UniPathwayi
UPA00223;UER01005

<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 dehydrogenase flavoprotein subunit (EC:1.3.5.11 Publication)
<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:sdhA
Ordered Locus Names:b0723, JW0713
<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>OrganismiEscherichia coli (strain K12)
<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 identifieri83333 [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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
<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
  • UP000000318 <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: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

Escherichia coli strain K12 genome database

More...
EcoGenei
EG10931 sdhA

<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

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

<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

<p>This subsection of the ‘Pathology and Biotech’ section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

No effect on anaerobic growth on glycerol fumarate medium.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'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>Mutagenesisi186E → M: Allows recovery of protein cross-linked to SdhE, SdhA is flavinylated. 1 Publication1
Mutagenesisi187T → M: No recovery of protein cross-linked to SdhE, SdhA is flavinylated. 1 Publication1

Chemistry databases

Drug and drug target database

More...
DrugBanki
DB04631 Atpenin A5
DB08690 UBIQUINONE-2

<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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001586521 – 588Succinate dehydrogenase flavoprotein subunitAdd BLAST588

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 residuei45Tele-8alpha-FAD histidine3 Publications1
Modified residuei267N6-acetyllysine1 Publication1

Keywords - PTMi

Acetylation

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
P0AC41

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

More...
PaxDbi
P0AC41

PRoteomics IDEntifications database

More...
PRIDEi
P0AC41

2D gel databases

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

More...
SWISS-2DPAGEi
P0AC41

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P0AC41

<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

Part of an enzyme complex containing four subunits: a flavoprotein, an iron-sulfur, cytochrome b-556, and a hydrophobic anchor protein. The complex forms trimers. Can be cross-linked to SdhE (PubMed:26644464).5 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">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="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

WithEntry#Exp.IntActNotes
sdhBP070142EBI-371263,EBI-1035514

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
4262907, 31 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-1931 Respiratory chain complex II

Database of interacting proteins

More...
DIPi
DIP-31877N

Protein interaction database and analysis system

More...
IntActi
P0AC41, 91 interactors

Molecular INTeraction database

More...
MINTi
P0AC41

STRING: functional protein association networks

More...
STRINGi
316385.ECDH10B_0790

<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

1588
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
P0AC41

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

More...
SMRi
P0AC41

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
P0AC41

<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

<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

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG4105C00 Bacteria
COG1053 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000160475

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P0AC41

KEGG Orthology (KO)

More...
KOi
K00239

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P0AC41

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.50.50.60, 1 hit
3.90.700.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR003953 FAD-binding_2
IPR036188 FAD/NAD-bd_sf
IPR003952 FRD_SDH_FAD_BS
IPR037099 Fum_R/Succ_DH_flav-like_C_sf
IPR015939 Fum_Rdtase/Succ_DH_flav-like_C
IPR027477 Succ_DH/fumarate_Rdtase_cat_sf
IPR011281 Succ_DH_flav_su_fwd
IPR014006 Succ_Dhase_FrdA_Gneg

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00890 FAD_binding_2, 1 hit
PF02910 Succ_DH_flav_C, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF46977 SSF46977, 1 hit
SSF51905 SSF51905, 1 hit
SSF56425 SSF56425, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR01816 sdhA_forward, 1 hit
TIGR01812 sdhA_frdA_Gneg, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00504 FRD_SDH_FAD_BINDING, 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: Complete.

P0AC41-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MKLPVREFDA VVIGAGGAGM RAALQISQSG QTCALLSKVF PTRSHTVSAQ
60 70 80 90 100
GGITVALGNT HEDNWEWHMY DTVKGSDYIG DQDAIEYMCK TGPEAILELE
110 120 130 140 150
HMGLPFSRLD DGRIYQRPFG GQSKNFGGEQ AARTAAAADR TGHALLHTLY
160 170 180 190 200
QQNLKNHTTI FSEWYALDLV KNQDGAVVGC TALCIETGEV VYFKARATVL
210 220 230 240 250
ATGGAGRIYQ STTNAHINTG DGVGMAIRAG VPVQDMEMWQ FHPTGIAGAG
260 270 280 290 300
VLVTEGCRGE GGYLLNKHGE RFMERYAPNA KDLAGRDVVA RSIMIEIREG
310 320 330 340 350
RGCDGPWGPH AKLKLDHLGK EVLESRLPGI LELSRTFAHV DPVKEPIPVI
360 370 380 390 400
PTCHYMMGGI PTKVTGQALT VNEKGEDVVV PGLFAVGEIA CVSVHGANRL
410 420 430 440 450
GGNSLLDLVV FGRAAGLHLQ ESIAEQGALR DASESDVEAS LDRLNRWNNN
460 470 480 490 500
RNGEDPVAIR KALQECMQHN FSVFREGDAM AKGLEQLKVI RERLKNARLD
510 520 530 540 550
DTSSEFNTQR VECLELDNLM ETAYATAVSA NFRTESRGAH SRFDFPDRDD
560 570 580
ENWLCHSLYL PESESMTRRS VNMEPKLRPA FPPKIRTY
Length:588
Mass (Da):64,422
Last modified:November 8, 2005 - 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:i837F9A63991B6CE8
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti20 – 22MRA → IAR in AAA23895 (PubMed:6383359).Curated3
Sequence conflicti20 – 22MRA → IAR in CAA25487 (PubMed:6383359).Curated3

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: AAA23895.1
X00980 Genomic DNA Translation: CAA25487.1
U00096 Genomic DNA Translation: AAC73817.1
AP009048 Genomic DNA Translation: BAA35390.1
X01070 Genomic DNA Translation: CAA25533.1

Protein sequence database of the Protein Information Resource

More...
PIRi
B64808 DEECSF

NCBI Reference Sequences

More...
RefSeqi
NP_415251.1, NC_000913.3
WP_000775540.1, NZ_LN832404.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAC73817; AAC73817; b0723
BAA35390; BAA35390; BAA35390

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
945402

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ecj:JW0713
eco:b0723

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|1411691.4.peg.1549

<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: AAA23895.1
X00980 Genomic DNA Translation: CAA25487.1
U00096 Genomic DNA Translation: AAC73817.1
AP009048 Genomic DNA Translation: BAA35390.1
X01070 Genomic DNA Translation: CAA25533.1
PIRiB64808 DEECSF
RefSeqiNP_415251.1, NC_000913.3
WP_000775540.1, NZ_LN832404.1

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
1NEKX-ray2.60A1-588[»]
1NENX-ray2.90A1-588[»]
2ACZX-ray3.10A1-588[»]
2AD0model-A1-588[»]
2WDQX-ray2.40A/E/I1-588[»]
2WDRX-ray3.20A/E/I1-588[»]
2WDVX-ray3.20A/E/I1-588[»]
2WP9X-ray2.70A/E/I1-588[»]
2WS3X-ray3.20A/E/I1-588[»]
2WU2X-ray2.50A/E/I1-588[»]
2WU5X-ray2.80A/E/I1-588[»]
ProteinModelPortaliP0AC41
SMRiP0AC41
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262907, 31 interactors
ComplexPortaliCPX-1931 Respiratory chain complex II
DIPiDIP-31877N
IntActiP0AC41, 91 interactors
MINTiP0AC41
STRINGi316385.ECDH10B_0790

Chemistry databases

DrugBankiDB04631 Atpenin A5
DB08690 UBIQUINONE-2

PTM databases

iPTMnetiP0AC41

2D gel databases

SWISS-2DPAGEiP0AC41

Proteomic databases

EPDiP0AC41
PaxDbiP0AC41
PRIDEiP0AC41

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73817; AAC73817; b0723
BAA35390; BAA35390; BAA35390
GeneIDi945402
KEGGiecj:JW0713
eco:b0723
PATRICifig|1411691.4.peg.1549

Organism-specific databases

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

More...
EchoBASEi
EB0924
EcoGeneiEG10931 sdhA

Phylogenomic databases

eggNOGiENOG4105C00 Bacteria
COG1053 LUCA
HOGENOMiHOG000160475
InParanoidiP0AC41
KOiK00239
PhylomeDBiP0AC41

Enzyme and pathway databases

UniPathwayi
UPA00223;UER01005

BioCyciEcoCyc:SDH-FLAVO
MetaCyc:SDH-FLAVO
BRENDAi1.3.5.1 2026

Miscellaneous databases

EvolutionaryTraceiP0AC41

Protein Ontology

More...
PROi
PR:P0AC41

Family and domain databases

Gene3Di3.50.50.60, 1 hit
3.90.700.10, 1 hit
InterProiView protein in InterPro
IPR003953 FAD-binding_2
IPR036188 FAD/NAD-bd_sf
IPR003952 FRD_SDH_FAD_BS
IPR037099 Fum_R/Succ_DH_flav-like_C_sf
IPR015939 Fum_Rdtase/Succ_DH_flav-like_C
IPR027477 Succ_DH/fumarate_Rdtase_cat_sf
IPR011281 Succ_DH_flav_su_fwd
IPR014006 Succ_Dhase_FrdA_Gneg
PfamiView protein in Pfam
PF00890 FAD_binding_2, 1 hit
PF02910 Succ_DH_flav_C, 1 hit
SUPFAMiSSF46977 SSF46977, 1 hit
SSF51905 SSF51905, 1 hit
SSF56425 SSF56425, 1 hit
TIGRFAMsiTIGR01816 sdhA_forward, 1 hit
TIGR01812 sdhA_frdA_Gneg, 1 hit
PROSITEiView protein in PROSITE
PS00504 FRD_SDH_FAD_BINDING, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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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 nameiSDHA_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: P0AC41
Secondary accession number(s): P10444, P78282
<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: November 8, 2005
Last sequence update: November 8, 2005
Last modified: December 5, 2018
This is version 120 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, 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
  4. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
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