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UniProtKB - P0ACB2 (HEM2_ECOLI)

Entry version 120 (17 Jun 2020)
Sequence version 2 (23 Jan 2007)
Previous versions | rss
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Protein

Delta-aminolevulinic acid dehydratase

Gene

hemB

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

Catalyzes an early step in the biosynthesis of tetrapyrroles. Binds two molecules of 5-aminolevulinate per subunit, each at a distinct site, and catalyzes their condensation to form porphobilinogen.

<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

Zn2+4 PublicationsNote: Binds 1 zinc ion per monomer.4 Publications

<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

Allosteric enzyme. Stimulated by magnesium ions.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: protoporphyrin-IX biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes coproporphyrinogen-III from 5-aminolevulinate.
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. Delta-aminolevulinic acid dehydratase (hemB)
  2. Porphobilinogen deaminase (hemC)
  3. Uroporphyrinogen-III synthase (hemD), Uroporphyrinogen-III synthase (hemD)
  4. Uroporphyrinogen decarboxylase (hemE), Uroporphyrinogen decarboxylase (hemE)
This subpathway is part of the pathway protoporphyrin-IX biosynthesis, which is itself part of Porphyrin-containing compound metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes coproporphyrinogen-III from 5-aminolevulinate, the pathway protoporphyrin-IX biosynthesis and in Porphyrin-containing compound metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 bindingi120Zinc; catalytic2 Publications1
Metal bindingi122Zinc; catalytic2 Publications1
Metal bindingi130Zinc; catalytic2 Publications1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 sitei195Schiff-base intermediate with substrate1
<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 sitei205Substrate 11
Binding sitei216Substrate 11
Metal bindingi232Magnesium2 Publications1
Active sitei247Schiff-base intermediate with substrate1
Binding sitei273Substrate 21
Binding sitei312Substrate 21

<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

Complete GO annotation on QuickGO ...

GO - Biological processi

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 functionAllosteric enzyme, Lyase
Biological processHeme biosynthesis, Porphyrin biosynthesis
LigandMagnesium, Metal-binding, Zinc

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		EcoCyc:PORPHOBILSYNTH-MONOMER
ECOL316407:JW0361-MONOMER
MetaCyc:PORPHOBILSYNTH-MONOMER

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		4.2.1.24 2026

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

More...UniPathwayi		UPA00251;UER00318

<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:
Delta-aminolevulinic acid dehydratase (EC:4.2.1.24)
Short name:
ALAD
Short name:
ALADH
Alternative name(s):
Porphobilinogen synthase
<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:hemB
Synonyms:ncf
Ordered Locus Names:b0369, JW0361
<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 lineageiBacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia ›
<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

Complete GO annotation on QuickGO ...

<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>Mutagenesisi127H → A: No significant effect on activity; when associated with A-129. 1 Publication1
Mutagenesisi129H → A: No significant effect on activity; when associated with A-127. 1 Publication1

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL3286083

Drug and drug target database

More...DrugBanki		DB04560 4,7-Dioxosebacic Acid
DB02260 4-Oxosebacic Acid
DB04530 S,S-(2-Hydroxyethyl)Thiocysteine

<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 <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved1 Publication
<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_00001405012 – 324Delta-aminolevulinic acid dehydrataseAdd BLAST323

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P0ACB2

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

More...PaxDbi		P0ACB2

PRoteomics IDEntifications database

More...PRIDEi		P0ACB2

2D gel databases

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

More...SWISS-2DPAGEi		P0ACB2

<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

Homooctamer.

3 Publications

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		4261502, 26 interactors

Database of interacting proteins

More...DIPi		DIP-36209N

Protein interaction database and analysis system

More...IntActi		P0ACB2, 8 interactors

Molecular INTeraction database

More...MINTi		P0ACB2

STRING: functional protein association networks

More...STRINGi		511145.b0369

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		P0ACB2

<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

1324
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		P0ACB2

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		P0ACB2

<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

Belongs to the ALAD family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		ENOG4105D52 Bacteria
COG0113 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_035731_0_0_6

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P0ACB2

KEGG Orthology (KO)

More...KOi		K01698

Database for complete collections of gene phylogenies

More...PhylomeDBi		P0ACB2

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		3.20.20.70, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR001731 ALAD
IPR030656 ALAD_AS
IPR013785 Aldolase_TIM

The PANTHER Classification System

More...PANTHERi		PTHR11458 PTHR11458, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00490 ALAD, 1 hit

PIRSF; a whole-protein classification database

More...PIRSFi		PIRSF001415 Porphbilin_synth, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00144 DALDHYDRTASE

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM01004 ALAD, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00169 D_ALA_DEHYDRATASE, 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.

<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 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.

P0ACB2-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MTDLIQRPRR LRKSPALRAM FEETTLSLND LVLPIFVEEE IDDYKAVEAM 
        60         70         80         90        100
PGVMRIPEKH LAREIERIAN AGIRSVMTFG ISHHTDETGS DAWREDGLVA 
       110        120        130        140        150
RMSRICKQTV PEMIVMSDTC FCEYTSHGHC GVLCEHGVDN DATLENLGKQ 
       160        170        180        190        200
AVVAAAAGAD FIAPSAAMDG QVQAIRQALD AAGFKDTAIM SYSTKFASSF 
       210        220        230        240        250
YGPFREAAGS ALKGDRKSYQ MNPMNRREAI RESLLDEAQG ADCLMVKPAG 
       260        270        280        290        300
AYLDIVRELR ERTELPIGAY QVSGEYAMIK FAALAGAIDE EKVVLESLGS 
       310        320 
IKRAGADLIF SYFALDLAEK KILR
Length:324
Mass (Da):35,625
Last modified:January 23, 2007 - 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:iCE814E5705BFD255
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 AAB18092 differs from that shown. Reason: Erroneous initiation. Extended N-terminus.Curated
The sequence BAA12842 differs from that shown. Reason: Erroneous initiation. Extended N-terminus.Curated

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 conflicti18 – 19RA → PR in AAA62629 (PubMed:2656410).Curated2
Sequence conflicti19 – 42AMFEE…EEEID → VCLKRQHLSLTTWCCRSLLK KKLT in CAA35467 (PubMed:2464127).CuratedAdd BLAST24
Sequence conflicti90 – 91SD → ER in AAA62629 (PubMed:2656410).Curated2
Sequence conflicti104R → P in AAA62629 (PubMed:2656410).Curated1
Sequence conflicti226R → P in CAA35467 (PubMed:2464127).Curated1
Sequence conflicti227R → A in AAA62629 (PubMed:2656410).Curated1
Sequence conflicti229A → G in AAA62629 (PubMed:2656410).Curated1
Sequence conflicti231R → A in AAA62629 (PubMed:2656410).Curated1
Sequence conflicti233S → Y in AAA62629 (PubMed:2656410).Curated1
Sequence conflicti241A → P in AAA62629 (PubMed:2656410).Curated1
Sequence conflicti254D → N in AAA62629 (PubMed:2656410).Curated1

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
M24488 Genomic DNA Translation: AAA62629.1
X17417 Genomic DNA Translation: CAA35467.1
L44595 Genomic DNA Translation: AAB52499.1
D85613 Genomic DNA Translation: BAA12842.1 Different initiation.
U73857 Genomic DNA Translation: AAB18092.1 Different initiation.
U00096 Genomic DNA Translation: AAC73472.2
AP009048 Genomic DNA Translation: BAE76150.1

Protein sequence database of the Protein Information Resource

More...PIRi		A64765 SYECPF

NCBI Reference Sequences

More...RefSeqi		NP_414903.4, NC_000913.3
WP_001295337.1, NZ_STEB01000036.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...EnsemblBacteriai		AAC73472; AAC73472; b0369
BAE76150; BAE76150; BAE76150

Database of genes from NCBI RefSeq genomes

More...GeneIDi		945017

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		ecj:JW0361
eco:b0369

Pathosystems Resource Integration Center (PATRIC)

More...PATRICi		fig|1411691.4.peg.1910

<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
M24488 Genomic DNA Translation: AAA62629.1
X17417 Genomic DNA Translation: CAA35467.1
L44595 Genomic DNA Translation: AAB52499.1
D85613 Genomic DNA Translation: BAA12842.1 Different initiation.
U73857 Genomic DNA Translation: AAB18092.1 Different initiation.
U00096 Genomic DNA Translation: AAC73472.2
AP009048 Genomic DNA Translation: BAE76150.1
PIRiA64765 SYECPF
RefSeqiNP_414903.4, NC_000913.3
WP_001295337.1, NZ_STEB01000036.1

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
1B4EX-ray2.00A2-324[»]
1I8JX-ray1.90A/B2-324[»]
1L6SX-ray1.70A/B2-324[»]
1L6YX-ray1.90A/B2-324[»]
5MHBX-ray2.10A1-324[»]
SMRiP0ACB2
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi4261502, 26 interactors
DIPiDIP-36209N
IntActiP0ACB2, 8 interactors
MINTiP0ACB2
STRINGi511145.b0369

Chemistry databases

BindingDBiP0ACB2
ChEMBLiCHEMBL3286083
DrugBankiDB04560 4,7-Dioxosebacic Acid
DB02260 4-Oxosebacic Acid
DB04530 S,S-(2-Hydroxyethyl)Thiocysteine

2D gel databases

SWISS-2DPAGEiP0ACB2

Proteomic databases

jPOSTiP0ACB2
PaxDbiP0ACB2
PRIDEiP0ACB2

Genome annotation databases

EnsemblBacteriaiAAC73472; AAC73472; b0369
BAE76150; BAE76150; BAE76150
GeneIDi945017
KEGGiecj:JW0361
eco:b0369
PATRICifig|1411691.4.peg.1910

Organism-specific databases

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

More...EchoBASEi		EB0423

Phylogenomic databases

eggNOGiENOG4105D52 Bacteria
COG0113 LUCA
HOGENOMiCLU_035731_0_0_6
InParanoidiP0ACB2
KOiK01698
PhylomeDBiP0ACB2

Enzyme and pathway databases

UniPathwayiUPA00251;UER00318
BioCyciEcoCyc:PORPHOBILSYNTH-MONOMER
ECOL316407:JW0361-MONOMER
MetaCyc:PORPHOBILSYNTH-MONOMER
BRENDAi4.2.1.24 2026

Miscellaneous databases

EvolutionaryTraceiP0ACB2

Protein Ontology

More...PROi		PR:P0ACB2

Family and domain databases

Gene3Di3.20.20.70, 1 hit
InterProiView protein in InterPro
IPR001731 ALAD
IPR030656 ALAD_AS
IPR013785 Aldolase_TIM
PANTHERiPTHR11458 PTHR11458, 1 hit
PfamiView protein in Pfam
PF00490 ALAD, 1 hit
PIRSFiPIRSF001415 Porphbilin_synth, 1 hit
PRINTSiPR00144 DALDHYDRTASE
SMARTiView protein in SMART
SM01004 ALAD, 1 hit
PROSITEiView protein in PROSITE
PS00169 D_ALA_DEHYDRATASE, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		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 nameiHEM2_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: P0ACB2
Secondary accession number(s): P15002, P78247, Q2MC56
<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: November 8, 2005
Last sequence update: January 23, 2007
Last modified: June 17, 2020
This is version 120 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 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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