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UniProtKB - P0AEA8 (CYSG_ECOLI)

Entry version 122 (11 Dec 2019)
Sequence version 1 (06 Dec 2005)
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Protein

Siroheme synthase

Gene

cysG

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

Multifunctional enzyme that catalyzes the SAM-dependent methylations of uroporphyrinogen III at position C-2 and C-7 to form precorrin-2 via precorrin-1. Then it catalyzes the NAD-dependent ring dehydrogenation of precorrin-2 to yield sirohydrochlorin. Finally, it catalyzes the ferrochelation of sirohydrochlorin to yield siroheme.UniRule annotation5 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 <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: adenosylcobalamin biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes precorrin-2 from uroporphyrinogen III.UniRule annotation
Proteins known to be involved in this subpathway in this organism are:
  1. Siroheme synthase (cysG)
This subpathway is part of the pathway adenosylcobalamin biosynthesis, which is itself part of Cofactor biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes precorrin-2 from uroporphyrinogen III, the pathway adenosylcobalamin biosynthesis and in Cofactor biosynthesis.

Pathwayi: adenosylcobalamin biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes sirohydrochlorin from precorrin-2.UniRule annotation
Proteins known to be involved in this subpathway in this organism are:
  1. Siroheme synthase (cobA), Siroheme synthase (cobA), Siroheme synthase (cysG)
This subpathway is part of the pathway adenosylcobalamin biosynthesis, which is itself part of Cofactor biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes sirohydrochlorin from precorrin-2, the pathway adenosylcobalamin biosynthesis and in Cofactor biosynthesis.

Pathwayi: siroheme biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes precorrin-2 from uroporphyrinogen III.UniRule annotation
Proteins known to be involved in this subpathway in this organism are:
  1. Siroheme synthase (cobA), Siroheme synthase (cobA), Siroheme synthase (cysG)
This subpathway is part of the pathway siroheme 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 precorrin-2 from uroporphyrinogen III, the pathway siroheme biosynthesis and in Porphyrin-containing compound metabolism.

Pathwayi: siroheme biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes siroheme from sirohydrochlorin.UniRule annotation
Proteins known to be involved in this subpathway in this organism are:
  1. Siroheme synthase (cobA), Siroheme synthase (cobA), Siroheme synthase (cysG)
This subpathway is part of the pathway siroheme 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 siroheme from sirohydrochlorin, the pathway siroheme biosynthesis and in Porphyrin-containing compound metabolism.

Pathwayi: siroheme biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes sirohydrochlorin from precorrin-2.UniRule annotation
Proteins known to be involved in this subpathway in this organism are:
  1. Siroheme synthase (cobA), Siroheme synthase (cobA), Siroheme synthase (cysG)
This subpathway is part of the pathway siroheme 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 sirohydrochlorin from precorrin-2, the pathway siroheme 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_section">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 sitei225S-adenosyl-L-methionine; via carbonyl oxygenUniRule annotation1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 sitei248Proton acceptorUniRule annotation1
Active sitei270Proton donorUniRule annotation1
Binding sitei306S-adenosyl-L-methionine; via carbonyl oxygenUniRule annotation1
Binding sitei382S-adenosyl-L-methionine; via amide nitrogenUniRule annotation1
Binding sitei411S-adenosyl-L-methionine; via amide nitrogen and carbonyl oxygenUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 bindingi22 – 23NADUniRule annotation2
Nucleotide bindingi43 – 44NADUniRule annotation2

<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 functionLyase, Methyltransferase, Multifunctional enzyme, Oxidoreductase, Transferase
Biological processCobalamin biosynthesis, Porphyrin biosynthesis
LigandNAD, S-adenosyl-L-methionine

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		EcoCyc:SIROHEMESYN-MONOMER
ECOL316407:JW3331-MONOMER
MetaCyc:SIROHEMESYN-MONOMER

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

More...UniPathwayi		UPA00148;UER00211
UPA00148;UER00222
UPA00262;UER00211
UPA00262;UER00222
UPA00262;UER00376

<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:
Siroheme synthaseUniRule annotation
Including the following 3 domains:
Uroporphyrinogen-III C-methyltransferaseUniRule annotation (EC:2.1.1.107UniRule annotation)
Short name:
Urogen III methylaseUniRule annotation
Alternative name(s):
SUMTUniRule annotation
Uroporphyrinogen III methylaseUniRule annotation
Short name:
UROMUniRule annotation
Precorrin-2 dehydrogenaseUniRule annotation (EC:1.3.1.76UniRule annotation)
Sirohydrochlorin ferrochelataseUniRule annotation (EC:4.99.1.4UniRule 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:cysGUniRule annotation
Ordered Locus Names:b3368, JW3331
<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 lineageiBacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia ›
<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

<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_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>Mutagenesisi21G → D: It has methyltransferase and ferrochelatase activities but a greatly reduced dehydrogenase activity. It is able to bind AdoMet. 1 Publication1
Mutagenesisi224G → A: It abolishes methyltransferase activity, but has dehydrogenase and ferrochelatase activities. It is unable to bind AdoMet. 1 Publication1
Mutagenesisi227D → A: It has all activities of CysG. 1 Publication1
Mutagenesisi248D → A: It abolishes methyltransferase activity, but has dehydrogenase and ferrochelatase activities. It is able to bind AdoMet. 1
Mutagenesisi270K → I: It has all activities of CysG. It is able to bind AdoMet. 1 Publication1
Mutagenesisi298R → L: It abolishes methyltransferase activity, but has dehydrogenase and ferrochelatase activities. It is unable to bind AdoMet. 1 Publication1
Mutagenesisi303D → A: It has all activities of CysG. It is able to bind AdoMet. 1 Publication1
Mutagenesisi309R → L: It abolishes methyltransferase activity, but has dehydrogenase and ferrochelatase activities. It is able to bind AdoMet. 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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001503781 – 457Siroheme synthaseAdd BLAST457

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 residuei128PhosphoserineUniRule annotation1

Keywords - PTMi

Phosphoprotein

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P0AEA8

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

More...PaxDbi		P0AEA8

PRoteomics IDEntifications database

More...PRIDEi		P0AEA8

<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

Monomer.

1 Publication

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		4262478, 6 interactors

Protein interaction database and analysis system

More...IntActi		P0AEA8, 1 interactor

STRING: functional protein association networks

More...STRINGi		511145.b3368

<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

3D structure databases

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

More...SMRi		P0AEA8

Database of comparative protein structure models

More...ModBasei		Search...

<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

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>Regioni4 – 204Precorrin-2 dehydrogenase /sirohydrochlorin ferrochelataseBy similarityAdd BLAST201
Regioni216 – 448Uroporphyrinogen-III C-methyltransferaseUniRule annotationAdd BLAST233
Regioni301 – 303S-adenosyl-L-methionine bindingUniRule annotation3
Regioni331 – 332S-adenosyl-L-methionine bindingUniRule annotation2

<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

In the N-terminal section; belongs to the precorrin-2 dehydrogenase / sirohydrochlorin ferrochelatase family.UniRule annotation
In the C-terminal section; belongs to the precorrin methyltransferase family.UniRule annotation

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		ENOG4105CB8 Bacteria
COG0007 LUCA
COG1648 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000290518

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P0AEA8

KEGG Orthology (KO)

More...KOi		K02302

Database for complete collections of gene phylogenies

More...PhylomeDBi		P0AEA8

Family and domain databases

Conserved Domains Database

More...CDDi		cd11642 SUMT, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		1.10.8.210, 1 hit
3.30.950.10, 1 hit
3.40.1010.10, 1 hit

HAMAP database of protein families

More...HAMAPi		MF_01646 Siroheme_synth, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR000878 4pyrrol_Mease
IPR035996 4pyrrol_Methylase_sf
IPR014777 4pyrrole_Mease_sub1
IPR014776 4pyrrole_Mease_sub2
IPR006366 CobA/CysG_C
IPR036291 NAD(P)-bd_dom_sf
IPR037115 Sirohaem_synt_dimer_dom_sf
IPR012409 Sirohaem_synth
IPR028281 Sirohaem_synthase_central
IPR019478 Sirohaem_synthase_dimer_dom
IPR006367 Sirohaem_synthase_N
IPR003043 Uropor_MeTrfase_CS

Pfam protein domain database

More...Pfami		View protein in Pfam
PF10414 CysG_dimeriser, 1 hit
PF14824 Sirohm_synth_M, 1 hit
PF00590 TP_methylase, 1 hit

PIRSF; a whole-protein classification database

More...PIRSFi		PIRSF036426 Sirohaem_synth, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF51735 SSF51735, 1 hit
SSF53790 SSF53790, 1 hit

TIGRFAMs; a protein family database

More...TIGRFAMsi		TIGR01469 cobA_cysG_Cterm, 1 hit
TIGR01470 cysG_Nterm, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00839 SUMT_1, 1 hit
PS00840 SUMT_2, 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>. 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_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.

P0AEA8-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MDHLPIFCQL RDRDCLIVGG GDVAERKARL LLDAGARLTV NALAFIPQFT 
        60         70         80         90        100
AWADAGMLTL VEGPFDESLL DTCWLAIAAT DDDALNQRVS EAAEARRIFC 
       110        120        130        140        150
NVVDAPKAAS FIMPSIIDRS PLMVAVSSGG TSPVLARLLR EKLESLLPLH 
       160        170        180        190        200
LGQVAKYAGQ LRGRVKQQFA TMGERRRFWE KLFVNDRLAQ SLANNDQKAI 
       210        220        230        240        250
TETTEQLINE PLDHRGEVVL VGAGPGDAGL LTLKGLQQIQ QADVVVYDRL 
       260        270        280        290        300
VSDDIMNLVR RDADRVFVGK RAGYHCVPQE EINQILLREA QKGKRVVRLK 
       310        320        330        340        350
GGDPFIFGRG GEELETLCNA GIPFSVVPGI TAASGCSAYS GIPLTHRDYA 
       360        370        380        390        400
QSVRLITGHL KTGGELDWEN LAAEKQTLVF YMGLNQAATI QQKLIEHGMP 
       410        420        430        440        450
GEMPVAIVEN GTAVTQRVID GTLTQLGELA QQMNSPSLII IGRVVGLRDK 

LNWFSNH
Length:457
Mass (Da):49,951
Last modified:December 6, 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:iDDDE0DC90C5CF2F4
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 conflicti26R → P in CAA32419 (PubMed:2543955).Curated1
Sequence conflicti26R → P in AAA58165 (PubMed:2200672).Curated1
Sequence conflicti90 – 91SE → RQ in CAA32419 (PubMed:2543955).Curated2
Sequence conflicti90 – 91SE → RQ in AAA58165 (PubMed:2200672).Curated2

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
X14202 Genomic DNA Translation: CAA32419.1
U18997 Genomic DNA Translation: AAA58165.1
U00096 Genomic DNA Translation: AAC76393.1
AP009048 Genomic DNA Translation: BAE77922.1

Protein sequence database of the Protein Information Resource

More...PIRi		C65131

NCBI Reference Sequences

More...RefSeqi		NP_417827.1, NC_000913.3
WP_000349855.1, NZ_STEB01000004.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...EnsemblBacteriai		AAC76393; AAC76393; b3368
BAE77922; BAE77922; BAE77922

Database of genes from NCBI RefSeq genomes

More...GeneIDi		947880

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		ecj:JW3331
eco:b3368

Pathosystems Resource Integration Center (PATRIC)

More...PATRICi		fig|1411691.4.peg.3361

<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
X14202 Genomic DNA Translation: CAA32419.1
U18997 Genomic DNA Translation: AAA58165.1
U00096 Genomic DNA Translation: AAC76393.1
AP009048 Genomic DNA Translation: BAE77922.1
PIRiC65131
RefSeqiNP_417827.1, NC_000913.3
WP_000349855.1, NZ_STEB01000004.1

3D structure databases

SMRiP0AEA8
ModBaseiSearch...

Protein-protein interaction databases

BioGridi4262478, 6 interactors
IntActiP0AEA8, 1 interactor
STRINGi511145.b3368

Proteomic databases

jPOSTiP0AEA8
PaxDbiP0AEA8
PRIDEiP0AEA8

Genome annotation databases

EnsemblBacteriaiAAC76393; AAC76393; b3368
BAE77922; BAE77922; BAE77922
GeneIDi947880
KEGGiecj:JW3331
eco:b3368
PATRICifig|1411691.4.peg.3361

Organism-specific databases

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

More...EchoBASEi		EB0185

Phylogenomic databases

eggNOGiENOG4105CB8 Bacteria
COG0007 LUCA
COG1648 LUCA
HOGENOMiHOG000290518
InParanoidiP0AEA8
KOiK02302
PhylomeDBiP0AEA8

Enzyme and pathway databases

UniPathwayiUPA00148;UER00211
UPA00148;UER00222
UPA00262;UER00211
UPA00262;UER00222
UPA00262;UER00376
BioCyciEcoCyc:SIROHEMESYN-MONOMER
ECOL316407:JW3331-MONOMER
MetaCyc:SIROHEMESYN-MONOMER

Miscellaneous databases

Protein Ontology

More...PROi		PR:P0AEA8

Family and domain databases

CDDicd11642 SUMT, 1 hit
Gene3Di1.10.8.210, 1 hit
3.30.950.10, 1 hit
3.40.1010.10, 1 hit
HAMAPiMF_01646 Siroheme_synth, 1 hit
InterProiView protein in InterPro
IPR000878 4pyrrol_Mease
IPR035996 4pyrrol_Methylase_sf
IPR014777 4pyrrole_Mease_sub1
IPR014776 4pyrrole_Mease_sub2
IPR006366 CobA/CysG_C
IPR036291 NAD(P)-bd_dom_sf
IPR037115 Sirohaem_synt_dimer_dom_sf
IPR012409 Sirohaem_synth
IPR028281 Sirohaem_synthase_central
IPR019478 Sirohaem_synthase_dimer_dom
IPR006367 Sirohaem_synthase_N
IPR003043 Uropor_MeTrfase_CS
PfamiView protein in Pfam
PF10414 CysG_dimeriser, 1 hit
PF14824 Sirohm_synth_M, 1 hit
PF00590 TP_methylase, 1 hit
PIRSFiPIRSF036426 Sirohaem_synth, 1 hit
SUPFAMiSSF51735 SSF51735, 1 hit
SSF53790 SSF53790, 1 hit
TIGRFAMsiTIGR01469 cobA_cysG_Cterm, 1 hit
TIGR01470 cysG_Nterm, 1 hit
PROSITEiView protein in PROSITE
PS00839 SUMT_1, 1 hit
PS00840 SUMT_2, 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 nameiCYSG_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: P0AEA8
Secondary accession number(s): P11098, P76685, Q2M734
<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: December 6, 2005
Last sequence update: December 6, 2005
Last modified: December 11, 2019
This is version 122 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

Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
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