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UniProtKB - P77455 (PAAZ_ECOLI)

Entry version 154 (25 May 2022)
Sequence version 1 (01 Feb 1997)
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Protein

Bifunctional protein PaaZ

Gene

paaZ

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 the hydrolytic ring cleavage of 2-oxepin-2(3H)-ylideneacetyl-CoA (oxepin-CoA) via the open-chain aldehyde intermediate to yield 3-oxo-5,6-dehydrosuberyl-CoA. The enzyme consists of a C-terminal (R)-specific enoyl-CoA hydratase domain (formerly MaoC) that cleaves the ring and produces the highly reactive 3-oxo-5,6-dehydrosuberyl-CoA semialdehyde and an N-terminal NADP-dependent aldehyde dehydrogenase domain that oxidizes the aldehyde to 3-oxo-5,6-dehydrosuberyl-CoA. Can also use crotonyl-CoA as substrate.

3 Publications

<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 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=11 µM for oxepin-CoA (at 22 degrees Celsius and pH 8)1 Publication
  2. KM=56 µM for NADP (at 22 degrees Celsius and pH 8)1 Publication

pH dependencei

Optimum pH is 8.1 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: phenylacetate degradation

This protein is involved in the pathway phenylacetate degradation, which is part of Aromatic compound metabolism.
View all proteins of this organism that are known to be involved in the pathway phenylacetate degradation and in Aromatic 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 is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei256By similarity1
Active sitei295By similarity1

<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

  • phenylacetate catabolic process Source: UniProtKB
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 functionHydrolase, Lyase, Multifunctional enzyme, Oxidoreductase
LigandNADP

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		EcoCyc:G6708-MONOMER

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		3.3.2.12, 2026

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

More...UniPathwayi		UPA00930

<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:
Bifunctional protein PaaZ
Including the following 2 domains:
2-oxepin-2(3H)-ylideneacetyl-CoA hydrolase (EC:3.3.2.12)
Alternative name(s):
Oxepin-CoA hydrolase
3-oxo-5,6-dehydrosuberyl-CoA semialdehyde dehydrogenase (EC:1.2.1.911 Publication)
<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:paaZ
Synonyms:maoC, ydbN
Ordered Locus Names:b1387, JW1382
<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 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

Disruption causes the conversion of phenylacetate (PA) into 2-hydroxyphenylacetate (2-HPA).1 Publication

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>Mutagenesisi256E → Q: Catalyzes the formation of 3-oxo-5,6-dehydrosuberyl-CoA semialdehyde instead of 3-oxo-5,6-dehydrosuberyl-CoA. 1 Publication1

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

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000565811 – 681Bifunctional protein PaaZAdd BLAST681

Proteomic databases

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

More...PaxDbi		P77455

PRoteomics IDEntifications database

More...PRIDEi		P77455

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Activated by cAMP receptor protein (CRP) and integration host factor (IHF). Inhibited by PaaX.1 Publication

<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

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		4260176, 262 interactors

Protein interaction database and analysis system

More...IntActi		P77455, 3 interactors

STRING: functional protein association networks

More...STRINGi		511145.b1387

<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

1681
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

AlphaFold Protein Structure Database

More...AlphaFoldDBi		P77455

Small Angle Scattering Biological Data Bank

More...SASBDBi		P77455

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

More...SMRi		P77455

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini537 – 648MaoC-likeAdd BLAST112

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>Regioni1 – 333Aldehyde dehydrogenaseAdd BLAST333
Regioni456 – 484DisorderedSequence analysisAdd BLAST29

<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 aldehyde dehydrogenase family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		COG1012, Bacteria
COG2030, Bacteria

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_025047_0_0_6

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P77455

Identification of Orthologs from Complete Genome Data

More...OMAi		DTFYAHM

Database for complete collections of gene phylogenies

More...PhylomeDBi		P77455

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		3.40.309.10, 1 hit
3.40.605.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR016161, Ald_DH/histidinol_DH
IPR016163, Ald_DH_C
IPR016162, Ald_DH_N
IPR015590, Aldehyde_DH_dom
IPR029069, HotDog_dom_sf
IPR002539, MaoC-like_dom
IPR011966, PaaN-DH

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00171, Aldedh, 1 hit
PF01575, MaoC_dehydratas, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF53720, SSF53720, 1 hit
SSF54637, SSF54637, 1 hit

TIGRFAMs; a protein family database

More...TIGRFAMsi		TIGR02278, PaaN-DH, 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.

P77455-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MQQLASFLSG TWQSGRGRSR LIHHAISGEA LWEVTSEGLD MAAARQFAIE 
        60         70         80         90        100
KGAPALRAMT FIERAAMLKA VAKHLLSEKE RFYALSAQTG ATRADSWVDI 
       110        120        130        140        150
EGGIGTLFTY ASLGSRELPD DTLWPEDELI PLSKEGGFAA RHLLTSKSGV 
       160        170        180        190        200
AVHINAFNFP CWGMLEKLAP TWLGGMPAII KPATATAQLT QAMVKSIVDS 
       210        220        230        240        250
GLVPEGAISL ICGSAGDLLD HLDSQDVVTF TGSAATGQML RVQPNIVAKS 
       260        270        280        290        300
IPFTMEADSL NCCVLGEDVT PDQPEFALFI REVVREMTTK AGQKCTAIRR 
       310        320        330        340        350
IIVPQALVNA VSDALVARLQ KVVVGDPAQE GVKMGALVNA EQRADVQEKV 
       360        370        380        390        400
NILLAAGCEI RLGGQADLSA AGAFFPPTLL YCPQPDETPA VHATEAFGPV 
       410        420        430        440        450
ATLMPAQNQR HALQLACAGG GSLAGTLVTA DPQIARQFIA DAARTHGRIQ 
       460        470        480        490        500
ILNEESAKES TGHGSPLPQL VHGGPGRAGG GEELGGLRAV KHYMQRTAVQ 
       510        520        530        540        550
GSPTMLAAIS KQWVRGAKVE EDRIHPFRKY FEELQPGDSL LTPRRTMTEA 
       560        570        580        590        600
DIVNFACLSG DHFYAHMDKI AAAESIFGER VVHGYFVLSA AAGLFVDAGV 
       610        620        630        640        650
GPVIANYGLE SLRFIEPVKP GDTIQVRLTC KRKTLKKQRS AEEKPTGVVE 
       660        670        680 
WAVEVFNQHQ TPVALYSILT LVARQHGDFV D
Length:681
Mass (Da):73,003
Last modified:February 1, 1997 - 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:iA631B97AA37A1C3E
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural varianti143L → V in strain: W. 1
Natural varianti440A → T in strain: W. 1
Natural varianti611S → N in strain: W. 1

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
X97452 Genomic DNA Translation: CAA66089.1
U00096 Genomic DNA Translation: AAC74469.1
AP009048 Genomic DNA Translation: BAA14997.1

Protein sequence database of the Protein Information Resource

More...PIRi		F64889

NCBI Reference Sequences

More...RefSeqi		NP_415905.1, NC_000913.3
WP_001186469.1, NZ_LN832404.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...EnsemblBacteriai		AAC74469; AAC74469; b1387
BAA14997; BAA14997; BAA14997

Database of genes from NCBI RefSeq genomes

More...GeneIDi		945954

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		ecj:JW1382
eco:b1387

Pathosystems Resource Integration Center (PATRIC)

More...PATRICi		fig|1411691.4.peg.884

<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
X97452 Genomic DNA Translation: CAA66089.1
U00096 Genomic DNA Translation: AAC74469.1
AP009048 Genomic DNA Translation: BAA14997.1
PIRiF64889
RefSeqiNP_415905.1, NC_000913.3
WP_001186469.1, 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
6JQLelectron microscopy2.90A/B/C/D/E/F2-681[»]
6JQMelectron microscopy3.30A/B/C/D/E/F2-681[»]
6JQNelectron microscopy3.10A/B/C/D/E/F2-681[»]
6JQOelectron microscopy3.10A/B/C/D/E/F2-681[»]
AlphaFoldDBiP77455
SASBDBiP77455
SMRiP77455
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi4260176, 262 interactors
IntActiP77455, 3 interactors
STRINGi511145.b1387

Proteomic databases

PaxDbiP77455
PRIDEiP77455

Genome annotation databases

EnsemblBacteriaiAAC74469; AAC74469; b1387
BAA14997; BAA14997; BAA14997
GeneIDi945954
KEGGiecj:JW1382
eco:b1387
PATRICifig|1411691.4.peg.884

Organism-specific databases

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

More...EchoBASEi		EB3498

Phylogenomic databases

eggNOGiCOG1012, Bacteria
COG2030, Bacteria
HOGENOMiCLU_025047_0_0_6
InParanoidiP77455
OMAiDTFYAHM
PhylomeDBiP77455

Enzyme and pathway databases

UniPathwayiUPA00930
BioCyciEcoCyc:G6708-MONOMER
BRENDAi3.3.2.12, 2026

Miscellaneous databases

Protein Ontology

More...PROi		PR:P77455

Family and domain databases

Gene3Di3.40.309.10, 1 hit
3.40.605.10, 1 hit
InterProiView protein in InterPro
IPR016161, Ald_DH/histidinol_DH
IPR016163, Ald_DH_C
IPR016162, Ald_DH_N
IPR015590, Aldehyde_DH_dom
IPR029069, HotDog_dom_sf
IPR002539, MaoC-like_dom
IPR011966, PaaN-DH
PfamiView protein in Pfam
PF00171, Aldedh, 1 hit
PF01575, MaoC_dehydratas, 1 hit
SUPFAMiSSF53720, SSF53720, 1 hit
SSF54637, SSF54637, 1 hit
TIGRFAMsiTIGR02278, PaaN-DH, 1 hit

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 nameiPAAZ_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: P77455
Secondary accession number(s): O53009
<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 1, 1997
Last sequence update: February 1, 1997
Last modified: May 25, 2022
This is version 154 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, 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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