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Entry version 41 (25 May 2022)
Sequence version 1 (16 Apr 2014)
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Protein

Acetyl-coenzyme A synthetase

Gene

acsA

Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
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 conversion of acetate into acetyl-CoA (AcCoA), an essential intermediate at the junction of anabolic and catabolic pathways. AcsA undergoes a two-step reaction. In the first half reaction, AcsA combines acetate with ATP to form acetyl-adenylate (AcAMP) intermediate. In the second half reaction, it can then transfer the acetyl group from AcAMP to the sulfhydryl group of CoA, forming the product AcCoA. M.tuberculosis may use AcsA for both acetate and propionate assimilation.

UniRule annotation2 Publications

Miscellaneous

Could be also autoacetylated on Lys-617 in the presence of acetate as an acetyl donor and ATP. Autoacetylation is effectively inhibited by CoA. If CoA is not available or the concentration of CoA is low in vivo, the enzyme can transfer acetyl group from AcAMP to itself, resulting in autoacetylation and inactivation. When CoA is available, the acetyl group is donated to CoA forming AcCoA (PubMed:21896569).1 Publication

<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

Mg2+UniRule annotation1 Publication, Ca2+UniRule annotation1 Publication, Mn2+UniRule annotation1 Publication, Ni2+UniRule annotation1 Publication, Zn2+UniRule annotation1 PublicationNote: Magnesium, but can also use calcium, manganese, nickel or zinc ions.UniRule annotation1 Publication

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=0.35 mM for CoA (at pH 8 and at 37 degrees Celsius)1 Publication
  2. KM=1.2 mM for acetate (at pH 8 and at 37 degrees Celsius)1 Publication
  3. KM=2.1 mM for propionate (at pH 8 and at 37 degrees Celsius)1 Publication
  4. KM=5.6 mM for ATP (at pH 8 and at 37 degrees Celsius)1 Publication
  5. KM=509 mM for butyrate (at pH 8 and at 37 degrees Celsius)1 Publication

pH dependencei

Optimum pH is around 8. The enzyme is stable under neutral and alkaline conditions, while its activity decreases rapidly below pH 6.0.1 Publication

Temperature dependencei

Optimum temperature is 37 degrees Celsius. It lost its activity rapidly below 25 degrees Celsius or above 45 degrees Celsius.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 sitei311Coenzyme AUniRule annotation1
Binding sitei508ATPUniRule annotation1
Binding sitei523ATPUniRule annotation1
Binding sitei531Coenzyme A; via carbonyl oxygenUniRule annotation1
Binding sitei534ATPUniRule annotation1
<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 bindingi545Magnesium; via carbonyl oxygenUniRule annotation1
Metal bindingi547Magnesium; via carbonyl oxygenUniRule annotation1
Metal bindingi550Magnesium; via carbonyl oxygenUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 bindingi387 – 389ATPUniRule annotation3
Nucleotide bindingi411 – 416ATPUniRule annotation6

<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

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionLigase
LigandATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
P9WQD1

<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:
Acetyl-coenzyme A synthetaseUniRule annotation (EC:6.2.1.1UniRule annotation)
Short name:
AcCoA synthetaseUniRule annotation
Short name:
AcsUniRule annotation
Alternative name(s):
Acetate--CoA ligaseUniRule annotation
Acyl-activating enzymeUniRule annotation
<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:acsAUniRule annotation
Synonyms:acs
Ordered Locus Names:Rv3667
ORF Names:MTV025.015
<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>OrganismiMycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
<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 identifieri83332 [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 lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
<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
  • UP000001584 <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

Organism-specific databases

Mycobacterium tuberculosis strain H37Rv genome database

More...
TubercuListi
Rv3667

<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

<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>Mutagenesisi617K → R: Complete loss of acetyl-coenzyme A synthetase activity. 2 Publications1

<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 methionineiRemovedCombined sources
<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_00002083692 – 651Acetyl-coenzyme A synthetaseAdd BLAST650

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 residuei2N-acetylserineCombined sources1
Modified residuei617N6-acetyllysineUniRule annotation1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Acetylated on Lys-617 by Pat in the presence of acetyl-CoA as an acetyl donor and ATP. Acetylation results in the inactivation of the enzyme. Deacetylation by the SIR2-homolog deacetylase CobB is required to activate the enzyme.1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

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

More...
PaxDbi
P9WQD1

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P9WQD1

<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

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
83332.Rv3667

<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

AlphaFold Protein Structure Database

More...
AlphaFoldDBi
P9WQD1

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

More...
SMRi
P9WQD1

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>Regioni190 – 193Coenzyme A bindingUniRule annotation4

<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 ATP-dependent AMP-binding enzyme family.UniRule annotation

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
COG0365, Bacteria

Identification of Orthologs from Complete Genome Data

More...
OMAi
DHWWHDL

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P9WQD1

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.30.300.30, 1 hit
3.40.50.12780, 1 hit

HAMAP database of protein families

More...
HAMAPi
MF_01123, Ac_CoA_synth, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR011904, Ac_CoA_lig
IPR032387, ACAS_N
IPR025110, AMP-bd_C
IPR045851, AMP-bd_C_sf
IPR020845, AMP-binding_CS
IPR000873, AMP-dep_Synth/Lig
IPR042099, ANL_N_sf

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF16177, ACAS_N, 1 hit
PF00501, AMP-binding, 1 hit
PF13193, AMP-binding_C, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR02188, Ac_CoA_lig_AcsA, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00455, AMP_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%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.

P9WQD1-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSESTPEVSS SYPPPAHFAE HANARAELYR EAEEDRLAFW AKQANRLSWT
60 70 80 90 100
TPFTEVLDWS GAPFAKWFVG GELNVAYNCV DRHVEAGHGD RVAIHWEGEP
110 120 130 140 150
VGDRRTLTYS DLLAEVSKAA NALTDLGLVA GDRVAIYLPL IPEAVIAMLA
160 170 180 190 200
CARLGIMHSV VFGGFTAAAL QARIVDAQAK LLITADGQFR RGKPSPLKAA
210 220 230 240 250
ADEALAAIPD CSVEHVLVVR RTGIEMAWSE GRDLWWHHVV GSASPAHTPE
260 270 280 290 300
PFDSEHPLFL LYTSGTTGKP KGIMHTSGGY LTQCCYTMRT IFDVKPDSDV
310 320 330 340 350
FWCTADIGWV TGHTYGVYGP LCNGVTEVLY EGTPDTPDRH RHFQIIEKYG
360 370 380 390 400
VTIYYTAPTL IRMFMKWGRE IPDSHDLSSL RLLGSVGEPI NPEAWRWYRD
410 420 430 440 450
VIGGGRTPLV DTWWQTETGS AMISPLPGIA AAKPGSAMTP LPGISAKIVD
460 470 480 490 500
DHGDPLPPHT EGAQHVTGYL VLDQPWPSML RGIWGDPARY WHSYWSKFSD
510 520 530 540 550
KGYYFAGDGA RIDPDGAIWV LGRIDDVMNV SGHRISTAEV ESALVAHSGV
560 570 580 590 600
AEAAVVGVTD ETTTQAICAF VVLRANYAPH DRTAEELRTE VARVISPIAR
610 620 630 640 650
PRDVHVVPEL PKTRSGKIMR RLLRDVAENR ELGDTSTLLD PTVFDAIRAA

K
Length:651
Mass (Da):71,476
Last modified:April 16, 2014 - 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:i94290C0517A0445B
GO

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
AL123456 Genomic DNA Translation: CCP46490.1

Protein sequence database of the Protein Information Resource

More...
PIRi
D70789

NCBI Reference Sequences

More...
RefSeqi
NP_218184.1, NC_000962.3
WP_003899631.1, NZ_NVQJ01000028.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
885479

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
mtu:Rv3667

<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
AL123456 Genomic DNA Translation: CCP46490.1
PIRiD70789
RefSeqiNP_218184.1, NC_000962.3
WP_003899631.1, NZ_NVQJ01000028.1

3D structure databases

AlphaFoldDBiP9WQD1
SMRiP9WQD1
ModBaseiSearch...

Protein-protein interaction databases

STRINGi83332.Rv3667

PTM databases

iPTMnetiP9WQD1

Proteomic databases

PaxDbiP9WQD1

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
885479

Genome annotation databases

GeneIDi885479
KEGGimtu:Rv3667

Organism-specific databases

TubercuListiRv3667

Phylogenomic databases

eggNOGiCOG0365, Bacteria
OMAiDHWWHDL
PhylomeDBiP9WQD1

Enzyme and pathway databases

SABIO-RKiP9WQD1

Family and domain databases

Gene3Di3.30.300.30, 1 hit
3.40.50.12780, 1 hit
HAMAPiMF_01123, Ac_CoA_synth, 1 hit
InterProiView protein in InterPro
IPR011904, Ac_CoA_lig
IPR032387, ACAS_N
IPR025110, AMP-bd_C
IPR045851, AMP-bd_C_sf
IPR020845, AMP-binding_CS
IPR000873, AMP-dep_Synth/Lig
IPR042099, ANL_N_sf
PfamiView protein in Pfam
PF16177, ACAS_N, 1 hit
PF00501, AMP-binding, 1 hit
PF13193, AMP-binding_C, 1 hit
TIGRFAMsiTIGR02188, Ac_CoA_lig_AcsA, 1 hit
PROSITEiView protein in PROSITE
PS00455, AMP_BINDING, 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 nameiACSA_MYCTU
<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: P9WQD1
Secondary accession number(s): L0TGD8, O69635
<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: April 16, 2014
Last sequence update: April 16, 2014
Last modified: May 25, 2022
This is version 41 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

Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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