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Entry version 188 (29 Sep 2021)
Sequence version 3 (23 Jan 2007)
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Protein

Glutamate synthase [NADPH] small chain

Gene

gltD

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 conversion of L-glutamine and 2-oxoglutarate into two molecules of L-glutamate.

1 Publication

Miscellaneous

Glutamine binds to the large subunit and transfers the amido group to 2-oxoglutarate that apparently binds to the small subunit.

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

[4Fe-4S] clusterPROSITE-ProRule annotationNote: Binds 1 [4Fe-4S] cluster.PROSITE-ProRule annotation

<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=7.3 µM for 2-oxoglutarate1 Publication
  2. KM=250 µM for L-glutamine1 Publication

pH dependencei

Optimum pH is 7.6.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: L-glutamate biosynthesis via GLT pathway

This protein is involved in step 1 of the subpathway that synthesizes L-glutamate from 2-oxoglutarate and L-glutamine (NADP(+) route). This subpathway is part of the pathway L-glutamate biosynthesis via GLT pathway, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-glutamate from 2-oxoglutarate and L-glutamine (NADP(+) route), the pathway L-glutamate biosynthesis via GLT pathway and in Amino-acid biosynthesis.

Pathwayi: nitrogen metabolism

This protein is involved in the pathway nitrogen metabolism, which is part of Energy metabolism.
View all proteins of this organism that are known to be involved in the pathway nitrogen metabolism and in Energy metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 bindingi47Iron-sulfur (4Fe-4S)PROSITE-ProRule annotation1
Metal bindingi50Iron-sulfur (4Fe-4S)PROSITE-ProRule annotation1
Metal bindingi55Iron-sulfur (4Fe-4S)PROSITE-ProRule annotation1
Metal bindingi59Iron-sulfur (4Fe-4S)PROSITE-ProRule annotation1

<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

  • 4 iron, 4 sulfur cluster binding Source: UniProtKB-KW
  • glutamate synthase (NADPH) activity Source: EcoCyc
  • metal ion binding Source: UniProtKB-KW

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 functionOxidoreductase
Biological processAmino-acid biosynthesis, Glutamate biosynthesis
Ligand4Fe-4S, Iron, Iron-sulfur, Metal-binding, NADP

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
EcoCyc:GLUSYNSMALL-MONOMER
MetaCyc:GLUSYNSMALL-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
1.4.1.13, 2026

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
P09832

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

More...
UniPathwayi
UPA00045
UPA00634;UER00689

<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:
Glutamate synthase [NADPH] small chain (EC:1.4.1.131 Publication)
Alternative name(s):
Glutamate synthase subunit beta
Short name:
GLTS beta chain
NADPH-GOGAT
<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:gltD
Synonyms:aspB
Ordered Locus Names:b3213, JW3180
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiEscherichia coli (strain K12)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri83333 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000318 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

<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 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_processing_section">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 methionineiRemoved2 Publications
<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_00001708002 – 472Glutamate synthase [NADPH] small chainAdd BLAST471

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P09832

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

More...
PaxDbi
P09832

PRoteomics IDEntifications database

More...
PRIDEi
P09832

2D gel databases

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

More...
SWISS-2DPAGEi
P09832

<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

Aggregate of 4 catalytic active heterodimers, consisting of a large and a small subunit.

1 Publication

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
4262427, 198 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-5041, Glutamate synthase [NADPH] complex

Database of interacting proteins

More...
DIPi
DIP-9803N

Protein interaction database and analysis system

More...
IntActi
P09832, 6 interactors

STRING: functional protein association networks

More...
STRINGi
511145.b3213

<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
P09832

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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">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>Domaini38 – 694Fe-4S ferredoxin-typePROSITE-ProRule annotationAdd BLAST32

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
COG0493, Bacteria

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_000422_3_3_6

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P09832

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P09832

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.10.1060.10, 1 hit
3.50.50.60, 2 hits

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR017896, 4Fe4S_Fe-S-bd
IPR028261, DPD_II
IPR036188, FAD/NAD-bd_sf
IPR023753, FAD/NAD-binding_dom
IPR006006, GltD-like
IPR009051, Helical_ferredxn

The PANTHER Classification System

More...
PANTHERi
PTHR42783:SF1, PTHR42783:SF1, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF14691, Fer4_20, 1 hit
PF07992, Pyr_redox_2, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR01318, gltD_gamma_fam, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS51379, 4FE4S_FER_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.

<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 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.

P09832-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSQNVYQFID LQRVDPPKKP LKIRKIEFVE IYEPFSEGQA KAQADRCLSC
60 70 80 90 100
GNPYCEWKCP VHNYIPNWLK LANEGRIFEA AELSHQTNTL PEVCGRVCPQ
110 120 130 140 150
DRLCEGSCTL NDEFGAVTIG NIERYINDKA FEMGWRPDMS GVKQTGKKVA
160 170 180 190 200
IIGAGPAGLA CADVLTRNGV KAVVFDRHPE IGGLLTFGIP AFKLEKEVMT
210 220 230 240 250
RRREIFTGMG IEFKLNTEVG RDVQLDDLLS DYDAVFLGVG TYQSMRGGLE
260 270 280 290 300
NEDADGVYAA LPFLIANTKQ LMGFGETRDE PFVSMEGKRV VVLGGGDTAM
310 320 330 340 350
DCVRTSVRQG AKHVTCAYRR DEENMPGSRR EVKNAREEGV EFKFNVQPLG
360 370 380 390 400
IEVNGNGKVS GVKMVRTEMG EPDAKGRRRA EIVAGSEHIV PADAVIMAFG
410 420 430 440 450
FRPHNMEWLA KHSVELDSQG RIIAPEGSDN AFQTSNPKIF AGGDIVRGSD
460 470
LVVTAIAEGR KAADGIMNWL EV
Length:472
Mass (Da):52,015
Last modified:January 23, 2007 - v3
<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:iF188CE1086040433
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 conflicti38 – 51GQAKA…CLSCG → ARPKRRLTAACRAA (PubMed:3326786).CuratedAdd BLAST14
Sequence conflicti123E → K in AAA23905 (PubMed:3326786).Curated1
Sequence conflicti174V → C in AAA23905 (PubMed:3326786).Curated1
Sequence conflicti257 – 270VYAAL…ANTKQ → CTQRCRSSSPTPNS (PubMed:3326786).CuratedAdd BLAST14
Sequence conflicti312 – 313KH → ND in AAA23905 (PubMed:3326786).Curated2
Sequence conflicti376 – 400GRRRA…IMAFG → ASPRGDRCRFRTYRTGRCGD HGVW in AAA23905 (PubMed:3326786).CuratedAdd BLAST25

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
M18747 Genomic DNA Translation: AAA23905.1
U18997 Genomic DNA Translation: AAA58015.1
U00096 Genomic DNA Translation: AAC76245.1
AP009048 Genomic DNA Translation: BAE77257.1

Protein sequence database of the Protein Information Resource

More...
PIRi
G65112

NCBI Reference Sequences

More...
RefSeqi
NP_417680.1, NC_000913.3
WP_000081674.1, NZ_STEB01000012.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAC76245; AAC76245; b3213
BAE77257; BAE77257; BAE77257

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
61751951
947723

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ecj:JW3180
eco:b3213

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|511145.12.peg.3308

<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
M18747 Genomic DNA Translation: AAA23905.1
U18997 Genomic DNA Translation: AAA58015.1
U00096 Genomic DNA Translation: AAC76245.1
AP009048 Genomic DNA Translation: BAE77257.1
PIRiG65112
RefSeqiNP_417680.1, NC_000913.3
WP_000081674.1, NZ_STEB01000012.1

3D structure databases

SMRiP09832
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi4262427, 198 interactors
ComplexPortaliCPX-5041, Glutamate synthase [NADPH] complex
DIPiDIP-9803N
IntActiP09832, 6 interactors
STRINGi511145.b3213

2D gel databases

SWISS-2DPAGEiP09832

Proteomic databases

jPOSTiP09832
PaxDbiP09832
PRIDEiP09832

Genome annotation databases

EnsemblBacteriaiAAC76245; AAC76245; b3213
BAE77257; BAE77257; BAE77257
GeneIDi61751951
947723
KEGGiecj:JW3180
eco:b3213
PATRICifig|511145.12.peg.3308

Organism-specific databases

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

More...
EchoBASEi
EB0399

Phylogenomic databases

eggNOGiCOG0493, Bacteria
HOGENOMiCLU_000422_3_3_6
InParanoidiP09832
PhylomeDBiP09832

Enzyme and pathway databases

UniPathwayiUPA00045
UPA00634;UER00689
BioCyciEcoCyc:GLUSYNSMALL-MONOMER
MetaCyc:GLUSYNSMALL-MONOMER
BRENDAi1.4.1.13, 2026
SABIO-RKiP09832

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P09832

Family and domain databases

Gene3Di1.10.1060.10, 1 hit
3.50.50.60, 2 hits
InterProiView protein in InterPro
IPR017896, 4Fe4S_Fe-S-bd
IPR028261, DPD_II
IPR036188, FAD/NAD-bd_sf
IPR023753, FAD/NAD-binding_dom
IPR006006, GltD-like
IPR009051, Helical_ferredxn
PANTHERiPTHR42783:SF1, PTHR42783:SF1, 1 hit
PfamiView protein in Pfam
PF14691, Fer4_20, 1 hit
PF07992, Pyr_redox_2, 1 hit
TIGRFAMsiTIGR01318, gltD_gamma_fam, 1 hit
PROSITEiView protein in PROSITE
PS51379, 4FE4S_FER_2, 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 nameiGLTD_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: P09832
Secondary accession number(s): Q2M8Z9
<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: July 1, 1989
Last sequence update: January 23, 2007
Last modified: September 29, 2021
This is version 188 of the entry and version 3 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
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