<p>Provides any useful information about the protein, mostly biological knowledge.</p><p><a href='../manual/function_section' target='_top'>More...</a></p>Functionⁱ

<p>Describes the catalytic activity of an enzyme, i.e. the chemical reaction it catalyzes. This information usually correlates with the presence of an EC (Enzyme Commission) number in the ‘Names and taxonomy’ section.</p><p><a href='../manual/catalytic_activity' target='_top'>More...</a></p>Catalytic activityⁱ

<p>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><p><a href='../manual/cofactor' target='_top'>More...</a></p>Cofactorⁱ

Sites

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
<p>Is used for enzymes and indicates the residues directly involved in catalysis.</p><p><a href='../manual/act_site' target='_top'>More...</a></p>Active sitei	152 – 152	1	Proton acceptorUniRule annotation <p>Information which has been generated by the UniProtKB automatic annotation system, without manual validation.</p> <p><a href="/manual/evidences#ECO:0000256">More…</a></p> Automatic assertion according to rulesi HAMAP-Rule:MF_01133
<p>Describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.</p><p><a href='../manual/binding' target='_top'>More...</a></p>Binding sitei	154 – 154	1	SubstrateUniRule annotation <p>Information which has been generated by the UniProtKB automatic annotation system, without manual validation.</p> <p><a href="/manual/evidences#ECO:0000256">More…</a></p> Automatic assertion according to rulesi HAMAP-Rule:MF_01133
<p>Indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.</p><p><a href='../manual/metal' target='_top'>More...</a></p>Metal bindingi	178 – 178	1	Magnesium; via carbamate groupUniRule annotation <p>Information which has been generated by the UniProtKB automatic annotation system, without manual validation.</p> <p><a href="/manual/evidences#ECO:0000256">More…</a></p> Automatic assertion according to rulesi HAMAP-Rule:MF_01133
<p>Indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.</p><p><a href='../manual/metal' target='_top'>More...</a></p>Metal bindingi	180 – 180	1	MagnesiumUniRule annotation <p>Information which has been generated by the UniProtKB automatic annotation system, without manual validation.</p> <p><a href="/manual/evidences#ECO:0000256">More…</a></p> Automatic assertion according to rulesi HAMAP-Rule:MF_01133
<p>Indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.</p><p><a href='../manual/metal' target='_top'>More...</a></p>Metal bindingi	181 – 181	1	MagnesiumUniRule annotation <p>Information which has been generated by the UniProtKB automatic annotation system, without manual validation.</p> <p><a href="/manual/evidences#ECO:0000256">More…</a></p> Automatic assertion according to rulesi HAMAP-Rule:MF_01133
<p>Is used for enzymes and indicates the residues directly involved in catalysis.</p><p><a href='../manual/act_site' target='_top'>More...</a></p>Active sitei	270 – 270	1	Proton acceptorUniRule annotation <p>Information which has been generated by the UniProtKB automatic annotation system, without manual validation.</p> <p><a href="/manual/evidences#ECO:0000256">More…</a></p> Automatic assertion according to rulesi HAMAP-Rule:MF_01133
<p>Describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.</p><p><a href='../manual/binding' target='_top'>More...</a></p>Binding sitei	271 – 271	1	SubstrateUniRule annotation <p>Information which has been generated by the UniProtKB automatic annotation system, without manual validation.</p> <p><a href="/manual/evidences#ECO:0000256">More…</a></p> Automatic assertion according to rulesi HAMAP-Rule:MF_01133
<p>Describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.</p><p><a href='../manual/binding' target='_top'>More...</a></p>Binding sitei	303 – 303	1	SubstrateUniRule annotation <p>Information which has been generated by the UniProtKB automatic annotation system, without manual validation.</p> <p><a href="/manual/evidences#ECO:0000256">More…</a></p> Automatic assertion according to rulesi HAMAP-Rule:MF_01133
<p>Describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.</p><p><a href='../manual/site' target='_top'>More...</a></p>Sitei	310 – 310	1	Transition state stabilizerUniRule annotation <p>Information which has been generated by the UniProtKB automatic annotation system, without manual validation.</p> <p><a href="/manual/evidences#ECO:0000256">More…</a></p> Automatic assertion according to rulesi HAMAP-Rule:MF_01133

<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><p><a href='../manual/gene_ontology' target='_top'>More...</a></p>GO - Molecular functionⁱ

1. magnesium ion binding Source: UniProtKB-HAMAP
2. oxidoreductase activity Source: UniProtKB-KW
3. ribulose-bisphosphate carboxylase activity Source: UniProtKB-HAMAP

<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><p><a href='../manual/gene_ontology' target='_top'>More...</a></p>GO - Biological processⁱ

1. AMP catabolic process Source: UniProtKB-HAMAP
2. carbon fixation Source: UniProtKB-KW

<p>UniProtKB Keywords constitute a <a target="_top" href="/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>Keywords - Molecular functionⁱ

<p>UniProtKB Keywords constitute a <a target="_top" href="/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>Keywords - Biological processⁱ

<p>UniProtKB Keywords constitute a <a target="_top" href="/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>Keywords - Ligandⁱ

Enzyme and pathway databases

<p>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><p><a href='../manual/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyⁱ

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

Amino acid modifications

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
<p>Specifies the position and type of each modified residue excluding <a href="/manual/lipid">lipids</a>, <a href="/manual/carbohyd">glycans</a> and <a href="/manual/crosslnk">protein cross-links</a>.</p><p><a href='../manual/mod_res' target='_top'>More...</a></p>Modified residuei	178 – 178	1	N6-carboxylysineUniRule annotation <p>Information which has been generated by the UniProtKB automatic annotation system, without manual validation.</p> <p><a href="/manual/evidences#ECO:0000256">More…</a></p> Automatic assertion according to rulesi HAMAP-Rule:MF_01133

<p>Provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.</p><p><a href='../manual/interaction_section' target='_top'>More...</a></p>Interactionⁱ

<p>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 ‘Function’ section).</p><p><a href='../manual/subunit_structure' target='_top'>More...</a></p>Subunit structureⁱ

<p>Provides information on the tertiary structure of a protein.</p><p><a href='../manual/structure_section' target='_top'>More...</a></p>Structureⁱ

3D structure databases

<p>Provides information on sequence similarities with other proteins and the domain(s) present in a protein.</p><p><a href='../manual/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsⁱ

Region

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
<p>Describes a region of interest that cannot be described in other subsections.</p><p><a href='../manual/region' target='_top'>More...</a></p>Regioni	353 – 355	3	Substrate bindingUniRule annotation <p>Information which has been generated by the UniProtKB automatic annotation system, without manual validation.</p> <p><a href="/manual/evidences#ECO:0000256">More…</a></p> Automatic assertion according to rulesi HAMAP-Rule:MF_01133

<p>Provides information about the sequence similarity with other proteins.</p><p><a href='../manual/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesⁱ

Phylogenomic databases

Family and domain databases

<p>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 length and molecular weight.</p><p><a href='../manual/sequences_section' target='_top'>More...</a></p>Sequenceⁱ

<p>Indicates if the canonical sequence displayed by default in the entry is complete or not.</p><p><a href='../manual/sequence_status' target='_top'>More...</a></p>Sequence statusⁱ: Complete.

        10         20         30         40         50
MAIDWYEEFV DTDHTPGSDE LVALYYFEPA AGISREEAVG RIASESSTGT 
        60         70         80         90        100
WTTLFTMPPR MRDLQAKAFE IEGNYVKIAY PLALWEEGNA PQLLSGIAGN 
       110        120        130        140        150
VFGMKALESL RLIDASLPAE YLRHFKGPHF GMEGIRDMMK VHGRPLTGAV 
       160        170        180        190        200
PKPKVGFTAE EHAEVGYETW MGGFDFVKDD ENLTSLAFNR FEDRVRAMTK 
       210        220        230        240        250
MRDRAEQETG DVKSAFINIT ADTETMKKRA EMLADYGWNY AMIDVVVTGT 
       260        270        280        290        300
AAVATLRDHC SDLGLAIHAH RAMHAAFDRD EKHGITMQFL AKIMRLIGVA 
       310        320        330        340        350
QIHTGTAVGK LVGTKAEATV LADMVREKHT NAVDHMALDQ DWGAIKSAFP 
       360        370        380        390        400
VSSGGLHPGL VPDVLDIYGS DLVLLVSGGI HGHPKGTRAG AMATMQAIEA 
       410        420        430
WSEGETLEEK AKKAPELREA LEKWGYYKPK                       

Sequence databases

Genome annotation databases

<p>Is used to point to information related to entries and found in data collections other than UniProtKB.</p><p><a href='../manual/cross_references_section' target='_top'>More...</a></p> Cross-referencesⁱ

Sequence databases

3D structure databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

<p>Contains the literature citations that are the sources of data used to annotate the entry. Each reference is numbered and contains several subsections allowing a precise description of a given citation.</p><p><a href='../manual/publications_section' target='_top'>More...</a></p>Publicationsⁱ

1. "Complete genome sequence of the hydrogenotrophic, methanogenic archaeon Methanoculleus bourgensis strain MS2T, isolated from a sewage sludge digester."
   Maus I., Wibberg D., Stantscheff R., Eikmeyer F.G., Seffner A., Boelter J., Szczepanowski R., Blom J., Jaenicke S., Konig H., Puhler A., Schluter A.
   J. Bacteriol. 194:5487-5488(2012) [PubMed] [Europe PMC] [Abstract]
   Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
   Strain: ATCC 43281 / DSM 3045 / OCM 15 / MS2Imported

   <p>Information which has been imported from another database using automatic procedures.</p> <p><a href="/manual/evidences#ECO:0000313">More…</a></p> Automatic assertion inferred from database entriesⁱ

   • Proteomes:UP000009007
   .
   

<p>Provides general information on the entry.</p><p><a href='../manual/entry_information_section' target='_top'>More...</a></p>Entry informationⁱ

<p>Contains any relevant information that doesn’t fit in any other defined sections</p><p><a href='../manual/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousⁱ

Miscellaneous

<p>UniProtKB Keywords constitute a <a target="_top" href="/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>Keywords - Technical termⁱ

External Data

<p>Provides links to the UniProt Reference Clusters (<a href="/help/uniref">UniRef</a>). UniRef consists of clusters for UniProtKB sequences (including isoforms) and selected UniParc sequences, in order to obtain complete coverage of the sequence space at resolutions of 100%, 90% and 50% identity.</p><p><a href='../manual/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsⁱ