UniProtKB - P0AF12 (MTNN_ECOLI)

BLAST

>sp|P0AF12|MTNN_ECOLI 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase OS=Escherichia coli (strain K12) OX=83333 GN=mtnN PE=1 SV=1
MKIGIIGAMEEEVTLLRDKIENRQTISLGGCEIYTGQLNGTEVALLKSGIGKVAAALGAT
LLLEHCKPDVIINTGSAGGLAPTLKVGDIVVSDEARYHDADVTAFGYEYGQLPGCPAGFK
ADDKLIAAAEACIAELNLNAVRGLIVSGDAFINGSVGLAKIRHNFPQAIAVEMEATAIAH
VCHNFNVPFVVVRAISDVADQQSHLSFDEFLAVAAKQSSLMVESLVQKLAHG

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History
Entry version 112 (07 Nov 2018)
Sequence version 1 (20 Dec 2005)
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Protein

5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase

Gene

mtnN

Organism

Escherichia coli (strain K12)

Status

Reviewed-Annotation score: -Experimental evidence at protein levelⁱ

Functionⁱ

Catalyzes the irreversible cleavage of the glycosidic bond in both 5'-methylthioadenosine (MTA) and S-adenosylhomocysteine (SAH/AdoHcy) to adenine and the corresponding thioribose, 5'-methylthioribose and S-ribosylhomocysteine, respectively. Can also use 5'-isobutylthioadenosine, 5'-n-butylthioadenosine, S-adenosyl-D-homocysteine, decarboxylated adenosylhomocysteine, deaminated adenosylhomocysteine and S-2-aza-adenosylhomocysteine as substrates.1 Publication

Catalytic activityⁱ

S-adenosyl-L-homocysteine + H₂O = S-(5-deoxy-D-ribos-5-yl)-L-homocysteine + adenine.1 Publication

S-methyl-5'-thioadenosine + H₂O = S-methyl-5-thio-D-ribose + adenine.1 Publication

Activity regulationⁱ

Strongly inhibited by aryl-substituted MTA analogs, alkyl-substituted MTA analogs, 5'-methylthioformycin, 5'-chloroformycin, S-formycinylhomocysteine, 5'-methylthiotubercidin, S-tubercidinylhomocysteine and S-8-aza-adenosylhomocysteine. Poorly inhibited by 5'-isobutylthioinosine, 5'-n-butylthioinosine, 5'-methylthio-3-deaza-adenosine, 5'-isobutylthio-3-deaza-adenosine, S-n-6-methyl-3-deaza-adenosylhomocysteine, S-adenosylhomocysteine sulphoxide and Sinefungin.4 Publications

Kineticsⁱ

kcat is 3.0 sec(-1) and 2.6 sec(-1) with 5'-methylthioadenosine and S-adenosylhomocysteine as substrate, respectively.1 Publication

pH dependenceⁱ

Exhibits activity across a broad pH range. Enzyme activity is moderately improved under acidic conditions.2 Publications

Temperature dependenceⁱ

Optimum temperature is 37-45 degrees Celsius. Rapidly inactivated after exposure for 10 minutes at 55 degrees Celsius.2 Publications

Pathwayⁱ: L-methionine biosynthesis via salvage pathway

This protein is involved in step 1 of the subpathway that synthesizes S-methyl-5-thio-alpha-D-ribose 1-phosphate from S-methyl-5'-thioadenosine (hydrolase route).
Proteins known to be involved in the 2 steps of the subpathway in this organism are:

5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase (mtnN)
no protein annotated in this organism

This subpathway is part of the pathway L-methionine biosynthesis via salvage 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 S-methyl-5-thio-alpha-D-ribose 1-phosphate from S-methyl-5'-thioadenosine (hydrolase route), the pathway L-methionine biosynthesis via salvage pathway and in Amino-acid biosynthesis.

Sites

Feature key	Position(s)	DescriptionActions	Length
Active siteⁱ	12	Proton acceptor1 Publication	1
Binding siteⁱ	78	Substrate; via amide nitrogen1 Publication	1
Binding siteⁱ	152	Substrate; via amide nitrogen and carbonyl oxygen1 Publication	1
Active siteⁱ	197	Proton donor1 Publication	1

GO - Molecular functionⁱ

adenosylhomocysteine nucleosidase activity
Source: EcoCyc
Inferred from direct assayⁱ
- 9524204
identical protein binding
Source: IntAct
Inferred from physical interactionⁱ
- 11591349
methylthioadenosine nucleosidase activity
Source: EcoCyc
Inferred from direct assayⁱ
- 9524204

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

L-methionine salvage from methylthioadenosine Source: UniProtKB-UniPathway
L-methionine salvage from S-adenosylmethionine
Source: EcoCyc
Inferred from direct assayⁱ
- 9524204
nucleoside catabolic process Source: InterPro

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Hydrolase
Biological process	Amino-acid biosynthesis, Methionine biosynthesis

Enzyme and pathway databases

BioCycⁱ	EcoCyc:EG11090-MONOMER MetaCyc:EG11090-MONOMER
BRENDAⁱ	3.2.2.30 2026 3.2.2.9 2026
UniPathwayⁱ	UPA00904;UER00871

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase (EC:3.2.2.9) Short name: MTA/SAH nucleosidase Short name: MTAN Alternative name(s): 5'-methylthioadenosine nucleosidase Short name: MTA nucleosidase P46 S-adenosylhomocysteine nucleosidase Short name: AdoHcy nucleosidase Short name: SAH nucleosidase Short name: SRH nucleosidase
Gene namesⁱ	Name:mtnN Synonyms:mtn, pfs, yadA Ordered Locus Names:b0159, JW0155
Organismⁱ	Escherichia coli (strain K12)
Taxonomic identifierⁱ	83333 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › Escherichia coli
Proteomesⁱ	UP000000318 Componentⁱ: Chromosome UP000000625 Componentⁱ: Chromosome

Organism-specific databases

EcoGeneⁱ	EG11090 pfs

EcoGeneⁱ

EG11090 pfs

Subcellular locationⁱ

GO - Cellular componentⁱ

cytosol
Source: EcoCyc
Inferred from direct assayⁱ
- 15911532

View the complete GO annotation on QuickGO ...

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	9	M → A: 13-19% of wild-type catalytic efficiency. 1 Publication	1
Mutagenesisⁱ	12	E → A or Q: Loss of catalytic activity. 1 Publication	1
Mutagenesisⁱ	50	I → A: 12-23% of wild-type catalytic efficiency. 1 Publication	1
Mutagenesisⁱ	76	S → A: 13-23% of wild-type catalytic efficiency. 1 Publication	1
Mutagenesisⁱ	151	F → A: 0.5% of wild-type catalytic efficiency. 1 Publication	1
Mutagenesisⁱ	173	M → A: 0.5% of wild-type catalytic efficiency. 1 Publication	1
Mutagenesisⁱ	174	E → A or Q: Loss of catalytic activity. 1 Publication	1
Mutagenesisⁱ	193	R → A: 13-28% of wild-type catalytic efficiency. 1 Publication	1
Mutagenesisⁱ	196	S → A: 2-4% of wild-type catalytic efficiency. 1 Publication	1
Mutagenesisⁱ	197	D → A or N: Loss of catalytic activity. 1 Publication	1
Mutagenesisⁱ	207	F → A: 2% of wild-type catalytic efficiency. 1 Publication	1

Chemistry databases

ChEMBLⁱ	CHEMBL2866
Drug and drug target database More...DrugBankⁱ	DB02933 5'-Deoxy-5'-(Methylthio)-Tubercidin DB00173 Adenine DB02281 Formycin

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000164439	1 – 232	5'-methylthioadenosine/S-adenosylhomocysteine nucleosidaseAdd BLAST		232

Proteomic databases

EPDⁱ	P0AF12
PaxDbⁱ	P0AF12
PRIDEⁱ	P0AF12

2D gel databases

SWISS-2DPAGEⁱ	P0AF12

SWISS-2DPAGEⁱ

P0AF12

Interactionⁱ

Subunit structureⁱ

Homodimer.4 Publications

Binary interactionsⁱ

With	Entry	#Exp.	IntAct	Notes
itself		2	EBI-1114261,EBI-1114261

With

Entry

#Exp.

IntAct

Notes

itself

EBI-1114261,EBI-1114261

GO - Molecular functionⁱ

identical protein binding
Source: IntAct
Inferred from physical interactionⁱ
- 11591349

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridⁱ	4260991, 38 interactors
Database of interacting proteins More...DIPⁱ	DIP-10270N
IntActⁱ	P0AF12, 7 interactors
STRINGⁱ	316385.ECDH10B_0139

Chemistry databases

BindingDBⁱ

P0AF12

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Beta strandⁱ	2 – 9	Combined sources	8
Helixⁱ	10 – 17	Combined sources	8
Beta strandⁱ	21 – 28	Combined sources	8
Beta strandⁱ	31 – 38	Combined sources	8
Beta strandⁱ	41 – 47	Combined sources	7
Helixⁱ	52 – 66	Combined sources	15
Beta strandⁱ	69 – 79	Combined sources	11
Beta strandⁱ	89 – 99	Combined sources	11
Helixⁱ	103 – 105	Combined sources	3
Beta strandⁱ	117 – 120	Combined sources	4
Helixⁱ	123 – 135	Combined sources	13
Beta strandⁱ	140 – 147	Combined sources	8
Helixⁱ	155 – 164	Combined sources	10
Beta strandⁱ	168 – 174	Combined sources	7
Helixⁱ	175 – 185	Combined sources	11
Beta strandⁱ	189 – 197	Combined sources	9
Helixⁱ	203 – 231	Combined sources	29

Show more details

3D structure databases

ProteinModelPortalⁱ	P0AF12
SMRⁱ	P0AF12
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ

P0AF12

Family & Domainsⁱ

Region

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Regionⁱ	173 – 174	Substrate binding		2

Sequence similaritiesⁱ

Belongs to the PNP/UDP phosphorylase family. MtnN subfamily.Curated

Phylogenomic databases

eggNOGⁱ	ENOG4105DUF Bacteria COG0775 LUCA
HOGENOMⁱ	HOG000259346
InParanoidⁱ	P0AF12
KEGG Orthology (KO) More...KOⁱ	K01243
PhylomeDBⁱ	P0AF12

Family and domain databases

HAMAPⁱ	MF_01684 Salvage_MtnN, 1 hit
InterProⁱ	View protein in InterPro IPR010049 MTA_SAH_Nsdase IPR000845 Nucleoside_phosphorylase_d IPR035994 Nucleoside_phosphorylase_sf
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF01048 PNP_UDP_1, 1 hit
SUPFAMⁱ	SSF53167 SSF53167, 1 hit
TIGRFAMsⁱ	TIGR01704 MTA/SAH-Nsdase, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

P0AF12-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MKIGIIGAME EEVTLLRDKI ENRQTISLGG CEIYTGQLNG TEVALLKSGI 
        60         70         80         90        100
GKVAAALGAT LLLEHCKPDV IINTGSAGGL APTLKVGDIV VSDEARYHDA 
       110        120        130        140        150
DVTAFGYEYG QLPGCPAGFK ADDKLIAAAE ACIAELNLNA VRGLIVSGDA 
       160        170        180        190        200
FINGSVGLAK IRHNFPQAIA VEMEATAIAH VCHNFNVPFV VVRAISDVAD 
       210        220        230 
QQSHLSFDEF LAVAAKQSSL MVESLVQKLA HG

Length:232

Mass (Da):24,354

Last modified:December 20, 2005 - v1

Checksum:ⁱ9B1FF9BEC39D4F2C

Sequence cautionⁱ

The sequence AAA23678 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Sequence conflictⁱ	212 – 232	AVAAK…KLAHG → LLPLNSPA in AAA23678 (PubMed:2157212).CuratedAdd BLAST		21
Sequence conflictⁱ	212 – 232	AVAAK…KLAHG → LLPLNSPA in AAA24322 (PubMed:2157212).CuratedAdd BLAST		21

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	M31772 Genomic DNA Translation: AAA23678.1 Different initiation. U24438 Genomic DNA Translation: AAC38291.1 M83735 Genomic DNA Translation: AAA24322.1 U70214 Genomic DNA Translation: AAB08589.1 U00096 Genomic DNA Translation: AAC73270.1 AP009048 Genomic DNA Translation: BAB96736.1
PIRⁱ	S45227
NCBI Reference Sequences More...RefSeqⁱ	NP_414701.1, NC_000913.3 WP_000689844.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaⁱ	AAC73270; AAC73270; b0159 BAB96736; BAB96736; BAB96736
GeneIDⁱ	948542
KEGGⁱ	ecj:JW0155 eco:b0159
PATRICⁱ	fig\|1411691.4.peg.2121

Protein	Similar proteins		Species	Score	Length	Source
P0AF12	5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase		ECO24		232	UniRef100_A7ZHQ1
5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase		ECO27		232
5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase		ECO45		232
5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase		ECO55		232
5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase	)	ECO57		232
+174

Protein	Similar proteins		Species	Score	Length	Source
P0AF12	5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase		SALAR		232	UniRef90_A9MPK2
5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase		SALCH		232
5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase		SALPC		232
5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase		ECO24		232
5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase		ECO27		232
+811

Protein	Similar proteins		Species	Score	Length	Source
P0AF12	5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase		YERE8		233	UniRef50_A1JJQ6
5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase		YERP3		233
5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase		YERPB		233
5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase		YERPS		233
5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase		YERPY		233
+1407

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	M31772 Genomic DNA Translation: AAA23678.1 Different initiation. U24438 Genomic DNA Translation: AAC38291.1 M83735 Genomic DNA Translation: AAA24322.1 U70214 Genomic DNA Translation: AAB08589.1 U00096 Genomic DNA Translation: AAC73270.1 AP009048 Genomic DNA Translation: BAB96736.1
PIRⁱ	S45227
RefSeqⁱ	NP_414701.1, NC_000913.3 WP_000689844.1, 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 entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	1JYS	X-ray	1.90	A/B	1-232	[»]
	1NC1	X-ray	2.00	A/B	1-232	[»]
	1NC3	X-ray	2.20	A/B	1-232	[»]
	1Y6Q	X-ray	2.20	A/B	1-232	[»]
	1Y6R	X-ray	2.20	A/B	1-232	[»]
	1Z5N	X-ray	2.10	A/B	1-232	[»]
	1Z5O	X-ray	2.00	A/B	1-232	[»]
	1Z5P	X-ray	2.00	A	1-232	[»]
	3O4V	X-ray	1.75	A/B	1-232	[»]
	4WKC	X-ray	1.64	A	1-232	[»]
	4YML	X-ray	1.75	A	1-232	[»]
ProteinModelPortalⁱ	P0AF12
SMRⁱ	P0AF12
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	4260991, 38 interactors
DIPⁱ	DIP-10270N
IntActⁱ	P0AF12, 7 interactors
STRINGⁱ	316385.ECDH10B_0139

Chemistry databases

BindingDBⁱ	P0AF12
ChEMBLⁱ	CHEMBL2866
DrugBankⁱ	DB02933 5'-Deoxy-5'-(Methylthio)-Tubercidin DB00173 Adenine DB02281 Formycin

2D gel databases

SWISS-2DPAGEⁱ	P0AF12

SWISS-2DPAGEⁱ

P0AF12

Proteomic databases

EPDⁱ	P0AF12
PaxDbⁱ	P0AF12
PRIDEⁱ	P0AF12

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

EnsemblBacteriaⁱ	AAC73270; AAC73270; b0159 BAB96736; BAB96736; BAB96736
GeneIDⁱ	948542
KEGGⁱ	ecj:JW0155 eco:b0159
PATRICⁱ	fig\|1411691.4.peg.2121

Organism-specific databases

EchoBASEⁱ	EB1082
EcoGeneⁱ	EG11090 pfs

Phylogenomic databases

eggNOGⁱ	ENOG4105DUF Bacteria COG0775 LUCA
HOGENOMⁱ	HOG000259346
InParanoidⁱ	P0AF12
KOⁱ	K01243
PhylomeDBⁱ	P0AF12

Enzyme and pathway databases

UniPathwayⁱ	UPA00904;UER00871
BioCycⁱ	EcoCyc:EG11090-MONOMER MetaCyc:EG11090-MONOMER
BRENDAⁱ	3.2.2.30 2026 3.2.2.9 2026

Miscellaneous databases

EvolutionaryTraceⁱ	P0AF12
Protein Ontology More...PROⁱ	PR:P0AF12

Family and domain databases

HAMAPⁱ	MF_01684 Salvage_MtnN, 1 hit
InterProⁱ	View protein in InterPro IPR010049 MTA_SAH_Nsdase IPR000845 Nucleoside_phosphorylase_d IPR035994 Nucleoside_phosphorylase_sf
Pfamⁱ	View protein in Pfam PF01048 PNP_UDP_1, 1 hit
SUPFAMⁱ	SSF53167 SSF53167, 1 hit
TIGRFAMsⁱ	TIGR01704 MTA/SAH-Nsdase, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	MTNN_ECOLI
Accessionⁱ	P0AF12Primary (citable) accession number: P0AF12 Secondary accession number(s): P24247
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	December 20, 2005
	Last sequence update:	December 20, 2005
	Last modified:	November 7, 2018
	This is version 112 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Prokaryotic Protein Annotation Program

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Complete proteome, Reference proteome

Documents

SIMILARITY comments
Index of protein domains and families
PATHWAY comments
Index of metabolic and biosynthesis pathways
PDB cross-references
Index of Protein Data Bank (PDB) cross-references
Escherichia coli
Escherichia coli (strain K12): entries and cross-references to EcoGene

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - P0AF12 (MTNN_ECOLI)

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5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase

mtnN

Select a section on the left to see content.

<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

<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

pH dependencei

Temperature dependencei

<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-methionine biosynthesis via salvage pathway

Sites

<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

Enzyme and pathway databases

<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

Organism-specific databases

<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

GO - Cellular componenti

<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

Chemistry databases

<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

Proteomic databases

2D gel databases

<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

Protein-protein interaction databases

Chemistry databases

<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

3D structure databases

Miscellaneous databases

<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

<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

Phylogenomic databases

Family and domain databases

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

Experimental Info

Sequence databases

Genome annotation databases

<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

3D structure databases

Protein-protein interaction databases

Chemistry databases

2D gel databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Family and domain databases

<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 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

Documents

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Functionⁱ

Kineticsⁱ

pH dependenceⁱ

Temperature dependenceⁱ

Pathwayⁱ: L-methionine biosynthesis via salvage pathway

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

GO - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Sequence cautionⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ