UniProtKB - P10868 (GAMT_RAT)

BLAST

>sp|P10868|GAMT_RAT Guanidinoacetate N-methyltransferase OS=Rattus norvegicus OX=10116 GN=Gamt PE=1 SV=2
MSSSAASPLFAPGEDCGPAWRAAPAAYDTSDTHLQILGKPVMERWETPYMHSLAAAAASR
GGRVLEVGFGMAIAASRVQQAPIKEHWIIECNDGVFQRLQNWALKQPHKVVPLKGLWEEE
APTLPDGHFDGILYDTYPLSEETWHTHQFNFIKTHAFRLLKPGGILTYCNLTSWGELMKS
KYTDITAMFEETQVPALLEAGFQRENICTEVMALVPPADCRYYAFPQMITPLVTKH

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History
Entry version 135 (23 May 2018)
Sequence version 2 (23 Jan 2007)
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Protein

Guanidinoacetate N-methyltransferase

Gene

Gamt

Organism

Rattus norvegicus (Rat)

Status

Reviewed-Annotation score: -Experimental evidence at protein levelⁱ

Functionⁱ

Converts guanidinoacetate to creatine, using S-adenosylmethionine as the methyl donor. Important in nervous system development.By similarity

Miscellaneous

The N-terminal first 36 amino acid residues are susceptible to proteolytic cleavage, leading to loss of activity.

Catalytic activityⁱ

S-adenosyl-L-methionine + guanidinoacetate = S-adenosyl-L-homocysteine + creatine.PROSITE-ProRule annotation

Pathwayⁱ: creatine biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes creatine from L-arginine and glycine.
Proteins known to be involved in the 2 steps of the subpathway in this organism are:

Glycine amidinotransferase, mitochondrial (Gatm)
Guanidinoacetate N-methyltransferase (Gamt), Guanidinoacetate N-methyltransferase (Gamt)

This subpathway is part of the pathway creatine biosynthesis, which is itself part of Amine and polyamine biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes creatine from L-arginine and glycine, the pathway creatine biosynthesis and in Amine and polyamine biosynthesis.

Sites

Feature key	Position(s)	DescriptionActions	Length
Binding siteⁱ	20	S-adenosyl-L-methionine	1
Binding siteⁱ	42	SubstratePROSITE-ProRule annotation1 Publication	1
Binding siteⁱ	46	SubstratePROSITE-ProRule annotation1 Publication	1
Binding siteⁱ	50	S-adenosyl-L-methionine	1
Binding siteⁱ	135	S-adenosyl-L-methionine and substrate	1

GO - Molecular functionⁱ

guanidinoacetate N-methyltransferase activity
Source: RGD
Inferred from direct assayⁱ
- 12069495
- 15533043
protein homodimerization activity
Source: RGD
Inferred from direct assayⁱ
- 12079381
S-adenosylmethionine-dependent methyltransferase activity
Source: RGD
Inferred from direct assayⁱ
- 15533043

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

creatine biosynthetic process
Source: RGD
Inferred from direct assayⁱ
- 15533043
embryonic liver development
Source: RGD
Inferred from expression patternⁱ
- 15918910
S-adenosylhomocysteine metabolic process
Source: RGD
Inferred from direct assayⁱ
- 15533043
S-adenosylmethionine metabolic process
Source: RGD
Inferred from direct assayⁱ
- 15533043

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Methyltransferase, Transferase
Ligand	S-adenosyl-L-methionine

Enzyme and pathway databases

BioCycⁱ	MetaCyc:MONOMER-7641
BRENDAⁱ	2.1.1.2 5301
SABIO-RKⁱ	P10868
UniPathwayⁱ	UPA00104;UER00580

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Guanidinoacetate N-methyltransferase (EC:2.1.1.2)
Gene namesⁱ	Name:Gamt
Organismⁱ	Rattus norvegicus (Rat)
Taxonomic identifierⁱ	10116 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus
Proteomesⁱ	UP000002494 Componentⁱ: Unplaced

Organism-specific databases

Rat genome database More...RGDⁱ	2659 Gamt

RGDⁱ

2659 Gamt

Subcellular locationⁱ

GO - Cellular component

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	46	E → D: Reduces affinity for substrate and S-adenosyl-L-methionine about 2-fold. 1 Publication	1
Mutagenesisⁱ	46	E → Q: Reduces affinity for substrate and S-adenosyl-L-methionine about 4-fold. 1 Publication	1
Mutagenesisⁱ	46	E → S: Loss of activity. 1 Publication	1
Mutagenesisⁱ	135	D → A: Loss of activity. 1 Publication	1
Mutagenesisⁱ	135	D → E: Reduces affinity for S-adenosyl-L-methionine 500-fold. Reduces affinity for substrate about 40-fold. 1 Publication	1
Mutagenesisⁱ	135	D → N: Reduces affinity for S-adenosyl-L-methionine 2000-fold. Reduces affinity for substrate about 40-fold. 1 Publication	1
Mutagenesisⁱ	222	Y → F: Reduces affinity for S-adenosyl-L-methionine about 5-fold. Reduces affinity for substrate about 40-fold. 1 Publication	1

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Initiator methionineⁱ		RemovedBy similarity
ChainⁱPRO_0000087432	2 – 236	Guanidinoacetate N-methyltransferaseAdd BLAST		235

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Modified residueⁱ	2	N-acetylserineBy similarity		1
Modified residueⁱ	7	PhosphoserineCombined sources		1

Keywords - PTMⁱ

Acetylation, Phosphoprotein

Proteomic databases

PaxDbⁱ	P10868
PRIDEⁱ	P10868

PTM databases

iPTMnetⁱ	P10868

iPTMnetⁱ

P10868

Expressionⁱ

Tissue specificityⁱ

Expressed in hepatic primordium in the embryo as soon as 12.5 days. In the adult, high levels of expression are found in liver and pancreas. Ubiquitously expressed in neuronal and glial cells in the brain.2 Publications

Interactionⁱ

Subunit structureⁱ

Monomer. May form homodimers upon proteolytic removal of the first 36 amino acid residues.4 Publications

GO - Molecular functionⁱ

protein homodimerization activity
Source: RGD
Inferred from direct assayⁱ
- 12079381

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

STRINGⁱ	10116.ENSRNOP00000036927

STRINGⁱ

10116.ENSRNOP00000036927

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Helixⁱ	17 – 20	Combined sources	4
Beta strandⁱ	33 – 36	Combined sources	4
Beta strandⁱ	39 – 43	Combined sources	5
Helixⁱ	44 – 46	Combined sources	3
Helixⁱ	47 – 57	Combined sources	11
Turnⁱ	58 – 60	Combined sources	3
Beta strandⁱ	62 – 67	Combined sources	6
Helixⁱ	73 – 80	Combined sources	8
Beta strandⁱ	84 – 90	Combined sources	7
Helixⁱ	93 – 103	Combined sources	11
Beta strandⁱ	107 – 115	Combined sources	9
Helixⁱ	117 – 120	Combined sources	4
Helixⁱ	121 – 123	Combined sources	3
Beta strandⁱ	129 – 134	Combined sources	6
Helixⁱ	141 – 143	Combined sources	3
Turnⁱ	144 – 146	Combined sources	3
Helixⁱ	147 – 154	Combined sources	8
Helixⁱ	156 – 159	Combined sources	4
Beta strandⁱ	160 – 168	Combined sources	9
Helixⁱ	171 – 180	Combined sources	10
Helixⁱ	185 – 192	Combined sources	8
Helixⁱ	194 – 200	Combined sources	7
Helixⁱ	204 – 206	Combined sources	3
Beta strandⁱ	207 – 213	Combined sources	7
Beta strandⁱ	226 – 234	Combined sources	9

Show more details

3D structure databases

ProteinModelPortalⁱ	P10868
SMRⁱ	P10868
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ

P10868

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Domainⁱ	13 – 236	RMT2PROSITE-ProRule annotationAdd BLAST		224

Region

Feature key	Position(s)	DescriptionActions	Length
Regionⁱ	69 – 74	S-adenosyl-L-methionine binding	6
Regionⁱ	90 – 92	S-adenosyl-L-methionine	3
Regionⁱ	117 – 118	S-adenosyl-L-methionine binding	2
Regionⁱ	171 – 172	Substrate binding	2

Sequence similaritiesⁱ

Belongs to the class I-like SAM-binding methyltransferase superfamily. RMT2 methyltransferase family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGⁱ	ENOG410ISNM Eukaryota ENOG410XPX4 LUCA
HOGENOMⁱ	HOG000010290
HOVERGENⁱ	HBG005801
InParanoidⁱ	P10868

Family and domain databases

InterProⁱ	View protein in InterPro IPR016550 GuanidinoAc_N-MeTrfase IPR026480 RMT2_dom IPR029063 SAM-dependent_MTases
PIRSFⁱ	PIRSF009285 GAMT, 1 hit
SUPFAMⁱ	SSF53335 SSF53335, 1 hit
PROSITEⁱ	View protein in PROSITE PS51559 SAM_RMT2, 1 hit

Sequence (1+)ⁱ

Sequence statusⁱ: Complete.

Sequence processingⁱ: The displayed sequence is further processed into a mature form.

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.ⁱShow all

P10868-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MSSSAASPLF APGEDCGPAW RAAPAAYDTS DTHLQILGKP VMERWETPYM 
        60         70         80         90        100
HSLAAAAASR GGRVLEVGFG MAIAASRVQQ APIKEHWIIE CNDGVFQRLQ 
       110        120        130        140        150
NWALKQPHKV VPLKGLWEEE APTLPDGHFD GILYDTYPLS EETWHTHQFN 
       160        170        180        190        200
FIKTHAFRLL KPGGILTYCN LTSWGELMKS KYTDITAMFE ETQVPALLEA 
       210        220        230 
GFQRENICTE VMALVPPADC RYYAFPQMIT PLVTKH

Length:236

Mass (Da):26,407

Last modified:January 23, 2007 - v2

Checksum:ⁱ738D6F0BC86DB1C3

Computationally mapped potential isoform sequencesⁱ

There is 1 potential isoform mapped to this entry.BLAST Align Show all Add to basket

	Entry	Entry name		Protein names	Gene names	Length	Annotation
	G3V960	G3V960_RAT		Guanidinoacetate N-methyltransferas... Guanidinoacetate N-methyltransferase, EC 2.1.1.2	Gamt rCG_29249	236	Annotation score:

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	J03588 mRNA Translation: AAA41258.1 X08056 Genomic DNA Translation: CAA30845.1
PIRⁱ	S01395
UniGeneⁱ	Rn.33890

Genome annotation databases

UCSC genome browser More...UCSCⁱ	RGD:2659 rat

UCSCⁱ

RGD:2659 rat

Protein	Similar proteins		Species	Score	Length	Source
P10868	Guanidinoacetate N-methyltransferase		MOUSE		236	UniRef90_P10868
Guanidinoacetate N-methyltransferase		NEOLE		236
Guanidinoacetate N-methyltransferase		CASCN		236
Guanidinoacetate N-methyltransferase		RAT		236
Guanidinoacetate N-methyltransferase		DIPOR		236
+14

Protein	Similar proteins		Species	Score	Length	Source
P10868	Isoform 2 of Guanidinoacetate N-methyltransferase		HUMAN		269	UniRef50_Q14353-2
Guanidinoacetate N-methyltransferase		BOVIN		236
Guanidinoacetate N-methyltransferase		MOUSE		236
GAMT isoform 1		PONAB		269
Guanidinoacetate N-methyltransferase		GORGO		269
+70

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	J03588 mRNA Translation: AAA41258.1 X08056 Genomic DNA Translation: CAA30845.1
PIRⁱ	S01395
UniGeneⁱ	Rn.33890

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
	1KHH	X-ray	2.50	A/B	39-236	[»]
	1P1B	X-ray	2.80	A/B/C/D	38-236	[»]
	1P1C	X-ray	2.50	A/B	38-236	[»]
	1XCJ	X-ray	2.00	A	2-236	[»]
	1XCL	X-ray	2.00	A	2-236	[»]
ProteinModelPortalⁱ	P10868
SMRⁱ	P10868
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

STRINGⁱ	10116.ENSRNOP00000036927

STRINGⁱ

10116.ENSRNOP00000036927

PTM databases

iPTMnetⁱ	P10868

iPTMnetⁱ

P10868

Proteomic databases

PaxDbⁱ	P10868
PRIDEⁱ	P10868

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

UCSCⁱ	RGD:2659 rat

UCSCⁱ

RGD:2659 rat

Organism-specific databases

RGDⁱ	2659 Gamt

RGDⁱ

2659 Gamt

Phylogenomic databases

eggNOGⁱ	ENOG410ISNM Eukaryota ENOG410XPX4 LUCA
HOGENOMⁱ	HOG000010290
HOVERGENⁱ	HBG005801
InParanoidⁱ	P10868

Enzyme and pathway databases

UniPathwayⁱ	UPA00104;UER00580
BioCycⁱ	MetaCyc:MONOMER-7641
BRENDAⁱ	2.1.1.2 5301
SABIO-RKⁱ	P10868

Miscellaneous databases

EvolutionaryTraceⁱ	P10868
Protein Ontology More...PROⁱ	PR:P10868

Family and domain databases

InterProⁱ	View protein in InterPro IPR016550 GuanidinoAc_N-MeTrfase IPR026480 RMT2_dom IPR029063 SAM-dependent_MTases
PIRSFⁱ	PIRSF009285 GAMT, 1 hit
SUPFAMⁱ	SSF53335 SSF53335, 1 hit
PROSITEⁱ	View protein in PROSITE PS51559 SAM_RMT2, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	GAMT_RAT
Accessionⁱ	P10868Primary (citable) accession number: P10868
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
	Last sequence update:	January 23, 2007
	Last modified:	May 23, 2018
	This is version 135 of the entry and version 2 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - P10868 (GAMT_RAT)

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Guanidinoacetate N-methyltransferase

Gamt

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

Miscellaneous

<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: creatine biosynthesis

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

Nucleus

Other locations

<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

<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

Amino acid modifications

Keywords - PTMi

Proteomic databases

PTM databases

<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 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

<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

Domains and Repeats

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

Computationally mapped potential isoform sequencesi

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

PTM 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

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Functionⁱ

Pathwayⁱ: creatine biosynthesis

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Computationally mapped potential isoform sequencesⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ