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Protein

Glycine amidinotransferase, mitochondrial

Gene

Gatm

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the biosynthesis of guanidinoacetate, the immediate precursor of creatine. Creatine plays a vital role in energy metabolism in muscle tissues. May play a role in embryonic and central nervous system development. Also capable of catalyzing the synthesis of a range of neuroactive guanidino compounds by utilizing alternative amidine donors and acceptors for the transamidination reaction.1 Publication

Catalytic activityi

L-arginine + glycine = L-ornithine + guanidinoacetate.2 Publications

Kineticsi

Two forms of the enzyme (denoted alpha and beta) with slightly different kinetic properties are present in cellular extracts. The molecular basis of the differences is unclear.

  1. KM=2.8 mM for arginine (alpha-transamidinase form)2 Publications
  2. KM=2.4 mM for arginine (beta-transamidinase form)2 Publications
  3. KM=3.0 mM for glycine (alpha-transamidinase form)2 Publications
  4. KM=3.1 mM for glycine (beta-transamidinase form)2 Publications
  5. KM=27.2 mM for 4-amino-butyrate (alpha-transamidinase form)2 Publications
  6. KM=24.9 mM for 4-amino-butyrate (beta-transamidinase form)2 Publications
  7. KM=23.0 mM for lysine (alpha-transamidinase form)2 Publications
  8. KM=23.5 mM for lysine (beta-transamidinase form)2 Publications
  9. KM=23.9 mM for 5-amino-valerate (alpha-transamidinase form)2 Publications
  10. KM=23.5 mM for 5-amino-valerate (beta-transamidinase form)2 Publications
  11. KM=57.4 mM for 3-amino-propanoate (alpha-transamidinase form)2 Publications
  12. KM=57.5 mM for 3-amino-propanoate (beta-transamidinase form)2 Publications
  13. KM=174 mM for ethanolamine (alpha-transamidinase form)2 Publications
  14. KM=171 mM for ethanolamine (beta-transamidinase form)2 Publications
  15. KM=392 mM for taurine (alpha-transamidinase form)2 Publications
  16. KM=450 mM for taurine (beta-transamidinase form)2 Publications
  1. Vmax=0.39 µmol/min/mg enzyme with L-arginine and glycine as substrates (alpha-transamidinase form)2 Publications
  2. Vmax=0.37 µmol/min/mg enzyme with L-arginine and glycine as substrates (beta-transamidinase form)2 Publications
  3. Vmax=39.8 µmol/h/mg enzyme with L-arginine and glycine as substrates (alpha-transamidinase form)2 Publications
  4. Vmax=27.0 µmol/h/mg enzyme with L-arginine and glycine as substrates (beta-transamidinase form)2 Publications
  5. Vmax=16.8 µmol/h/mg enzyme with L-arginine and 4-amino-butyrate as substrates (alpha-transamidinase form)2 Publications
  6. Vmax=11.8 µmol/h/mg enzyme with L-arginine and 4-amino-butyrate as substrates (beta-transamidinase form)2 Publications
  7. Vmax=12.0 µmol/h/µg enzyme with L-arginine and lysine as substrates (alpha-transamidinase form)2 Publications
  8. Vmax=10.1 µmol/h/µg enzyme with L-arginine and lysine as substrates (beta-transamidinase form)2 Publications
  9. Vmax=13.9 µmol/h/µg enzyme with L-arginine and 5-amino-valerate as substrates (alpha-transamidinase form)2 Publications
  10. Vmax=9.7 µmol/h/µg enzyme with L-arginine and 5-amino-valerate as substrates (beta-transamidinase form)2 Publications
  11. Vmax=10.8 µmol/h/µg enzyme with L-arginine and 3-amino-proponoate as substrates (alpha-transamidinase form)2 Publications
  12. Vmax=7.7 µmol/h/µg enzyme with L-arginine and 3-amino-proponoate as substrates (beta-transamidinase form)2 Publications
  13. Vmax=12.4 µmol/h/µg enzyme with L-arginine and ethanolamine as substrates (alpha-transamidinase form)2 Publications
  14. Vmax=9.4 µmol/h/µg enzyme with L-arginine and ethanolamine as substrates (beta-transamidinase form)2 Publications
  15. Vmax=2.8 µmol/h/µg enzyme with L-arginine and taurine as substrates (alpha-transamidinase form)2 Publications
  16. Vmax=2.1 µmol/h/µg enzyme with L-arginine and taurine as substrates (beta-transamidinase form)2 Publications

Pathwayi: creatine biosynthesis

This protein is involved in step 1 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:
  1. Glycine amidinotransferase, mitochondrial (Gatm)
  2. 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 keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei254 – 2541By similarity
Active sitei303 – 3031By similarity
Active sitei407 – 4071Amidino-cysteine intermediateBy similarity

GO - Molecular functioni

  • amidinotransferase activity Source: RGD
  • glycine amidinotransferase activity Source: UniProtKB-EC

GO - Biological processi

  • creatine biosynthetic process Source: RGD
  • embryonic liver development Source: RGD
  • response to mercury ion Source: RGD
  • response to nutrient Source: RGD
  • response to organic substance Source: RGD
  • response to oxidative stress Source: RGD
  • response to peptide hormone Source: RGD
  • tissue regeneration Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-7583.
BRENDAi2.1.4.1. 5301.
UniPathwayiUPA00104; UER00579.

Names & Taxonomyi

Protein namesi
Recommended name:
Glycine amidinotransferase, mitochondrial (EC:2.1.4.12 Publications)
Alternative name(s):
L-arginine:glycine amidinotransferase
Transamidinase
Gene namesi
Name:Gatm
Synonyms:Agat
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi71090. Gatm.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3737MitochondrionAdd
BLAST
Chaini38 – 423386Glycine amidinotransferase, mitochondrialPRO_0000001208Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei46 – 461PhosphoserineBy similarity
Modified residuei49 – 491PhosphoserineBy similarity
Modified residuei385 – 3851N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP50442.
PRIDEiP50442.

PTM databases

iPTMnetiP50442.
PhosphoSiteiP50442.

Expressioni

Tissue specificityi

Highly expressed in the kidney and pancreas, especially in the proximal tubules of the kidney, and alpha cells of the pancreatic islets (at protein level). Moderately expressed in liver hepatocytes (at protein level). Expressed in the kidney, pancreas, liver, colon, ileum, jejunum, heart and skeletal muscle. In reproductive tissues, expressed in the testis, epididymis, ovary, oviduct and uterus. Expressed throughout the brain in neurons, astrocytes and oligodendrocytes. In E12.5 embryos, it is expressed in the middle part of the somites, hepatic primordium and wall of the dorsal aorta. Expressed in E15.5 embryos in isolated cells throughout the central nervous system, skeletal muscles, gonad primordia, caudal somites, liver and pancreas, but not in the choroid plexus, root ganglia or kidney. Expressed in skeletal muscle, kidney, pancreas, central nervous system, liver and intestine epithelial cells, but not in epidermis, dermis, olfactory epithelium, trachea, lung, stomach or heart in E18.5 embryos.5 Publications

Developmental stagei

Expressed throughout embryogenesis. Expression in the colon and small intestine is highest in newborns and declines with age. Expression in the kidney increases with age.2 Publications

Inductioni

Expression is induced by growth hormone and repressed by dietary intake of creatine.3 Publications

Gene expression databases

BgeeiENSRNOG00000000168.
GenevisibleiP50442. RN.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000000181.

Chemistry

BindingDBiP50442.

Structurei

3D structure databases

ProteinModelPortaliP50442.
SMRiP50442. Positions 64-423.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the amidinotransferase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiENOG410IFBR. Eukaryota.
ENOG410Y45M. LUCA.
HOVERGENiHBG002492.
InParanoidiP50442.
KOiK00613.
OrthoDBiEOG091G07LX.
PhylomeDBiP50442.

Family and domain databases

InterProiIPR033195. AmidinoTrfase.
[Graphical view]
PANTHERiPTHR10488. PTHR10488. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P50442-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLRVRCLRGG SRGAEAVHYI GSRLGGSLTG WVQRTFQSTQ AATASSQNSC
60 70 80 90 100
AAEDKATHPL PKDCPVSSYN EWDPLEEVIV GRAENACVPP FTVEVKANTY
110 120 130 140 150
EKYWPFYQKN GGLYFPKDHL KKAVAEVEEM CNILSMEGVT VKRPDPIDWS
160 170 180 190 200
LKYKTPDFES TGLYSAMPRD ILMVVGNEII EAPMAWRSRF FEYRAYRSII
210 220 230 240 250
KDYFHRGAKW TTAPKPTMAD ELYDQDYPIH SVEDRHKLAA QGKFVTTEFE
260 270 280 290 300
PCFDAADFIR AGRDIFAQRS QVTNYLGIEW MRRHLAPDYR VHIISFKDPN
310 320 330 340 350
PMHIDATFNI IGPGLVLSNP DRPCHQIDLF KKAGWTIVTP PTPVIPDDHP
360 370 380 390 400
LWMSSKWLSM NVLMLDEKRV MVDANEVPIQ KMFEKLGIST IKVNIRNANS
410 420
LGGGFHCWTC DVRRRGTLQS YFD
Length:423
Mass (Da):48,242
Last modified:October 1, 1996 - v1
Checksum:i442D7FBA4984DEA0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U07971 mRNA. Translation: AAA21250.1.
BC081785 mRNA. Translation: AAH81785.1.
AY625271 mRNA. Translation: AAT39897.1.
PIRiA54140.
RefSeqiNP_112293.1. NM_031031.2.
UniGeneiRn.17661.

Genome annotation databases

GeneIDi81660.
KEGGirno:81660.
UCSCiRGD:71090. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U07971 mRNA. Translation: AAA21250.1.
BC081785 mRNA. Translation: AAH81785.1.
AY625271 mRNA. Translation: AAT39897.1.
PIRiA54140.
RefSeqiNP_112293.1. NM_031031.2.
UniGeneiRn.17661.

3D structure databases

ProteinModelPortaliP50442.
SMRiP50442. Positions 64-423.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000000181.

Chemistry

BindingDBiP50442.

PTM databases

iPTMnetiP50442.
PhosphoSiteiP50442.

Proteomic databases

PaxDbiP50442.
PRIDEiP50442.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi81660.
KEGGirno:81660.
UCSCiRGD:71090. rat.

Organism-specific databases

CTDi2628.
RGDi71090. Gatm.

Phylogenomic databases

eggNOGiENOG410IFBR. Eukaryota.
ENOG410Y45M. LUCA.
HOVERGENiHBG002492.
InParanoidiP50442.
KOiK00613.
OrthoDBiEOG091G07LX.
PhylomeDBiP50442.

Enzyme and pathway databases

UniPathwayiUPA00104; UER00579.
BioCyciMetaCyc:MONOMER-7583.
BRENDAi2.1.4.1. 5301.

Miscellaneous databases

PROiP50442.

Gene expression databases

BgeeiENSRNOG00000000168.
GenevisibleiP50442. RN.

Family and domain databases

InterProiIPR033195. AmidinoTrfase.
[Graphical view]
PANTHERiPTHR10488. PTHR10488. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiGATM_RAT
AccessioniPrimary (citable) accession number: P50442
Secondary accession number(s): Q6ITZ7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: September 7, 2016
This is version 122 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.