ID   GATM_PONAB              Reviewed;         423 AA.
AC   Q5RFB9;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Glycine amidinotransferase, mitochondrial;
DE            EC=2.1.4.1 {ECO:0000250|UniProtKB:P50440};
DE   AltName: Full=L-arginine:glycine amidinotransferase;
DE   AltName: Full=Transamidinase;
DE   Flags: Precursor;
GN   Name=GATM;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the biosynthesis of guanidinoacetate, the immediate
CC       precursor of creatine. Creatine plays a vital role in energy metabolism
CC       in muscle tissues. May play a role in embryonic and central nervous
CC       system development (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glycine + L-arginine = guanidinoacetate + L-ornithine;
CC         Xref=Rhea:RHEA:13201, ChEBI:CHEBI:32682, ChEBI:CHEBI:46911,
CC         ChEBI:CHEBI:57305, ChEBI:CHEBI:57742; EC=2.1.4.1;
CC         Evidence={ECO:0000250|UniProtKB:P50440};
CC   -!- PATHWAY: Amine and polyamine biosynthesis; creatine biosynthesis;
CC       creatine from L-arginine and glycine: step 1/2.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the amidinotransferase family. {ECO:0000305}.
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DR   EMBL; CR857241; CAH89538.1; -; mRNA.
DR   RefSeq; NP_001124668.1; NM_001131196.2.
DR   AlphaFoldDB; Q5RFB9; -.
DR   SMR; Q5RFB9; -.
DR   STRING; 9601.ENSPPYP00000007301; -.
DR   Ensembl; ENSPPYT00000007603; ENSPPYP00000007301; ENSPPYG00000006444.
DR   GeneID; 100171513; -.
DR   KEGG; pon:100171513; -.
DR   CTD; 2628; -.
DR   eggNOG; ENOG502QVCA; Eukaryota.
DR   GeneTree; ENSGT00390000011613; -.
DR   InParanoid; Q5RFB9; -.
DR   OrthoDB; 636718at2759; -.
DR   UniPathway; UPA00104; UER00579.
DR   Proteomes; UP000001595; Chromosome 15.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IEA:Ensembl.
DR   GO; GO:0015068; F:glycine amidinotransferase activity; ISS:UniProtKB.
DR   GO; GO:0006601; P:creatine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0007611; P:learning or memory; IEA:Ensembl.
DR   GO; GO:0014889; P:muscle atrophy; IEA:Ensembl.
DR   GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; IEA:Ensembl.
DR   InterPro; IPR033195; AmidinoTrfase.
DR   PANTHER; PTHR10488; PTHR10488; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW   Phosphoprotein; Reference proteome; Transferase; Transit peptide.
FT   TRANSIT         1..37
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000250"
FT   CHAIN           38..423
FT                   /note="Glycine amidinotransferase, mitochondrial"
FT                   /id="PRO_0000231595"
FT   REGION          39..65
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        39..53
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        254
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        303
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        407
FT                   /note="Amidino-cysteine intermediate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         46
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P50440"
FT   MOD_RES         49
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P50440"
FT   MOD_RES         385
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P50440"
SQ   SEQUENCE   423 AA;  48443 MW;  F6AB95D835C2CA36 CRC64;
     MLRVRCLRGG SRGAEAVHYI GSRLGRTLTG WVQRTFQSTQ AATASSRNSS AADDKATEPL
     PKDCPVSSYN EWDPLEEVIV GRAENACVPP FTIEVKANTN EKYWPFYQKH GGHYFPKDHL
     KKAVAEIEEM CNILKMEGVT VRRPDPIDWS LKYKTPDFES TGLYSAMPRD ILIVVGNEII
     EAPMAWRSRF FEYRAYRSII KDYFHRGAKW TTAPKPTMAD ELYNQDYPIH SIEDRHKLAA
     QGKFVTTEFE PCFDAADFIR AGRDIFAQRS QVTNYLGIEW MRRHLAPDYR VHIISFKDPN
     PMHIDATFNI IGPGIVLSNP DRPCHQIDLF KKAGWTIITP PTPIIPDDHP LWMSSKWLSM
     NVLMLDEKRV MVDANEVPIQ KMFEKLGITT IKVNIRNANS LGGGFHCWTC DVRRRGTLQS
     YLD