ID   GATM_BOVIN              Reviewed;         423 AA.
AC   Q2HJ74;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 92.
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   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Uterus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (FEB-2006) 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; BC113272; AAI13273.1; -; mRNA.
DR   RefSeq; NP_001039343.1; NM_001045878.1.
DR   AlphaFoldDB; Q2HJ74; -.
DR   SMR; Q2HJ74; -.
DR   STRING; 9913.ENSBTAP00000007338; -.
DR   PaxDb; Q2HJ74; -.
DR   PeptideAtlas; Q2HJ74; -.
DR   Ensembl; ENSBTAT00000007338; ENSBTAP00000007338; ENSBTAG00000005586.
DR   GeneID; 414732; -.
DR   KEGG; bta:414732; -.
DR   CTD; 2628; -.
DR   VEuPathDB; HostDB:ENSBTAG00000005586; -.
DR   VGNC; VGNC:29274; GATM.
DR   eggNOG; ENOG502QVCA; Eukaryota.
DR   GeneTree; ENSGT00390000011613; -.
DR   HOGENOM; CLU_047415_1_0_1; -.
DR   InParanoid; Q2HJ74; -.
DR   OMA; SHNEWDP; -.
DR   OrthoDB; 636718at2759; -.
DR   TreeFam; TF300256; -.
DR   Reactome; R-BTA-71288; Creatine metabolism.
DR   UniPathway; UPA00104; UER00579.
DR   Proteomes; UP000009136; Chromosome 10.
DR   Bgee; ENSBTAG00000005586; Expressed in metanephros cortex and 108 other tissues.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; ISS:AgBase.
DR   GO; GO:0005739; C:mitochondrion; ISS:AgBase.
DR   GO; GO:0015067; F:amidinotransferase activity; IBA:GO_Central.
DR   GO; GO:0015068; F:glycine amidinotransferase activity; ISS:AgBase.
DR   GO; GO:0006601; P:creatine biosynthetic process; ISS:AgBase.
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_0000286940"
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;  48357 MW;  A330454DB84EE5BB CRC64;
     MLRVRCLRGG SRGAEALHYI GSRLGRTVTG WVQRTFQSTQ AATASSRNSC AADDKATDPL
     PKDCPVSSFN EWDPLEEVIV GRAENACVPP FTVEVKANTY DKHWPFYQKY GGSYFPKDHL
     QKAVAEIEEM CNILKMEGVT VRRPDPIDWS LKYKTPDFES TGLYGAMPRD ILIVVGNEII
     EAPMAWRARF FEYRAYRTII KDYFRRGAKW TTAPKPTMAD ELYDQDYPIH SVEDRHKLAA
     QGKFVTTEFE PCFDAADFIR AGRDIFVQRS QVTNYMGIEW MRKHLAPDYR VHIVSFKDPN
     PMHIDATFNI IGPGLVLSNP DRPCHQIDLF KKAGWTIVTP PTPIIPDDHP LWMSSKWLSM
     NVLMLDEKRV MVDANEVPIQ KMFEKLGIST IKVSIRNANS LGGGFHCWTC DVRRRGTLQS
     YFD