ID   GATM_XENTR              Reviewed;         422 AA.
AC   Q6P832; Q28HI2;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Glycine amidinotransferase, mitochondrial {ECO:0000250|UniProtKB:P50440};
DE            EC=2.1.4.1 {ECO:0000250|UniProtKB:P50440};
DE   AltName: Full=L-arginine:glycine amidinotransferase {ECO:0000250|UniProtKB:P50440};
DE   AltName: Full=Transamidinase {ECO:0000250|UniProtKB:P50440};
DE   Flags: Precursor;
GN   Name=gatm {ECO:0000312|EMBL:CAJ82904.1,
GN   ECO:0000312|Xenbase:XB-GENE-974514};
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1] {ECO:0000312|EMBL:CAJ82904.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Tadpole {ECO:0000312|EMBL:CAJ82904.1};
RG   Sanger Xenopus tropicalis EST/cDNA project;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000312|EMBL:CAJ82904.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Neurula {ECO:0000312|EMBL:AAH61399.1};
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (NOV-2003) 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       {ECO:0000250|UniProtKB:P50440}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P50440}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000250|UniProtKB:P50440}.
CC   -!- SIMILARITY: Belongs to the amidinotransferase family. {ECO:0000255}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CR760875; CAJ82904.1; -; mRNA.
DR   EMBL; BC061399; AAH61399.1; -; mRNA.
DR   RefSeq; NP_988971.1; NM_203640.1.
DR   AlphaFoldDB; Q6P832; -.
DR   SMR; Q6P832; -.
DR   STRING; 8364.ENSXETP00000035125; -.
DR   PaxDb; Q6P832; -.
DR   DNASU; 394568; -.
DR   Ensembl; ENSXETT00000035125; ENSXETP00000035125; ENSXETG00000016109.
DR   GeneID; 394568; -.
DR   KEGG; xtr:394568; -.
DR   CTD; 2628; -.
DR   Xenbase; XB-GENE-974514; gatm.
DR   eggNOG; ENOG502QVCA; Eukaryota.
DR   HOGENOM; CLU_047415_1_0_1; -.
DR   InParanoid; Q6P832; -.
DR   OMA; GGFHCAT; -.
DR   OrthoDB; 636718at2759; -.
DR   PhylomeDB; Q6P832; -.
DR   TreeFam; TF300256; -.
DR   Reactome; R-XTR-71288; Creatine metabolism.
DR   UniPathway; UPA00104; UER00579.
DR   Proteomes; UP000008143; Chromosome 3.
DR   Proteomes; UP000790000; Unplaced.
DR   Bgee; ENSXETG00000016109; Expressed in neurula embryo and 4 other tissues.
DR   ExpressionAtlas; Q6P832; baseline.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0015067; F:amidinotransferase activity; IBA:GO_Central.
DR   GO; GO:0015068; F:glycine amidinotransferase activity; ISS:UniProtKB.
DR   GO; GO:0006601; P:creatine biosynthetic process; IBA:GO_Central.
DR   InterPro; IPR033195; AmidinoTrfase.
DR   PANTHER; PTHR10488; PTHR10488; 1.
PE   2: Evidence at transcript level;
KW   Membrane; Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW   Transferase; Transit peptide.
FT   TRANSIT         1..37
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000250|UniProtKB:P50441"
FT   CHAIN           38..422
FT                   /note="Glycine amidinotransferase, mitochondrial"
FT                   /evidence="ECO:0000250|UniProtKB:P50441"
FT                   /id="PRO_0000399098"
FT   ACT_SITE        253
FT                   /evidence="ECO:0000250|UniProtKB:P50440"
FT   ACT_SITE        302
FT                   /evidence="ECO:0000250|UniProtKB:P50440"
FT   ACT_SITE        406
FT                   /note="Amidino-cysteine intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:P50440"
FT   CONFLICT        50
FT                   /note="A -> T (in Ref. 1; CAJ82904)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   422 AA;  48424 MW;  EF4EA3FDC393A67E CRC64;
     MLRVRCVRGG SRGAEAVHYI GSMLRKGFVG WVQRSFQSTQ AAAVSEKPCA ADEKVSDTAV
     QECPVCSYNE WDPLEEVIVG RPENANVPPF SVEVKANTYE KYWPFYQKHG GQSFPVEHVK
     KATEEIEEMC NVLRHEGVVV QRPEVIDWSV KYKTPDFEST GMYAAMPRDI LLVVGNEIIE
     APMAWRARFF EYRAYRPLIK DYFRRGAKWT TAPKPTMADE LYDQDYPIRT VEDRHKLAAM
     GKFVTTEFEP CFDAADFMRA GRDIFAQRSQ VTNYLGIEWM RRHLAPDYKV HIISFKDPNP
     MHIDATFNII GPGLVLSNPD RPCHQIELFK KAGWTVVTPP IPLIPDNHPL WMSSKWLSMN
     VLMLDEKRVM VDANETSIQK MFEKLGISTI KVNIRHANSL GGGFHCWTCD IRRRGTLQSY
     FS