ID   GATM_XENLA              Reviewed;         422 AA.
AC   Q9IAJ6;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 2.
DT   03-AUG-2022, entry version 77.
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:0000303|PubMed:11466533};
DE   AltName: Full=Transamidinase {ECO:0000250|UniProtKB:P50440};
DE   Flags: Precursor;
GN   Name=gatm {ECO:0000312|Xenbase:XB-GENE-974520};
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:AAF31361.2}
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC   TISSUE=Ectoderm {ECO:0000312|EMBL:AAF31361.2};
RX   PubMed=11466533; DOI=10.1007/s004270100161;
RA   Zhao H., Cao Y., Grunz H.;
RT   "Expression of Xenopus L-arginine:glycine amidinotransferase (XAT) during
RT   early embryonic development.";
RL   Dev. Genes Evol. 211:358-360(2001).
RN   [2] {ECO:0000312|EMBL:AAH47973.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Tail bud {ECO:0000312|EMBL:AAH47973.1};
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (MAR-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   -!- TISSUE SPECIFICITY: Ubiquitously expressed in adult tissues, with
CC       highest levels in muscle and intermediate levels in eye, heart, liver,
CC       stomach and testis. In stage 28 embryos, expression is higher in the
CC       dorsal and ventral parts of the trunk than in the head. In middle
CC       gastrulae, expression is highest around the yolk plug, while in stage
CC       15 and tailbud stage embryos, expression is largely restricted to the
CC       region around the presumptive notochord and gut.
CC       {ECO:0000269|PubMed:11466533}.
CC   -!- DEVELOPMENTAL STAGE: Expressed during embryonic development from the
CC       mid-gastrula stage onwards. {ECO:0000269|PubMed:11466533}.
CC   -!- SIMILARITY: Belongs to the amidinotransferase family. {ECO:0000255}.
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DR   EMBL; AF187863; AAF31361.2; -; mRNA.
DR   EMBL; BC047973; AAH47973.1; -; mRNA.
DR   RefSeq; NP_001079699.1; NM_001086230.1.
DR   AlphaFoldDB; Q9IAJ6; -.
DR   SMR; Q9IAJ6; -.
DR   DNASU; 379386; -.
DR   GeneID; 379386; -.
DR   KEGG; xla:379386; -.
DR   CTD; 379386; -.
DR   Xenbase; XB-GENE-974520; gatm.L.
DR   OrthoDB; 636718at2759; -.
DR   BRENDA; 2.1.4.1; 6725.
DR   UniPathway; UPA00104; UER00579.
DR   Proteomes; UP000186698; Chromosome 3L.
DR   Bgee; 379386; Expressed in gastrula and 12 other tissues.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015068; F:glycine amidinotransferase activity; ISS:UniProtKB.
DR   GO; GO:0006601; P:creatine biosynthetic process; IEA:UniProtKB-UniPathway.
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_0000399097"
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"
SQ   SEQUENCE   422 AA;  48573 MW;  5C60EF378767515B CRC64;
     MLRVRCLRGG SRGAEAVHYI GSMLRKSFVG WVQRSFQSTQ AAAVSEKPCA ADEKVRDTAA
     QECPVCSYNE WDPLEEVIVG RPENANVPPF SVEVKANTYE KYWPFYQKHG GQSFPVDHVK
     KAIEEIEEMC KVLKHEGVIV QRPEVIDWSV KYKTPDFEST GMYAAMPRDI LLVVGNEIIE
     APMAWRARFF EYRAYRPLIK DYFRRGAKWT TAPKPTMADE LYDQDYPIRT VEDRHKLAAM
     GKFVTTEFEP CFDAADFMRA GRDIFAQRSQ VTNYLGIEWM RRHLAPDYKV HIISFKDPNP
     MHIDATFNII GPGLVLSNPD RPCHQIELFK KAGWTVVTPP TPLIPDNHPL WMSSKWLSMN
     VLMLDEKRVM VDANETSIHK MFEKLGISTI KVNIRHANSL GGGFHCWTCD IRRRGTLQSY
     FR