GATM_MACFA
ID GATM_MACFA Reviewed; 423 AA.
AC Q4R806;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 25-MAY-2022, entry version 60.
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; ORFNames=QtsA-13880;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (JUN-2005) 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}.
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; AB168655; BAE00766.1; -; mRNA.
DR AlphaFoldDB; Q4R806; -.
DR SMR; Q4R806; -.
DR STRING; 9541.XP_005559493.1; -.
DR eggNOG; ENOG502QVCA; Eukaryota.
DR UniPathway; UPA00104; UER00579.
DR Proteomes; UP000233100; Unplaced.
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 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_0000231594"
FT REGION 43..63
FT /note="Disordered"
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; 48599 MW; 9D902170C8DE6D16 CRC64;
MLRVRCLRGG SRGAEAVHYI GSRLGRTLTG WVQRTFQSTQ AATASSRNSF AADDKATEPL
PKDCPVSSYN EWDPLEEVIV GRAENARVPP FTIEVKANTY EKYWPFYQKH GGHYFPKDHL
KKAVTEIEEM CNILKMEGVT VRRPDPIDWS LKYKTPDFES TGLYSAMPRD ILIVVGNEII
EAPMAWRSRF FEYRAYRSII KDYFHRGAKW TTAPKPTMAD ELYDRDYPIH SVEDRHKLAA
QGKFVTTEFE PCFDAADFIR AGKDIFAQRS QVTNYLGIEW MRRHLAPDYR VHIISFKDPN
PMHIDATFNI IGPGTVLSNP DRPCHQIDLF KKAGWTIITP PTPIIPDDHP LWMSSKWLSM
NVLMLDEKRV MVDANEVPTQ KMFEKLGITT IKVNIRNANS LGGGFHCWTC DVRRRGTLQS
YLD
