GATM_DANRE
ID GATM_DANRE Reviewed; 422 AA.
AC Q6PH19;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 85.
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:AAH56747.1};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1] {ECO:0000312|EMBL:AAH56747.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo {ECO:0000312|EMBL:AAH56747.1};
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000305}
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=17486546; DOI=10.1387/ijdb.062218lw;
RA Wang L., Zhang Y., Shao M., Zhang H.;
RT "Spatiotemporal expression of the creatine metabolism related genes agat,
RT gamt and ct1 during zebrafish embryogenesis.";
RL Int. J. Dev. Biol. 51:247-253(2007).
RN [3] {ECO:0000305}
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=20409172; DOI=10.1111/j.1095-8649.2010.02555.x;
RA Wang L., Chen D., Yang L., Huang S., Zhang Y., Zhang H.;
RT "Expression patterns of the creatine metabolism-related molecules AGAT,
RT GAMT and CT1 in adult zebrafish Danio rerio.";
RL J. Fish Biol. 76:1212-1219(2010).
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: Strongly expressed in neurons and glia of the
CC brain, the lamina propria, submucosa and serosa of the small intestine,
CC in oocytes and on the fringes of the pancreas. Not expressed in the
CC retina, eye lens, heart or bulbus arteriosus. Expressed in the yolk
CC syncytial layer in gastrula stage embryos, in the yolk syncytial layer
CC and mature somites in early segmentation embryos and in the yolk
CC syncytial layer and the liver of long-pec stage (48 hours post-
CC fertilization) embryos. {ECO:0000269|PubMed:17486546,
CC ECO:0000269|PubMed:20409172}.
CC -!- DEVELOPMENTAL STAGE: Widely expressed during maturation of oocytes.
CC Also expressed in embryos from gastrulation onwards in the yolk
CC syncytial layer and somites. Expression declines in the somites, but is
CC up-regulated in the yolk syncytial layer throughout embryonic
CC development. {ECO:0000269|PubMed:17486546,
CC ECO:0000269|PubMed:20409172}.
CC -!- SIMILARITY: Belongs to the amidinotransferase family. {ECO:0000255}.
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DR EMBL; BC056747; AAH56747.1; -; mRNA.
DR RefSeq; NP_955825.1; NM_199531.1.
DR AlphaFoldDB; Q6PH19; -.
DR SMR; Q6PH19; -.
DR STRING; 7955.ENSDARP00000052640; -.
DR PaxDb; Q6PH19; -.
DR GeneID; 266799; -.
DR KEGG; dre:266799; -.
DR CTD; 2628; -.
DR ZFIN; ZDB-GENE-021015-1; gatm.
DR eggNOG; ENOG502QVCA; Eukaryota.
DR InParanoid; Q6PH19; -.
DR OrthoDB; 636718at2759; -.
DR PhylomeDB; Q6PH19; -.
DR Reactome; R-DRE-71288; Creatine metabolism.
DR UniPathway; UPA00104; UER00579.
DR PRO; PR:Q6PH19; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
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; 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..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000250|UniProtKB:P50441"
FT CHAIN ?..422
FT /note="Glycine amidinotransferase, mitochondrial"
FT /evidence="ECO:0000250|UniProtKB:P50441"
FT /id="PRO_0000399096"
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; 48075 MW; B453639A69E24E12 CRC64;
MLRVRCLRGG SRGAEAAHLI GALVGRALSG RLSRASRSSS SSAAAQLPLS AHEQVPEPTA
EECPVCAHNE WDPLEEVIVG RAENACVPPF TVEVKANTYE KYWPFYQQYG GQTFPKEHVQ
KAVAEIEEMC NILQHEGVTV RRPEPVDWSL EYRTPDFSST GMYAAMPRDI LMVVGNEIIE
APMAWRARFF EYRAYRPLIK EYFRRGARWT TAPKPTMADQ LYDQDYPIRT VEDRHKLAAQ
GKFVTTEFEP CFDAADFIRA GTDIFVQRSQ VTNYMGIEWM RRHLSPTYKI HIISFKDPNP
MHIDATFNII GPGLVLSNPD RPCRQIEMFK KAGWTVVTPP TPLIPDNHPL WMSSKWLSMN
VLMLDEKRVM VDANESTIQK MFESLGIKTV KVSIRHANSL GGGFHCWTTD VRRRGTLQSY
FL
