GATM_CHICK
ID GATM_CHICK Reviewed; 422 AA.
AC Q9I9K9;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 2.
DT 03-AUG-2022, entry version 92.
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:0000250|UniProtKB:P50440};
GN Synonyms=AT {ECO:0000312|EMBL:AAF61951.2};
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-198.
RC STRAIN=White Leghorn Hisex {ECO:0000305};
RX PubMed=12445392; DOI=10.1016/s0960-9822(02)01296-4;
RA Boardman P.E., Sanz-Ezquerro J., Overton I.M., Burt D.W., Bosch E.,
RA Fong W.T., Tickle C., Brown W.R., Wilson S.A., Hubbard S.J.;
RT "A comprehensive collection of chicken cDNAs.";
RL Curr. Biol. 12:1965-1969(2002).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAF61951.2}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 13-422, AND INDUCTION.
RX PubMed=11506177; DOI=10.1023/a:1010946414017;
RA Zhu Y., Evans M.I.;
RT "Estrogen modulates the expression of L-arginine:glycine amidinotransferase
RT in chick liver.";
RL Mol. Cell. Biochem. 221:139-145(2001).
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 -!- INDUCTION: Transiently induced by estrogen, with levels peaking an hour
CC after hormone injection. {ECO:0000269|PubMed:11506177}.
CC -!- SIMILARITY: Belongs to the amidinotransferase family. {ECO:0000255}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF61951.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; BU129729; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AF237950; AAF61951.2; ALT_INIT; mRNA.
DR RefSeq; NP_990076.1; NM_204745.1.
DR AlphaFoldDB; Q9I9K9; -.
DR SMR; Q9I9K9; -.
DR STRING; 9031.ENSGALP00000037948; -.
DR PaxDb; Q9I9K9; -.
DR GeneID; 395504; -.
DR KEGG; gga:395504; -.
DR CTD; 2628; -.
DR VEuPathDB; HostDB:geneid_395504; -.
DR eggNOG; ENOG502QVCA; Eukaryota.
DR InParanoid; Q9I9K9; -.
DR OrthoDB; 636718at2759; -.
DR PhylomeDB; Q9I9K9; -.
DR BRENDA; 2.1.4.1; 1306.
DR UniPathway; UPA00104; UER00579.
DR PRO; PR:Q9I9K9; -.
DR Proteomes; UP000000539; 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 Membrane; Mitochondrion; Mitochondrion inner membrane; Phosphoprotein;
KW Reference proteome; 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_0000399095"
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 MOD_RES 416
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9D964"
FT CONFLICT 18
FT /note="H -> N (in Ref. 2; AAF61951)"
FT /evidence="ECO:0000305"
FT CONFLICT 20
FT /note="I -> M (in Ref. 2; AAF61951)"
FT /evidence="ECO:0000305"
FT CONFLICT 50
FT /note="A -> P (in Ref. 2; AAF61951)"
FT /evidence="ECO:0000305"
FT CONFLICT 149
FT /note="S -> P (in Ref. 2; AAF61951)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 422 AA; 48311 MW; D4896DCF97C7FD27 CRC64;
MLRVRCLRGG SRGAEAAHFI GSRLGRAFTG WVQRSLQSTQ AAAASQNRCA AEDKAQSPAP
KECPVCSYNE WDPLEEVIVG RAENACVPPF SVEVKANTYE KYWGFYQKFG GESFPKDHVK
KAIAEIEEMC NILKKEGVIV KRPDPIDWSV KYRTPDFEST GMYAAMPRDI LLVVGNEIIE
APMAWRARFF EYRAYRRIIK DYFNNGAKWT TAPKPTMADE LYDQDYPIRS VEDRHKLAAQ
GKFVTTEFEP CFDAADFIRA GRDIFVQRSQ VTNYMGIEWM RRHLAPDYRV HVISFKDPNP
MHIDTTFNII GPGLVLSNPD RPCHQIELFK KAGWTVIHPP VPLIPDDHPL WMSSKWLSMN
VLMLDEKRVM VDANETSIQK MFENLGISTI KVNIRHANSL GGGFHCWTCD IRRRGTLQSY
FD
