ID H0VB49_CAVPO Unreviewed; 423 AA.
AC H0VB49;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=Glycine amidinotransferase {ECO:0000256|RuleBase:RU367092};
DE EC=2.1.4.1 {ECO:0000256|RuleBase:RU367092};
DE AltName: Full=L-arginine:glycine amidinotransferase {ECO:0000256|RuleBase:RU367092};
GN Name=GATM {ECO:0000313|Ensembl:ENSCPOP00000007115.2};
OS Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141 {ECO:0000313|Ensembl:ENSCPOP00000007115.2, ECO:0000313|Proteomes:UP000005447};
RN [1] {ECO:0000313|Proteomes:UP000005447}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2N {ECO:0000313|Proteomes:UP000005447};
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSCPOP00000007115.2}
RP IDENTIFICATION.
RC STRAIN=2N {ECO:0000313|Ensembl:ENSCPOP00000007115.2};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Transamidinase that catalyzes the transfer of the amidino
CC group of L-arginine onto the amino moiety of acceptor metabolites such
CC as glycine, beta-alanine, gamma-aminobutyric acid (GABA) and taurine
CC yielding the corresponding guanidine derivatives. Catalyzes the rate-
CC limiting step of creatine biosynthesis, namely the transfer of the
CC amidino group from L-arginine to glycine to generate guanidinoacetate,
CC which is then methylated by GAMT to form creatine. Provides creatine as
CC a source for ATP generation in tissues with high energy demands, in
CC particular skeletal muscle, heart and brain.
CC {ECO:0000256|RuleBase:RU367092}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-aminobutanoate + L-arginine = 4-guanidinobutanoate + L-
CC ornithine; Xref=Rhea:RHEA:75939, ChEBI:CHEBI:32682,
CC ChEBI:CHEBI:46911, ChEBI:CHEBI:57486, ChEBI:CHEBI:59888;
CC Evidence={ECO:0000256|ARBA:ARBA00035092};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75940;
CC Evidence={ECO:0000256|ARBA:ARBA00035092};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-arginine + taurine = L-ornithine + taurocyamine;
CC Xref=Rhea:RHEA:75947, ChEBI:CHEBI:32682, ChEBI:CHEBI:46911,
CC ChEBI:CHEBI:58064, ChEBI:CHEBI:507393;
CC Evidence={ECO:0000256|ARBA:ARBA00035096};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75948;
CC Evidence={ECO:0000256|ARBA:ARBA00035096};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-alanine + L-arginine = 3-guanidinopropanoate + L-
CC ornithine; Xref=Rhea:RHEA:75943, ChEBI:CHEBI:32682,
CC ChEBI:CHEBI:46911, ChEBI:CHEBI:57593, ChEBI:CHEBI:57966;
CC Evidence={ECO:0000256|ARBA:ARBA00035094};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75944;
CC Evidence={ECO:0000256|ARBA:ARBA00035094};
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:0000256|ARBA:ARBA00035078};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13202;
CC Evidence={ECO:0000256|ARBA:ARBA00035078};
CC -!- PATHWAY: Amine and polyamine biosynthesis; creatine biosynthesis;
CC creatine from L-arginine and glycine: step 1/2.
CC {ECO:0000256|ARBA:ARBA00004858, ECO:0000256|RuleBase:RU367092}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|RuleBase:RU367092}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000256|RuleBase:RU367092}.
CC -!- SIMILARITY: Belongs to the amidinotransferase family.
CC {ECO:0000256|ARBA:ARBA00006943, ECO:0000256|RuleBase:RU367092}.
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DR EMBL; AAKN02027665; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_003471896.1; XM_003471848.3.
DR AlphaFoldDB; H0VB49; -.
DR STRING; 10141.ENSCPOP00000007115; -.
DR Ensembl; ENSCPOT00000007979.3; ENSCPOP00000007115.2; ENSCPOG00000007904.4.
DR GeneID; 100714491; -.
DR KEGG; cpoc:100714491; -.
DR CTD; 2628; -.
DR VEuPathDB; HostDB:ENSCPOG00000007904; -.
DR eggNOG; ENOG502QVCA; Eukaryota.
DR GeneTree; ENSGT00390000011613; -.
DR HOGENOM; CLU_047415_1_0_1; -.
DR InParanoid; H0VB49; -.
DR OMA; SHNEWDP; -.
DR OrthoDB; 2347075at2759; -.
DR TreeFam; TF300256; -.
DR UniPathway; UPA00104; UER00579.
DR Proteomes; UP000005447; Unassembled WGS sequence.
DR Bgee; ENSCPOG00000007904; Expressed in thyroid gland and 13 other cell types or tissues.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IEA:Ensembl.
DR GO; GO:0015068; F:glycine amidinotransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006601; P:creatine biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0007611; P:learning or memory; IEA:Ensembl.
DR GO; GO:0014889; P:muscle atrophy; IEA:Ensembl.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; IEA:Ensembl.
DR CDD; cd21136; amidinotransferase_AGAT-like; 1.
DR InterPro; IPR033195; AmidinoTrfase.
DR PANTHER; PTHR10488; GLYCINE AMIDINOTRANSFERASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR10488:SF1; GLYCINE AMIDINOTRANSFERASE, MITOCHONDRIAL; 1.
DR SUPFAM; SSF55909; Pentein; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|RuleBase:RU367092};
KW Mitochondrion {ECO:0000256|RuleBase:RU367092};
KW Mitochondrion inner membrane {ECO:0000256|RuleBase:RU367092};
KW Reference proteome {ECO:0000313|Proteomes:UP000005447};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU367092}.
FT ACT_SITE 254
FT /evidence="ECO:0000256|PIRSR:PIRSR633195-1"
FT ACT_SITE 303
FT /evidence="ECO:0000256|PIRSR:PIRSR633195-1"
FT ACT_SITE 407
FT /note="Amidino-cysteine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR633195-1"
SQ SEQUENCE 423 AA; 48629 MW; 3CA6A8FC71AEB611 CRC64;
MLRVRCVRGG SRGAEALHYL GSRLGRTLTG WVQRTFQSTQ AAPASSQKSC AADDKATDPL
PKDCPVSSYN EWDPLEEVIV GRAENACVPP FTVEVKANTY EKYWPFYQKY GGQYFPKDHL
KKAVAEIEEM CNILKMEGVI VRRPDPIDWS FQYKTPDFES TGLYSAMPRD ILIVVGNEII
EAPMAWRSRF FEYRAYRSLI KDYFHRGAKW TTAPKPMMVD ELYDKDYPIH NVEDRHRLAA
QGKFVTTEFE PCFDAADFIR AGRDIFAQRS QVTNYLGIEW MRRHLAPDYR VHIISFKDPN
PMHIDATFNI IGPGLVLSNP DRPCHQIDLF KKAGWTIVTP PTPIIPDDHP LWMSSKWLSM
NVLMLDEKRV MVDANEIPTQ KMFEKLGIST VKVNIRHANS LGGGFHCWTC DVRRRGSLQS
YFD
//
