ID F6ZA35_CIOIN Unreviewed; 410 AA.
AC F6ZA35; A0A1W2WDH0;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 2.
DT 27-MAR-2024, entry version 61.
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=LOC100186832 {ECO:0000313|Ensembl:ENSCINP00000026713.2};
OS Ciona intestinalis (Transparent sea squirt) (Ascidia intestinalis).
OC Eukaryota; Metazoa; Chordata; Tunicata; Ascidiacea; Phlebobranchia;
OC Cionidae; Ciona.
OX NCBI_TaxID=7719 {ECO:0000313|Ensembl:ENSCINP00000026713.2, ECO:0000313|Proteomes:UP000008144};
RN [1] {ECO:0000313|Proteomes:UP000008144}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12481130; DOI=10.1126/science.1080049;
RA Dehal P., Satou Y., Campbell R.K., Chapman J., Degnan B., De Tomaso A.,
RA Davidson B., Di Gregorio A., Gelpke M., Goodstein D.M., Harafuji N.,
RA Hastings K.E., Ho I., Hotta K., Huang W., Kawashima T., Lemaire P.,
RA Martinez D., Meinertzhagen I.A., Necula S., Nonaka M., Putnam N., Rash S.,
RA Saiga H., Satake M., Terry A., Yamada L., Wang H.G., Awazu S., Azumi K.,
RA Boore J., Branno M., Chin-Bow S., DeSantis R., Doyle S., Francino P.,
RA Keys D.N., Haga S., Hayashi H., Hino K., Imai K.S., Inaba K., Kano S.,
RA Kobayashi K., Kobayashi M., Lee B.I., Makabe K.W., Manohar C., Matassi G.,
RA Medina M., Mochizuki Y., Mount S., Morishita T., Miura S., Nakayama A.,
RA Nishizaka S., Nomoto H., Ohta F., Oishi K., Rigoutsos I., Sano M.,
RA Sasaki A., Sasakura Y., Shoguchi E., Shin-i T., Spagnuolo A., Stainier D.,
RA Suzuki M.M., Tassy O., Takatori N., Tokuoka M., Yagi K., Yoshizaki F.,
RA Wada S., Zhang C., Hyatt P.D., Larimer F., Detter C., Doggett N.,
RA Glavina T., Hawkins T., Richardson P., Lucas S., Kohara Y., Levine M.,
RA Satoh N., Rokhsar D.S.;
RT "The draft genome of Ciona intestinalis: insights into chordate and
RT vertebrate origins.";
RL Science 298:2157-2167(2002).
RN [2] {ECO:0000313|Ensembl:ENSCINP00000026713.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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. {ECO:0000256|RuleBase:RU367092}.
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|RuleBase:RU367092};
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 RefSeq; XP_002125524.1; XM_002125488.3.
DR AlphaFoldDB; F6ZA35; -.
DR STRING; 7719.ENSCINP00000026713; -.
DR Ensembl; ENSCINT00000026959.2; ENSCINP00000026713.2; ENSCING00000014878.2.
DR GeneID; 100186832; -.
DR KEGG; cin:100186832; -.
DR GeneTree; ENSGT00390000011613; -.
DR HOGENOM; CLU_047415_1_0_1; -.
DR InParanoid; F6ZA35; -.
DR OMA; SHNEWDP; -.
DR OrthoDB; 2347075at2759; -.
DR TreeFam; TF300256; -.
DR UniPathway; UPA00104; UER00579.
DR Proteomes; UP000008144; 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; IEA:UniProtKB-UniRule.
DR GO; GO:0006601; P:creatine biosynthetic process; IEA:UniProtKB-UniRule.
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:UP000008144};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU367092}.
FT ACT_SITE 242
FT /evidence="ECO:0000256|PIRSR:PIRSR633195-1"
FT ACT_SITE 291
FT /evidence="ECO:0000256|PIRSR:PIRSR633195-1"
FT ACT_SITE 395
FT /note="Amidino-cysteine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR633195-1"
SQ SEQUENCE 410 AA; 47105 MW; ED1C13D7262ED8D4 CRC64;
MKTLQSVSAV LRQTKLVSDV LLKATGSGSV LTARTQHAKR VVPGEIPQPS IPVNSHNEWD
PLEEVIVGRP DGACVPQFTT EVKANTNEKY WDFYKKYGGT PFPDKHIEKA KQEVEEMCNV
LRHEGVIVRR PDVINWEKDY KTPDFSSPVG LYSAMPRDIL IVFGNEIMEA PMAWRSRFFE
YRAYRSLLKE YFKAGAKWTA APKPLMGDEL YDNTYPIESI EDRHRLAKEG RFVTTEFEPC
FDAADFIRAG RDIFVQRSQV TNHLGIEWLR RHLGPEYRVH ELTFHDPNPM HIDATFNIIG
PGLVIANPDR PCNQLKMFEK FGWKIVQAPK PTLSDDHPLW MSSKWLSMNV LMLDEDRVLC
SKVEKPIIKM FEKLGIKTVQ VDITHANSLG GGFHCWTTDV RRRGELQSYI
//
