位置:首页 > 蛋白库 > GCST_CHICK
GCST_CHICK
ID   GCST_CHICK              Reviewed;         392 AA.
AC   P28337;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 2.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=Aminomethyltransferase, mitochondrial {ECO:0000305};
DE            EC=2.1.2.10 {ECO:0000269|PubMed:1526969};
DE   AltName: Full=Glycine cleavage system T protein {ECO:0000303|PubMed:1526969};
DE            Short=GCVT;
DE   Flags: Precursor;
GN   Name=AMT {ECO:0000250|UniProtKB:P48728};
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]
RP   NUCLEOTIDE SEQUENCE [MRNA], TRANSIT PEPTIDE CLEAVAGE SITE, CATALYTIC
RP   ACTIVITY, AND FUNCTION.
RX   PubMed=1526969; DOI=10.1016/s0021-9258(19)36957-1;
RA   Okamura-Ikeda K., Fujiwara K., Motokawa Y.;
RT   "Molecular cloning of a cDNA encoding chicken T-protein of the glycine
RT   cleavage system and expression of the functional protein in Escherichia
RT   coli. Effect of mRNA secondary structure in the translational initiation
RT   region on expression.";
RL   J. Biol. Chem. 267:18284-18290(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 179-392.
RC   TISSUE=Liver;
RX   PubMed=2002038; DOI=10.1016/s0021-9258(19)67736-7;
RA   Okamura-Ikeda K., Fujiwara K., Yamamoto M., Hiraga K., Motokawa Y.;
RT   "Isolation and sequence determination of cDNA encoding T-protein of the
RT   glycine cleavage system.";
RL   J. Biol. Chem. 266:4917-4921(1991).
CC   -!- FUNCTION: The glycine cleavage system catalyzes the degradation of
CC       glycine. {ECO:0000269|PubMed:1526969}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6S)-5,6,7,8-tetrahydrofolate + (R)-N(6)-(S(8)-
CC         aminomethyldihydrolipoyl)-L-lysyl-[protein] = (6R)-5,10-methylene-
CC         5,6,7,8-tetrahydrofolate + (R)-N(6)-dihydrolipoyl-L-lysyl-[protein] +
CC         NH4(+); Xref=Rhea:RHEA:16945, Rhea:RHEA-COMP:10475, Rhea:RHEA-
CC         COMP:10492, ChEBI:CHEBI:15636, ChEBI:CHEBI:28938, ChEBI:CHEBI:57453,
CC         ChEBI:CHEBI:83100, ChEBI:CHEBI:83143; EC=2.1.2.10;
CC         Evidence={ECO:0000269|PubMed:1526969};
CC   -!- SUBUNIT: The glycine cleavage system is composed of four proteins: P,
CC       T, L and H. {ECO:0000305|PubMed:1526969}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000305|PubMed:1526969}.
CC   -!- SIMILARITY: Belongs to the GcvT 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; D11162; BAA01937.1; -; mRNA.
DR   PIR; A44167; A44167.
DR   AlphaFoldDB; P28337; -.
DR   SMR; P28337; -.
DR   STRING; 9031.ENSGALP00000042238; -.
DR   VEuPathDB; HostDB:geneid_395566; -.
DR   eggNOG; KOG2770; Eukaryota.
DR   InParanoid; P28337; -.
DR   OrthoDB; 673132at2759; -.
DR   PhylomeDB; P28337; -.
DR   BioCyc; MetaCyc:MON-12927; -.
DR   BRENDA; 1.4.1.27; 1306.
DR   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0004047; F:aminomethyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR   GO; GO:0019464; P:glycine decarboxylation via glycine cleavage system; IDA:UniProtKB.
DR   Gene3D; 3.30.1360.120; -; 1.
DR   InterPro; IPR006223; GCS_T.
DR   InterPro; IPR028896; GCST/YgfZ/DmdA.
DR   InterPro; IPR013977; GCV_T_C.
DR   InterPro; IPR006222; GCV_T_N.
DR   InterPro; IPR029043; GcvT/YgfZ_C.
DR   InterPro; IPR027266; TrmE/GcvT_dom1.
DR   PANTHER; PTHR43757; PTHR43757; 1.
DR   Pfam; PF01571; GCV_T; 1.
DR   Pfam; PF08669; GCV_T_C; 1.
DR   SUPFAM; SSF101790; SSF101790; 1.
DR   TIGRFAMs; TIGR00528; gcvT; 1.
PE   1: Evidence at protein level;
KW   Aminotransferase; Mitochondrion; Reference proteome; Transferase;
KW   Transit peptide.
FT   TRANSIT         1..16
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000269|PubMed:1526969"
FT   CHAIN           17..392
FT                   /note="Aminomethyltransferase, mitochondrial"
FT                   /id="PRO_0000010757"
FT   BINDING         221
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P48728"
FT   BINDING         250
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P48728"
FT   BINDING         388
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P48728"
SQ   SEQUENCE   392 AA;  42058 MW;  A022434038AF71E0 CRC64;
     MLRAGCRAAL ARRHLSSAPE GLKQTPLDAL HRARGGRMVP FAGWSLPVQY GRGHLESHLH
     TRRHCSLFDV SHMLQTRVYG RDRVRFLESL VVGDIAELRP GQGTLTLLTN ERGDIVDDLI
     VTNTAEDHLY VVSNAGCADK DRAVMEGRAA ELRAAGGDVH LEVSGQRAAG VQGPSMAQVL
     QAGLPDDLTK LTFMTSTATT VFGVPGCRVT RCGYTGEDGV EISVPAGRAV ELAERLLGCP
     EVWPAGLAAR DSLRLEAGLC LYGNDIDEST TPVEAGLLWT LGKRRRTAMD FPGAAIIMEQ
     VKEKPKRKRV GLTSVGPPLR PPAAILGPEG TPVGTVTSGC PSPSLGKNIA MGYVQAAHSR
     PGTTLTVEVR KKQHPALVTK MPFVPTHYYM AK
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024