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GLYC_BOVIN
ID   GLYC_BOVIN              Reviewed;         484 AA.
AC   Q5E9P9; Q2KIP4;
DT   13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   25-MAY-2022, entry version 109.
DE   RecName: Full=Serine hydroxymethyltransferase, cytosolic;
DE            Short=SHMT;
DE            EC=2.1.2.1 {ECO:0000250|UniProtKB:P34896};
DE   AltName: Full=Glycine hydroxymethyltransferase;
DE   AltName: Full=Serine methylase;
GN   Name=SHMT1;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Testis;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Interconversion of serine and glycine.
CC       {ECO:0000250|UniProtKB:P34896}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + glycine + H2O =
CC         (6S)-5,6,7,8-tetrahydrofolate + L-serine; Xref=Rhea:RHEA:15481,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15636, ChEBI:CHEBI:33384,
CC         ChEBI:CHEBI:57305, ChEBI:CHEBI:57453; EC=2.1.2.1;
CC         Evidence={ECO:0000250|UniProtKB:P34896};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250|UniProtKB:P34896};
CC   -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion.
CC       {ECO:0000250|UniProtKB:P34896}.
CC   -!- SUBUNIT: Homotetramer. Identified in complex with ABRAXAS2 and the
CC       other subunits of the BRISC complex, at least composed of ABRAXAS2,
CC       BRCC3/BRCC36, BABAM2 and BABAM1/NBA1. {ECO:0000250|UniProtKB:P34896}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- MISCELLANEOUS: In eukaryotes there are two forms of the enzymes: a
CC       cytosolic one and a mitochondrial one. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the SHMT family. {ECO:0000305}.
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DR   EMBL; BT020871; AAX08888.1; -; mRNA.
DR   EMBL; BC112563; AAI12564.1; -; mRNA.
DR   RefSeq; NP_001015553.1; NM_001015553.1.
DR   RefSeq; XP_005220393.1; XM_005220336.3.
DR   RefSeq; XP_015314201.1; XM_015458715.1.
DR   AlphaFoldDB; Q5E9P9; -.
DR   SMR; Q5E9P9; -.
DR   STRING; 9913.ENSBTAP00000022732; -.
DR   PaxDb; Q5E9P9; -.
DR   PeptideAtlas; Q5E9P9; -.
DR   GeneID; 509002; -.
DR   KEGG; bta:509002; -.
DR   CTD; 6470; -.
DR   eggNOG; KOG2467; Eukaryota.
DR   HOGENOM; CLU_022477_0_1_1; -.
DR   InParanoid; Q5E9P9; -.
DR   OrthoDB; 372408at2759; -.
DR   TreeFam; TF314667; -.
DR   UniPathway; UPA00193; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0004372; F:glycine hydroxymethyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; ISS:UniProtKB.
DR   GO; GO:0019264; P:glycine biosynthetic process from serine; IEA:InterPro.
DR   GO; GO:0006544; P:glycine metabolic process; ISS:UniProtKB.
DR   GO; GO:0006563; P:L-serine metabolic process; ISS:UniProtKB.
DR   GO; GO:0051289; P:protein homotetramerization; ISS:UniProtKB.
DR   GO; GO:0035999; P:tetrahydrofolate interconversion; IEA:UniProtKB-UniPathway.
DR   GO; GO:0046653; P:tetrahydrofolate metabolic process; ISS:UniProtKB.
DR   CDD; cd00378; SHMT; 1.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   HAMAP; MF_00051; SHMT; 1.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   InterPro; IPR001085; Ser_HO-MeTrfase.
DR   InterPro; IPR019798; Ser_HO-MeTrfase_PLP_BS.
DR   InterPro; IPR039429; SHMT-like_dom.
DR   PANTHER; PTHR11680; PTHR11680; 1.
DR   Pfam; PF00464; SHMT; 1.
DR   PIRSF; PIRSF000412; SHMT; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   PROSITE; PS00096; SHMT; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Cytoplasm; One-carbon metabolism; Pyridoxal phosphate;
KW   Reference proteome; Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P07511"
FT   CHAIN           2..484
FT                   /note="Serine hydroxymethyltransferase, cytosolic"
FT                   /id="PRO_0000239698"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:P07511"
FT   MOD_RES         257
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250|UniProtKB:P34896"
FT   CONFLICT        459
FT                   /note="H -> Q (in Ref. 2; AAI12564)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   484 AA;  52978 MW;  B17A018307125C11 CRC64;
     MAAPVNKAPR DANLWSLHEK MLAQPLKDND VEVYNIIKKE SNRQRVGLEL IASENFASRA
     VLEALGSCLN NKYSEGYPGQ RYYGGTEFID ELEVLCQKRA LQVYGLDSQC WGVNVQPYSG
     SPANFAVYTA LVEPHGRIMG LDLPDGGHLT HGFMTDKKKI SATSIFFESM PYKVNPDTGY
     INYDQLEENA RLFHPRLIIA GTSCYSRNLD YARLRKIADD NGAYLMADMA HVSGLVAAGV
     VPSPFEHCHV VSTTTHKTLR GCRAGMIFYR KGVRSVDPKT GRETRYNLES LINSAVFPGL
     QGGPHNHAIA GVAVALKQAM TPEFRAYQRQ VVANCRALAE ALMGLGYRVV TGGSDNHLIL
     VDLRSKGTDG GRAEKVLEAC SIACNKNTCP GDKSALRPSG LRLGTPALTS RGLLEEDFQK
     VAHFIHRGIE LTLQIQDAVG VKATLKEFME KLAGAEEHHR AVAALRAEVE SFATLFPLPG
     LPGF
 
 
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