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GLYA_STRT1
ID   GLYA_STRT1              Reviewed;         416 AA.
AC   Q5M0B4;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Serine hydroxymethyltransferase {ECO:0000255|HAMAP-Rule:MF_00051};
DE            Short=SHMT {ECO:0000255|HAMAP-Rule:MF_00051};
DE            Short=Serine methylase {ECO:0000255|HAMAP-Rule:MF_00051};
DE            EC=2.1.2.1 {ECO:0000255|HAMAP-Rule:MF_00051};
GN   Name=glyA {ECO:0000255|HAMAP-Rule:MF_00051}; OrderedLocusNames=str0755;
OS   Streptococcus thermophilus (strain CNRZ 1066).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=299768;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CNRZ 1066;
RX   PubMed=15543133; DOI=10.1038/nbt1034;
RA   Bolotin A., Quinquis B., Renault P., Sorokin A., Ehrlich S.D.,
RA   Kulakauskas S., Lapidus A., Goltsman E., Mazur M., Pusch G.D., Fonstein M.,
RA   Overbeek R., Kyprides N., Purnelle B., Prozzi D., Ngui K., Masuy D.,
RA   Hancy F., Burteau S., Boutry M., Delcour J., Goffeau A., Hols P.;
RT   "Complete sequence and comparative genome analysis of the dairy bacterium
RT   Streptococcus thermophilus.";
RL   Nat. Biotechnol. 22:1554-1558(2004).
CC   -!- FUNCTION: Catalyzes the reversible interconversion of serine and
CC       glycine with tetrahydrofolate (THF) serving as the one-carbon carrier.
CC       This reaction serves as the major source of one-carbon groups required
CC       for the biosynthesis of purines, thymidylate, methionine, and other
CC       important biomolecules. Also exhibits THF-independent aldolase activity
CC       toward beta-hydroxyamino acids, producing glycine and aldehydes, via a
CC       retro-aldol mechanism. {ECO:0000255|HAMAP-Rule:MF_00051}.
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:0000255|HAMAP-Rule:MF_00051};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00051};
CC   -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion.
CC       {ECO:0000255|HAMAP-Rule:MF_00051}.
CC   -!- PATHWAY: Amino-acid biosynthesis; glycine biosynthesis; glycine from L-
CC       serine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00051}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00051}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00051}.
CC   -!- SIMILARITY: Belongs to the SHMT family. {ECO:0000255|HAMAP-
CC       Rule:MF_00051}.
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DR   EMBL; CP000024; AAV62348.1; -; Genomic_DNA.
DR   RefSeq; WP_011227085.1; NC_006449.1.
DR   PDB; 4WXB; X-ray; 2.05 A; A/B/C/D=1-416.
DR   PDB; 4WXF; X-ray; 2.40 A; A/C=1-416.
DR   PDB; 4WXG; X-ray; 2.00 A; A/C=1-416.
DR   PDB; 6TGH; X-ray; 2.12 A; A/B/C/D=2-416.
DR   PDB; 6TI1; X-ray; 2.00 A; A/C=1-416.
DR   PDB; 6TI3; X-ray; 1.96 A; A/B/C/D=1-416.
DR   PDB; 6YRW; X-ray; 2.50 A; A/B/C/D=1-416.
DR   PDBsum; 4WXB; -.
DR   PDBsum; 4WXF; -.
DR   PDBsum; 4WXG; -.
DR   PDBsum; 6TGH; -.
DR   PDBsum; 6TI1; -.
DR   PDBsum; 6TI3; -.
DR   PDBsum; 6YRW; -.
DR   AlphaFoldDB; Q5M0B4; -.
DR   SMR; Q5M0B4; -.
DR   KEGG; stc:str0755; -.
DR   HOGENOM; CLU_022477_2_1_9; -.
DR   OMA; SHPAGLI; -.
DR   BRENDA; 2.1.2.1; 5956.
DR   UniPathway; UPA00193; -.
DR   UniPathway; UPA00288; UER01023.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004372; F:glycine hydroxymethyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0019264; P:glycine biosynthetic process from serine; IEA:UniProtKB-UniRule.
DR   GO; GO:0035999; P:tetrahydrofolate interconversion; IEA:UniProtKB-UniPathway.
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   1: Evidence at protein level;
KW   3D-structure; Amino-acid biosynthesis; Cytoplasm; One-carbon metabolism;
KW   Pyridoxal phosphate; Transferase.
FT   CHAIN           1..416
FT                   /note="Serine hydroxymethyltransferase"
FT                   /id="PRO_0000235033"
FT   BINDING         121
FT                   /ligand="(6S)-5,6,7,8-tetrahydrofolate"
FT                   /ligand_id="ChEBI:CHEBI:57453"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00051"
FT   BINDING         125..127
FT                   /ligand="(6S)-5,6,7,8-tetrahydrofolate"
FT                   /ligand_id="ChEBI:CHEBI:57453"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00051"
FT   BINDING         355..357
FT                   /ligand="(6S)-5,6,7,8-tetrahydrofolate"
FT                   /ligand_id="ChEBI:CHEBI:57453"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00051"
FT   SITE            229
FT                   /note="Plays an important role in substrate specificity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00051"
FT   MOD_RES         230
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00051"
FT   TURN            8..10
FT                   /evidence="ECO:0007829|PDB:6TI3"
FT   HELIX           13..27
FT                   /evidence="ECO:0007829|PDB:6TI3"
FT   STRAND          29..31
FT                   /evidence="ECO:0007829|PDB:4WXG"
FT   HELIX           41..47
FT                   /evidence="ECO:0007829|PDB:6TI3"
FT   HELIX           50..53
FT                   /evidence="ECO:0007829|PDB:6TI3"
FT   STRAND          62..67
FT                   /evidence="ECO:0007829|PDB:6TI3"
FT   HELIX           69..86
FT                   /evidence="ECO:0007829|PDB:6TI3"
FT   STRAND          89..92
FT                   /evidence="ECO:0007829|PDB:6TI3"
FT   HELIX           98..109
FT                   /evidence="ECO:0007829|PDB:6TI3"
FT   STRAND          115..119
FT                   /evidence="ECO:0007829|PDB:6TI3"
FT   TURN            121..124
FT                   /evidence="ECO:0007829|PDB:6TI3"
FT   HELIX           127..129
FT                   /evidence="ECO:0007829|PDB:6TI3"
FT   HELIX           135..139
FT                   /evidence="ECO:0007829|PDB:6TI3"
FT   STRAND          140..145
FT                   /evidence="ECO:0007829|PDB:6TI3"
FT   TURN            149..151
FT                   /evidence="ECO:0007829|PDB:6TI3"
FT   HELIX           156..166
FT                   /evidence="ECO:0007829|PDB:6TI3"
FT   STRAND          169..173
FT                   /evidence="ECO:0007829|PDB:6TI3"
FT   HELIX           184..193
FT                   /evidence="ECO:0007829|PDB:6TI3"
FT   STRAND          197..201
FT                   /evidence="ECO:0007829|PDB:6TI3"
FT   TURN            203..205
FT                   /evidence="ECO:0007829|PDB:6TI3"
FT   HELIX           206..210
FT                   /evidence="ECO:0007829|PDB:6TI3"
FT   TURN            218..220
FT                   /evidence="ECO:0007829|PDB:6TI3"
FT   STRAND          222..230
FT                   /evidence="ECO:0007829|PDB:6TI3"
FT   STRAND          238..243
FT                   /evidence="ECO:0007829|PDB:6TI3"
FT   HELIX           245..255
FT                   /evidence="ECO:0007829|PDB:6TI3"
FT   TURN            256..259
FT                   /evidence="ECO:0007829|PDB:6TI3"
FT   HELIX           265..279
FT                   /evidence="ECO:0007829|PDB:6TI3"
FT   HELIX           281..303
FT                   /evidence="ECO:0007829|PDB:6TI3"
FT   STRAND          304..306
FT                   /evidence="ECO:0007829|PDB:4WXF"
FT   HELIX           310..312
FT                   /evidence="ECO:0007829|PDB:6TI3"
FT   STRAND          315..322
FT                   /evidence="ECO:0007829|PDB:6TI3"
FT   TURN            324..326
FT                   /evidence="ECO:0007829|PDB:6TI3"
FT   STRAND          327..329
FT                   /evidence="ECO:0007829|PDB:6YRW"
FT   HELIX           330..338
FT                   /evidence="ECO:0007829|PDB:6TI3"
FT   TURN            339..341
FT                   /evidence="ECO:0007829|PDB:6TI3"
FT   STRAND          345..347
FT                   /evidence="ECO:0007829|PDB:4WXG"
FT   TURN            356..358
FT                   /evidence="ECO:0007829|PDB:6TI3"
FT   STRAND          360..365
FT                   /evidence="ECO:0007829|PDB:6TI3"
FT   HELIX           367..371
FT                   /evidence="ECO:0007829|PDB:6TI3"
FT   HELIX           376..391
FT                   /evidence="ECO:0007829|PDB:6TI3"
FT   TURN            392..394
FT                   /evidence="ECO:0007829|PDB:6TI3"
FT   HELIX           396..412
FT                   /evidence="ECO:0007829|PDB:6TI3"
SQ   SEQUENCE   416 AA;  45086 MW;  2F6437A39A42094A CRC64;
     MIFDKEDYKA FDPELWNAID AEAERQQNNI ELIASENVVS KAVMAAQGTL LTNKYAEGYP
     GKRYYGGTAV IDVVETLAIE RAKKLFGAKF ANVQPHSGSQ ANAAVYMSLI QPGDTVMGMD
     LSAGGHLTHG APVSFSGKTY NFVSYNVDKE SELLDYDAIL AQAKEVRPKL IVAGASAYSR
     IIDFAKFREI ADAVGAYLMV DMAHIAGLVA SGHHPSPVPY AHVTTTTTHK TLRGPRGGLI
     LTDDEDIAKK LNSAVFPGLQ GGPLEHVIAA KAVALKEALD PAFKEYGENV IKNAAAMADV
     FNQHPDFRVI SGGTNNHLFL VDVTKVVENG KVAQNVLEEV NITLNKNSIP YEQLSPFKTS
     GIRVGSPAIT SRGMGEAESR QIAEWMVEAL ENHDKPEVLE RIRGDVKVLT DAFPLY
 
 
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