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Database: UniProt
Entry: A5VIP9
LinkDB: A5VIP9
Original site: A5VIP9 
ID   GLYA_LACRD              Reviewed;         411 AA.
AC   A5VIP9;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   19-FEB-2014, entry version 55.
DE   RecName: Full=Serine hydroxymethyltransferase;
DE            Short=SHMT;
DE            Short=Serine methylase;
DE            EC=2.1.2.1;
GN   Name=glyA; OrderedLocusNames=Lreu_0455;
OS   Lactobacillus reuteri (strain DSM 20016).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=557436;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 20016;
RX   PubMed=21379339; DOI=10.1371/journal.pgen.1001314;
RA   Frese S.A., Benson A.K., Tannock G.W., Loach D.M., Kim J., Zhang M.,
RA   Oh P.L., Heng N.C., Patil P.B., Juge N., Mackenzie D.A., Pearson B.M.,
RA   Lapidus A., Dalin E., Tice H., Goltsman E., Land M., Hauser L.,
RA   Ivanova N., Kyrpides N.C., Walter J.;
RT   "The evolution of host specialization in the vertebrate gut symbiont
RT   Lactobacillus reuteri.";
RL   PLoS Genet. 7:E1001314-E1001314(2011).
CC   -!- FUNCTION: Catalyzes the reversible interconversion of serine and
CC       glycine with tetrahydrofolate (THF) serving as the one-carbon
CC       carrier. This reaction serves as the major source of one-carbon
CC       groups required for the biosynthesis of purines, thymidylate,
CC       methionine, and other important biomolecules. Also exhibits THF-
CC       independent aldolase activity toward beta-hydroxyamino acids,
CC       producing glycine and aldehydes, via a retro-aldol mechanism (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: 5,10-methylenetetrahydrofolate + glycine +
CC       H(2)O = tetrahydrofolate + L-serine.
CC   -!- COFACTOR: Pyridoxal phosphate (By similarity).
CC   -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion.
CC   -!- PATHWAY: Amino-acid biosynthesis; glycine biosynthesis; glycine
CC       from L-serine: step 1/1.
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the SHMT family.
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DR   EMBL; CP000705; ABQ82723.1; -; Genomic_DNA.
DR   RefSeq; YP_001271060.1; NC_009513.1.
DR   ProteinModelPortal; A5VIP9; -.
DR   SMR; A5VIP9; 5-399.
DR   STRING; 557436.Lreu_0455; -.
DR   EnsemblBacteria; ABQ82723; ABQ82723; Lreu_0455.
DR   GeneID; 5189900; -.
DR   KEGG; lre:Lreu_0455; -.
DR   PATRIC; 22254029; VBILacReu87937_0471.
DR   eggNOG; COG0112; -.
DR   HOGENOM; HOG000239404; -.
DR   KO; K00600; -.
DR   OMA; MLIDLRN; -.
DR   OrthoDB; EOG6Z0QB2; -.
DR   ProtClustDB; PRK00011; -.
DR   BioCyc; LREU557436:GC7Y-473-MONOMER; -.
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-HAMAP.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0019264; P:glycine biosynthetic process from serine; IEA:UniProtKB-HAMAP.
DR   GO; GO:0035999; P:tetrahydrofolate interconversion; IEA:UniProtKB-UniPathway.
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_sub1.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_major_sub2.
DR   InterPro; IPR001085; Ser_HO-MeTrfase.
DR   InterPro; IPR019798; Ser_HO-MeTrfase_PLP_BS.
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   3: Inferred from homology;
KW   Amino-acid biosynthesis; Complete proteome; Cytoplasm;
KW   One-carbon metabolism; Pyridoxal phosphate; Transferase.
FT   CHAIN         1    411       Serine hydroxymethyltransferase.
FT                                /FTId=PRO_1000057368.
FT   REGION      120    122       Substrate binding (By similarity).
FT   REGION      350    352       Substrate binding (By similarity).
FT   BINDING      30     30       Pyridoxal phosphate (By similarity).
FT   BINDING      50     50       Pyridoxal phosphate (By similarity).
FT   BINDING      52     52       Substrate (By similarity).
FT   BINDING      59     59       Substrate (By similarity).
FT   BINDING      60     60       Pyridoxal phosphate (By similarity).
FT   BINDING      94     94       Pyridoxal phosphate (By similarity).
FT   BINDING     171    171       Pyridoxal phosphate (By similarity).
FT   BINDING     199    199       Pyridoxal phosphate (By similarity).
FT   BINDING     224    224       Pyridoxal phosphate (By similarity).
FT   BINDING     231    231       Pyridoxal phosphate (By similarity).
FT   BINDING     257    257       Pyridoxal phosphate; via amide nitrogen
FT                                and carbonyl oxygen (By similarity).
FT   BINDING     358    358       Pyridoxal phosphate (By similarity).
FT   MOD_RES     225    225       N6-(pyridoxal phosphate)lysine (By
FT                                similarity).
SQ   SEQUENCE   411 AA;  44951 MW;  1A24E135C2DE1C28 CRC64;
     MNYGKKSPQL WAAIENEEQR QQDTIELIAS ENIVSDAVRE AQGSVLTNKY AEGYPNKRYY
     GGCEFIDQVE QLAIDYAKKL FNAAYVNVQP HSGSQANMAV YQALLKPGDV ILGMGMDAGG
     HLTHGATVNF SGKLYKTYGY GLNPDTEELD YDEIMALAKK VKPQLIVAGA SAYSRIIDWQ
     AFRKIADEVG AYLMVDMAHI AGLVATGTHP SPLPIADVVT TTTHKTLRGP RGGMILSKST
     ELGRKINSAV FPGIQGGPLE HVIAGKAQAF YEDLQPEYAE YIQQVVKNAQ AMEKVFNTSK
     QIRVVSGKTE NHLLVLDLTK TGLTGKDAQN LLDRVHITTN KEAIPNDPRS PFITSGLRIG
     TPAITSRGFK EEDAQKVAEL ISTALTNPTD EERLQEVAKG VHELTTKYPL N
//
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