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 01-MAY-2013, entry version 51.
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; TAIHHYD; -.
DR ProtClustDB; PRK00011; -.
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:HAMAP.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:HAMAP.
DR GO; GO:0019264; P:glycine biosynthetic process from serine; IEA: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; PyrdxlP-dep_Trfase_major; 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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