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Database: UniProt
Entry: Q3B2I7
LinkDB: Q3B2I7
Original site: Q3B2I7 
ID   GLYA_PELLD              Reviewed;         440 AA.
AC   Q3B2I7;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   01-OCT-2014, entry version 63.
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};
GN   OrderedLocusNames=Plut_1590;
OS   Pelodictyon luteolum (strain DSM 273) (Chlorobium luteolum (strain DSM
OS   273)).
OC   Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae;
OC   Chlorobium/Pelodictyon group; Pelodictyon.
OX   NCBI_TaxID=319225;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 273;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Bryant D., Schmutz J., Larimer F.,
RA   Land M., Kyrpides N., Ivanova N., Richardson P.;
RT   "Complete sequence of Pelodictyon luteolum DSM 273.";
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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.
CC       {ECO:0000255|HAMAP-Rule:MF_00051}.
CC   -!- CATALYTIC ACTIVITY: 5,10-methylenetetrahydrofolate + glycine +
CC       H(2)O = tetrahydrofolate + L-serine. {ECO:0000255|HAMAP-
CC       Rule:MF_00051}.
CC   -!- COFACTOR: Pyridoxal phosphate. {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
CC       from L-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; CP000096; ABB24444.1; -; Genomic_DNA.
DR   RefSeq; YP_375487.1; NC_007512.1.
DR   ProteinModelPortal; Q3B2I7; -.
DR   SMR; Q3B2I7; 4-428.
DR   STRING; 319225.Plut_1590; -.
DR   PRIDE; Q3B2I7; -.
DR   EnsemblBacteria; ABB24444; ABB24444; Plut_1590.
DR   GeneID; 3746116; -.
DR   KEGG; plt:Plut_1590; -.
DR   PATRIC; 21380822; VBIChlLut1287_1669.
DR   eggNOG; COG0112; -.
DR   HOGENOM; HOG000239405; -.
DR   KO; K00600; -.
DR   OMA; HLMLVDV; -.
DR   OrthoDB; EOG6Z0QB2; -.
DR   BioCyc; PLUT319225:GHDM-1595-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; Reference proteome;
KW   Transferase.
FT   CHAIN         1    440       Serine hydroxymethyltransferase.
FT                                /FTId=PRO_0000234997.
FT   REGION      123    125       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00051}.
FT   REGION      370    372       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00051}.
FT   BINDING      33     33       Pyridoxal phosphate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00051}.
FT   BINDING      53     53       Pyridoxal phosphate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00051}.
FT   BINDING      55     55       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00051}.
FT   BINDING      62     62       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00051}.
FT   BINDING      63     63       Pyridoxal phosphate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00051}.
FT   BINDING      97     97       Pyridoxal phosphate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00051}.
FT   BINDING     119    119       Substrate; via carbonyl oxygen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00051}.
FT   BINDING     174    174       Pyridoxal phosphate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00051}.
FT   BINDING     202    202       Pyridoxal phosphate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00051}.
FT   BINDING     227    227       Pyridoxal phosphate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00051}.
FT   BINDING     234    234       Pyridoxal phosphate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00051}.
FT   BINDING     278    278       Pyridoxal phosphate; via amide nitrogen
FT                                and carbonyl oxygen. {ECO:0000255|HAMAP-
FT                                Rule:MF_00051}.
FT   BINDING     378    378       Pyridoxal phosphate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00051}.
FT   MOD_RES     228    228       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000255|HAMAP-Rule:MF_00051}.
SQ   SEQUENCE   440 AA;  47799 MW;  2CA44417FC89D757 CRC64;
     MDTDILKMQD REVFDAIAGE TVRQMETLEL IASENFTSRA VMQACGSVMT NKYAEGYPGK
     RYYGGCEFVD IAEDLARERA RKLFGCEYVN VQPHSGSSAN MAVLFSVLKP GDRIMGLDLS
     HGGHLTHGSS VNFSGQMFDA RSYGVDRETG IIDMNKVEEM ALDFKPRLII CGASAYSQGF
     DFKAFREIAD KVGAFLMADI AHPAGLIAAG LLTDPMPHCH FVTTTTHKTL RGPRGGMIMM
     GKDFENPMGI TIKTKNGPRV KMMSEVMDAE VMPGIQGGPL MHIIAGKAVA FGEALRPEFR
     EYAVQVRKNA ASMAERFTSL GYNIVSGGTK NHLMLLDLRN KDVNGKVAEN LLHDAGITVN
     KNMVPFDDKS PFVTSGIRIG TAAMTTRGMK EADATLIAEL IDRVITGAAE STIAATCKDV
     KAEIRSLCLQ NPLEGYGVTP
//
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