ID   A0A257AC01_9CREN        Unreviewed;       416 AA.
AC   A0A257AC01;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   12-SEP-2018, entry version 5.
DE   RecName: Full=Serine hydroxymethyltransferase {ECO:0000256|HAMAP-Rule:MF_00051};
DE            Short=SHMT {ECO:0000256|HAMAP-Rule:MF_00051};
DE            Short=Serine methylase {ECO:0000256|HAMAP-Rule:MF_00051};
DE            EC=2.1.2.- {ECO:0000256|HAMAP-Rule:MF_00051};
GN   Name=glyA {ECO:0000256|HAMAP-Rule:MF_00051};
GN   ORFNames=B6U69_02640 {ECO:0000313|EMBL:OYT61950.1};
OS   Thermofilum sp. ex4484_15.
OC   Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermofilaceae;
OC   Thermofilum.
OX   NCBI_TaxID=2012526 {ECO:0000313|EMBL:OYT61950.1};
RN   [1] {ECO:0000313|EMBL:OYT61950.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Ex4484_15 {ECO:0000313|EMBL:OYT61950.1};
RX   PubMed=28835260; DOI=.1186/s40168-017-0322-2;
RA   Dombrowski N., Seitz K.W., Teske A.P., Baker B.J.;
RT   "Genomic insights into potential interdependencies in microbial
RT   hydrocarbon and nutrient cycling in hydrothermal sediments.";
RL   Microbiome 5:106-106(2017).
CC   -!- FUNCTION: Catalyzes the reversible interconversion of serine and
CC       glycine with a modified folate serving as the one-carbon carrier.
CC       Also exhibits a pteridine-independent aldolase activity toward
CC       beta-hydroxyamino acids, producing glycine and aldehydes, via a
CC       retro-aldol mechanism. {ECO:0000256|HAMAP-Rule:MF_00051}.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00051};
CC   -!- PATHWAY: Amino-acid biosynthesis; glycine biosynthesis; glycine
CC       from L-serine: step 1/1. {ECO:0000256|HAMAP-Rule:MF_00051}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00051}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00051}.
CC   -!- SIMILARITY: Belongs to the SHMT family. {ECO:0000256|HAMAP-
CC       Rule:MF_00051}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00051}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:OYT61950.1}.
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DR   EMBL; NJEH01000032; OYT61950.1; -; Genomic_DNA.
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:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
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:InterPro.
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; IPR015422; PyrdxlP-dep_Trfase_dom1.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR001085; Ser_HO-MeTrfase.
DR   PIRSF; PIRSF000412; SHMT; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00051};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00051};
KW   Methyltransferase {ECO:0000313|EMBL:OYT61950.1};
KW   One-carbon metabolism {ECO:0000256|HAMAP-Rule:MF_00051};
KW   Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_00051,
KW   ECO:0000256|PIRSR:PIRSR000412-50};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00051,
KW   ECO:0000313|EMBL:OYT61950.1}.
FT   BINDING      31     31       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_00051}.
FT   BINDING      51     51       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_00051}.
FT   BINDING      53     53       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00051}.
FT   BINDING      60     60       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00051}.
FT   BINDING      61     61       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_00051}.
FT   BINDING      95     95       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_00051}.
FT   BINDING     117    117       Substrate; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00051}.
FT   BINDING     172    172       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_00051}.
FT   BINDING     200    200       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_00051}.
FT   BINDING     226    226       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_00051}.
FT   BINDING     361    361       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_00051}.
FT   MOD_RES     227    227       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_00051,
FT                                ECO:0000256|PIRSR:PIRSR000412-50}.
SQ   SEQUENCE   416 AA;  46290 MW;  EEBE3F35D042F65B CRC64;
     MELPGEALRI LKLNEAHNKW RREETVNLIA SENLTSPLVD SLYLSDAMHR YAEGLPFKRF
     YQGTKYIDEI EVLCEELMRK LFKAKYIDVR PISGTIANGA VFYALGKSGD TTCICPLPGG
     GHVSHSKYGI MGALGLKPLP LPFNVEEFNI DVEGASKLIK EVRPKFVVLG ASVILFPHPV
     KELGDAANEV GSKIIFDAAH VLGLIAGGKY PNPLSEGANV VTSSTHKTFP GPQGGVILTN
     EEEIYKKVKK VVFPVFVSNH HLHRLAATAM AAVEMLYFGE AYASQIIKNA KRLAECLYNR
     GFKVLGEKKG FTETHQVLLD VRELGGGTKV ALMLEKANII VNKNMLPWDR PEDIKNPSGI
     RIGVQEVTRI GMREGDMEVL AEYFYKVLIK REDPAKVAEE VREFRGKFKE LLYTFK
//