ID   A0A8A3S7R1_9EURY        Unreviewed;       414 AA.
AC   A0A8A3S7R1;
DT   29-SEP-2021, integrated into UniProtKB/TrEMBL.
DT   29-SEP-2021, sequence version 1.
DT   25-MAY-2022, entry version 3.
DE   RecName: Full=Serine hydroxymethyltransferase {ECO:0000256|ARBA:ARBA00016846, 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=2.1.2.1 {ECO:0000256|HAMAP-Rule:MF_00051};
GN   Name=glyA {ECO:0000256|HAMAP-Rule:MF_00051};
GN   ORFNames=RJ40_09470 {ECO:0000313|EMBL:QSZ67720.1};
OS   Methanofollis aquaemaris.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanomicrobiales; Methanomicrobiaceae; Methanofollis.
OX   NCBI_TaxID=126734 {ECO:0000313|EMBL:QSZ67720.1};
RN   [1] {ECO:0000313|EMBL:QSZ67720.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=N2F9704 {ECO:0000313|EMBL:QSZ67720.1};
RX   PubMed=11594621;
RA   Lai M.C., Chen S.C.;
RT   "Methanofollis aquaemaris sp. nov., a methanogen isolated from an
RT   aquaculture fish pond.";
RL   Int. J. Syst. Evol. Microbiol. 51:1873-1880(2001).
RN   [2] {ECO:0000313|EMBL:QSZ67720.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=N2F9704 {ECO:0000313|EMBL:QSZ67720.1};
RA   Chen S.-C., Chien H.-H., Lai M.-C.;
RL   Submitted (FEB-2019) 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 carrier.
CC       Also exhibits THF-independent aldolase activity toward beta-
CC       hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol
CC       mechanism. {ECO:0000256|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:0000256|HAMAP-Rule:MF_00051};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|HAMAP-Rule:MF_00051, ECO:0000256|PIRSR:PIRSR000412-50};
CC   -!- PATHWAY: Amino-acid biosynthesis; glycine biosynthesis; glycine from L-
CC       serine: step 1/1. {ECO:0000256|ARBA:ARBA00004697, ECO:0000256|HAMAP-
CC       Rule:MF_00051}.
CC   -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion.
CC       {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|ARBA:ARBA00006376,
CC       ECO:0000256|HAMAP-Rule:MF_00051}.
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DR   EMBL; CP036172; QSZ67720.1; -; Genomic_DNA.
DR   UniPathway; UPA00193; -.
DR   UniPathway; UPA00288; UER01023.
DR   GO; GO:0004372; F:glycine hydroxymethyltransferase activity; IEA:InterPro.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0019264; P:glycine biosynthetic process from serine; IEA:InterPro.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
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; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   InterPro; IPR001085; Ser_HO-MeTrfase.
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.
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:QSZ67720.1};
KW   One-carbon metabolism {ECO:0000256|HAMAP-Rule:MF_00051};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, ECO:0000256|HAMAP-
KW   Rule:MF_00051};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00051}.
FT   DOMAIN          4..380
FT                   /note="SHMT"
FT                   /evidence="ECO:0000259|Pfam:PF00464"
FT   REGION          121..123
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00051"
FT   REGION          349..351
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00051"
FT   BINDING         31
FT                   /note="Pyridoxal phosphate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00051"
FT   BINDING         51
FT                   /note="Pyridoxal phosphate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00051"
FT   BINDING         53
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00051"
FT   BINDING         60
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00051"
FT   BINDING         61
FT                   /note="Pyridoxal phosphate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00051"
FT   BINDING         95
FT                   /note="Pyridoxal phosphate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00051"
FT   BINDING         117
FT                   /note="Substrate; via carbonyl oxygen"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00051"
FT   BINDING         172
FT                   /note="Pyridoxal phosphate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00051"
FT   BINDING         200
FT                   /note="Pyridoxal phosphate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00051"
FT   BINDING         225
FT                   /note="Pyridoxal phosphate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00051"
FT   BINDING         232
FT                   /note="Pyridoxal phosphate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00051"
FT   BINDING         257
FT                   /note="Pyridoxal phosphate; via amide nitrogen and carbonyl
FT                   oxygen"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00051"
FT   BINDING         357
FT                   /note="Pyridoxal phosphate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00051"
FT   MOD_RES         226
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00051,
FT                   ECO:0000256|PIRSR:PIRSR000412-50"
SQ   SEQUENCE   414 AA;  44569 MW;  292D1513CD272618 CRC64;
     MSSLADTDPE IAALIEKERL RQTNGLELIA SENVVSKAVL ETAGSILTNK YAEGYPGKRY
     YGGCEYYDMI ENLAKDRLCK LFGAEYANVQ PHSGSGANMA VYFSAINYGD KIMSMKLSEG
     GHLSHGSPVS FSGKMYDVVQ YGVDHETEVI DYAALADMAR KEKPQMIVCG ASAYPREIDF
     KAFGEIAEEV GSSCVADIAH IAGLVATGLH NSPIDVLPFT TTTTHKTLRG PRGGAIMCRE
     EFGQAINKAV FPGLQGGPLM HIIAAKAVCF KEALTQSYKD YCKQVVNNAQ TLAATLDSEG
     YRLVSGGTDN HLMLLDLSDK GLTGLQAENA LHDAGITVNK NTIPRETLSP FVTSGLRIGT
     PAVTSRGMKE EEMKAIGHFI ATVLNDIENK EKIAGVKTEV EALASKFSIY AVTE
//