ID   A0A1X4HC41_9EURY        Unreviewed;       415 AA.
AC   A0A1X4HC41;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   12-AUG-2020, entry version 12.
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=B9H04_00680 {ECO:0000313|EMBL:OSP11252.1};
OS   Halorubrum ezzemoulense DSM 17463.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Halorubraceae; Halorubrum.
OX   NCBI_TaxID=1121945 {ECO:0000313|EMBL:OSP11252.1, ECO:0000313|Proteomes:UP000193587};
RN   [1] {ECO:0000313|EMBL:OSP11252.1, ECO:0000313|Proteomes:UP000193587}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17463 {ECO:0000313|EMBL:OSP11252.1,
RC   ECO:0000313|Proteomes:UP000193587};
RA   De La Haba R., Sanchez-Porro C., Infante-Dominguez C., Ventosa A.;
RT   "MLSA of the genus Halorubrum.";
RL   Submitted (APR-2017) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OSP11252.1}.
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DR   EMBL; NEDJ01000001; OSP11252.1; -; Genomic_DNA.
DR   RefSeq; WP_049930449.1; NZ_NEDJ01000001.1.
DR   STRING; 1121945.ATXS01000002_gene778; -.
DR   eggNOG; arCOG00070; Archaea.
DR   UniPathway; UPA00193; -.
DR   UniPathway; UPA00288; UER01023.
DR   Proteomes; UP000193587; Unassembled WGS sequence.
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:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0035999; P:tetrahydrofolate interconversion; IEA:UniProtKB-UniPathway.
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   InterPro; IPR019798; Ser_HO-MeTrfase_PLP_BS.
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.
DR   PROSITE; PS00096; SHMT; 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:OSP11252.1};
KW   One-carbon metabolism {ECO:0000256|ARBA:ARBA00022563, ECO:0000256|HAMAP-
KW   Rule:MF_00051};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, ECO:0000256|HAMAP-
KW   Rule:MF_00051, ECO:0000256|PIRSR:PIRSR000412-50};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00051, ECO:0000313|EMBL:OSP11252.1}.
FT   DOMAIN          7..384
FT                   /note="SHMT"
FT                   /evidence="ECO:0000259|Pfam:PF00464"
FT   REGION          123..125
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00051"
FT   REGION          353..355
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00051"
FT   BINDING         33
FT                   /note="Pyridoxal phosphate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00051"
FT   BINDING         53
FT                   /note="Pyridoxal phosphate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00051"
FT   BINDING         55
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00051"
FT   BINDING         62
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00051"
FT   BINDING         63
FT                   /note="Pyridoxal phosphate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00051"
FT   BINDING         97
FT                   /note="Pyridoxal phosphate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00051"
FT   BINDING         119
FT                   /note="Substrate; via carbonyl oxygen"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00051"
FT   BINDING         174
FT                   /note="Pyridoxal phosphate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00051"
FT   BINDING         202
FT                   /note="Pyridoxal phosphate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00051"
FT   BINDING         227
FT                   /note="Pyridoxal phosphate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00051"
FT   BINDING         234
FT                   /note="Pyridoxal phosphate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00051"
FT   BINDING         259
FT                   /note="Pyridoxal phosphate; via amide nitrogen and carbonyl
FT                   oxygen"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00051"
FT   BINDING         361
FT                   /note="Pyridoxal phosphate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00051"
FT   MOD_RES         228
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00051,
FT                   ECO:0000256|PIRSR:PIRSR000412-50"
SQ   SEQUENCE   415 AA;  44444 MW;  E08BAFAB73AD9555 CRC64;
     MDHEHVREVD PAVADALAGE RDRQEQTLAM IASENHVSEA VLEAQGSVLT NKYAEGYPGS
     RYYAGCEYAD EVEELAIERA KELWGADHVN VQPHSGTQAN QAVYYSVLEP GDKILSLKLN
     DGGHLSHGHP ANFTGQLYEV EQYEVDPETG YIDYEGLREV AEEFDPDIVV SGYSAYPRAV
     EWEKIQAAAD AVDAYHLADI AHITGLVAAG VHPSPVGVAD FVTGSTHKTI RAGRGGIVMC
     DAEFADDIDS AVFPGGQGGP LMHNVAGKAV GFKEALEPEF EEYAQQVVDN AEVLAETLQE
     HGLSLVSGGT DNHLVLADLR DSHPDLSGGD AEDALAAANI VLNGNTVPGE TRSAFDPSGI
     RAGTAGLTTR GFDADAIEEV GDLIYRVVDD VDSDDVIYEV GERVVELCEA HPLYE
//