ID   A0A1X4HC41_9EURY        Unreviewed;       415 AA.
AC   A0A1X4HC41;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   10-APR-2019, entry version 10.
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=2.1.2.1 {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;
OC   Haloferacales; 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
CC       carrier. Also exhibits THF-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   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + glycine +
CC         H2O = (6S)-5,6,7,8-tetrahydrofolate + L-serine;
CC         Xref=Rhea:RHEA:15481, ChEBI:CHEBI:15377, ChEBI:CHEBI:15636,
CC         ChEBI:CHEBI:33384, ChEBI:CHEBI:57305, ChEBI:CHEBI:57453;
CC         EC=2.1.2.1; Evidence={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         ECO:0000256|PIRSR:PIRSR000412-50};
CC   -!- PATHWAY: Amino-acid biosynthesis; glycine biosynthesis; glycine
CC       from L-serine: step 1/1. {ECO:0000256|HAMAP-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|HAMAP-
CC       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: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   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: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   Complete proteome {ECO:0000313|Proteomes:UP000193587};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00051};
KW   Methyltransferase {ECO:0000313|EMBL:OSP11252.1};
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:OSP11252.1}.
FT   DOMAIN        7    384       SHMT. {ECO:0000259|Pfam:PF00464}.
FT   REGION      123    125       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00051}.
FT   REGION      353    355       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00051}.
FT   BINDING      33     33       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_00051}.
FT   BINDING      53     53       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_00051}.
FT   BINDING      55     55       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00051}.
FT   BINDING      62     62       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00051}.
FT   BINDING      63     63       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_00051}.
FT   BINDING      97     97       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_00051}.
FT   BINDING     119    119       Substrate; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00051}.
FT   BINDING     174    174       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_00051}.
FT   BINDING     202    202       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_00051}.
FT   BINDING     227    227       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_00051}.
FT   BINDING     234    234       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_00051}.
FT   BINDING     259    259       Pyridoxal phosphate; via amide nitrogen
FT                                and carbonyl oxygen. {ECO:0000256|HAMAP-
FT                                Rule:MF_00051}.
FT   BINDING     361    361       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_00051}.
FT   MOD_RES     228    228       N6-(pyridoxal phosphate)lysine.
FT                                {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
//