ID   A0A2D6WNW7_9BACT        Unreviewed;       418 AA.
AC   A0A2D6WNW7;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   23-MAY-2018, entry version 2.
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=CML08_03030 {ECO:0000313|EMBL:MAH40359.1};
OS   Puniceicoccaceae bacterium.
OC   Bacteria; Verrucomicrobia; Opitutae; Puniceicoccales;
OC   Puniceicoccaceae.
OX   NCBI_TaxID=2026784 {ECO:0000313|EMBL:MAH40359.1, ECO:0000313|Proteomes:UP000226557};
RN   [1] {ECO:0000313|EMBL:MAH40359.1, ECO:0000313|Proteomes:UP000226557}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ARS1008 {ECO:0000313|EMBL:MAH40359.1};
RA   Tully B.J., Graham E.D., Heidelberg J.F.;
RT   "The Reconstruction of 2,631 Draft Metagenome-Assembled Genomes from
RT   the Global Oceans.";
RL   Submitted (SEP-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. 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:0000256|HAMAP-Rule:MF_00051}.
CC   -!- CATALYTIC ACTIVITY: 5,10-methylenetetrahydrofolate + glycine +
CC       H(2)O = tetrahydrofolate + L-serine. {ECO:0000256|HAMAP-
CC       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   -!- 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:MAH40359.1}.
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DR   EMBL; NZEM01000048; MAH40359.1; -; Genomic_DNA.
DR   UniPathway; UPA00193; -.
DR   UniPathway; UPA00288; UER01023.
DR   Proteomes; UP000226557; Unassembled WGS sequence.
DR   CDD; cd00378; SHMT; 1.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 2.
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   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:UP000226557};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00051};
KW   Methyltransferase {ECO:0000313|EMBL:MAH40359.1};
KW   One-carbon metabolism {ECO:0000256|HAMAP-Rule:MF_00051};
KW   Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_00051};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00051,
KW   ECO:0000313|EMBL:MAH40359.1}.
FT   REGION      126    128       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00051}.
FT   REGION      356    358       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00051}.
FT   BINDING      36     36       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_00051}.
FT   BINDING      56     56       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_00051}.
FT   BINDING      58     58       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00051}.
FT   BINDING      65     65       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00051}.
FT   BINDING      66     66       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_00051}.
FT   BINDING     100    100       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_00051}.
FT   BINDING     122    122       Substrate; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00051}.
FT   BINDING     177    177       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_00051}.
FT   BINDING     205    205       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_00051}.
FT   BINDING     230    230       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_00051}.
FT   BINDING     237    237       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_00051}.
FT   BINDING     262    262       Pyridoxal phosphate; via amide nitrogen
FT                                and carbonyl oxygen. {ECO:0000256|HAMAP-
FT                                Rule:MF_00051}.
FT   BINDING     364    364       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_00051}.
FT   MOD_RES     231    231       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_00051}.
SQ   SEQUENCE   418 AA;  45097 MW;  EDCB295AF0C975D3 CRC64;
     MNPLNDTALD QLDPEIAQLI AREKARQQSH IELIASENFT YPAIMEAQGS ILTNKYAEGY
     PNKRYYGGCD FVDSIETIAI ERAKALFRAD HANVQPHAGS QANAAVYLSV LKPGDKILTM
     NLSDGGHLTH GHPMNFSGIY HEVVHYGVSI ENGLIDYDAI AESAEREQPK MITVGASAYS
     RVIDFKRMSE IARSVGAYLL ADIAHIAGLV AAGVHPSPVP YADFVTTTTH KTLRGPRGGL
     ILCKTDHAKK IDSAVFPGTQ GGPLMHVIAA KATCFKEANT DAFKTYQKQV ASNANTLANA
     LLEAGHNIVS GGTENHLFMI DLRKKYPQLT GKRAQIALDQ AHITANKNTV PGETRSPFQT
     SGIRIGTPAV TSRGFVEADM LKVAKAINLV LDSADNETTN AEAKSIALAL CSQYPLPY
//