ID   A1R450_ARTAT            Unreviewed;       430 AA.
AC   A1R450;
DT   06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2007, sequence version 1.
DT   11-MAY-2016, entry version 87.
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   ECO:0000313|EMBL:ABM08285.1};
GN   OrderedLocusNames=AAur_1227 {ECO:0000313|EMBL:ABM08285.1};
OS   Arthrobacter aurescens (strain TC1).
OC   Bacteria; Actinobacteria; Micrococcales; Micrococcaceae;
OC   Paenarthrobacter.
OX   NCBI_TaxID=290340 {ECO:0000313|EMBL:ABM08285.1, ECO:0000313|Proteomes:UP000000637};
RN   [1] {ECO:0000313|EMBL:ABM08285.1, ECO:0000313|Proteomes:UP000000637}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TC1 {ECO:0000313|EMBL:ABM08285.1,
RC   ECO:0000313|Proteomes:UP000000637};
RX   PubMed=17194220; DOI=10.1371/journal.pgen.0020214;
RA   Mongodin E.F., Shapir N., Daugherty S.C., DeBoy R.T., Emerson J.B.,
RA   Shvartzbeyn A., Radune D., Vamathevan J., Riggs F., Grinberg V.,
RA   Khouri H., Wackett L.P., Nelson K.E., Sadowsky M.J.;
RT   "Secrets of soil survival revealed by the genome sequence of
RT   Arthrobacter aurescens TC1.";
RL   PLoS Genet. 2:2094-2106(2006).
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         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, ECO:0000256|RuleBase:RU004104}.
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DR   EMBL; CP000474; ABM08285.1; -; Genomic_DNA.
DR   ProteinModelPortal; A1R450; -.
DR   SMR; A1R450; 13-418.
DR   STRING; 290340.AAur_1227; -.
DR   EnsemblBacteria; ABM08285; ABM08285; AAur_1227.
DR   KEGG; aau:AAur_1227; -.
DR   PATRIC; 20977806; VBIArtAur67810_1245.
DR   eggNOG; ENOG4105C65; Bacteria.
DR   eggNOG; COG0112; LUCA.
DR   HOGENOM; HOG000239404; -.
DR   KO; K00600; -.
DR   OMA; SAYPRHE; -.
DR   OrthoDB; EOG6Z0QB2; -.
DR   BioCyc; AAUR290340:GI59-1227-MONOMER; -.
DR   UniPathway; UPA00193; -.
DR   UniPathway; UPA00288; UER01023.
DR   Proteomes; UP000000637; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004372; F:glycine hydroxymethyltransferase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0019264; P:glycine biosynthetic process from serine; IEA:UniProtKB-HAMAP.
DR   GO; GO:0035999; P:tetrahydrofolate interconversion; IEA:UniProtKB-UniPathway.
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_sub1.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_major_sub2.
DR   InterPro; IPR001085; Ser_HO-MeTrfase.
DR   InterPro; IPR019798; Ser_HO-MeTrfase_PLP_BS.
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:UP000000637};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00051};
KW   Methyltransferase {ECO:0000313|EMBL:ABM08285.1};
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   Reference proteome {ECO:0000313|Proteomes:UP000000637};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00051,
KW   ECO:0000313|EMBL:ABM08285.1}.
FT   BINDING      41     41       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_00051}.
FT   BINDING      61     61       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_00051}.
FT   BINDING      63     63       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00051}.
FT   BINDING      70     70       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00051}.
FT   BINDING      71     71       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_00051}.
FT   BINDING     127    127       Substrate; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00051}.
FT   BINDING     182    182       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_00051}.
FT   BINDING     210    210       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_00051}.
FT   BINDING     235    235       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_00051}.
FT   BINDING     242    242       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_00051}.
FT   BINDING     267    267       Pyridoxal phosphate; via amide nitrogen
FT                                and carbonyl oxygen. {ECO:0000256|HAMAP-
FT                                Rule:MF_00051}.
FT   BINDING     372    372       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_00051}.
FT   MOD_RES     236    236       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_00051,
FT                                ECO:0000256|PIRSR:PIRSR000412-50}.
SQ   SEQUENCE   430 AA;  46054 MW;  C477D9DDA44314E8 CRC64;
     MTTTTSASVS NQSLADLDPE IAAVLNQELG RQRGTLEMIA SENFAPRAVM EAQGSVLTNK
     YAEGYPGRRY YGGCEYVDVA EQLAIDRVKE LFGAEYANVQ PHSGAQANAA ALSAMITPGD
     KILGLSLAHG GHLTHGMKLN FSGKLYNVAA YQVEEDNFRI DMDKLREQAI AEKPQVIIAG
     WSAYPRHLDF AAFRSIADEV GALLWTDMAH FAGLVAAGLH PSPVPHSDVV TSTVHKTLAG
     PRSGVILGKQ EWAKKLNSSV FPGQQGGPLM HVIAAKAVAF KIAGGEEFKE RQERVLEGAR
     IIADRLNQSD VAEAGVSVLT GGTDVHLVLV DLRNSQLDGQ QAEDLLHSVG ITVNRNAVPF
     DPRPPMVTSG LRIGTPALAT RGFGATEFTE VAEIIATALK AGSSADVESL QARVDKLAAD
     FPLYPQHEQW
//