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Serine hydroxymethyltransferase (SHMT) (Serine methylase) (EC 2.1.2.1)

 F7XUP6_MIDMI            Unreviewed;       423 AA.
F7XUP6;
21-SEP-2011, integrated into UniProtKB/TrEMBL.
21-SEP-2011, sequence version 1.
27-SEP-2017, entry version 47.
RecName: Full=Serine hydroxymethyltransferase {ECO:0000256|HAMAP-Rule:MF_00051};
Short=SHMT {ECO:0000256|HAMAP-Rule:MF_00051};
Short=Serine methylase {ECO:0000256|HAMAP-Rule:MF_00051};
EC=2.1.2.1 {ECO:0000256|HAMAP-Rule:MF_00051};
Name=glyA {ECO:0000256|HAMAP-Rule:MF_00051,
ECO:0000313|EMBL:AEI88395.1};
OrderedLocusNames=midi_00070 {ECO:0000313|EMBL:AEI88395.1};
Midichloria mitochondrii (strain IricVA).
Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
Candidatus Midichloriaceae; Candidatus Midichloria.
NCBI_TaxID=696127 {ECO:0000313|EMBL:AEI88395.1, ECO:0000313|Proteomes:UP000006639};
[1] {ECO:0000313|EMBL:AEI88395.1, ECO:0000313|Proteomes:UP000006639}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=IricVA {ECO:0000313|EMBL:AEI88395.1,
ECO:0000313|Proteomes:UP000006639};
PubMed=21690562; DOI=10.1093/molbev/msr159;
Sassera D., Lo N., Epis S., D'Auria G., Montagna M., Comandatore F.,
Horner D., Pereto J., Luciano A.M., Franciosi F., Ferri E., Crotti E.,
Bazzocchi C., Daffonchio D., Sacchi L., Moya A., Latorre A., Bandi C.;
"Phylogenomic evidence for the presence of a flagellum and cbb3
oxidase in the free-living mitochondrial ancestor.";
Mol. Biol. Evol. 28:3285-3296(2011).
-!- FUNCTION: Catalyzes the reversible interconversion of serine and
glycine with tetrahydrofolate (THF) serving as the one-carbon
carrier. This reaction serves as the major source of one-carbon
groups required for the biosynthesis of purines, thymidylate,
methionine, and other important biomolecules. Also exhibits THF-
independent aldolase activity toward beta-hydroxyamino acids,
producing glycine and aldehydes, via a retro-aldol mechanism.
{ECO:0000256|HAMAP-Rule:MF_00051}.
-!- CATALYTIC ACTIVITY: 5,10-methylenetetrahydrofolate + glycine +
H(2)O = tetrahydrofolate + L-serine. {ECO:0000256|HAMAP-
Rule:MF_00051}.
-!- COFACTOR:
Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
Evidence={ECO:0000256|HAMAP-Rule:MF_00051,
ECO:0000256|PIRSR:PIRSR000412-50};
-!- PATHWAY: Amino-acid biosynthesis; glycine biosynthesis; glycine
from L-serine: step 1/1. {ECO:0000256|HAMAP-Rule:MF_00051}.
-!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion.
{ECO:0000256|HAMAP-Rule:MF_00051}.
-!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00051}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00051}.
-!- SIMILARITY: Belongs to the SHMT family. {ECO:0000256|HAMAP-
Rule:MF_00051}.
-!- CAUTION: Lacks conserved residue(s) required for the propagation
of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00051}.
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EMBL; CP002130; AEI88395.1; -; Genomic_DNA.
RefSeq; WP_013950613.1; NC_015722.1.
STRING; 696127.midi_00070; -.
EnsemblBacteria; AEI88395; AEI88395; midi_00070.
KEGG; mmn:midi_00070; -.
eggNOG; ENOG4105C65; Bacteria.
eggNOG; COG0112; LUCA.
KO; K00600; -.
OMA; PLEHIIA; -.
OrthoDB; POG091H02WA; -.
UniPathway; UPA00193; -.
UniPathway; UPA00288; UER01023.
Proteomes; UP000006639; Chromosome.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0004372; F:glycine hydroxymethyltransferase activity; IEA:UniProtKB-UniRule.
GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
GO; GO:0019264; P:glycine biosynthetic process from serine; IEA:UniProtKB-UniRule.
GO; GO:0035999; P:tetrahydrofolate interconversion; IEA:UniProtKB-UniPathway.
CDD; cd00378; SHMT; 1.
Gene3D; 3.40.640.10; -; 1.
Gene3D; 3.90.1150.10; -; 1.
HAMAP; MF_00051; SHMT; 1.
InterPro; IPR015424; PyrdxlP-dep_Trfase.
InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1.
InterPro; IPR015422; PyrdxlP-dep_Trfase_sub2.
InterPro; IPR001085; Ser_HO-MeTrfase.
InterPro; IPR019798; Ser_HO-MeTrfase_PLP_BS.
PIRSF; PIRSF000412; SHMT; 1.
SUPFAM; SSF53383; SSF53383; 1.
PROSITE; PS00096; SHMT; 1.
3: Inferred from homology;
Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00051};
Complete proteome {ECO:0000313|Proteomes:UP000006639};
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00051};
Methyltransferase {ECO:0000313|EMBL:AEI88395.1};
One-carbon metabolism {ECO:0000256|HAMAP-Rule:MF_00051};
Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_00051,
ECO:0000256|PIRSR:PIRSR000412-50};
Reference proteome {ECO:0000313|Proteomes:UP000006639};
Transferase {ECO:0000313|EMBL:AEI88395.1}.
BINDING 38 38 Pyridoxal phosphate. {ECO:0000256|HAMAP-
Rule:MF_00051}.
BINDING 58 58 Pyridoxal phosphate. {ECO:0000256|HAMAP-
Rule:MF_00051}.
BINDING 60 60 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00051}.
BINDING 67 67 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00051}.
BINDING 68 68 Pyridoxal phosphate. {ECO:0000256|HAMAP-
Rule:MF_00051}.
BINDING 102 102 Pyridoxal phosphate. {ECO:0000256|HAMAP-
Rule:MF_00051}.
BINDING 124 124 Substrate; via carbonyl oxygen.
{ECO:0000256|HAMAP-Rule:MF_00051}.
BINDING 179 179 Pyridoxal phosphate. {ECO:0000256|HAMAP-
Rule:MF_00051}.
BINDING 207 207 Pyridoxal phosphate. {ECO:0000256|HAMAP-
Rule:MF_00051}.
BINDING 232 232 Pyridoxal phosphate. {ECO:0000256|HAMAP-
Rule:MF_00051}.
BINDING 239 239 Pyridoxal phosphate. {ECO:0000256|HAMAP-
Rule:MF_00051}.
BINDING 265 265 Pyridoxal phosphate; via amide nitrogen
and carbonyl oxygen. {ECO:0000256|HAMAP-
Rule:MF_00051}.
BINDING 365 365 Pyridoxal phosphate. {ECO:0000256|HAMAP-
Rule:MF_00051}.
MOD_RES 233 233 N6-(pyridoxal phosphate)lysine.
{ECO:0000256|HAMAP-Rule:MF_00051,
ECO:0000256|PIRSR:PIRSR000412-50}.
SEQUENCE 423 AA; 46733 MW; 5AE33BD9CB3192AB CRC64;
MAKSPFFANS LANADPIIFQ QIQNELDRQQ DGLELIASEN IVSKAVLEAQ GSILTNKYAE
GYPGKRYYGG CQYVDEIENI AIERAKLLFE AQFASVQPHS GSQANQAVFL ALLKPGDAIL
SLSLDCGGHL THGSPVNQSG KWFQAMHYTL NPENFLLDYD QIKKLALEHK PKLIIAGYSA
YPRQIDFAKF REIADQVGAR LMVDMAHIAG LVAVGIYDNP LRYAHVVTTT THKTLRGPRG
GMILTNHQDI AKLINSAIFP GLQGGPLVHV IAAKAVALAE ALKPEYKDYI RNVVSNCKIL
ADNLLQRGCS ITTNGTDNHL LIMDLRKQGL TGKDLEESLE RAGLTCNKNN IPFDTQKPTV
TSGIRLGTAA CTTRGLQEED FVEIADWIAE IIHYMKTDPE NLNLAEITIR QKVNNVCKRY
PIY


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