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

 GLYA_ORITB              Reviewed;         426 AA.
A5CCC4;
14-APR-2009, integrated into UniProtKB/Swiss-Prot.
12-JUN-2007, sequence version 1.
05-JUL-2017, entry version 77.
RecName: Full=Serine hydroxymethyltransferase {ECO:0000255|HAMAP-Rule:MF_00051};
Short=SHMT {ECO:0000255|HAMAP-Rule:MF_00051};
Short=Serine methylase {ECO:0000255|HAMAP-Rule:MF_00051};
EC=2.1.2.1 {ECO:0000255|HAMAP-Rule:MF_00051};
Name=glyA {ECO:0000255|HAMAP-Rule:MF_00051};
OrderedLocusNames=OTBS_0253;
Orientia tsutsugamushi (strain Boryong) (Rickettsia tsutsugamushi).
Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
Rickettsiaceae; Rickettsieae; Orientia.
NCBI_TaxID=357244;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Boryong;
PubMed=17483455; DOI=10.1073/pnas.0611553104;
Cho N.-H., Kim H.-R., Lee J.-H., Kim S.-Y., Kim J., Cha S., Kim S.-Y.,
Darby A.C., Fuxelius H.-H., Yin J., Kim J.H., Kim J., Lee S.J.,
Koh Y.-S., Jang W.-J., Park K.-H., Andersson S.G.E., Choi M.-S.,
Kim I.-S.;
"The Orientia tsutsugamushi genome reveals massive proliferation of
conjugative type IV secretion system and host-cell interaction
genes.";
Proc. Natl. Acad. Sci. U.S.A. 104:7981-7986(2007).
-!- 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:0000255|HAMAP-Rule:MF_00051}.
-!- CATALYTIC ACTIVITY: 5,10-methylenetetrahydrofolate + glycine +
H(2)O = tetrahydrofolate + L-serine. {ECO:0000255|HAMAP-
Rule:MF_00051}.
-!- COFACTOR:
Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
Evidence={ECO:0000255|HAMAP-Rule:MF_00051};
-!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion.
{ECO:0000255|HAMAP-Rule:MF_00051}.
-!- PATHWAY: Amino-acid biosynthesis; glycine biosynthesis; glycine
from L-serine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00051}.
-!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00051}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00051}.
-!- SIMILARITY: Belongs to the SHMT family. {ECO:0000255|HAMAP-
Rule:MF_00051}.
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EMBL; AM494475; CAM79319.1; -; Genomic_DNA.
RefSeq; WP_011944361.1; NC_009488.1.
ProteinModelPortal; A5CCC4; -.
SMR; A5CCC4; -.
STRING; 357244.OTBS_0253; -.
EnsemblBacteria; CAM79319; CAM79319; OTBS_0253.
GeneID; 29642834; -.
KEGG; ots:OTBS_0253; -.
eggNOG; ENOG4105C65; Bacteria.
eggNOG; COG0112; LUCA.
HOGENOM; HOG000239404; -.
KO; K00600; -.
OMA; PLEHIIA; -.
OrthoDB; POG091H02WA; -.
UniPathway; UPA00193; -.
UniPathway; UPA00288; UER01023.
Proteomes; UP000001565; Chromosome.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0004372; F:glycine hydroxymethyltransferase activity; IEA:UniProtKB-EC.
GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
GO; GO:0006545; P:glycine biosynthetic process; IEA:UniProtKB-UniPathway.
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; Complete proteome; Cytoplasm;
One-carbon metabolism; Pyridoxal phosphate; Reference proteome;
Transferase.
CHAIN 1 426 Serine hydroxymethyltransferase.
/FTId=PRO_0000369943.
REGION 115 117 Substrate binding. {ECO:0000255|HAMAP-
Rule:MF_00051}.
BINDING 25 25 Pyridoxal phosphate. {ECO:0000255|HAMAP-
Rule:MF_00051}.
BINDING 45 45 Pyridoxal phosphate. {ECO:0000255|HAMAP-
Rule:MF_00051}.
BINDING 47 47 Substrate. {ECO:0000255|HAMAP-
Rule:MF_00051}.
BINDING 54 54 Substrate. {ECO:0000255|HAMAP-
Rule:MF_00051}.
BINDING 55 55 Pyridoxal phosphate. {ECO:0000255|HAMAP-
Rule:MF_00051}.
BINDING 89 89 Pyridoxal phosphate. {ECO:0000255|HAMAP-
Rule:MF_00051}.
BINDING 111 111 Substrate; via carbonyl oxygen.
{ECO:0000255|HAMAP-Rule:MF_00051}.
BINDING 166 166 Pyridoxal phosphate. {ECO:0000255|HAMAP-
Rule:MF_00051}.
BINDING 194 194 Pyridoxal phosphate. {ECO:0000255|HAMAP-
Rule:MF_00051}.
BINDING 219 219 Pyridoxal phosphate. {ECO:0000255|HAMAP-
Rule:MF_00051}.
BINDING 226 226 Pyridoxal phosphate. {ECO:0000255|HAMAP-
Rule:MF_00051}.
BINDING 252 252 Pyridoxal phosphate; via amide nitrogen
and carbonyl oxygen. {ECO:0000255|HAMAP-
Rule:MF_00051}.
BINDING 352 352 Pyridoxal phosphate. {ECO:0000255|HAMAP-
Rule:MF_00051}.
MOD_RES 220 220 N6-(pyridoxal phosphate)lysine.
{ECO:0000255|HAMAP-Rule:MF_00051}.
SEQUENCE 426 AA; 47007 MW; 1C9A94B36B78BA15 CRC64;
MCKEIYDLIA KELYRQQSTI ELIASENFTS KAVMLAQGSI LTNKYAEGYI NKRYYGGCEF
IDEVESMAID RVKKLFKCNY ANVQPHSGSQ ANQAVFLALL KPGDTILAMD LNSGGHLTHG
AKPNISGKFF NAVHYCVNKD SYLIDYNEVE MLAQQHKPKL IIVGYSAYSR KINFATFKEI
ADKVGAYLLA DIAHIAGLVA TEYHSSPIPY AHIVTSTTHK TLRGPRGGLI LSNDESISKK
INSAVFPGMQ GGPLMHVIAA KAIAFSEALM PQYKEYINQV MLNAKVLAKL LQDRGYNILT
GGTDNHMLLV DLRGKNITGQ EAEYLLDAAG ITCNKQVMPF DTTSPTITSG IRLGTPACTT
RGFKENEFIT VGKYIADILD NIAIIKSAKK NEGITITEIE KSLNSVITRT KHHVQELCNC
FPIYTN


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