ID F0T2B8_SYNGF Unreviewed; 419 AA.
AC F0T2B8;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 69.
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 OrderedLocusNames=Sgly_3283 {ECO:0000313|EMBL:ADY57546.1};
OS Syntrophobotulus glycolicus (strain DSM 8271 / FlGlyR).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC Syntrophobotulus.
OX NCBI_TaxID=645991 {ECO:0000313|EMBL:ADY57546.1, ECO:0000313|Proteomes:UP000007488};
RN [1] {ECO:0000313|EMBL:ADY57546.1, ECO:0000313|Proteomes:UP000007488}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 8271 / FlGlyR {ECO:0000313|Proteomes:UP000007488};
RX PubMed=21886864;
RA Han C., Mwirichia R., Chertkov O., Held B., Lapidus A., Nolan M., Lucas S.,
RA Hammon N., Deshpande S., Cheng J.F., Tapia R., Goodwin L., Pitluck S.,
RA Huntemann M., Liolios K., Ivanova N., Pagani I., Mavromatis K.,
RA Ovchinikova G., Pati A., Chen A., Palaniappan K., Land M., Hauser L.,
RA Brambilla E.M., Rohde M., Spring S., Sikorski J., Goker M., Woyke T.,
RA Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C.,
RA Klenk H.P., Detter J.C.;
RT "Complete genome sequence of Syntrophobotulus glycolicus type strain
RT (FlGlyR).";
RL Stand. Genomic Sci. 4:371-380(2011).
RN [2] {ECO:0000313|Proteomes:UP000007488}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 8271 / FlGlyR {ECO:0000313|Proteomes:UP000007488};
RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA Kyrpides N., Mavromatis K., Pagani I., Ivanova N., Mikhailova N.,
RA Chertkov O., Held B., Detter J.C., Tapia R., Han C., Land M., Hauser L.,
RA Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S.,
RA Schroeder M., Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Syntrophobotulus glycolicus DSM 8271.";
RL Submitted (FEB-2011) 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 carrier.
CC This reaction serves as the major source of one-carbon groups required
CC for the biosynthesis of purines, thymidylate, methionine, and other
CC important biomolecules. Also exhibits THF-independent aldolase activity
CC toward 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 + H2O =
CC (6S)-5,6,7,8-tetrahydrofolate + L-serine; Xref=Rhea:RHEA:15481,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15636, ChEBI:CHEBI:33384,
CC ChEBI:CHEBI:57305, ChEBI:CHEBI:57453; EC=2.1.2.1;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00051};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|HAMAP-Rule:MF_00051, ECO:0000256|PIRSR:PIRSR000412-50};
CC -!- PATHWAY: Amino-acid biosynthesis; glycine biosynthesis; glycine from L-
CC 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|ARBA:ARBA00011738, ECO:0000256|HAMAP-
CC Rule:MF_00051}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00051}.
CC -!- SIMILARITY: Belongs to the SHMT family. {ECO:0000256|ARBA:ARBA00006376,
CC ECO:0000256|HAMAP-Rule:MF_00051}.
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DR EMBL; CP002547; ADY57546.1; -; Genomic_DNA.
DR RefSeq; WP_013626271.1; NC_015172.1.
DR AlphaFoldDB; F0T2B8; -.
DR STRING; 645991.Sgly_3283; -.
DR KEGG; sgy:Sgly_3283; -.
DR eggNOG; COG0112; Bacteria.
DR HOGENOM; CLU_022477_2_1_9; -.
DR OrthoDB; 9803846at2; -.
DR UniPathway; UPA00193; -.
DR UniPathway; UPA00288; UER01023.
DR Proteomes; UP000007488; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004372; F:glycine hydroxymethyltransferase activity; IEA:UniProtKB-UniRule.
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; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR HAMAP; MF_00051; SHMT; 1.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR InterPro; IPR001085; Ser_HO-MeTrfase.
DR InterPro; IPR019798; Ser_HO-MeTrfase_PLP_BS.
DR InterPro; IPR039429; SHMT-like_dom.
DR PANTHER; PTHR11680; SERINE HYDROXYMETHYLTRANSFERASE; 1.
DR PANTHER; PTHR11680:SF28; SERINE HYDROXYMETHYLTRANSFERASE; 1.
DR Pfam; PF00464; SHMT; 1.
DR PIRSF; PIRSF000412; SHMT; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00096; SHMT; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00051};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00051};
KW One-carbon metabolism {ECO:0000256|ARBA:ARBA00022563, ECO:0000256|HAMAP-
KW Rule:MF_00051};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, ECO:0000256|HAMAP-
KW Rule:MF_00051}; Reference proteome {ECO:0000313|Proteomes:UP000007488};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00051}.
FT DOMAIN 11..383
FT /note="Serine hydroxymethyltransferase-like"
FT /evidence="ECO:0000259|Pfam:PF00464"
FT BINDING 121
FT /ligand="(6S)-5,6,7,8-tetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:57453"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00051"
FT BINDING 125..127
FT /ligand="(6S)-5,6,7,8-tetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:57453"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00051"
FT BINDING 244
FT /ligand="(6S)-5,6,7,8-tetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:57453"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00051"
FT BINDING 353..355
FT /ligand="(6S)-5,6,7,8-tetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:57453"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00051"
FT SITE 229
FT /note="Plays an important role in substrate specificity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00051"
FT MOD_RES 230
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00051,
FT ECO:0000256|PIRSR:PIRSR000412-50"
SQ SEQUENCE 419 AA; 45432 MW; 84DA6108B1AA843D CRC64;
MDYILKYIAP EDPEVAEAIE LEQGRQENKI ELIASENFVS RAVMAAQGSV LTNKYAEGYP
GKRYYGGCEY VDIVENLARD RVKKLFGAEH ANVQPHSGAQ ANTAVYFAMI KPGDTVMGMN
LSHGGHLTHG SPVNLSGAYF NFVEYGVEKD SEVVDYDKLR AIALECKPKM LVGGASAYPR
VIDFAVMREI ADEVGAYLMI DMAHIAGLVA TGLHPSPVPH AHFVTSTTHK TLRGPRGGLI
LCKEEFAQKI DKSIFPGIQG GPLMHVIAAK AVAFGEALKP EFKEYQQRII NNAQALAKGF
IARGFRLVSG GTDNHLVLLD VRSKNVTGKV AERVLDDVGI TVNKNTIPFD PESPFVTSGV
RIGAPAVTAR GMKEPEMEKI TEAINLAITA GSDESKLEQA KAIVADLCQK FPLYLASDK
//