MSHMT_ENSSX
ID MSHMT_ENSSX Reviewed; 425 AA.
AC B2DEV1;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=2-methylserine hydroxymethyltransferase {ECO:0000255|HAMAP-Rule:MF_00051, ECO:0000305};
DE Short=MSHMT {ECO:0000255|HAMAP-Rule:MF_00051, ECO:0000303|PubMed:18997407};
DE EC=2.1.2.7 {ECO:0000255|HAMAP-Rule:MF_00051, ECO:0000269|PubMed:18997407};
DE AltName: Full=Alpha-methylserine hydroxymethyltransferase {ECO:0000255|HAMAP-Rule:MF_00051, ECO:0000303|PubMed:18997407};
DE AltName: Full=D-alanine 2-hydroxymethyltransferase {ECO:0000255|HAMAP-Rule:MF_00051, ECO:0000305};
DE AltName: Full=EHMT {ECO:0000303|PubMed:18997407};
GN Name=mshmt {ECO:0000255|HAMAP-Rule:MF_00051, ECO:0000312|EMBL:BAG31004.1};
OS Ensifer sp.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Ensifer; unclassified Ensifer.
OX NCBI_TaxID=1872086;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC STRAIN=AJ110404;
RX PubMed=18997407; DOI=10.1271/bbb.80255;
RA Nozaki H., Kuroda S., Watanabe K., Yokozeki K.;
RT "Cloning of the gene encoding alpha-methylserine hydroxymethyltransferase
RT from Aminobacter sp. AJ110403 and Ensifer sp. AJ110404 and characterization
RT of the recombinant enzyme.";
RL Biosci. Biotechnol. Biochem. 72:3002-3005(2008).
CC -!- FUNCTION: Catalyzes the reversible interconversion of alpha-methyl-L-
CC serine to D-alanine with tetrahydrofolate (THF) serving as the one-
CC carbon carrier. Cannot use alpha-methyl-D-serine, L-serine, D-serine or
CC L-alanine. {ECO:0000269|PubMed:18997407}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + D-alanine + H2O
CC = (6S)-5,6,7,8-tetrahydrofolate + 2-methylserine;
CC Xref=Rhea:RHEA:10064, ChEBI:CHEBI:15377, ChEBI:CHEBI:15636,
CC ChEBI:CHEBI:57416, ChEBI:CHEBI:57453, ChEBI:CHEBI:58275; EC=2.1.2.7;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00051,
CC ECO:0000269|PubMed:18997407};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00051,
CC ECO:0000269|PubMed:18997407};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1880 uM for alpha-methyl-L-serine {ECO:0000269|PubMed:18997407};
CC KM=228 uM for tetrahydrofolate {ECO:0000269|PubMed:18997407};
CC Vmax=15.4 umol/min/mg enzyme with alpha-methyl-L-serine as substrate
CC {ECO:0000269|PubMed:18997407};
CC Vmax=5.48 umol/min/mg enzyme with D-alanine as substrate
CC {ECO:0000269|PubMed:18997407};
CC -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion.
CC {ECO:0000255|HAMAP-Rule:MF_00051}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00051,
CC ECO:0000269|PubMed:18997407}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00051}.
CC -!- SIMILARITY: Belongs to the SHMT family. {ECO:0000255|HAMAP-
CC Rule:MF_00051}.
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DR EMBL; AB426470; BAG31004.1; -; Genomic_DNA.
DR BRENDA; 2.1.2.7; 11478.
DR UniPathway; UPA00193; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004372; F:glycine hydroxymethyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
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:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0035999; P:tetrahydrofolate interconversion; IEA:UniProtKB-UniPathway.
DR CDD; cd00378; SHMT; 1.
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.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR InterPro; IPR001085; Ser_HO-MeTrfase.
DR InterPro; IPR039429; SHMT-like_dom.
DR PANTHER; PTHR11680; PTHR11680; 1.
DR Pfam; PF00464; SHMT; 1.
DR PIRSF; PIRSF000412; SHMT; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; One-carbon metabolism; Pyridoxal phosphate; Transferase.
FT CHAIN 1..425
FT /note="2-methylserine hydroxymethyltransferase"
FT /id="PRO_0000455996"
FT BINDING 126
FT /ligand="(6S)-5,6,7,8-tetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:57453"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00051"
FT BINDING 130..132
FT /ligand="(6S)-5,6,7,8-tetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:57453"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00051"
FT BINDING 251
FT /ligand="(6S)-5,6,7,8-tetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:57453"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00051"
FT SITE 234
FT /note="Plays an important role in substrate specificity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00051,
FT ECO:0000305|PubMed:18997407"
FT MOD_RES 235
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00051"
SQ SEQUENCE 425 AA; 45600 MW; 7EBCA8C1304B0950 CRC64;
MDHATRAHFT MTVGEVDPLL ADALASERGR QQNQIELIAS ENIVSRAVLD ALGHEITNKT
LEGYPGNRFH GGGQFVDIAE QAAIDRAKQL FNCGYANVQP HSGTQANLAV FFLLLKPGEK
VLSLDLAAGG HLSHGMKANL SGRWFDATNY NVNPQNEVID LDEMERLAEE IRPKLLITGG
SAYPRELDFE RMSRIAKKVG AYFLVDMAHI AGLVAGGVHP SPFPHADIVT CTTTKTLRGP
RGGLILTNNE EWYKKLQAAV FPGVQGSLHS NVLAAKAICL GEAMLDDFKV YARQVVANAK
VLANTLAERG VRIVSGGTDT HIVLLDLASK GLLGKQAETL LAKANITSNK NPIPGDSPRP
PEWVGMRLGS SAATTRGLKE AEFRVLGTVI ADLIDAEVAG KADDVVEGAK AKIAELTNTF
PVYGQ
