MSHMT_AMISX
ID MSHMT_AMISX Reviewed; 425 AA.
AC B2DEU8;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 66.
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=AHMT {ECO:0000303|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};
GN Name=mshmt {ECO:0000255|HAMAP-Rule:MF_00051, ECO:0000312|EMBL:BAG31001.1};
OS Aminobacter sp.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Phyllobacteriaceae; Aminobacter; unclassified Aminobacter.
OX NCBI_TaxID=1872490;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC STRAIN=AJ110403;
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=1500 uM for alpha-methyl-L-serine {ECO:0000269|PubMed:18997407};
CC KM=90 uM for tetrahydrofolate {ECO:0000269|PubMed:18997407};
CC Vmax=22.1 umol/min/mg enzyme with alpha-methyl-L-serine as substrate
CC {ECO:0000269|PubMed:18997407};
CC Vmax=7.75 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; AB426469; BAG31001.1; -; Genomic_DNA.
DR BRENDA; 2.1.2.7; 11477.
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_0000455995"
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 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; 45718 MW; 438568FE255C1886 CRC64;
MTEQTKAYFN TPVHERDPLV AQALDNERKR QQDQIELIAS ENIVSRAVLD ALGHEMTNKT
LEGYPGNRFH GGGQFVDVVE QAAIDRAKEL FGCAYANVQP HSGTQANLAV FFLLLKPGDK
VLSLDLAAGG HLSHGMKGNL SGRWFESHNY NVDPETEVID YDEMERIAEE VRPTLLITGG
SAYPRELDFE RMGKIAKKVG AWFLVDMAHI AGLVAGGAHP SPFPHADIVT CTTTKTLRGP
RGGLILTNNE AWFKKLQSAV FPGVQGSLHS NVLAAKAVCL GEALRPDFKV YAAQVKANAR
VLAETLIARG VRIVSGGTDT HIVLVDLSSK GLNGKQAEDL LARANITANK NPIPNDSPRP
AEWVGMRLGV SAATTRGMKE DEFRTLGTVI ADLIEAEAAG NADGVVEGAK AKVATLTAAF
PVYAH
