MSHMT_PARSX
ID MSHMT_PARSX Reviewed; 425 AA.
AC B2DEU7;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 64.
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|Ref.1};
DE EC=2.1.2.7 {ECO:0000255|HAMAP-Rule:MF_00051, ECO:0000269|Ref.1};
DE AltName: Full=Alpha-methylserine hydroxymethyltransferase {ECO:0000255|HAMAP-Rule:MF_00051, ECO:0000303|Ref.1};
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:0000303|Ref.1};
OS Paracoccus sp.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Paracoccus; unclassified Paracoccus (in: Bacteria).
OX NCBI_TaxID=267;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-31, FUNCTION,
RP CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND SUBUNIT.
RC STRAIN=AJ110402;
RX DOI=10.1016/j.molcatb.2008.05.002;
RA Nozaki H., Kuroda S., Watanabe K., Yokozeki K.;
RT "Screening of microorganisms producing alpha-methylserine
RT hydroxymethyltransferase, purification of the enzyme, gene cloning, and
RT application to the enzymatic synthesis of alpha-methyl-L-serine.";
RL J. Mol. Catal., B Enzym. 56:221-226(2009).
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|Ref.1}.
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, ECO:0000269|Ref.1};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00051, ECO:0000269|Ref.1};
CC -!- ACTIVITY REGULATION: Inhibited by hydroxylamine and sodium borohydride.
CC {ECO:0000269|Ref.1}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=540 uM for alpha-methyl-L-serine {ECO:0000269|Ref.1};
CC KM=73 uM for tetrahydrofolate {ECO:0000269|Ref.1};
CC Vmax=8.15 umol/min/mg enzyme with alpha-methyl-L-serine as substrate
CC {ECO:0000269|Ref.1};
CC pH dependence:
CC Optimum pH is 7.4-8.0. {ECO:0000269|Ref.1};
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|Ref.1}.
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; AB426468; BAG31000.1; -; Genomic_DNA.
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; Direct protein sequencing; One-carbon metabolism;
KW Pyridoxal phosphate; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.1"
FT CHAIN 2..425
FT /note="2-methylserine hydroxymethyltransferase"
FT /id="PRO_0000455997"
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|Ref.1"
FT MOD_RES 235
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00051"
FT CONFLICT 5
FT /note="Missing (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 425 AA; 46056 MW; ED60F2B2B6D6B395 CRC64;
MNELTRTFFN SSVHDTDPLI AQALDDERAR QKNQIELIAS ENIVSQAVLD ALGHEMTNKT
LEGYPGNRFH GGGQFVDVVE QAAIDRAKQL FNCGYANVQP HSGTQANLAV FFLLVKPGDR
ILSLDLAAGG HLSHGMKGNL SGRWFEAHNY NVDPQNEVIN YDEMERIAEE VKPKLLITGG
SAYPRELDFA RMAQIAKKVG AFFMVDMAHI AGLVAGGAHP SPFPHADIVT CTTTKTLRGP
RGGLILTNNE EWYKKLQTAV FPGVQGSLHS NVLAAKAICL GEALRPEFRD YVAQVVKNAK
VLAETLTSRG IRIVSGGTDT HIVLLDLSSK GLNGKQAEDA LARANITSNK NPIPNDSPRP
AEWVGMRLGV SAATTRGMKE DEFRKLGNVV ADLLEAESAG NGPEAAEKAK VTVRELTEAF
PVYAH
