GLYA_METTH
ID GLYA_METTH Reviewed; 423 AA.
AC O27433;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 27-MAR-2002, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Serine hydroxymethyltransferase {ECO:0000255|HAMAP-Rule:MF_00051};
DE Short=SHMT {ECO:0000255|HAMAP-Rule:MF_00051};
DE Short=Serine methylase {ECO:0000255|HAMAP-Rule:MF_00051};
DE EC=2.1.2.- {ECO:0000255|HAMAP-Rule:MF_00051, ECO:0000269|Ref.2};
GN Name=glyA {ECO:0000255|HAMAP-Rule:MF_00051}; OrderedLocusNames=MTH_1380;
OS Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM
OS 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX NCBI_TaxID=187420;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX PubMed=9371463; DOI=10.1128/jb.179.22.7135-7155.1997;
RA Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J.,
RA Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D.,
RA Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R.,
RA Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D.,
RA Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A.,
RA Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J.,
RA Reeve J.N.;
RT "Complete genome sequence of Methanobacterium thermoautotrophicum deltaH:
RT functional analysis and comparative genomics.";
RL J. Bacteriol. 179:7135-7155(1997).
RN [2]
RP FUNCTION, H4MPT-DEPENDENT SERINE HYDROXYMETHYLTRANSFERASE ACTIVITY,
RP CATALYTIC ACTIVITY, COFACTOR, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND SUBUNIT.
RC STRAIN=strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX DOI=10.1007/BF00446773;
RA Hoyt J.C., Oren A., Escalante-Semerena J.C., Wolfe R.S.;
RT "Tetrahydromethanopterin-dependent serine transhydroxymethylase from
RT Methanobacterium thermoautotrophicum.";
RL Arch. Microbiol. 145:153-158(1986).
CC -!- FUNCTION: Catalyzes the reversible interconversion of serine and
CC glycine with tetrahydromethanopterin (H4MPT) serving as the one-carbon
CC carrier. Cannot use tetrahydrofolate (THF or H4PteGlu) instead of H4MPT
CC as the pteridine substrate. Also probably exhibits a pteridine-
CC independent aldolase activity toward beta-hydroxyamino acids, producing
CC glycine and aldehydes, via a retro-aldol mechanism.
CC {ECO:0000269|Ref.2}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5,10-methylenetetrahydromethanopterin + glycine + H2O =
CC 5,6,7,8-tetrahydromethanopterin + L-serine; Xref=Rhea:RHEA:47104,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:33384, ChEBI:CHEBI:57305,
CC ChEBI:CHEBI:57818, ChEBI:CHEBI:58103; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00051, ECO:0000269|Ref.2};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00051, ECO:0000269|Ref.2};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 8.1. {ECO:0000269|Ref.2};
CC Temperature dependence:
CC Optimum temperature is 60 degrees Celsius. {ECO:0000269|Ref.2};
CC -!- PATHWAY: Amino-acid biosynthesis; glycine biosynthesis; glycine from L-
CC serine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00051}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00051,
CC ECO:0000269|Ref.2}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00051}.
CC -!- SIMILARITY: Belongs to the SHMT family. {ECO:0000255|HAMAP-
CC Rule:MF_00051, ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB85857.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE000666; AAB85857.1; ALT_INIT; Genomic_DNA.
DR PIR; F69050; F69050.
DR RefSeq; WP_048061037.1; NC_000916.1.
DR AlphaFoldDB; O27433; -.
DR SMR; O27433; -.
DR STRING; 187420.MTH_1380; -.
DR EnsemblBacteria; AAB85857; AAB85857; MTH_1380.
DR GeneID; 1471097; -.
DR KEGG; mth:MTH_1380; -.
DR PATRIC; fig|187420.15.peg.1345; -.
DR HOGENOM; CLU_022477_2_1_2; -.
DR OMA; SHPAGLI; -.
DR UniPathway; UPA00288; UER01023.
DR Proteomes; UP000005223; 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:InterPro.
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; IPR019798; Ser_HO-MeTrfase_PLP_BS.
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.
DR PROSITE; PS00096; SHMT; 1.
PE 1: Evidence at protein level;
KW Amino-acid biosynthesis; Cytoplasm; One-carbon metabolism;
KW Pyridoxal phosphate; Reference proteome; Transferase.
FT CHAIN 1..423
FT /note="Serine hydroxymethyltransferase"
FT /id="PRO_0000113716"
FT BINDING 121..123
FT /ligand="(6S)-5,6,7,8-tetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:57453"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00051"
FT BINDING 242
FT /ligand="(6S)-5,6,7,8-tetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:57453"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00051"
FT SITE 226
FT /note="Plays an important role in substrate specificity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00051"
FT MOD_RES 227
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00051"
SQ SEQUENCE 423 AA; 47223 MW; 04D473A659BD24D9 CRC64;
MVSNQDYTEK IRQLMKDHNS WMESSINLIA SENITSSRVK EALLSDLSHR YAEGLPGERL
YEGCRYIDEI EELTIELSKR LFRAEHANVQ PTSGVVANLA CFFATAEVGD PIMAMEVPYG
GHISHARVSA AGVRGFQIYT HPFDFENMNI DADAMKKKIL EVKPRIILFG GSLFLFPHPV
EEALEAAEEV GARIMYDGAH VLGLIAGGYF QDPLREGADM LVGSTHKTFP GPQGGIILCR
EELAADIDEA VFPGLVSNHH LHHVAGLGIA TAEMLEFGAE YAAQTINNAR KLAENLHELG
FNVLCEHLDF TESHQVVMDV SDIGRAAEIS KRLEANNIIL NKNLLPWDDV NRSDDPSGIR
IGTQEITRRG MKESEMSEVA EYIKRVVMDG KDVRDEVAEF MSSYTRVHYA FEDSEAYKYM
EIQ
