GLYA_RICRS
ID GLYA_RICRS Reviewed; 420 AA.
AC A8GTI9;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 1.
DT 03-AUG-2022, entry version 83.
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=2.1.2.1 {ECO:0000255|HAMAP-Rule:MF_00051};
GN Name=glyA {ECO:0000255|HAMAP-Rule:MF_00051}; OrderedLocusNames=A1G_06305;
OS Rickettsia rickettsii (strain Sheila Smith).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX NCBI_TaxID=392021;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sheila Smith;
RA Madan A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S.,
RA Sanchez A., Dasch G., Eremeeva M.;
RT "Complete genome sequence of Rickettsia rickettsii.";
RL Submitted (SEP-2007) 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:0000255|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:0000255|HAMAP-Rule:MF_00051};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00051};
CC -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion.
CC {ECO:0000255|HAMAP-Rule:MF_00051}.
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 -!- 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; CP000848; ABV76714.1; -; Genomic_DNA.
DR RefSeq; WP_012151264.1; NC_009882.1.
DR PDB; 4J5U; X-ray; 1.70 A; A/B=1-420.
DR PDBsum; 4J5U; -.
DR AlphaFoldDB; A8GTI9; -.
DR SMR; A8GTI9; -.
DR EnsemblBacteria; ABV76714; ABV76714; A1G_06305.
DR GeneID; 45539639; -.
DR KEGG; rri:A1G_06305; -.
DR HOGENOM; CLU_022477_2_1_5; -.
DR OMA; RCQHSEV; -.
DR BRENDA; 2.1.2.1; 14408.
DR UniPathway; UPA00193; -.
DR UniPathway; UPA00288; UER01023.
DR Proteomes; UP000006832; 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; 3.40.640.10; -; 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 3D-structure; Amino-acid biosynthesis; Cytoplasm; One-carbon metabolism;
KW Pyridoxal phosphate; Transferase.
FT CHAIN 1..420
FT /note="Serine hydroxymethyltransferase"
FT /id="PRO_1000006309"
FT BINDING 121
FT /ligand="(6S)-5,6,7,8-tetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:57453"
FT /evidence="ECO:0000255|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:0000255|HAMAP-Rule:MF_00051"
FT BINDING 246
FT /ligand="(6S)-5,6,7,8-tetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:57453"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00051"
FT BINDING 354..356
FT /ligand="(6S)-5,6,7,8-tetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:57453"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00051"
FT SITE 229
FT /note="Plays an important role in substrate specificity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00051"
FT MOD_RES 230
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00051"
FT HELIX 3..5
FT /evidence="ECO:0007829|PDB:4J5U"
FT HELIX 8..11
FT /evidence="ECO:0007829|PDB:4J5U"
FT HELIX 13..28
FT /evidence="ECO:0007829|PDB:4J5U"
FT STRAND 29..31
FT /evidence="ECO:0007829|PDB:4J5U"
FT HELIX 41..47
FT /evidence="ECO:0007829|PDB:4J5U"
FT HELIX 50..53
FT /evidence="ECO:0007829|PDB:4J5U"
FT STRAND 62..66
FT /evidence="ECO:0007829|PDB:4J5U"
FT HELIX 69..86
FT /evidence="ECO:0007829|PDB:4J5U"
FT STRAND 89..92
FT /evidence="ECO:0007829|PDB:4J5U"
FT HELIX 98..109
FT /evidence="ECO:0007829|PDB:4J5U"
FT STRAND 115..119
FT /evidence="ECO:0007829|PDB:4J5U"
FT HELIX 121..123
FT /evidence="ECO:0007829|PDB:4J5U"
FT HELIX 127..129
FT /evidence="ECO:0007829|PDB:4J5U"
FT HELIX 135..138
FT /evidence="ECO:0007829|PDB:4J5U"
FT STRAND 139..145
FT /evidence="ECO:0007829|PDB:4J5U"
FT TURN 149..151
FT /evidence="ECO:0007829|PDB:4J5U"
FT HELIX 156..166
FT /evidence="ECO:0007829|PDB:4J5U"
FT STRAND 169..174
FT /evidence="ECO:0007829|PDB:4J5U"
FT HELIX 184..194
FT /evidence="ECO:0007829|PDB:4J5U"
FT STRAND 197..201
FT /evidence="ECO:0007829|PDB:4J5U"
FT TURN 203..205
FT /evidence="ECO:0007829|PDB:4J5U"
FT HELIX 206..210
FT /evidence="ECO:0007829|PDB:4J5U"
FT TURN 218..220
FT /evidence="ECO:0007829|PDB:4J5U"
FT STRAND 222..227
FT /evidence="ECO:0007829|PDB:4J5U"
FT STRAND 238..243
FT /evidence="ECO:0007829|PDB:4J5U"
FT HELIX 245..255
FT /evidence="ECO:0007829|PDB:4J5U"
FT TURN 256..259
FT /evidence="ECO:0007829|PDB:4J5U"
FT HELIX 265..278
FT /evidence="ECO:0007829|PDB:4J5U"
FT HELIX 281..303
FT /evidence="ECO:0007829|PDB:4J5U"
FT HELIX 309..311
FT /evidence="ECO:0007829|PDB:4J5U"
FT STRAND 314..321
FT /evidence="ECO:0007829|PDB:4J5U"
FT HELIX 323..325
FT /evidence="ECO:0007829|PDB:4J5U"
FT HELIX 329..338
FT /evidence="ECO:0007829|PDB:4J5U"
FT TURN 355..357
FT /evidence="ECO:0007829|PDB:4J5U"
FT STRAND 359..364
FT /evidence="ECO:0007829|PDB:4J5U"
FT HELIX 366..370
FT /evidence="ECO:0007829|PDB:4J5U"
FT HELIX 375..394
FT /evidence="ECO:0007829|PDB:4J5U"
FT HELIX 399..413
FT /evidence="ECO:0007829|PDB:4J5U"
SQ SEQUENCE 420 AA; 46015 MW; 35B1024E9C9BDA7D CRC64;
MNIFNNNLHE TDKEINEIIK HEKLRQSSVI ELIASENFVS PAVLEAQGAL LTNKYAEGYP
SKRFYNGCEE VDKAENLAIE RVKKLFNCKY ANVQPHSGSQ ANQAVYLALL QPGDTVLGMS
LDSGGHLTHG AAPNMSGKWF NAVSYSVNKE TYLIDYDEIE RLADLHKPKL LIAGFSAYPR
NIDFAKFREI VDKVGAYFMA DIAHIAGLVA TGEHQSPIPY AHAVTSTTHK TLRGPRGGLI
LSNDEEIGHK INSALFPGLQ GGPLMHIIAA KAVAFLENLQ PEYKSYIQQV ISNAKALASS
LQERGYDILT GGTDNHIVLV DLRKDGITGK LAANSLDRAG ITCNKNAIPF DETSPFITSG
IRLGTPACTT RGFKEKDFVL VGHMVADILD GLKNNEDNSA LEQQVLNEVT KLIELFPFYG
