GLYA_CAMJE
ID GLYA_CAMJE Reviewed; 414 AA.
AC P24531; Q0PBA8; Q9PIA3;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 140.
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=Cj0402;
OS Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS 11168).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=192222;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 43431 / TGH 9011 / Serotype O:3;
RX PubMed=2060796; DOI=10.1016/0378-1119(91)90223-x;
RA Chan V.L., Bingham H.L.;
RT "Complete sequence of the Campylobacter jejuni glyA gene encoding serine
RT hydroxymethyltransferase.";
RL Gene 101:51-58(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700819 / NCTC 11168;
RX PubMed=10688204; DOI=10.1038/35001088;
RA Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA Barrell B.G.;
RT "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT reveals hypervariable sequences.";
RL Nature 403:665-668(2000).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS), AND SUBUNIT.
RG Center for structural genomics of infectious diseases (CSGID);
RA Anderson S.M., Wawrzak Z., Onopriyenko O., Hasseman J., Anderson W.F.,
RA Savchenko A.;
RT "Crystal structure of serine hydroxymethyltransferase from Campylobacter
RT jejuni.";
RL Submitted (MAY-2010) to the PDB data bank.
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 ECO:0000269|Ref.3}.
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}.
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DR EMBL; X53816; CAA37812.1; -; Genomic_DNA.
DR EMBL; AL111168; CAL34552.1; -; Genomic_DNA.
DR PIR; H81383; H81383.
DR PIR; JQ1016; JQ1016.
DR RefSeq; WP_002858710.1; NC_002163.1.
DR RefSeq; YP_002343839.1; NC_002163.1.
DR PDB; 3N0L; X-ray; 1.80 A; A/B=1-414.
DR PDBsum; 3N0L; -.
DR AlphaFoldDB; P24531; -.
DR SMR; P24531; -.
DR IntAct; P24531; 45.
DR STRING; 192222.Cj0402; -.
DR PaxDb; P24531; -.
DR PRIDE; P24531; -.
DR EnsemblBacteria; CAL34552; CAL34552; Cj0402.
DR GeneID; 904726; -.
DR KEGG; cje:Cj0402; -.
DR PATRIC; fig|192222.6.peg.393; -.
DR eggNOG; COG0112; Bacteria.
DR HOGENOM; CLU_022477_2_1_7; -.
DR OMA; SHPAGLI; -.
DR UniPathway; UPA00193; -.
DR UniPathway; UPA00288; UER01023.
DR EvolutionaryTrace; P24531; -.
DR Proteomes; UP000000799; 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; Reference proteome; Transferase.
FT CHAIN 1..414
FT /note="Serine hydroxymethyltransferase"
FT /id="PRO_0000113554"
FT BINDING 116
FT /ligand="(6S)-5,6,7,8-tetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:57453"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00051"
FT BINDING 120..122
FT /ligand="(6S)-5,6,7,8-tetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:57453"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00051"
FT BINDING 240
FT /ligand="(6S)-5,6,7,8-tetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:57453"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00051"
FT BINDING 348..350
FT /ligand="(6S)-5,6,7,8-tetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:57453"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00051"
FT SITE 223
FT /note="Plays an important role in substrate specificity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00051"
FT MOD_RES 224
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00051"
FT CONFLICT 188
FT /note="I -> V (in Ref. 1; CAA37812)"
FT /evidence="ECO:0000305"
FT CONFLICT 214
FT /note="Y -> H (in Ref. 1; CAA37812)"
FT /evidence="ECO:0000305"
FT CONFLICT 386
FT /note="V -> I (in Ref. 1; CAA37812)"
FT /evidence="ECO:0000305"
FT HELIX 1..6
FT /evidence="ECO:0007829|PDB:3N0L"
FT HELIX 8..23
FT /evidence="ECO:0007829|PDB:3N0L"
FT STRAND 24..26
FT /evidence="ECO:0007829|PDB:3N0L"
FT HELIX 36..42
FT /evidence="ECO:0007829|PDB:3N0L"
FT HELIX 45..48
FT /evidence="ECO:0007829|PDB:3N0L"
FT STRAND 57..61
FT /evidence="ECO:0007829|PDB:3N0L"
FT HELIX 64..81
FT /evidence="ECO:0007829|PDB:3N0L"
FT STRAND 84..87
FT /evidence="ECO:0007829|PDB:3N0L"
FT HELIX 93..104
FT /evidence="ECO:0007829|PDB:3N0L"
FT STRAND 110..114
FT /evidence="ECO:0007829|PDB:3N0L"
FT STRAND 135..140
FT /evidence="ECO:0007829|PDB:3N0L"
FT HELIX 150..160
FT /evidence="ECO:0007829|PDB:3N0L"
FT STRAND 163..167
FT /evidence="ECO:0007829|PDB:3N0L"
FT HELIX 178..188
FT /evidence="ECO:0007829|PDB:3N0L"
FT STRAND 191..195
FT /evidence="ECO:0007829|PDB:3N0L"
FT TURN 197..199
FT /evidence="ECO:0007829|PDB:3N0L"
FT HELIX 200..204
FT /evidence="ECO:0007829|PDB:3N0L"
FT TURN 212..214
FT /evidence="ECO:0007829|PDB:3N0L"
FT STRAND 216..223
FT /evidence="ECO:0007829|PDB:3N0L"
FT TURN 224..226
FT /evidence="ECO:0007829|PDB:3N0L"
FT STRAND 232..237
FT /evidence="ECO:0007829|PDB:3N0L"
FT HELIX 239..249
FT /evidence="ECO:0007829|PDB:3N0L"
FT TURN 250..253
FT /evidence="ECO:0007829|PDB:3N0L"
FT HELIX 259..272
FT /evidence="ECO:0007829|PDB:3N0L"
FT HELIX 275..297
FT /evidence="ECO:0007829|PDB:3N0L"
FT HELIX 303..305
FT /evidence="ECO:0007829|PDB:3N0L"
FT STRAND 308..315
FT /evidence="ECO:0007829|PDB:3N0L"
FT STRAND 319..321
FT /evidence="ECO:0007829|PDB:3N0L"
FT HELIX 323..332
FT /evidence="ECO:0007829|PDB:3N0L"
FT TURN 349..351
FT /evidence="ECO:0007829|PDB:3N0L"
FT STRAND 353..358
FT /evidence="ECO:0007829|PDB:3N0L"
FT HELIX 360..364
FT /evidence="ECO:0007829|PDB:3N0L"
FT HELIX 369..384
FT /evidence="ECO:0007829|PDB:3N0L"
FT TURN 385..387
FT /evidence="ECO:0007829|PDB:3N0L"
FT HELIX 389..403
FT /evidence="ECO:0007829|PDB:3N0L"
SQ SEQUENCE 414 AA; 45778 MW; 91225A45CD9193E6 CRC64;
MSLEMFDKEI FDLTNKELER QCEGLEMIAS ENFTLPEVME VMGSILTNKY AEGYPGKRYY
GGCEFVDEIE TLAIERCKKL FNCKFANVQP NSGSQANQGV YAALINPGDK ILGMDLSHGG
HLTHGAKVSS SGKMYESCFY GVELDGRIDY EKVREIAKKE KPKLIVCGAS AYARVIDFAK
FREIADEIGA YLFADIAHIA GLVVAGEHPS PFPYAHVVSS TTHKTLRGPR GGIIMTNDEE
LAKKINSAIF PGIQGGPLMH VIAAKAVGFK FNLSDEWKVY AKQVRTNAQV LANVLMDRKF
KLVSDGTDNH LVLMSFLDRE FSGKDADLAL GNAGITANKN TVPGEIRSPF ITSGLRLGTP
ALTARGFKEK EMEIVSNYIA DILDDVNNEK LQENIKQELK KLASNFIIYE RAMF
