ID A0A402B222_9CHLR Unreviewed; 431 AA.
AC A0A402B222;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE SubName: Full=Serine hydroxymethyltransferase {ECO:0000313|EMBL:GCE25357.1};
GN ORFNames=KDA_08410 {ECO:0000313|EMBL:GCE25357.1};
OS Dictyobacter alpinus.
OC Bacteria; Chloroflexota; Ktedonobacteria; Ktedonobacterales;
OC Dictyobacteraceae; Dictyobacter.
OX NCBI_TaxID=2014873 {ECO:0000313|EMBL:GCE25357.1, ECO:0000313|Proteomes:UP000287171};
RN [1] {ECO:0000313|Proteomes:UP000287171}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Uno16 {ECO:0000313|Proteomes:UP000287171};
RA Wang C.M., Zheng Y., Sakai Y., Toyoda A., Minakuchi Y., Abe K., Yokota A.,
RA Yabe S.;
RT "Tengunoibacter tsumagoiensis gen. nov., sp. nov., Dictyobacter kobayashii
RT sp. nov., D. alpinus sp. nov., and D. joshuensis sp. nov. and description
RT of Dictyobacteraceae fam. nov. within the order Ktedonobacterales isolated
RT from Tengu-no-mugimeshi.";
RL Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|PIRSR:PIRSR000412-50};
CC -!- SIMILARITY: Belongs to the SHMT family.
CC {ECO:0000256|ARBA:ARBA00006376}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GCE25357.1}.
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DR EMBL; BIFT01000001; GCE25357.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A402B222; -.
DR OrthoDB; 9803871at2; -.
DR Proteomes; UP000287171; Unassembled WGS sequence.
DR GO; GO:0004372; F:glycine hydroxymethyltransferase activity; IEA:InterPro.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0019264; P:glycine biosynthetic process from serine; IEA:InterPro.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0035999; P:tetrahydrofolate interconversion; IEA:InterPro.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 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; SERINE HYDROXYMETHYLTRANSFERASE; 1.
DR PANTHER; PTHR11680:SF28; SERINE HYDROXYMETHYLTRANSFERASE; 1.
DR Pfam; PF00464; SHMT; 1.
DR PIRSF; PIRSF000412; SHMT; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000313|EMBL:GCE25357.1};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000412-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000287171};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:GCE25357.1}.
FT DOMAIN 12..405
FT /note="Serine hydroxymethyltransferase-like"
FT /evidence="ECO:0000259|Pfam:PF00464"
FT MOD_RES 244
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000412-50"
SQ SEQUENCE 431 AA; 47581 MW; 248C82B2F78A309D CRC64;
MTINIHDIEA LIEQQETWRQ KQTINLIASE NTPSEAVRRV QTSDFMGRYA EGHPNEGEQV
NRYYQGTRYI DQIERMAEQE LLTLFGAKQV DVRPISGNAS NTALALSILR GGDTVIANST
DAGGHISHGA VGVFGRRIQS RGQSLKIGSE HAIHLHYLPL TEDRYHVDPQ KTIELVDQLN
PQLVILGKSL FLFPEPVTEI AAFCKTKDIP VLYDGAHVLG LIAGGQFQSP LQEGATWLTG
STHKTFPGPQ RGVILANLTD PAAIKKCWQP ADRGVFPGSS SNHHLHTLPA LLVATREMQR
YGHEYAAQIV RNAQALGRSL DELGTPVEAR EFGYTRSHMI AVNVAQWGGG VDVAKRLEES
DIIVNYNMLP GDVDPRNPSG LRIGVSEMTR FGMDEQAMGE LAQLIHEAVR GKAVKEQVNA
LRGRYVEMQY V
//
