ID A0A0M4FZQ2_9BACI Unreviewed; 447 AA.
AC A0A0M4FZQ2;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Serine hydroxymethyltransferase {ECO:0000313|EMBL:ALC83125.1};
GN ORFNames=AM592_17270 {ECO:0000313|EMBL:ALC83125.1};
OS Bacillus gobiensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1441095 {ECO:0000313|EMBL:ALC83125.1, ECO:0000313|Proteomes:UP000067625};
RN [1] {ECO:0000313|Proteomes:UP000067625}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FJAT-4402 {ECO:0000313|Proteomes:UP000067625};
RA Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Lan J., Che J., Ge C.,
RA Shi H., Pan Z., Liu X.;
RT "Genome sequencing project for genomic taxonomy and phylogenomics of
RT Bacillus-like bacteria.";
RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ALC83125.1, ECO:0000313|Proteomes:UP000067625}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FJAT-4402 {ECO:0000313|EMBL:ALC83125.1,
RC ECO:0000313|Proteomes:UP000067625};
RX PubMed=26530456; DOI=10.1099/ijsem.0.000729;
RA Liu B., Liu G.H., Cetin S., Schumann P., Pan Z.Z., Chen Q.Q.;
RT "Bacillus gobiensis sp. nov., isolated from a soil sample.";
RL Int. J. Syst. Evol. Microbiol. 66:379-384(2016).
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}.
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DR EMBL; CP012600; ALC83125.1; -; Genomic_DNA.
DR RefSeq; WP_053604960.1; NZ_CP012600.1.
DR AlphaFoldDB; A0A0M4FZQ2; -.
DR STRING; 1441095.AM592_17270; -.
DR PATRIC; fig|1441095.3.peg.3835; -.
DR OrthoDB; 9803871at2; -.
DR Proteomes; UP000067625; Chromosome.
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:ALC83125.1};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000412-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000067625};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ALC83125.1}.
FT DOMAIN 36..415
FT /note="Serine hydroxymethyltransferase-like"
FT /evidence="ECO:0000259|Pfam:PF00464"
FT MOD_RES 258
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000412-50"
SQ SEQUENCE 447 AA; 49027 MW; 7030456656B58B30 CRC64;
MSTPTYQKDA HEVHDPEVLS KARAIIEKCS SPKLMQKEVI DAVERNAIWR GEECLNLLAP
EAPTSPTVRK LLASEVGTRA AEGHIGPTQR WFAGTTHIDE IEALCVELLK KVFKSNYADH
RLVASMLGNL TVYAALTKPG DNIMTIPQPT GGHSSNRYDG PAGIRGLNIY DVPMDPQELT
VDLDAFAKKA REIKPRLVAL GASMTLFPFP LKEMTQIVQE WGGKIFFDGA HQLGLIGGGQ
FQDPLSEGAC VMTGSSGKTF SGPQSGIILW NDPEINKPIT DAIFPALAAT HQVNRVAALA
AAAAEFLAFG EEYMAQIVKN SKALGKALHD RGVTMLGAHK GFTKTHQVIA DVRSFGNGLD
IAKKLGDANI ITNKNLIPSD KPEDWDYPSG LRIGTTEVTR LGMKENDMET VADFMIDVLE
DRKQTEQVRK EVIEFRKAYQ KIHYCFD
//
