ID A0A0B4DT58_9RHOB Unreviewed; 439 AA.
AC A0A0B4DT58;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Serine hydroxymethyltransferase {ECO:0000313|EMBL:KID08581.1};
GN ORFNames=GC1_15735 {ECO:0000313|EMBL:KID08581.1};
OS Leisingera sp. ANG1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Leisingera.
OX NCBI_TaxID=1002340 {ECO:0000313|EMBL:KID08581.1, ECO:0000313|Proteomes:UP000031201};
RN [1] {ECO:0000313|EMBL:KID08581.1, ECO:0000313|Proteomes:UP000031201}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ANG1 {ECO:0000313|EMBL:KID08581.1,
RC ECO:0000313|Proteomes:UP000031201};
RX PubMed=21551313; DOI=10.1128/JB.05139-11;
RA Collins A.J., Nyholm S.V.;
RT "Draft genome of Phaeobacter gallaeciensis ANG1, a dominant member of the
RT accessory nidamental gland of Euprymna scolopes.";
RL J. Bacteriol. 193:3397-3398(2011).
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:KID08581.1}.
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DR EMBL; AFCF02000008; KID08581.1; -; Genomic_DNA.
DR RefSeq; WP_019298210.1; NZ_AFCF02000008.1.
DR AlphaFoldDB; A0A0B4DT58; -.
DR STRING; 1002340.GC1_15735; -.
DR eggNOG; COG0112; Bacteria.
DR OrthoDB; 9019276at2; -.
DR Proteomes; UP000031201; 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:KID08581.1};
KW One-carbon metabolism {ECO:0000256|ARBA:ARBA00022563};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000412-50};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KID08581.1}.
FT DOMAIN 53..409
FT /note="Serine hydroxymethyltransferase-like"
FT /evidence="ECO:0000259|Pfam:PF00464"
FT MOD_RES 254
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000412-50"
SQ SEQUENCE 439 AA; 45729 MW; FD6601BF3A1FEF1A CRC64;
MTELARRNWV PAACEDYVQT VAAKTAAATS AETAARLTAL ADRNAEIHDR DCFNLNPATN
VMNPAAEALL ATGLGSRPSL GYPGDKYEMG LEAIEEIEVI AAEVAAQVFN ARYAEIRVGS
GALANLYGFM ALTKPGDAII APPAAVGGHV THHAGGCAGL YGLQTHPAPV DGDGYTVDLD
ALRDLAREVQ PKLITIGGSL NLFPHPVPEI RAIADEVGAK VLFDAAHQCG MIAGGHWGNP
LEQGAHLMTM STYKSLGGPA GGLIVTNDAD IAERLDAIAF PGMTANFDAA KSAALAMSLL
DWVEHGADYA KAMADLSLAL AEALAGQGLP VFAAARGMTQ SHQFALEAAE FGGGQAASKH
LRKAGFLACG IGLPIAEVPG DMNGLRIGTP ELVRRGVTVK HAPQLAELIT RALRTEDPAA
MAAEVAEFRA AFQGMHYVR
//
