ID A0A061SL84_9RHOB Unreviewed; 436 AA.
AC A0A061SL84;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Serine hydroxymethyltransferase {ECO:0000313|EMBL:KAJ01622.1};
GN ORFNames=PM02_18420 {ECO:0000313|EMBL:KAJ01622.1};
OS Sulfitobacter mediterraneus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Sulfitobacter.
OX NCBI_TaxID=83219 {ECO:0000313|EMBL:KAJ01622.1, ECO:0000313|Proteomes:UP000027337};
RN [1] {ECO:0000313|EMBL:KAJ01622.1, ECO:0000313|Proteomes:UP000027337}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1FIGIMAR09 {ECO:0000313|EMBL:KAJ01622.1,
RC ECO:0000313|Proteomes:UP000027337};
RX PubMed=24855294;
RA Mas-Llado M., Pina-Villalonga J.M., Brunet-Galmes I., Nogales B., Bosch R.;
RT "Draft Genome Sequences of Two Isolates of the Roseobacter Group,
RT Sulfitobacter sp. Strains 3SOLIMAR09 and 1FIGIMAR09, from Harbors of
RT Mallorca Island (Mediterranean Sea).";
RL Genome Announc. 2:e00350-14(2014).
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:KAJ01622.1}.
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DR EMBL; JEMU01000023; KAJ01622.1; -; Genomic_DNA.
DR RefSeq; WP_037911305.1; NZ_JEMU01000023.1.
DR AlphaFoldDB; A0A061SL84; -.
DR STRING; 83219.PM02_18420; -.
DR eggNOG; COG0112; Bacteria.
DR Proteomes; UP000027337; 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:KAJ01622.1};
KW One-carbon metabolism {ECO:0000256|ARBA:ARBA00022563};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000412-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000027337};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KAJ01622.1}.
FT DOMAIN 40..407
FT /note="Serine hydroxymethyltransferase-like"
FT /evidence="ECO:0000259|Pfam:PF00464"
FT MOD_RES 253
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000412-50"
SQ SEQUENCE 436 AA; 45846 MW; DE635BD9581426D7 CRC64;
MTLAKRNWVP AQCETRVQEI AGQTTQASSE ALMTQIERLV QRNKQIHEVD CFNLNPATNV
MNPKAEALLA SGLGSRPSLG YPGDKYEMGL EAIEEIEVIS AALCAEVFDA NFAEIRVPSG
AIANLYGFMA ICKPGDTIIV PPATIGGHVT HHNAGCAGLY GLRIIEAPVT ADGYTVDLDG
LRALALKERP KLITIGGSLN LFEHPVAGVR SIADEVEAKV LFDAAHQCGI IAGKAWSNPL
VEGAHLMTMS TYKSLGGPAG GLIVSNDEEI AKALDAIAFP GMTANFDAAK SAALAVTMLD
WRDHGQAYAA QMIAMAKALS KALQDQGVPV FSGAGGATQS HQFAVLAEGF GGGQAASKTL
RQAGFLACGI GLPIDPVEGD LNGLRIGTPE LVRWGMTEAD APRLAGLIAA GLRGEAISPE
VSKWRQTFDK VHFVHS
//
