ID D7DJX9_METV0 Unreviewed; 260 AA.
AC D7DJX9;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=serine O-acetyltransferase {ECO:0000256|ARBA:ARBA00013266};
DE EC=2.3.1.30 {ECO:0000256|ARBA:ARBA00013266};
GN OrderedLocusNames=M301_1968 {ECO:0000313|EMBL:ADI30340.1};
OS Methylotenera versatilis (strain 301).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Methylophilaceae; Methylotenera.
OX NCBI_TaxID=666681 {ECO:0000313|EMBL:ADI30340.1, ECO:0000313|Proteomes:UP000000383};
RN [1] {ECO:0000313|Proteomes:UP000000383}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 {ECO:0000313|Proteomes:UP000000383};
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Clum A., Land M., Hauser L., Kyrpides N., Ivanova N.,
RA Chistoservova L., Kalyuzhnaya M., Woyke T.;
RT "Complete sequence of Methylotenera sp. 301.";
RL Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADI30340.1, ECO:0000313|Proteomes:UP000000383}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 {ECO:0000313|EMBL:ADI30340.1,
RC ECO:0000313|Proteomes:UP000000383};
RX PubMed=21622745; DOI=10.1128/JB.00404-11;
RA Lapidus A., Clum A., Labutti K., Kaluzhnaya M.G., Lim S., Beck D.A.,
RA Glavina Del Rio T., Nolan M., Mavromatis K., Huntemann M., Lucas S.,
RA Lidstrom M.E., Ivanova N., Chistoserdova L.;
RT "Genomes of three methylotrophs from a single niche uncover genetic and
RT metabolic divergence of Methylophilaceae.";
RL J. Bacteriol. 193:3757-3764(2011).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + L-serine = CoA + O-acetyl-L-serine;
CC Xref=Rhea:RHEA:24560, ChEBI:CHEBI:33384, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57288, ChEBI:CHEBI:58340; EC=2.3.1.30;
CC Evidence={ECO:0000256|ARBA:ARBA00000169};
CC -!- SIMILARITY: Belongs to the transferase hexapeptide repeat family.
CC {ECO:0000256|ARBA:ARBA00007274}.
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DR EMBL; CP002056; ADI30340.1; -; Genomic_DNA.
DR RefSeq; WP_013148652.1; NC_014207.1.
DR AlphaFoldDB; D7DJX9; -.
DR STRING; 666681.M301_1968; -.
DR KEGG; meh:M301_1968; -.
DR eggNOG; COG1045; Bacteria.
DR HOGENOM; CLU_051638_10_0_4; -.
DR OrthoDB; 9801456at2; -.
DR Proteomes; UP000000383; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0009001; F:serine O-acetyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006535; P:cysteine biosynthetic process from serine; IEA:InterPro.
DR CDD; cd03354; LbH_SAT; 1.
DR Gene3D; 2.160.10.10; Hexapeptide repeat proteins; 1.
DR Gene3D; 1.10.3130.10; serine acetyltransferase, domain 1; 1.
DR InterPro; IPR001451; Hexapep.
DR InterPro; IPR018357; Hexapep_transf_CS.
DR InterPro; IPR045304; LbH_SAT.
DR InterPro; IPR042122; Ser_AcTrfase_N_sf.
DR InterPro; IPR005881; Ser_O-AcTrfase.
DR InterPro; IPR011004; Trimer_LpxA-like_sf.
DR NCBIfam; TIGR01172; cysE; 1.
DR NCBIfam; NF041874; EPS_EpsC; 1.
DR PANTHER; PTHR42811; SERINE ACETYLTRANSFERASE; 1.
DR PANTHER; PTHR42811:SF5; SERINE ACETYLTRANSFERASE-RELATED; 1.
DR Pfam; PF00132; Hexapep; 1.
DR SUPFAM; SSF51161; Trimeric LpxA-like enzymes; 1.
DR PROSITE; PS00101; HEXAPEP_TRANSFERASES; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW ECO:0000313|EMBL:ADI30340.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000383};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ADI30340.1}.
SQ SEQUENCE 260 AA; 28344 MW; BDDD60BF9D5CD3EC CRC64;
MFNHLKEDIS IVFERDPAAR THWEILTTYP GVHALLMHRL SHWLWKQHLY WLARFNSHLA
RWLTGIEIHP GATIGRRVFI DHGMGVVVGE TAVIGDDCTL YHGVTLGGTS WNKGKRHPTL
ESGVVIGAGA KVLGPITVGT GAKIGSNAVV VKNVPANATA VGIPARILEE EKANKEESSK
SASFTAYAVI DDNDKFNHEA MSKALQVLLE HSAAQDAKLA ELTLQLQALS NDETSDTKVA
TAFDVKQPIK SKVTKKITSE
//
