ID A0A176VRW6_MARPO Unreviewed; 408 AA.
AC A0A176VRW6;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=serine O-acetyltransferase {ECO:0000256|ARBA:ARBA00013266};
DE EC=2.3.1.30 {ECO:0000256|ARBA:ARBA00013266};
GN ORFNames=AXG93_1877s1020 {ECO:0000313|EMBL:OAE23560.1};
OS Marchantia polymorpha subsp. ruderalis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Marchantiophyta;
OC Marchantiopsida; Marchantiidae; Marchantiales; Marchantiaceae; Marchantia.
OX NCBI_TaxID=1480154 {ECO:0000313|EMBL:OAE23560.1, ECO:0000313|Proteomes:UP000077202};
RN [1] {ECO:0000313|EMBL:OAE23560.1, ECO:0000313|Proteomes:UP000077202}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Tak-1 and cv. Tak-2 {ECO:0000313|Proteomes:UP000077202};
RC TISSUE=Whole gametophyte {ECO:0000313|EMBL:OAE23560.1};
RA Honkanen S., Jones V.A., Morieri G., Champion C., Hetherington A.J.,
RA Kelly S., Saint-Marcoux D., Proust H., Prescott H., Dolan L.;
RT "Mechanisms controlling the formation of the plant cell surface in tip-
RT growing cells are functionally conserved among land plants.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
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 -!- PATHWAY: Amino-acid biosynthesis; L-cysteine biosynthesis; L-cysteine
CC from L-serine: step 1/2. {ECO:0000256|ARBA:ARBA00004876}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the transferase hexapeptide repeat family.
CC {ECO:0000256|ARBA:ARBA00007274}.
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:OAE23560.1}.
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DR EMBL; LVLJ01002824; OAE23560.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A176VRW6; -.
DR OrthoDB; 24625at2759; -.
DR UniPathway; UPA00136; UER00199.
DR Proteomes; UP000077202; Unassembled WGS sequence.
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; IPR010493; Ser_AcTrfase_N.
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 PANTHER; PTHR42811; SERINE ACETYLTRANSFERASE; 1.
DR PANTHER; PTHR42811:SF5; SERINE ACETYLTRANSFERASE-RELATED; 1.
DR Pfam; PF00132; Hexapep; 1.
DR Pfam; PF06426; SATase_N; 1.
DR SMART; SM00971; SATase_N; 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 Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Reference proteome {ECO:0000313|Proteomes:UP000077202};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 129..233
FT /note="Serine acetyltransferase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00971"
SQ SEQUENCE 408 AA; 43601 MW; E980B172C3538565 CRC64;
MARLFEPAVS SISAFGKSSS AALSFPTADS LKVSTSFSPS NVNTSVLVWS SSSAWGKKNT
KRSRNADIIV PSSLLMEERG AGSDQHALTI IRENFRGAFE HSLSDTAGRA VEAPIATSRV
PLLDEEDEIW MAMRAEARID SEQEPALASY LYSTILAHRS LERSLAFHLG NKLCSVTFLS
TQLVSVIIDT IMEDNTIRSS IRADIVAVKD RDPACISYSQ CLLNFKGFLA LQAHRVAHRL
WSQGRQSLAL AIQSRVSEVF HVDIHPAAKI GSGILFDHAT GVVVGETATI GNNVSILHHV
TLGGTGSMGG DRHPKIGDGV LIGAGATILG PICVGEGAKI GAGSVVLNDV PPHTTAVGNP
ARLVGGKQRP AELKDIPSET MDHTSFISIW SLRLFFVPNE ESRKTGSL
//