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Database: UniProt
Entry: A0A176VRW6_MARPO
LinkDB: A0A176VRW6_MARPO
Original site: A0A176VRW6_MARPO 
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
//
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