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Database: UniProt
Entry: A0A1I5JB25_9BRAD
LinkDB: A0A1I5JB25_9BRAD
Original site: A0A1I5JB25_9BRAD 
ID   A0A1I5JB25_9BRAD        Unreviewed;       274 AA.
AC   A0A1I5JB25;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=Serine acetyltransferase {ECO:0000256|ARBA:ARBA00018522, ECO:0000256|PIRNR:PIRNR000441};
DE            EC=2.3.1.30 {ECO:0000256|ARBA:ARBA00013266, ECO:0000256|PIRNR:PIRNR000441};
GN   ORFNames=SAMN05216330_104240 {ECO:0000313|EMBL:SFO70015.1};
OS   Bradyrhizobium sp. Ghvi.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Bradyrhizobium.
OX   NCBI_TaxID=1855319 {ECO:0000313|EMBL:SFO70015.1, ECO:0000313|Proteomes:UP000198509};
RN   [1] {ECO:0000313|EMBL:SFO70015.1, ECO:0000313|Proteomes:UP000198509}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ghvi {ECO:0000313|EMBL:SFO70015.1,
RC   ECO:0000313|Proteomes:UP000198509};
RA   de Groot N.N.;
RL   Submitted (OCT-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         ECO:0000256|PIRNR:PIRNR000441};
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, ECO:0000256|PIRNR:PIRNR000441}.
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DR   EMBL; FOVU01000004; SFO70015.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I5JB25; -.
DR   STRING; 1855319.SAMN05216330_104240; -.
DR   OrthoDB; 9801456at2; -.
DR   UniPathway; UPA00136; UER00199.
DR   Proteomes; UP000198509; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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   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   Pfam; PF06426; SATase_N; 1.
DR   PIRSF; PIRSF000441; CysE; 2.
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   ECO:0000256|PIRNR:PIRNR000441}; Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000441}.
FT   DOMAIN          18..122
FT                   /note="Serine acetyltransferase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00971"
SQ   SEQUENCE   274 AA;  29946 MW;  DF4843E3E5FBFBCF CRC64;
     MAVHQVNPGG KLATLDPIWD RIRGEAEDIV HREPELATFI YSTVLHHSRL EDSVIHRVAD
     RLDHSALSGD LVRQTYDEAL RDDPDLGNAF RADLVAVYDR DPATSRFIDP LLYFKGFHAI
     QTHRLAHWLY LKGRKDFAYY LQSRASAVFQ TDINPAARIG RGIFLDHATG FVCGETAVIE
     DDVSILHGVT LGGTGKENED RHPKIRHGVL IGAGAKILGN IEIGHCARIA AGSVVVKPVP
     HNVTVAGVPA KIVGEAGCAE PSRTMDQMIN AMGL
//
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