ID A0A1F8RRH0_9CHLR Unreviewed; 242 AA.
AC A0A1F8RRH0;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
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=A2148_06450 {ECO:0000313|EMBL:OGO50277.1};
OS Chloroflexi bacterium RBG_16_68_14.
OC Bacteria; Chloroflexota.
OX NCBI_TaxID=1797660 {ECO:0000313|EMBL:OGO50277.1, ECO:0000313|Proteomes:UP000176790};
RN [1] {ECO:0000313|EMBL:OGO50277.1, ECO:0000313|Proteomes:UP000176790}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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}.
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:OGO50277.1}.
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DR EMBL; MGOB01000077; OGO50277.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F8RRH0; -.
DR STRING; 1797660.A2148_06450; -.
DR UniPathway; UPA00136; UER00199.
DR Proteomes; UP000176790; 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; 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 3..38
FT /note="Serine acetyltransferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF06426"
FT REGION 210..242
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 210..231
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 242 AA; 25969 MW; 54B16A88616F7DE2 CRC64;
MSLLKSIARD IQAARERDPA ATSNLEVILA YPGFQARQLH RLAHALHRRR VPVFPRLISH
VNRFVTGIEI HPGAKIGDGL FIDHGMGVVI GETAEIGDNC HLYQGVTLGG TSTKREKRHP
TLGDNVSVGA GAKLIGAITV GENASIGAGS VVVTNVPPNA TVIGVPGHVV AYRDPGSDTV
LHLPDPEWER ITALEERIEK LSERLHALEE RLQAAPTDSK GSRRRADPGE QPSEPGRTAE
ST
//
