ID A0A0F0LWL7_9MICO Unreviewed; 192 AA.
AC A0A0F0LWL7;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Serine acetyltransferase {ECO:0000256|PIRNR:PIRNR000441};
DE EC=2.3.1.30 {ECO:0000256|PIRNR:PIRNR000441};
GN Name=cysE {ECO:0000313|EMBL:KJL38598.1};
GN ORFNames=RR49_00685 {ECO:0000313|EMBL:KJL38598.1};
OS Microbacterium ginsengisoli.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=400772 {ECO:0000313|EMBL:KJL38598.1, ECO:0000313|Proteomes:UP000033451};
RN [1] {ECO:0000313|EMBL:KJL38598.1, ECO:0000313|Proteomes:UP000033451}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18659 {ECO:0000313|EMBL:KJL38598.1,
RC ECO:0000313|Proteomes:UP000033451};
RA Corretto E.;
RT "Draft genome sequences of ten Microbacterium spp. with emphasis on heavy
RT metal contaminated environments.";
RL Submitted (FEB-2015) 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 -!- 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:KJL38598.1}.
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DR EMBL; JYIY01000061; KJL38598.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F0LWL7; -.
DR STRING; 400772.RR49_00685; -.
DR PATRIC; fig|400772.4.peg.718; -.
DR Proteomes; UP000033451; 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; 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 PIRSF; PIRSF000441; CysE; 1.
DR SUPFAM; SSF51161; Trimeric LpxA-like enzymes; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW ECO:0000256|PIRNR:PIRNR000441};
KW Reference proteome {ECO:0000313|Proteomes:UP000033451};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000441}.
FT REGION 172..192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..186
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 192 AA; 20578 MW; 03F72050DEFCB5B5 CRC64;
MTGGGMLRRL REDLAAARLR DPAARSSLEI ALLYPGLHAV WSHRVWHALW VRRVRFLARA
GSQLTRWLTG IEIHPGATIG RRLFIDHGMG VVIGETAEVG DDVLLYHGVT LGGRTRDAGK
RHPTIGDGVA IGAGAKVLGP VRIGAGSVIG ANAVVTRDAP DDSVIVGIPA KARPRRDGDD
TRSILTTPEY HI
//
