ID A0A0K1JNL5_9MICO Unreviewed; 208 AA.
AC A0A0K1JNL5;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=VV02_24755 {ECO:0000313|EMBL:AKU18302.1};
OS Luteipulveratus mongoliensis.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermacoccaceae;
OC Luteipulveratus.
OX NCBI_TaxID=571913 {ECO:0000313|EMBL:AKU18302.1, ECO:0000313|Proteomes:UP000066480};
RN [1] {ECO:0000313|EMBL:AKU18302.1, ECO:0000313|Proteomes:UP000066480}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MN07-A0370 {ECO:0000313|EMBL:AKU18302.1,
RC ECO:0000313|Proteomes:UP000066480};
RA Juboi H., Basik A., Shamsul S.S., Arnold P., Schmitt E.K., Sanglier J.-J.,
RA Yeo T.;
RT "Luteipulveratus halotolerans sp. nov., a novel actinobacterium
RT (Dermacoccaceae) from Sarawak, Malaysia.";
RL Submitted (MAR-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 -!- 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; CP011112; AKU18302.1; -; Genomic_DNA.
DR RefSeq; WP_052595976.1; NZ_CP011112.1.
DR AlphaFoldDB; A0A0K1JNL5; -.
DR STRING; 571913.VV02_24755; -.
DR KEGG; lmoi:VV02_24755; -.
DR PATRIC; fig|571913.6.peg.5019; -.
DR OrthoDB; 9801456at2; -.
DR UniPathway; UPA00136; UER00199.
DR Proteomes; UP000066480; Chromosome.
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 Reference proteome {ECO:0000313|Proteomes:UP000066480};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000441}.
FT DOMAIN 15..57
FT /note="Serine acetyltransferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF06426"
SQ SEQUENCE 208 AA; 22102 MW; BDF1E7330B89D976 CRC64;
MGADVLLTGG VPRKKVTQSV RRAVESVRAD IDAAIERDPA VDSRLEMALA SPGLHAIWSH
RLAHRMWTKG GRWRLPARML SQTARAVTGV EIHPGAQIGK RFFIDHGMGV VIGETAEVGD
DVLLYHGVTL GGRSLARVKR HPTVGDGVTI GAGARILGPV RVGDRAQVGA NAVVVKDVPP
QAVATGIPAK VRFPEPTYDP FADPALLI
//