ID   B4RF65_PHEZH            Unreviewed;       282 AA.
AC   B4RF65;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   02-SEP-2026, entry version 76.
DE   RecName: Full=Serine acetyltransferase {ECO:0000256|ARBA:ARBA00018522};
DE            EC=2.3.1.30 {ECO:0000256|ARBA:ARBA00013266};
GN   Name=cysE {ECO:0000313|EMBL:ACG78635.1};
GN   OrderedLocusNames=PHZ_c2225 {ECO:0000313|EMBL:ACG78635.1};
OS   Phenylobacterium zucineum (strain HLK1).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC   Caulobacterales; Caulobacteraceae; Phenylobacterium.
OX   NCBI_TaxID=450851 {ECO:0000313|EMBL:ACG78635.1, ECO:0000313|Proteomes:UP000001868};
RN   [1] {ECO:0000313|EMBL:ACG78635.1, ECO:0000313|Proteomes:UP000001868}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HLK1 {ECO:0000313|EMBL:ACG78635.1,
RC   ECO:0000313|Proteomes:UP000001868};
RX   PubMed=18700039; DOI=10.1186/1471-2164-9-386;
RA   Luo Y., Xu X., Ding Z., Liu Z., Zhang B., Yan Z., Sun J., Hu S., Hu X.;
RT   "Complete genome of Phenylobacterium zucineum - a novel facultative
RT   intracellular bacterium isolated from human erythroleukemia cell line
RT   K562.";
RL   BMC Genomics 9:386-386(2008).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-serine + acetyl-CoA = O-acetyl-L-serine + CoA;
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:ARBA00049486};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-cysteine biosynthesis; L-cysteine
CC       from L-serine: step 1/2. {ECO:0000256|ARBA:ARBA00004876}.
CC   -!- SIMILARITY: Belongs to the transferase hexapeptide repeat family.
CC       {ECO:0000256|ARBA:ARBA00007274}.
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DR   EMBL; CP000747; ACG78635.1; -; Genomic_DNA.
DR   AlphaFoldDB; B4RF65; -.
DR   STRING; 450851.PHZ_c2225; -.
DR   KEGG; pzu:PHZ_c2225; -.
DR   eggNOG; COG1045; Bacteria.
DR   HOGENOM; CLU_051638_0_1_5; -.
DR   UniPathway; UPA00136; UER00199.
DR   Proteomes; UP000001868; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0009001; F:L-serine O-acetyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019344; P:L-cysteine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd03354; LbH_SAT; 1.
DR   FunFam; 2.160.10.10:FF:000002; Serine acetyltransferase; 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; IPR053376; Serine_acetyltransferase.
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   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   Reference proteome {ECO:0000313|Proteomes:UP000001868};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ACG78635.1}.
FT   DOMAIN          22..126
FT                   /note="Serine acetyltransferase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00971"
SQ   SEQUENCE   282 AA;  30236 MW;  AA9961CB2EF8EADB CRC64;
     MGREEPMSQR LEVVDPATPP PVWAALRNEA YAAAKSEAAL ASLLAAVILN HETLGDALSY
     QLARKLGDQE LRAMTLRDIL EEAYESDPSL VEIAEADLKA VFERDPACRG YVQPFLFFKG
     FQALQTHRVA HWLWKAGRET LAFYLQSRSS ELFQVDINPA TRIGRGVFID HGTGIVIGET
     AVIGDDVSML QGVTLGGTGA ERGDRHPKVG NGVLLGAGAK VLGNITIGDH AKVASGSVVL
     KPVPPHCTAA GVPARLVNCP TCDEPAKSMD HTLADAVYDY VI
//