ID D8JYZ7_HYPDA Unreviewed; 275 AA.
AC D8JYZ7;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 55.
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 OrderedLocusNames=Hden_1796 {ECO:0000313|EMBL:ADJ23599.1};
OS Hyphomicrobium denitrificans (strain ATCC 51888 / DSM 1869 / NCIMB 11706 /
OS TK 0415).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Hyphomicrobiaceae; Hyphomicrobium.
OX NCBI_TaxID=582899 {ECO:0000313|EMBL:ADJ23599.1, ECO:0000313|Proteomes:UP000002033};
RN [1] {ECO:0000313|Proteomes:UP000002033}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51888 / DSM 1869 / NCIB 11706 / TK 0415
RC {ECO:0000313|Proteomes:UP000002033};
RX PubMed=21705585; DOI=10.1128/JB.05453-11;
RG US DOE Joint Genome Institute;
RA Brown P.J., Kysela D.T., Buechlein A., Hemmerich C., Brun Y.V.;
RT "Genome sequences of eight morphologically diverse alphaproteobacteria.";
RL J. Bacteriol. 193:4567-4568(2011).
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; CP002083; ADJ23599.1; -; Genomic_DNA.
DR RefSeq; WP_013215758.1; NC_014313.1.
DR AlphaFoldDB; D8JYZ7; -.
DR STRING; 582899.Hden_1796; -.
DR KEGG; hdn:Hden_1796; -.
DR eggNOG; COG1045; Bacteria.
DR HOGENOM; CLU_051638_0_1_5; -.
DR OrthoDB; 9801456at2; -.
DR UniPathway; UPA00136; UER00199.
DR Proteomes; UP000002033; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000002033};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000441}.
FT DOMAIN 17..121
FT /note="Serine acetyltransferase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00971"
SQ SEQUENCE 275 AA; 29338 MW; 94118DE34F2B0AB2 CRC64;
MSNAKTATTK IQIVDPIWAQ IRSEAQAAMT AEPALGSFIF ATVLSHEHLE EAICHRLAQR
LNHTDVDAGL ISQTFLGVLQ DDNKLGKIFR ADLSAVYDRD PACTRYLDPL LYFKGFHALV
THRFAHALWK RGRRDFALYL QSQGSRFFGV DIHPAARFGQ GIMLDHATGF VVGETAAAGD
NCSFLHAVTL GGSGKETGDR HPKIGDNVLV GAGAKILGNI KVGSCSRIAA GSVVLSDVPP
NVTVAGVPAK IVGSAGCSEP ARSMEQGWVD DFGGL
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