ID   CYSE_MYCTU              Reviewed;         229 AA.
AC   P95231; L0TAX3;
DT   30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 132.
DE   RecName: Full=Serine acetyltransferase;
DE            Short=SAT;
DE            EC=2.3.1.30;
GN   Name=cysE; OrderedLocusNames=Rv2335;
OS   Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83332;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=9634230; DOI=10.1038/31159;
RA   Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA   Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA   Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA   Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA   Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA   Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA   Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA   Barrell B.G.;
RT   "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT   genome sequence.";
RL   Nature 393:537-544(1998).
RN   [2]
RP   DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=14569030; DOI=10.1073/pnas.2134250100;
RA   Sassetti C.M., Rubin E.J.;
RT   "Genetic requirements for mycobacterial survival during infection.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:12989-12994(2003).
RN   [3]
RP   IDENTIFICATION AS A DRUG TARGET [LARGE SCALE ANALYSIS].
RX   PubMed=19099550; DOI=10.1186/1752-0509-2-109;
RA   Raman K., Yeturu K., Chandra N.;
RT   "targetTB: a target identification pipeline for Mycobacterium tuberculosis
RT   through an interactome, reactome and genome-scale structural analysis.";
RL   BMC Syst. Biol. 2:109-109(2008).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA   Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA   Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA   Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA   Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT   "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT   mass spectrometry.";
RL   Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
CC   -!- FUNCTION: Catalyzes the acetylation of serine by acetyl-CoA to produce
CC       O-acetylserine (OAS). {ECO:0000250}.
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   -!- PATHWAY: Amino-acid biosynthesis; L-cysteine biosynthesis; L-cysteine
CC       from L-serine: step 1/2.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- DISRUPTION PHENOTYPE: Strains lacking this gene are shown to be
CC       attenuated in a mouse tuberculosis model.
CC       {ECO:0000269|PubMed:14569030}.
CC   -!- MISCELLANEOUS: Was identified as a high-confidence drug target.
CC   -!- SIMILARITY: Belongs to the transferase hexapeptide repeat family.
CC       {ECO:0000305}.
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DR   EMBL; AL123456; CCP45123.1; -; Genomic_DNA.
DR   PIR; H70660; H70660.
DR   RefSeq; NP_216851.1; NC_000962.3.
DR   RefSeq; WP_003411985.1; NZ_NVQJ01000012.1.
DR   AlphaFoldDB; P95231; -.
DR   SMR; P95231; -.
DR   STRING; 83332.Rv2335; -.
DR   PaxDb; P95231; -.
DR   PRIDE; P95231; -.
DR   DNASU; 886012; -.
DR   GeneID; 45426319; -.
DR   GeneID; 886012; -.
DR   KEGG; mtu:Rv2335; -.
DR   TubercuList; Rv2335; -.
DR   eggNOG; COG1045; Bacteria.
DR   InParanoid; P95231; -.
DR   OMA; GDDVMLY; -.
DR   PhylomeDB; P95231; -.
DR   BRENDA; 2.3.1.30; 3445.
DR   Reactome; R-MTU-936721; Cysteine synthesis from O-acetylserine.
DR   UniPathway; UPA00136; UER00199.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0009001; F:serine O-acetyltransferase activity; IBA:GO_Central.
DR   GO; GO:0006535; P:cysteine biosynthetic process from serine; TAS:Reactome.
DR   CDD; cd03354; LbH_SAT; 1.
DR   Gene3D; 1.10.3130.10; -; 1.
DR   InterPro; IPR001451; Hexapep.
DR   InterPro; IPR018357; Hexapep_transf_CS.
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   Pfam; PF00132; Hexapep; 2.
DR   SUPFAM; SSF51161; SSF51161; 1.
DR   TIGRFAMs; TIGR01172; cysE; 1.
DR   PROSITE; PS00101; HEXAPEP_TRANSFERASES; 1.
PE   1: Evidence at protein level;
KW   Acyltransferase; Amino-acid biosynthesis; Cysteine biosynthesis; Cytoplasm;
KW   Reference proteome; Repeat; Transferase.
FT   CHAIN           1..229
FT                   /note="Serine acetyltransferase"
FT                   /id="PRO_0000401135"
SQ   SEQUENCE   229 AA;  23770 MW;  3C3E8F311DAB2D0F CRC64;
     MLTAMRGDIR AARERDPAAP TALEVIFCYP GVHAVWGHRL AHWLWQRGAR LLARAAAEFT
     RILTGVDIHP GAVIGARVFI DHATGVVIGE TAEVGDDVTI YHGVTLGGSG MVGGKRHPTV
     GDRVIIGAGA KVLGPIKIGE DSRIGANAVV VKPVPPSAVV VGVPGQVIGQ SQPSPGGPFD
     WRLPDLVGAS LDSLLTRVAR LEALGGGPQA AGVIRPPEAG IWHGEDFSI