METAS_SALTY
ID METAS_SALTY Reviewed; 309 AA.
AC P37413;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Homoserine O-succinyltransferase {ECO:0000255|HAMAP-Rule:MF_00295};
DE Short=HST {ECO:0000255|HAMAP-Rule:MF_00295};
DE EC=2.3.1.46 {ECO:0000255|HAMAP-Rule:MF_00295};
DE AltName: Full=Homoserine transsuccinylase {ECO:0000255|HAMAP-Rule:MF_00295};
DE Short=HTS {ECO:0000255|HAMAP-Rule:MF_00295};
GN Name=metAS {ECO:0000255|HAMAP-Rule:MF_00295}; Synonyms=metA;
GN OrderedLocusNames=STM4182;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-69.
RX PubMed=1729233; DOI=10.1128/jb.174.2.390-397.1992;
RA Mares R., Urbanowski M.L., Stauffer G.V.;
RT "Regulation of the Salmonella typhimurium metA gene by the metR protein and
RT homocysteine.";
RL J. Bacteriol. 174:390-397(1992).
CC -!- FUNCTION: Transfers a succinyl group from succinyl-CoA to L-homoserine,
CC forming succinyl-L-homoserine. {ECO:0000255|HAMAP-Rule:MF_00295}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-homoserine + succinyl-CoA = CoA + O-succinyl-L-homoserine;
CC Xref=Rhea:RHEA:22008, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292,
CC ChEBI:CHEBI:57476, ChEBI:CHEBI:57661; EC=2.3.1.46;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00295};
CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo
CC pathway; O-succinyl-L-homoserine from L-homoserine: step 1/1.
CC {ECO:0000255|HAMAP-Rule:MF_00295}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00295}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00295}.
CC -!- SIMILARITY: Belongs to the MetA family. {ECO:0000255|HAMAP-
CC Rule:MF_00295}.
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DR EMBL; AE006468; AAL23006.1; -; Genomic_DNA.
DR EMBL; M74188; AAA27161.1; -; Genomic_DNA.
DR RefSeq; NP_463047.1; NC_003197.2.
DR RefSeq; WP_001122767.1; NC_003197.2.
DR AlphaFoldDB; P37413; -.
DR SMR; P37413; -.
DR STRING; 99287.STM4182; -.
DR PaxDb; P37413; -.
DR EnsemblBacteria; AAL23006; AAL23006; STM4182.
DR GeneID; 1255708; -.
DR KEGG; stm:STM4182; -.
DR PATRIC; fig|99287.12.peg.4394; -.
DR HOGENOM; CLU_057851_0_1_6; -.
DR OMA; WLWFCYQ; -.
DR PhylomeDB; P37413; -.
DR BioCyc; SENT99287:STM4182-MON; -.
DR UniPathway; UPA00051; UER00075.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004414; F:homoserine O-acetyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008899; F:homoserine O-succinyltransferase activity; IBA:GO_Central.
DR GO; GO:0019281; P:L-methionine biosynthetic process from homoserine via O-succinyl-L-homoserine and cystathionine; IEA:InterPro.
DR CDD; cd03131; GATase1_HTS; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR HAMAP; MF_00295; MetA_acyltransf; 1.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR005697; HST_MetA.
DR InterPro; IPR033752; MetA_family.
DR PANTHER; PTHR20919; PTHR20919; 1.
DR Pfam; PF04204; HTS; 1.
DR PIRSF; PIRSF000450; H_ser_succinyltr; 1.
DR SUPFAM; SSF52317; SSF52317; 1.
DR TIGRFAMs; TIGR01001; metA; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Amino-acid biosynthesis; Cytoplasm;
KW Methionine biosynthesis; Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..309
FT /note="Homoserine O-succinyltransferase"
FT /id="PRO_0000199758"
FT ACT_SITE 142
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00295"
FT ACT_SITE 235
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00295"
FT ACT_SITE 237
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00295"
FT BINDING 163
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00295"
FT BINDING 192
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00295"
FT BINDING 249
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00295"
FT SITE 111
FT /note="Important for acyl-CoA specificity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00295"
FT SITE 192
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00295"
FT CONFLICT 22
FT /note="V -> D (in Ref. 2; AAA27161)"
FT /evidence="ECO:0000305"
FT CONFLICT 52
FT /note="N -> I (in Ref. 2; AAA27161)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 309 AA; 35670 MW; 45C7705C81A35B20 CRC64;
MPIRVLDELP AVNFLREENV FVMTTSRASG QEIRPLKVLI LNLMPKKIET ENQFLRLLSN
SPLQVDIQLL RIDARESRNT PAEHLNNFYC NFDDICDQNF DGLIVTGAPL GLVEFNDVAY
WPQIRQVLEW AKDHVTSTLF VCWAVQAALN ILYGIPKQTR TDKLSGVYEH HILHPHALLT
RGFDDSFLAP HSRYADFPAA LIRDYTDLEI LAETEEGDAY LFASKDKRIA FVTGHPEYDA
HTLAGEYFRD VEAGLNPEVP YNYFPKNDPQ NIPRATWRSH GNLLFTNWLN YYVYQITPYD
LRHMNPTLD
