SST_XYLFA
ID SST_XYLFA Reviewed; 370 AA.
AC Q9PAN0;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Serine O-succinyltransferase {ECO:0000255|HAMAP-Rule:MF_00296};
DE Short=SST {ECO:0000255|HAMAP-Rule:MF_00296};
DE EC=2.3.1.- {ECO:0000255|HAMAP-Rule:MF_00296};
GN Name=metX; OrderedLocusNames=XF_2465;
OS Xylella fastidiosa (strain 9a5c).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xylella.
OX NCBI_TaxID=160492;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=9a5c;
RX PubMed=10910347; DOI=10.1038/35018003;
RA Simpson A.J.G., Reinach F.C., Arruda P., Abreu F.A., Acencio M.,
RA Alvarenga R., Alves L.M.C., Araya J.E., Baia G.S., Baptista C.S.,
RA Barros M.H., Bonaccorsi E.D., Bordin S., Bove J.M., Briones M.R.S.,
RA Bueno M.R.P., Camargo A.A., Camargo L.E.A., Carraro D.M., Carrer H.,
RA Colauto N.B., Colombo C., Costa F.F., Costa M.C.R., Costa-Neto C.M.,
RA Coutinho L.L., Cristofani M., Dias-Neto E., Docena C., El-Dorry H.,
RA Facincani A.P., Ferreira A.J.S., Ferreira V.C.A., Ferro J.A., Fraga J.S.,
RA Franca S.C., Franco M.C., Frohme M., Furlan L.R., Garnier M., Goldman G.H.,
RA Goldman M.H.S., Gomes S.L., Gruber A., Ho P.L., Hoheisel J.D.,
RA Junqueira M.L., Kemper E.L., Kitajima J.P., Krieger J.E., Kuramae E.E.,
RA Laigret F., Lambais M.R., Leite L.C.C., Lemos E.G.M., Lemos M.V.F.,
RA Lopes S.A., Lopes C.R., Machado J.A., Machado M.A., Madeira A.M.B.N.,
RA Madeira H.M.F., Marino C.L., Marques M.V., Martins E.A.L., Martins E.M.F.,
RA Matsukuma A.Y., Menck C.F.M., Miracca E.C., Miyaki C.Y.,
RA Monteiro-Vitorello C.B., Moon D.H., Nagai M.A., Nascimento A.L.T.O.,
RA Netto L.E.S., Nhani A. Jr., Nobrega F.G., Nunes L.R., Oliveira M.A.,
RA de Oliveira M.C., de Oliveira R.C., Palmieri D.A., Paris A., Peixoto B.R.,
RA Pereira G.A.G., Pereira H.A. Jr., Pesquero J.B., Quaggio R.B.,
RA Roberto P.G., Rodrigues V., de Rosa A.J.M., de Rosa V.E. Jr., de Sa R.G.,
RA Santelli R.V., Sawasaki H.E., da Silva A.C.R., da Silva A.M.,
RA da Silva F.R., Silva W.A. Jr., da Silveira J.F., Silvestri M.L.Z.,
RA Siqueira W.J., de Souza A.A., de Souza A.P., Terenzi M.F., Truffi D.,
RA Tsai S.M., Tsuhako M.H., Vallada H., Van Sluys M.A., Verjovski-Almeida S.,
RA Vettore A.L., Zago M.A., Zatz M., Meidanis J., Setubal J.C.;
RT "The genome sequence of the plant pathogen Xylella fastidiosa.";
RL Nature 406:151-159(2000).
CC -!- FUNCTION: Transfers a succinyl group from succinyl-CoA to L-serine,
CC forming succinyl-L-serine. {ECO:0000255|HAMAP-Rule:MF_00296}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-serine + succinyl-CoA = CoA + O-succinyl-L-serine;
CC Xref=Rhea:RHEA:52820, ChEBI:CHEBI:33384, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57292, ChEBI:CHEBI:136856; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00296};
CC -!- PATHWAY: Amino-acid biosynthesis; L-cysteine biosynthesis; L-cysteine
CC from L-serine: step 1/2. {ECO:0000255|HAMAP-Rule:MF_00296}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00296}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00296}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. MetX family.
CC {ECO:0000255|HAMAP-Rule:MF_00296}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE003849; AAF85264.1; -; Genomic_DNA.
DR PIR; C82553; C82553.
DR RefSeq; WP_010894909.1; NC_002488.3.
DR AlphaFoldDB; Q9PAN0; -.
DR SMR; Q9PAN0; -.
DR STRING; 160492.XF_2465; -.
DR ESTHER; xylfa-metx; Homoserine_transacetylase.
DR EnsemblBacteria; AAF85264; AAF85264; XF_2465.
DR KEGG; xfa:XF_2465; -.
DR PATRIC; fig|160492.11.peg.2616; -.
DR eggNOG; COG2021; Bacteria.
DR HOGENOM; CLU_028760_1_2_6; -.
DR OMA; TRFCVVS; -.
DR UniPathway; UPA00136; UER00199.
DR Proteomes; UP000000812; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016750; F:O-succinyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006535; P:cysteine biosynthetic process from serine; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.1820; -; 1.
DR HAMAP; MF_00296; MetX_acyltransf; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR InterPro; IPR008220; HAT_MetX-like.
DR PANTHER; PTHR32268; PTHR32268; 1.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR PIRSF; PIRSF000443; Homoser_Ac_trans; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR TIGRFAMs; TIGR01392; homoserO_Ac_trn; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Amino-acid biosynthesis; Cysteine biosynthesis; Cytoplasm;
KW Reference proteome; Transferase.
FT CHAIN 1..370
FT /note="Serine O-succinyltransferase"
FT /id="PRO_0000155748"
FT DOMAIN 45..354
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT REGION 52..55
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT ACT_SITE 149
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT ACT_SITE 316
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT ACT_SITE 349
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT BINDING 218
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT BINDING 350
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT SITE 186
FT /note="Important for acyl-CoA specificity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
SQ SEQUENCE 370 AA; 40766 MW; 15FA1F4BB98BB395 CRC64;
MTEFIPPGSL FHALSSPFPM KRGGQLHRAR IAYETWGHLN ASATNAILIM PGLSPNAHAA
HHDSNAEPGW WESMLGPGKP IDTDRWFVIC VNSLGSCKGS TGPASYNPIT QAMYRLDFPA
LSIEDGANAA IEVVHALGIK QLASLIGNSM GGMTALAILL LHPDIARSHI NISGSAQALP
FSIAIRSLQR EAIRLDPHWN QGHYDDTHYP ESGLRIARKL GVITYRSALE WDGRFGRVRL
DSDQTNDTPF GLEFQIENYL ESHAHRFVHT FDPNCYLYLS RSMDWFDVAE YANGDILAGL
ARIRIQRALA IGSHTDILFP IQQQQQIAEG LRRGGTHATF LGLDSPQGHD AFLVDIAGFG
PPVKEFLDEL
