METAS_METTV
ID METAS_METTV Reviewed; 354 AA.
AC G3ISL7;
DT 07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 1.
DT 03-AUG-2022, entry version 43.
DE RecName: Full=Homoserine O-succinyltransferase {ECO:0000255|HAMAP-Rule:MF_00295};
DE Short=HST {ECO:0000255|HAMAP-Rule:MF_00295, ECO:0000303|PubMed:28581482};
DE EC=2.3.1.46 {ECO:0000255|HAMAP-Rule:MF_00295, ECO:0000269|PubMed:28581482};
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, ECO:0000303|PubMed:28581482};
GN ORFNames=Mettu_1201 {ECO:0000312|EMBL:EGW22387.1};
OS Methylobacter tundripaludum (strain ATCC BAA-1195 / DSM 17260 / SV96).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Methylococcales;
OC Methylococcaceae; Methylobacter.
OX NCBI_TaxID=697282;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1195 / DSM 17260 / SV96;
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., Held B.,
RA Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N., Ivanova N.,
RA Ovchinnikova G., Pagani I., Klotz M.G., Dispirito A.A., Murrell J.C.,
RA Dunfield P., Kalyuzhnaya M.G., Svenning M., Trotsenko Y.A., Stein L.Y.,
RA Woyke T.;
RT "Genomic sequence of Methylobacter tundripaludum SV96.";
RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=28581482; DOI=10.1038/nchembio.2397;
RA Bastard K., Perret A., Mariage A., Bessonnet T., Pinet-Turpault A.,
RA Petit J.L., Darii E., Bazire P., Vergne-Vaxelaire C., Brewee C., Debard A.,
RA Pellouin V., Besnard-Gonnet M., Artiguenave F., Medigue C., Vallenet D.,
RA Danchin A., Zaparucha A., Weissenbach J., Salanoubat M., de Berardinis V.;
RT "Parallel evolution of non-homologous isofunctional enzymes in methionine
RT biosynthesis.";
RL Nat. Chem. Biol. 13:858-866(2017).
CC -!- FUNCTION: Transfers a succinyl group from succinyl-CoA to L-homoserine,
CC forming succinyl-L-homoserine. {ECO:0000255|HAMAP-Rule:MF_00295,
CC ECO:0000269|PubMed:28581482}.
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 ECO:0000269|PubMed:28581482};
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 -!- 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; JH109152; EGW22387.1; -; Genomic_DNA.
DR RefSeq; WP_006890358.1; NZ_JH109152.1.
DR AlphaFoldDB; G3ISL7; -.
DR SMR; G3ISL7; -.
DR STRING; 697282.Mettu_1201; -.
DR EnsemblBacteria; EGW22387; EGW22387; Mettu_1201.
DR eggNOG; COG1897; Bacteria.
DR HOGENOM; CLU_057851_0_1_6; -.
DR OMA; WLWFCYQ; -.
DR OrthoDB; 1601420at2; -.
DR UniPathway; UPA00051; UER00075.
DR Proteomes; UP000004664; Unassembled WGS sequence.
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; IEA:UniProtKB-EC.
DR GO; GO:0009086; P:methionine biosynthetic process; IEA:UniProtKB-UniRule.
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; 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.
PE 1: Evidence at protein level;
KW Acyltransferase; Amino-acid biosynthesis; Cytoplasm;
KW Methionine biosynthesis; Reference proteome; Transferase.
FT CHAIN 1..354
FT /note="Homoserine O-succinyltransferase"
FT /id="PRO_0000440353"
FT ACT_SITE 146
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00295"
FT ACT_SITE 239
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00295"
FT ACT_SITE 241
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00295"
FT BINDING 167
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00295"
FT BINDING 196
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00295"
FT BINDING 253
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00295"
FT SITE 113
FT /note="Important for acyl-CoA specificity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00295"
FT SITE 147
FT /note="Important for acyl-CoA specificity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00295"
FT SITE 196
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00295"
SQ SEQUENCE 354 AA; 41079 MW; 8FB6FC50F39F6D75 CRC64;
MPLVAHTDLP TFQRLREEGE EILDPDRASN QDIREMHIGL LNMMPDAALE ATERQFFRLV
GACNQIVQFH VHPFTIEGLK RSPEAQAHIA KYYESFEQIK RDGLDALIIS GANVSHPRLP
EEDFWQPLSE VFFWAKENVT SILCSCLATH ALIQYCYGIE RTRLPAKRWG VFSHKLTDRT
HPLVAEINTR FDVPHSRFNE IFQSDMERHG LKVLAVSKEA GVHLAVSPDG FRIVFFQGHP
EYDDISLLKE YKREILRFYR AERDDYPPFP ENYFNDVVQQ ILVDYEQRVR SAKQSGQRLE
EFPESLILEH IDNTWSDTAK AVFNNWLGKI YQLTHQERGL PFMDGVDPNN PLGL
