METAS_THINJ
ID METAS_THINJ Reviewed; 360 AA.
AC I3BN39;
DT 07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2012, sequence version 1.
DT 03-AUG-2022, entry version 39.
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=Thini_0115 {ECO:0000312|EMBL:EIJ32782.1};
OS Thiothrix nivea (strain ATCC 35100 / DSM 5205 / JP2).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC Thiotrichaceae; Thiothrix.
OX NCBI_TaxID=870187;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35100 / DSM 5205 / JP2;
RX PubMed=22675589; DOI=10.4056/sigs.2344929;
RA Lapidus A., Nolan M., Lucas S., Glavina Del Rio T., Tice H., Cheng J.F.,
RA Tapia R., Han C., Goodwin L., Pitluck S., Liolios K., Pagani I.,
RA Ivanova N., Huntemann M., Mavromatis K., Mikhailova N., Pati A., Chen A.,
RA Palaniappan K., Land M., Brambilla E.M., Rohde M., Abt B., Verbarg S.,
RA Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P., Woyke T.;
RT "Genome sequence of the filamentous, gliding Thiothrix nivea neotype strain
RT (JP2(T)).";
RL Stand. Genomic Sci. 5:398-406(2011).
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. In vitro, can also use glutaryl-CoA as
CC acyl donor. {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; JH651384; EIJ32782.1; -; Genomic_DNA.
DR RefSeq; WP_002706699.1; NZ_JH651384.1.
DR AlphaFoldDB; I3BN39; -.
DR SMR; I3BN39; -.
DR EnsemblBacteria; EIJ32782; EIJ32782; Thini_0115.
DR eggNOG; COG1897; Bacteria.
DR HOGENOM; CLU_057851_0_1_6; -.
DR OrthoDB; 1601420at2; -.
DR UniPathway; UPA00051; UER00075.
DR Proteomes; UP000005317; 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 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..360
FT /note="Homoserine O-succinyltransferase"
FT /id="PRO_0000440361"
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 115
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 360 AA; 41437 MW; FB2C42E6D99F099E CRC64;
MPLVAHTRLP TFERLKQEGQ TVLSEDYAFQ QDIRELHIGF LNMMPDAALA ATERQFLRLV
NESNLIAQFH IHPFTLGTLP RGDKAQAHIA QYYDKFEDLQ EQGLDALIIT GANPAAPHLE
DEPFWDGLCE VVAWAQENVT STLCSCLASH ALVQHLWGIR RRPLGFKRWG VYSHAVTMPE
HPLVNDLNTR FDVPHSRFNQ IDREPLEAVG VQVLVESTEA GVHMAVSPDL FRMVFMQGHP
EYDTVSLLKE YRREVTRWFD GTRADYPPFP QNYLRPKAKA ILNEYRLEQE KAKRLGKPLP
DFPEKLLLPM LHNTWCDTAK VFYSNWIGKV YQLTNNDRRK PFMEGVNPDD PLGLRQQLGI
