METAA_THEMA
ID METAA_THEMA Reviewed; 304 AA.
AC Q9WZY3;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Homoserine O-acetyltransferase {ECO:0000255|HAMAP-Rule:MF_00295, ECO:0000305};
DE Short=HAT {ECO:0000255|HAMAP-Rule:MF_00295, ECO:0000305};
DE EC=2.3.1.31 {ECO:0000255|HAMAP-Rule:MF_00295, ECO:0000269|PubMed:16708165};
DE AltName: Full=HTS-like HTA {ECO:0000303|PubMed:16708165};
DE AltName: Full=Homoserine transacetylase {ECO:0000255|HAMAP-Rule:MF_00295, ECO:0000303|PubMed:16708165};
DE Short=HTA {ECO:0000255|HAMAP-Rule:MF_00295, ECO:0000303|PubMed:16708165};
GN Name=metAA {ECO:0000255|HAMAP-Rule:MF_00295}; Synonyms=metA;
GN OrderedLocusNames=TM_0881;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
RN [2]
RP FUNCTION AS AN ACETYLTRANSFERASE, CATALYTIC ACTIVITY, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND PATHWAY.
RX PubMed=16708165; DOI=10.1007/s00792-006-0522-3;
RA Goudarzi M., Born T.L.;
RT "Purification and characterization of Thermotoga maritima homoserine
RT transsuccinylase indicates it is a transacetylase.";
RL Extremophiles 10:469-478(2006).
RN [3] {ECO:0007744|PDB:2H2W}
RP X-RAY CRYSTALLOGRAPHY (2.52 ANGSTROMS) OF 1-300.
RG Joint center for structural genomics (JCSG);
RT "Crystal structure of homoserine O-succinyltransferase (EC 2.3.1.46)
RT (homoserine O-transsuccinylase) (HTS) (tm0881) from Thermotoga maritima at
RT 2.52 A resolution.";
RL Submitted (MAY-2006) to the PDB data bank.
CC -!- FUNCTION: Transfers an acetyl group from acetyl-CoA to L-homoserine,
CC forming acetyl-L-homoserine. Utilizes a ping-pong kinetic mechanism in
CC which the acetyl group of acetyl-CoA is initially transferred to the
CC enzyme to form an acetyl-enzyme intermediate before subsequent transfer
CC to homoserine to form the final product, O-acetylhomoserine. Has weak
CC activity with succinyl-CoA as the acyl donor.
CC {ECO:0000269|PubMed:16708165}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + L-homoserine = CoA + O-acetyl-L-homoserine;
CC Xref=Rhea:RHEA:13701, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:57476, ChEBI:CHEBI:57716; EC=2.3.1.31;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00295,
CC ECO:0000269|PubMed:16708165};
CC -!- ACTIVITY REGULATION: Inhibited by iodoacetamide in a pH-dependent
CC manner. {ECO:0000269|PubMed:16708165}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=83 uM for acetyl-CoA {ECO:0000269|PubMed:16708165};
CC KM=130 uM for L-homoserine {ECO:0000269|PubMed:16708165};
CC KM=280 uM for D-homoserine {ECO:0000269|PubMed:16708165};
CC KM=1700 uM for O-acetylhomoserine {ECO:0000269|PubMed:16708165};
CC KM=140 uM for coenzyme A {ECO:0000269|PubMed:16708165};
CC KM=17 uM for malonyl-CoA {ECO:0000269|PubMed:16708165};
CC KM=44 uM for propionyl-CoA {ECO:0000269|PubMed:16708165};
CC KM=51 uM for succinyl-CoA {ECO:0000269|PubMed:16708165};
CC KM=58 uM for beta-hydroxybutyryl-CoA {ECO:0000269|PubMed:16708165};
CC KM=68 uM for isobutyryl-CoA {ECO:0000269|PubMed:16708165};
CC KM=180 uM for glutaryl-CoA {ECO:0000269|PubMed:16708165};
CC Note=kcat is 9.49 sec(-1) with acetyl-CoA as substrate. kcat is 2.6
CC sec(-1) with propionyl-CoA as substrate. kcat is 0.19 sec(-1) with
CC succinyl-CoA as substrate. {ECO:0000269|PubMed:16708165};
CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo
CC pathway; O-acetyl-L-homoserine from L-homoserine: step 1/1.
CC {ECO:0000255|HAMAP-Rule:MF_00295, ECO:0000305|PubMed:16708165}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00295,
CC ECO:0000305}.
CC -!- SIMILARITY: Belongs to the MetA family. {ECO:0000255|HAMAP-
CC Rule:MF_00295}.
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DR EMBL; AE000512; AAD35962.1; -; Genomic_DNA.
DR PIR; C72324; C72324.
DR RefSeq; NP_228689.1; NC_000853.1.
DR RefSeq; WP_004080711.1; NZ_CP011107.1.
DR PDB; 2H2W; X-ray; 2.52 A; A=1-300.
DR PDBsum; 2H2W; -.
DR AlphaFoldDB; Q9WZY3; -.
DR SMR; Q9WZY3; -.
DR STRING; 243274.THEMA_00230; -.
DR PRIDE; Q9WZY3; -.
DR EnsemblBacteria; AAD35962; AAD35962; TM_0881.
DR KEGG; tma:TM0881; -.
DR eggNOG; COG1897; Bacteria.
DR InParanoid; Q9WZY3; -.
DR OMA; WLWFCYQ; -.
DR OrthoDB; 1601420at2; -.
DR UniPathway; UPA00051; UER00074.
DR EvolutionaryTrace; Q9WZY3; -.
DR Proteomes; UP000008183; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004414; F:homoserine O-acetyltransferase activity; IEA:UniProtKB-EC.
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 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Amino-acid biosynthesis; Cytoplasm;
KW Methionine biosynthesis; Reference proteome; Transferase.
FT CHAIN 1..304
FT /note="Homoserine O-acetyltransferase"
FT /id="PRO_0000199763"
FT ACT_SITE 142
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00295"
FT ACT_SITE 234
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00295"
FT ACT_SITE 236
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00295"
FT BINDING 163
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00295"
FT BINDING 191
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00295"
FT BINDING 248
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 191
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00295"
FT HELIX 10..16
FT /evidence="ECO:0007829|PDB:2H2W"
FT TURN 17..19
FT /evidence="ECO:0007829|PDB:2H2W"
FT STRAND 36..41
FT /evidence="ECO:0007829|PDB:2H2W"
FT HELIX 47..59
FT /evidence="ECO:0007829|PDB:2H2W"
FT STRAND 60..63
FT /evidence="ECO:0007829|PDB:2H2W"
FT STRAND 65..70
FT /evidence="ECO:0007829|PDB:2H2W"
FT HELIX 82..88
FT /evidence="ECO:0007829|PDB:2H2W"
FT HELIX 92..94
FT /evidence="ECO:0007829|PDB:2H2W"
FT TURN 95..97
FT /evidence="ECO:0007829|PDB:2H2W"
FT STRAND 100..105
FT /evidence="ECO:0007829|PDB:2H2W"
FT HELIX 115..117
FT /evidence="ECO:0007829|PDB:2H2W"
FT HELIX 121..134
FT /evidence="ECO:0007829|PDB:2H2W"
FT STRAND 135..141
FT /evidence="ECO:0007829|PDB:2H2W"
FT HELIX 143..153
FT /evidence="ECO:0007829|PDB:2H2W"
FT STRAND 158..174
FT /evidence="ECO:0007829|PDB:2H2W"
FT HELIX 177..179
FT /evidence="ECO:0007829|PDB:2H2W"
FT STRAND 184..195
FT /evidence="ECO:0007829|PDB:2H2W"
FT HELIX 198..201
FT /evidence="ECO:0007829|PDB:2H2W"
FT STRAND 207..213
FT /evidence="ECO:0007829|PDB:2H2W"
FT TURN 214..216
FT /evidence="ECO:0007829|PDB:2H2W"
FT STRAND 217..231
FT /evidence="ECO:0007829|PDB:2H2W"
FT HELIX 241..251
FT /evidence="ECO:0007829|PDB:2H2W"
FT HELIX 264..266
FT /evidence="ECO:0007829|PDB:2H2W"
FT HELIX 277..290
FT /evidence="ECO:0007829|PDB:2H2W"
FT TURN 291..295
FT /evidence="ECO:0007829|PDB:2H2W"
SQ SEQUENCE 304 AA; 35759 MW; 3ED8226AA8F8044E CRC64;
MPINVPSGLP AVKVLAKEGI FVMTEKRAIH QDIRPLEILI LNLMPDKIKT EIQLLRLLGN
TPLQVNVTLL YTETHKPKHT PIEHILKFYT TFSAVKDRKF DGFIITGAPV ELLPFEEVDY
WEELTEIMEW SRHNVYSTMF ICWAAQAGLY YFYGIPKYEL PQKLSGVYKH RVAKDSVLFR
GHDDFFWAPH SRYTEVKKED IDKVPELEIL AESDEAGVYV VANKSERQIF VTGHPEYDRY
TLRDEYYRDI GRNLKVPIPA NYFPNDDPTK TPILTWWSHA HLFFSNWLNY CIYQKTPYRL
EDIH
