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Database: UniProt
Entry: D1CFQ3_THET1
LinkDB: D1CFQ3_THET1
Original site: D1CFQ3_THET1 
ID   D1CFQ3_THET1            Unreviewed;       383 AA.
AC   D1CFQ3;
DT   19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2010, sequence version 1.
DT   27-MAR-2024, entry version 80.
DE   RecName: Full=Homoserine O-acetyltransferase {ECO:0000256|HAMAP-Rule:MF_00296};
DE            Short=HAT {ECO:0000256|HAMAP-Rule:MF_00296};
DE            EC=2.3.1.31 {ECO:0000256|HAMAP-Rule:MF_00296};
DE   AltName: Full=Homoserine transacetylase {ECO:0000256|HAMAP-Rule:MF_00296};
DE            Short=HTA {ECO:0000256|HAMAP-Rule:MF_00296};
GN   Name=metXA {ECO:0000256|HAMAP-Rule:MF_00296};
GN   OrderedLocusNames=Tter_0842 {ECO:0000313|EMBL:ACZ41759.1};
OS   Thermobaculum terrenum (strain ATCC BAA-798 / YNP1).
OC   Bacteria; Chloroflexota; Thermobaculum.
OX   NCBI_TaxID=525904 {ECO:0000313|EMBL:ACZ41759.1, ECO:0000313|Proteomes:UP000000323};
RN   [1] {ECO:0000313|EMBL:ACZ41759.1, ECO:0000313|Proteomes:UP000000323}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-798 / YNP1 {ECO:0000313|Proteomes:UP000000323};
RX   PubMed=21304745;
RA   Kiss H., Cleland D., Lapidus A., Lucas S., Del Rio T.G., Nolan M., Tice H.,
RA   Han C., Goodwin L., Pitluck S., Liolios K., Ivanova N., Mavromatis K.,
RA   Ovchinnikova G., Pati A., Chen A., Palaniappan K., Land M., Hauser L.,
RA   Chang Y.J., Jeffries C.D., Lu M., Brettin T., Detter J.C., Goker M.,
RA   Tindall B.J., Beck B., McDermott T.R., Woyke T., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Cheng J.F.;
RT   "Complete genome sequence of 'Thermobaculum terrenum' type strain (YNP1).";
RL   Stand. Genomic Sci. 3:153-162(2010).
RN   [2] {ECO:0000313|Proteomes:UP000000323}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-798 / YNP1 {ECO:0000313|Proteomes:UP000000323};
RX   DOI=10.4056/sigs.1153107;
RA   Kiss H., Cleland D., Lapidus A., Lucas S., Glavina Del Rio T., Nolan M.,
RA   Tice H., Han C., Goodwin L., Pitluck S., Liolios K., Ivanova N.,
RA   Mavromatis K., Ovchinnikova G., Pati A., Chen A., Palaniappan K., Land M.,
RA   Hauser L., Chang Y., Jeffries C., Lu M., Brettin T., Detter J., Goker M.,
RA   Tindall B., Beck B., McDermott T., Woyke T., Bristow J., Eisen J.,
RA   Markowitz V., Hugenholtz P., Kyrpides N., Klenk H., Cheng J.;
RT   "Complete genome sequence of Thermobaculum terrenum type strain (YNP1T).";
RL   Stand. Genomic Sci. 3:153-162(2010).
CC   -!- FUNCTION: Transfers an acetyl group from acetyl-CoA to L-homoserine,
CC       forming acetyl-L-homoserine. {ECO:0000256|HAMAP-Rule:MF_00296}.
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:0000256|HAMAP-Rule:MF_00296};
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:0000256|HAMAP-Rule:MF_00296}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00296}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00296}.
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. MetX family.
CC       {ECO:0000256|HAMAP-Rule:MF_00296}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00296}.
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DR   EMBL; CP001825; ACZ41759.1; -; Genomic_DNA.
DR   RefSeq; WP_012874794.1; NC_013525.1.
DR   AlphaFoldDB; D1CFQ3; -.
DR   STRING; 525904.Tter_0842; -.
DR   KEGG; ttr:Tter_0842; -.
DR   eggNOG; COG2021; Bacteria.
DR   HOGENOM; CLU_028760_1_2_0; -.
DR   UniPathway; UPA00051; UER00074.
DR   Proteomes; UP000000323; Chromosome 1.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004414; F:homoserine O-acetyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009086; P:methionine biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.1740.110; -; 1.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 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   NCBIfam; TIGR01392; homoserO_Ac_trn; 1.
DR   PANTHER; PTHR32268; HOMOSERINE O-ACETYLTRANSFERASE; 1.
DR   PANTHER; PTHR32268:SF11; HOMOSERINE O-ACETYLTRANSFERASE; 1.
DR   Pfam; PF00561; Abhydrolase_1; 1.
DR   PIRSF; PIRSF000443; Homoser_Ac_trans; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|HAMAP-Rule:MF_00296,
KW   ECO:0000313|EMBL:ACZ41759.1};
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00296};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00296};
KW   Methionine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00296};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000323};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00296}.
FT   DOMAIN          41..348
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000259|Pfam:PF00561"
FT   ACT_SITE        147
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00296,
FT                   ECO:0000256|PIRSR:PIRSR000443-1"
FT   ACT_SITE        311
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00296,
FT                   ECO:0000256|PIRSR:PIRSR000443-1"
FT   ACT_SITE        344
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00296,
FT                   ECO:0000256|PIRSR:PIRSR000443-1"
FT   BINDING         216
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00296"
FT   BINDING         345
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00296"
SQ   SEQUENCE   383 AA;  42845 MW;  323D5705DC5C6981 CRC64;
     MISRKQFYTL AEPLKLWRGG SLYPVTIAYE TWGELSPERD NVILVLHALT GDSHAAGKYS
     EDEDKCGWWD PLIGPGRAFD TNRYFVICSN VIGGCQGSTG PSSINPETGY PYAMDFPVIT
     IQDMVAAQVE LLKALGINKL LAVTGGSIGG MQAIEWVIRY PDWVENALIF GALPKTSPQS
     IGFNAVGRQA IMIDPEWKGG KYYPSPGPVA GLSVARMVGM ITYQSYEGMW IRFGRKLATR
     PTTYSPLGEK FDVEGYLEYQ GYKLTQRFDA NSYLYLTRAM DLYDASEGFD SELEAYDRIR
     ANILLVGIST DWLYPPHEVK AFANQLRDLG KNAVYEELDS IHGHDAFLKE WEQMTRIITL
     YMENLGDEAH YVTSPLGDGE LIK
//
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