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Database: UniProt
Entry: I0I3B9_CALAS
LinkDB: I0I3B9_CALAS
Original site: I0I3B9_CALAS 
ID   I0I3B9_CALAS            Unreviewed;       410 AA.
AC   I0I3B9;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   27-MAR-2024, entry version 60.
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=metX {ECO:0000313|EMBL:BAL99756.1};
GN   Synonyms=metXA {ECO:0000256|HAMAP-Rule:MF_00296};
GN   OrderedLocusNames=CLDAP_17170 {ECO:0000313|EMBL:BAL99756.1};
OS   Caldilinea aerophila (strain DSM 14535 / JCM 11387 / NBRC 104270 /
OS   STL-6-O1).
OC   Bacteria; Chloroflexota; Caldilineae; Caldilineales; Caldilineaceae;
OC   Caldilinea.
OX   NCBI_TaxID=926550 {ECO:0000313|EMBL:BAL99756.1, ECO:0000313|Proteomes:UP000007880};
RN   [1] {ECO:0000313|EMBL:BAL99756.1, ECO:0000313|Proteomes:UP000007880}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14535 / JCM 11387 / NBRC 104270 / STL-6-O1
RC   {ECO:0000313|Proteomes:UP000007880};
RA   Oguchi A., Hosoyama A., Sekine M., Fukai R., Kato Y., Nakamura S.,
RA   Hanada S., Yamazaki S., Fujita N.;
RT   "Complete genome sequence of Caldilinea aerophila DSM 14535 (= NBRC
RT   102666).";
RL   Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
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; AP012337; BAL99756.1; -; Genomic_DNA.
DR   RefSeq; WP_014432994.1; NC_017079.1.
DR   AlphaFoldDB; I0I3B9; -.
DR   STRING; 926550.CLDAP_17170; -.
DR   KEGG; cap:CLDAP_17170; -.
DR   PATRIC; fig|926550.5.peg.1916; -.
DR   eggNOG; COG2021; Bacteria.
DR   HOGENOM; CLU_028760_1_2_0; -.
DR   OrthoDB; 9800754at2; -.
DR   UniPathway; UPA00051; UER00074.
DR   Proteomes; UP000007880; Chromosome.
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   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:UP000007880};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00296}.
FT   DOMAIN          48..357
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000259|Pfam:PF00561"
FT   ACT_SITE        154
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00296,
FT                   ECO:0000256|PIRSR:PIRSR000443-1"
FT   ACT_SITE        320
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00296,
FT                   ECO:0000256|PIRSR:PIRSR000443-1"
FT   ACT_SITE        353
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00296,
FT                   ECO:0000256|PIRSR:PIRSR000443-1"
FT   BINDING         224
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00296"
FT   BINDING         354
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00296"
SQ   SEQUENCE   410 AA;  45153 MW;  79B33F44530863D1 CRC64;
     MHNSVGAVST QYFTFAEDEP FCLESGETLS PVRLAYETYG TLNADRSNAI LICHALSGSA
     HAAGYLDGDP TKPGWWEECI GPGKAFDTDR FFVICSNVIG SCYGSTGPAS INPATGKPYG
     LNFPVVTIGD MVRAQVKLID HLGIERLLCV AGGSMGGMQV LEWAARHPQR VRSAIPIATT
     AHHSPMLIAF SEVGRQAIYA DPAWNRGDYY DKPQKPDAGL AVARMIGHIT YLSEESMQMK
     FGRRLQGLEK YGYEFETEFE VESYLKYNGH KFTRRFDANS YLYITKAMDY FDLAQPTGSL
     AAAFANATHI KFLVISFTSD WLYPSYHSKE LVSALTAVGA DVTYLDVKSS WGHDAFLLEV
     DTMTHLVGSF LDRLVREEQV APPVGYTPRA HLLSASPDAQ LRTHLAETLA
//
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