METXA_METAC
ID METXA_METAC Reviewed; 540 AA.
AC Q8TME4;
DT 07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Homoserine O-acetyltransferase {ECO:0000255|HAMAP-Rule:MF_00296};
DE Short=HAT {ECO:0000255|HAMAP-Rule:MF_00296, ECO:0000303|PubMed:28581482};
DE EC=2.3.1.31 {ECO:0000255|HAMAP-Rule:MF_00296, ECO:0000269|PubMed:28581482};
DE AltName: Full=Homoserine transacetylase {ECO:0000255|HAMAP-Rule:MF_00296};
DE Short=HTA {ECO:0000255|HAMAP-Rule:MF_00296};
GN Name=metXA {ECO:0000255|HAMAP-Rule:MF_00296, ECO:0000303|PubMed:28581482};
GN Synonyms=metA {ECO:0000312|EMBL:AAM06093.1};
GN OrderedLocusNames=MA_2714 {ECO:0000312|EMBL:AAM06093.1};
OS Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 /
OS C2A).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=188937;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35395 / DSM 2834 / JCM 12185 / C2A;
RX PubMed=11932238; DOI=10.1101/gr.223902;
RA Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P., FitzHugh W.,
RA Calvo S., Engels R., Smirnov S., Atnoor D., Brown A., Allen N., Naylor J.,
RA Stange-Thomann N., DeArellano K., Johnson R., Linton L., McEwan P.,
RA McKernan K., Talamas J., Tirrell A., Ye W., Zimmer A., Barber R.D.,
RA Cann I., Graham D.E., Grahame D.A., Guss A.M., Hedderich R.,
RA Ingram-Smith C., Kuettner H.C., Krzycki J.A., Leigh J.A., Li W., Liu J.,
RA Mukhopadhyay B., Reeve J.N., Smith K., Springer T.A., Umayam L.A.,
RA White O., White R.H., de Macario E.C., Ferry J.G., Jarrell K.F., Jing H.,
RA Macario A.J.L., Paulsen I.T., Pritchett M., Sowers K.R., Swanson R.V.,
RA Zinder S.H., Lander E., Metcalf W.W., Birren B.;
RT "The genome of Methanosarcina acetivorans reveals extensive metabolic and
RT physiological diversity.";
RL Genome Res. 12:532-542(2002).
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 an acetyl group from acetyl-CoA to L-homoserine,
CC forming acetyl-L-homoserine. In vitro, can also use propionyl-CoA or
CC butiryl-CoA as acyl donor. {ECO:0000269|PubMed:28581482}.
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_00296,
CC ECO:0000269|PubMed:28581482};
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_00296}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00296}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00296}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. MetX family.
CC {ECO:0000255|HAMAP-Rule:MF_00296}.
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DR EMBL; AE010299; AAM06093.1; -; Genomic_DNA.
DR RefSeq; WP_011022674.1; NC_003552.1.
DR AlphaFoldDB; Q8TME4; -.
DR SMR; Q8TME4; -.
DR STRING; 188937.MA_2714; -.
DR ESTHER; metac-META; Homoserine_transacetylase.
DR EnsemblBacteria; AAM06093; AAM06093; MA_2714.
DR GeneID; 1474607; -.
DR KEGG; mac:MA_2714; -.
DR HOGENOM; CLU_028760_1_1_2; -.
DR InParanoid; Q8TME4; -.
DR OMA; TRFCVVS; -.
DR OrthoDB; 8770at2157; -.
DR PhylomeDB; Q8TME4; -.
DR UniPathway; UPA00051; UER00074.
DR Proteomes; UP000002487; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004414; F:homoserine O-acetyltransferase activity; IBA:GO_Central.
DR GO; GO:0009092; P:homoserine metabolic process; IBA:GO_Central.
DR GO; GO:0009086; P:methionine biosynthetic process; IBA:GO_Central.
DR Gene3D; 3.10.580.10; -; 1.
DR Gene3D; 3.40.50.1820; -; 1.
DR HAMAP; MF_00296; MetX_acyltransf; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR InterPro; IPR000644; CBS_dom.
DR InterPro; IPR046342; CBS_dom_sf.
DR InterPro; IPR008220; HAT_MetX-like.
DR PANTHER; PTHR32268; PTHR32268; 1.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR Pfam; PF00571; CBS; 2.
DR SMART; SM00116; CBS; 2.
DR SUPFAM; SSF53474; SSF53474; 1.
DR SUPFAM; SSF54631; SSF54631; 1.
DR TIGRFAMs; TIGR01392; homoserO_Ac_trn; 1.
DR PROSITE; PS51371; CBS; 2.
PE 1: Evidence at protein level;
KW Acyltransferase; Amino-acid biosynthesis; CBS domain; Cytoplasm;
KW Methionine biosynthesis; Reference proteome; Repeat; Transferase.
FT CHAIN 1..540
FT /note="Homoserine O-acetyltransferase"
FT /id="PRO_0000440285"
FT DOMAIN 66..404
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT DOMAIN 425..484
FT /note="CBS 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT DOMAIN 486..540
FT /note="CBS 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT REGION 262..284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 171
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT ACT_SITE 365
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT ACT_SITE 398
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT BINDING 240
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT BINDING 399
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
SQ SEQUENCE 540 AA; 59169 MW; 12EB654216C117AB CRC64;
MAVSSGNSSV NSSKKLFSGK KGQSIGIVRS MNYKIPGTFG LESGKTLSGV RVEYEMYGKM
NADKSNVILI CHALTGDAHA AGFHEGDKKP GWWEIVIGPN KAFDTEKYCV ICSNILGGCK
GSTGPSSIDP ETGKHYGISF PVITVKDMVN AQKKLIEHLG VKQLFAVAGG SMGGMQVLQW
TVSYPEMVRK AIAIATTAST TPQQIAFGAI GRKAITDDPK WNGGDYYGKE IPSQGLALAR
MIGHITYLSD ASMQNKFGRL QQDTDKSGIK GTTGTEGKNS SEISSEISSI SSEISSELSY
DFTPNFQVES YLNYKGDNFT KRFDANSYLY ITKAVDYFDL AKNGSLIEGF SGVTAKYLVI
SISSDWLYPP YQSQEIVSAL TANGVDARYE EIRSQHGHDA FLLEEGQLSY LLRSFLSHIL
VSDVMNRNFY TVSRDETIEH SSKLMVKECV SHLPVISEDG KLEGIVTSWD ITKAVACKIN
ELDEIITRDV KYVYEDEKIE HASSIMEKHS ISALPVIDSE HRIIGIVTSE SISALFGKYD
