MET2_SCHPO
ID MET2_SCHPO Reviewed; 489 AA.
AC O60062;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 25-MAY-2022, entry version 147.
DE RecName: Full=Homoserine O-acetyltransferase;
DE EC=2.3.1.31;
DE AltName: Full=Homoserine O-trans-acetylase;
GN Name=met6; ORFNames=SPBC56F2.11;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9829945; DOI=10.1128/jb.180.23.6338-6341.1998;
RA Schweingruber A.-M., Hilti N., Edenharter E., Schweingruber M.;
RT "Methionine induces sexual development in the fission yeast
RT Schizosaccharomyces pombe via an ste11-dependent signalling pathway.";
RL J. Bacteriol. 180:6338-6341(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [3]
RP REVISION OF GENE MODEL.
RX PubMed=21511999; DOI=10.1126/science.1203357;
RA Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT "Comparative functional genomics of the fission yeasts.";
RL Science 332:930-936(2011).
RN [4]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
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 -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo
CC pathway; O-acetyl-L-homoserine from L-homoserine: step 1/1.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. MetX family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA18890.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AJ223985; CAA11759.1; -; Genomic_DNA.
DR EMBL; CU329671; CAA18890.2; ALT_SEQ; Genomic_DNA.
DR PIR; T43422; T43422.
DR RefSeq; NP_596706.2; NM_001022631.2.
DR AlphaFoldDB; O60062; -.
DR SMR; O60062; -.
DR STRING; 4896.SPBC56F2.11.1; -.
DR ESTHER; schpo-met2; Homoserine_transacetylase.
DR MaxQB; O60062; -.
DR PaxDb; O60062; -.
DR GeneID; 2540848; -.
DR KEGG; spo:SPBC56F2.11; -.
DR PomBase; SPBC56F2.11; met6.
DR eggNOG; ENOG502QRIX; Eukaryota.
DR HOGENOM; CLU_028760_5_0_1; -.
DR InParanoid; O60062; -.
DR PhylomeDB; O60062; -.
DR UniPathway; UPA00051; UER00074.
DR PRO; PR:O60062; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0004414; F:homoserine O-acetyltransferase activity; IDA:PomBase.
DR GO; GO:0071266; P:'de novo' L-methionine biosynthetic process; IDA:PomBase.
DR GO; GO:0009092; P:homoserine metabolic process; ISO:PomBase.
DR GO; GO:0009086; P:methionine biosynthetic process; IMP:PomBase.
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; IPR008220; HAT_MetX-like.
DR PANTHER; PTHR32268; PTHR32268; 1.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR PIRSF; PIRSF000443; Homoser_Ac_trans; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR TIGRFAMs; TIGR01392; homoserO_Ac_trn; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Amino-acid biosynthesis; Cytoplasm;
KW Methionine biosynthesis; Reference proteome; Transferase.
FT CHAIN 1..489
FT /note="Homoserine O-acetyltransferase"
FT /id="PRO_0000155756"
FT DOMAIN 69..438
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255"
FT REGION 255..329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 291..329
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 163
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P45131"
FT ACT_SITE 403
FT /evidence="ECO:0000250|UniProtKB:P45131"
FT ACT_SITE 432
FT /evidence="ECO:0000250|UniProtKB:P45131"
SQ SEQUENCE 489 AA; 54311 MW; 46B95C30A099041E CRC64;
MESQSPIESI VFTDSCHPSQ QENKFVQLIS DQKIAIVPKF TLECGDILYD VPVAFKTWGT
LNKEGNNCLL LCHALSGSAD AGDWWGPLLG PGRAFDPSHF FIVCLNSLGS PYGSASPVTW
NAETHSVYGP EFPLATIRDD VNIHKLILQR LGVKQIAMAV GGSMGGMLVL EWAFDKEFVR
SIVPISTSLR HSAWCISWSE AQRQSIYSDP KFNDGYYGID DQPVSGLGAA RMSALLTYRS
KCSFERRFAR TVPDASRHPY PDRLPTPLTP SNAHWVVHNE GNRNRRERPC RSNGSSPTSE
SALNSPASSV SSLPSLGASQ TTDSSSLNQS SLLRRPANTY FSAQSYLRYQ AKKFVSRFDA
NCYISITKKL DTHDITRGRG SDSPKEVMKD LSLPVLVLGI ESDGLFTFDE QVEIAKSFPN
ATLEKIISAE GHDGFLLEFT QVNSHIQKFQ KEHLIDIMSQ TNSFERLDSQ VNDTNRESVF
GEMEDITSW
