(data stored in SCRATCH zone)

SWISSPROT: D4YX75_SPHJU

ID   D4YX75_SPHJU            Unreviewed;       383 AA.
AC   D4YX75;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   30-AUG-2017, entry version 55.
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:BAI94957.1};
GN   Synonyms=metXA {ECO:0000256|HAMAP-Rule:MF_00296};
GN   OrderedLocusNames=SJA_C1-01230 {ECO:0000313|EMBL:BAI94957.1};
OS   Sphingobium japonicum (strain NBRC 101211 / UT26S).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingobium.
OX   NCBI_TaxID=452662 {ECO:0000313|EMBL:BAI94957.1, ECO:0000313|Proteomes:UP000007753};
RN   [1] {ECO:0000313|EMBL:BAI94957.1, ECO:0000313|Proteomes:UP000007753}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101211 / UT26S {ECO:0000313|Proteomes:UP000007753};
RX   PubMed=20817768; DOI=10.1128/JB.00961-10;
RA   Nagata Y., Ohtsubo Y., Endo R., Ichikawa N., Ankai A., Oguchi A.,
RA   Fukui S., Fujita N., Tsuda M.;
RT   "Complete genome sequence of the representative gamma-
RT   hexachlorocyclohexane-degrading bacterium Sphingobium japonicum
RT   UT26.";
RL   J. Bacteriol. 192:5852-5853(2010).
CC   -!- FUNCTION: Transfers an acetyl group from acetyl-CoA to L-
CC       homoserine, forming acetyl-L-homoserine. {ECO:0000256|HAMAP-
CC       Rule:MF_00296}.
CC   -!- CATALYTIC ACTIVITY: Acetyl-CoA + L-homoserine = CoA + O-acetyl-L-
CC       homoserine. {ECO:0000256|HAMAP-Rule:MF_00296}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de
CC       novo 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, ECO:0000256|SAAS:SAAS00851697}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00296}.
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DR   EMBL; AP010803; BAI94957.1; -; Genomic_DNA.
DR   RefSeq; WP_013038777.1; NC_014006.1.
DR   STRING; 452662.SJA_C1-01230; -.
DR   EnsemblBacteria; BAI94957; BAI94957; SJA_C1-01230.
DR   GeneID; 29271835; -.
DR   KEGG; sjp:SJA_C1-01230; -.
DR   eggNOG; ENOG4105DWV; Bacteria.
DR   eggNOG; COG2021; LUCA.
DR   HOGENOM; HOG000246301; -.
DR   KO; K00641; -.
DR   OMA; CQGTTGP; -.
DR   OrthoDB; POG091H08NY; -.
DR   UniPathway; UPA00051; UER00074.
DR   Proteomes; UP000007753; Chromosome 1.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004414; F:homoserine O-acetyltransferase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0009086; P:methionine biosynthetic process; IEA:UniProtKB-HAMAP.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   HAMAP; MF_00296; Homoser_O_acetyltr; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR000073; AB_hydrolase_1.
DR   InterPro; IPR008220; HAT_MetX-like.
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;
DR   PRODOM; D4YX75.
DR   SWISS-2DPAGE; D4YX75.
KW   Acyltransferase {ECO:0000256|HAMAP-Rule:MF_00296,
KW   ECO:0000256|SAAS:SAAS00851686, ECO:0000313|EMBL:BAI94957.1};
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00296,
KW   ECO:0000256|SAAS:SAAS00851695};
KW   Complete proteome {ECO:0000313|Proteomes:UP000007753};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00296};
KW   Methionine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00296};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007753};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00296,
KW   ECO:0000256|SAAS:SAAS00842824, ECO:0000313|EMBL:BAI94957.1}.
FT   DOMAIN       51    365       AB hydrolase-1 (Alpha/Beta hydrolase fold
FT                                1). {ECO:0000259|Pfam:PF00561}.
FT   ACT_SITE    156    156       Nucleophile. {ECO:0000256|HAMAP-Rule:
FT                                MF_00296, ECO:0000256|PIRSR:PIRSR000443-
FT                                1}.
FT   ACT_SITE    327    327       {ECO:0000256|HAMAP-Rule:MF_00296,
FT                                ECO:0000256|PIRSR:PIRSR000443-1}.
FT   ACT_SITE    360    360       {ECO:0000256|HAMAP-Rule:MF_00296,
FT                                ECO:0000256|PIRSR:PIRSR000443-1}.
FT   BINDING     226    226       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00296}.
FT   BINDING     361    361       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00296}.
SQ   SEQUENCE   383 AA;  41515 MW;  DDE41A16C84004EE CRC64;
     MASASFPDDN RFGLRRQARL PGPLRLDSGA ALGPVDIAYE TYGRMDADRS NVILICHALT
     GDQYVASAHP VTGKPGWWWR LVGEGKPVDP ARHFIVCANV IGSCMGSSGP ASIDPATGEP
     HAMRFPVITI ADMVRAQAML LDHLGVDRLR AVIGGSMGGM QALSWPTLYP DRVESCIVIA
     STARHSAQNI AFHEVGRQAI MADPNWRGGD YYADGAIPSA GLAVARMAAH ITYLSEAGLT
     EKFGRRLQGR PENPNGSKTF GFDADFQVES YLRHQGLSFV ERFDANSYLY ITRAMDYYDI
     AEDHGGSLAR AFAASKARFC LVSFDTDWLY PTAESRLIVH ALNAGGAQAS FVELSSPFGH
     DAFLLECPEL NRVVDGFLKG GRA
//

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