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METAA_AGRFC
ID   METAA_AGRFC             Reviewed;         308 AA.
AC   Q7CWE8;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 2.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Homoserine O-acetyltransferase {ECO:0000255|HAMAP-Rule:MF_00295, ECO:0000305};
DE            Short=HAT {ECO:0000255|HAMAP-Rule:MF_00295, ECO:0000305};
DE            EC=2.3.1.31 {ECO:0000255|HAMAP-Rule:MF_00295, ECO:0000269|PubMed:23085540};
DE   AltName: Full=Homoserine transacetylase {ECO:0000255|HAMAP-Rule:MF_00295, ECO:0000303|PubMed:23085540};
DE            Short=HTA {ECO:0000255|HAMAP-Rule:MF_00295, ECO:0000305};
GN   Name=metAA {ECO:0000255|HAMAP-Rule:MF_00295};
GN   Synonyms=metA {ECO:0000303|PubMed:23085540}; OrderedLocusNames=Atu2718;
GN   ORFNames=AGR_C_4927;
OS   Agrobacterium fabrum (strain C58 / ATCC 33970) (Agrobacterium tumefaciens
OS   (strain C58)).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium;
OC   Agrobacterium tumefaciens complex.
OX   NCBI_TaxID=176299;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C58 / ATCC 33970;
RX   PubMed=11743194; DOI=10.1126/science.1066803;
RA   Goodner B., Hinkle G., Gattung S., Miller N., Blanchard M., Qurollo B.,
RA   Goldman B.S., Cao Y., Askenazi M., Halling C., Mullin L., Houmiel K.,
RA   Gordon J., Vaudin M., Iartchouk O., Epp A., Liu F., Wollam C., Allinger M.,
RA   Doughty D., Scott C., Lappas C., Markelz B., Flanagan C., Crowell C.,
RA   Gurson J., Lomo C., Sear C., Strub G., Cielo C., Slater S.;
RT   "Genome sequence of the plant pathogen and biotechnology agent
RT   Agrobacterium tumefaciens C58.";
RL   Science 294:2323-2328(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C58 / ATCC 33970;
RX   PubMed=11743193; DOI=10.1126/science.1066804;
RA   Wood D.W., Setubal J.C., Kaul R., Monks D.E., Kitajima J.P., Okura V.K.,
RA   Zhou Y., Chen L., Wood G.E., Almeida N.F. Jr., Woo L., Chen Y.,
RA   Paulsen I.T., Eisen J.A., Karp P.D., Bovee D. Sr., Chapman P.,
RA   Clendenning J., Deatherage G., Gillet W., Grant C., Kutyavin T., Levy R.,
RA   Li M.-J., McClelland E., Palmieri A., Raymond C., Rouse G.,
RA   Saenphimmachak C., Wu Z., Romero P., Gordon D., Zhang S., Yoo H., Tao Y.,
RA   Biddle P., Jung M., Krespan W., Perry M., Gordon-Kamm B., Liao L., Kim S.,
RA   Hendrick C., Zhao Z.-Y., Dolan M., Chumley F., Tingey S.V., Tomb J.-F.,
RA   Gordon M.P., Olson M.V., Nester E.W.;
RT   "The genome of the natural genetic engineer Agrobacterium tumefaciens
RT   C58.";
RL   Science 294:2317-2323(2001).
RN   [3]
RP   FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND INDUCTION.
RC   STRAIN=C58 / ATCC 33970;
RX   PubMed=23085540; DOI=10.1016/j.resmic.2012.10.005;
RA   Rotem O., Biran D., Ron E.Z.;
RT   "Methionine biosynthesis in Agrobacterium tumefaciens: study of the first
RT   enzyme.";
RL   Res. Microbiol. 164:12-16(2013).
CC   -!- FUNCTION: Transfers an acetyl group from acetyl-CoA to L-homoserine,
CC       forming acetyl-L-homoserine. {ECO:0000255|HAMAP-Rule:MF_00295,
CC       ECO:0000269|PubMed:23085540}.
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_00295,
CC         ECO:0000269|PubMed:23085540};
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_00295, ECO:0000305|PubMed:23085540}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00295}.
CC   -!- INDUCTION: Induced by elevated temperatures via the sigma-32 factor
CC       RpoH. Repressed by a SAM riboswitch, which is also effective when
CC       transcription is sigma-32-mediated. {ECO:0000269|PubMed:23085540}.
CC   -!- SIMILARITY: Belongs to the MetA family. {ECO:0000255|HAMAP-
CC       Rule:MF_00295}.
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DR   EMBL; AE007869; AAK88436.2; -; Genomic_DNA.
DR   RefSeq; NP_355651.2; NC_003062.2.
DR   RefSeq; WP_010972516.1; NC_003062.2.
DR   AlphaFoldDB; Q7CWE8; -.
DR   SMR; Q7CWE8; -.
DR   STRING; 176299.Atu2718; -.
DR   DNASU; 1134756; -.
DR   EnsemblBacteria; AAK88436; AAK88436; Atu2718.
DR   GeneID; 66222902; -.
DR   KEGG; atu:Atu2718; -.
DR   PATRIC; fig|176299.10.peg.2726; -.
DR   eggNOG; COG1897; Bacteria.
DR   HOGENOM; CLU_057851_0_1_5; -.
DR   OMA; WLWFCYQ; -.
DR   PhylomeDB; Q7CWE8; -.
DR   BioCyc; AGRO:ATU2718-MON; -.
DR   BioCyc; MetaCyc:MON-17841; -.
DR   UniPathway; UPA00051; UER00074.
DR   Proteomes; UP000000813; Chromosome circular.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004414; F:homoserine O-acetyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008899; F:homoserine O-succinyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0019281; P:L-methionine biosynthetic process from homoserine via O-succinyl-L-homoserine and cystathionine; IEA:InterPro.
DR   CDD; cd03131; GATase1_HTS; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   HAMAP; MF_00295; MetA_acyltransf; 1.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR005697; HST_MetA.
DR   InterPro; IPR033752; MetA_family.
DR   PANTHER; PTHR20919; PTHR20919; 1.
DR   Pfam; PF04204; HTS; 1.
DR   PIRSF; PIRSF000450; H_ser_succinyltr; 1.
DR   SUPFAM; SSF52317; SSF52317; 1.
DR   TIGRFAMs; TIGR01001; metA; 1.
PE   1: Evidence at protein level;
KW   Acyltransferase; Amino-acid biosynthesis; Cytoplasm;
KW   Methionine biosynthesis; Reference proteome; Transferase.
FT   CHAIN           1..308
FT                   /note="Homoserine O-acetyltransferase"
FT                   /id="PRO_1000059288"
FT   ACT_SITE        142
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00295"
FT   ACT_SITE        235
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00295"
FT   ACT_SITE        237
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00295"
FT   BINDING         163
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00295"
FT   BINDING         192
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00295"
FT   BINDING         249
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00295"
FT   SITE            111
FT                   /note="Important for acyl-CoA specificity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00295"
FT   SITE            192
FT                   /note="Important for substrate specificity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00295"
SQ   SEQUENCE   308 AA;  35691 MW;  9DFDF167F80C60F6 CRC64;
     MPIKIPDTLP AFETLVHEGV RVMTETAAIR QDIRPLQIGL LNLMPNKIKT EIQMARLVGA
     SPLQVELSLI RIGGHRAKNT PEEHLLSFYQ TWEEVRHRKF DGFIITGAPI ELLDYEDVTY
     WNEMQQIFEW TQTNVHSTLN VCWGAMAAIY HFHGVPKYEL KEKAFGVYRH RNLSPSSIYL
     NGFSDDFQVP VSRWTEVRRA DIEKHPELEI LMESDEMGVC LAHEKAGNRL YMFNHVEYDS
     TSLADEYFRD VNSGVPIKLP HDYFPHNDPE LAPLNRWRSH AHLFFGNWIN EIYQTTPYDP
     QAIGKLAA
 
 
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