(data stored in ACNUC7421 zone)

SWISSPROT: METAS_AERHH

ID   METAS_AERHH             Reviewed;         317 AA.
AC   A0KFJ6;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   08-MAY-2019, entry version 79.
DE   RecName: Full=Homoserine O-succinyltransferase {ECO:0000255|HAMAP-Rule:MF_00295};
DE            Short=HST {ECO:0000255|HAMAP-Rule:MF_00295};
DE            EC=2.3.1.46 {ECO:0000255|HAMAP-Rule:MF_00295};
DE   AltName: Full=Homoserine transsuccinylase {ECO:0000255|HAMAP-Rule:MF_00295};
DE            Short=HTS {ECO:0000255|HAMAP-Rule:MF_00295};
GN   Name=metAS {ECO:0000255|HAMAP-Rule:MF_00295};
GN   OrderedLocusNames=AHA_0489;
OS   Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / DSM 30187 /
OS   JCM 1027 / KCTC 2358 / NCIMB 9240).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=380703;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 7966 / DSM 30187 / JCM 1027 / KCTC 2358 / NCIMB 9240;
RX   PubMed=16980456; DOI=10.1128/JB.00621-06;
RA   Seshadri R., Joseph S.W., Chopra A.K., Sha J., Shaw J., Graf J.,
RA   Haft D.H., Wu M., Ren Q., Rosovitz M.J., Madupu R., Tallon L., Kim M.,
RA   Jin S., Vuong H., Stine O.C., Ali A., Horneman A.J., Heidelberg J.F.;
RT   "Genome sequence of Aeromonas hydrophila ATCC 7966T: jack of all
RT   trades.";
RL   J. Bacteriol. 188:8272-8282(2006).
CC   -!- FUNCTION: Transfers a succinyl group from succinyl-CoA to L-
CC       homoserine, forming succinyl-L-homoserine. {ECO:0000255|HAMAP-
CC       Rule:MF_00295}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-homoserine + succinyl-CoA = CoA + O-succinyl-L-
CC         homoserine; Xref=Rhea:RHEA:22008, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:57292, ChEBI:CHEBI:57476, ChEBI:CHEBI:57661;
CC         EC=2.3.1.46; Evidence={ECO:0000255|HAMAP-Rule:MF_00295};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de
CC       novo pathway; O-succinyl-L-homoserine from L-homoserine: step 1/1.
CC       {ECO:0000255|HAMAP-Rule:MF_00295}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00295}.
CC   -!- SIMILARITY: Belongs to the MetA family. {ECO:0000255|HAMAP-
CC       Rule:MF_00295}.
DR   EMBL; CP000462; ABK39388.1; -; Genomic_DNA.
DR   RefSeq; WP_011704462.1; NC_008570.1.
DR   RefSeq; YP_855022.1; NC_008570.1.
DR   SMR; A0KFJ6; -.
DR   STRING; 380703.AHA_0489; -.
DR   PRIDE; A0KFJ6; -.
DR   EnsemblBacteria; ABK39388; ABK39388; AHA_0489.
DR   GeneID; 4490071; -.
DR   KEGG; aha:AHA_0489; -.
DR   PATRIC; fig|380703.7.peg.482; -.
DR   eggNOG; ENOG4105CVG; Bacteria.
DR   eggNOG; COG1897; LUCA.
DR   HOGENOM; HOG000115049; -.
DR   KO; K00651; -.
DR   OMA; CWAAHAA; -.
DR   BioCyc; AHYD380703:G1G7B-490-MONOMER; -.
DR   UniPathway; UPA00051; UER00075.
DR   Proteomes; UP000000756; 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:0008899; F:homoserine O-succinyltransferase activity; IEA:UniProtKB-EC.
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   3: Inferred from homology;
DR   PRODOM; A0KFJ6.
DR   SWISS-2DPAGE; A0KFJ6.
KW   Acyltransferase; Amino-acid biosynthesis; Complete proteome;
KW   Cytoplasm; Methionine biosynthesis; Reference proteome; Transferase.
FT   CHAIN         1    317       Homoserine O-succinyltransferase.
FT                                /FTId=PRO_1000021794.
FT   ACT_SITE    142    142       Acyl-thioester intermediate.
FT                                {ECO:0000255|HAMAP-Rule:MF_00295}.
FT   ACT_SITE    235    235       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00295}.
FT   ACT_SITE    237    237       {ECO:0000255|HAMAP-Rule:MF_00295}.
FT   BINDING     163    163       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00295}.
FT   BINDING     192    192       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00295}.
FT   BINDING     249    249       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00295}.
FT   SITE        111    111       Important for acyl-CoA specificity.
FT                                {ECO:0000255|HAMAP-Rule:MF_00295}.
FT   SITE        192    192       Important for substrate specificity.
FT                                {ECO:0000255|HAMAP-Rule:MF_00295}.
SQ   SEQUENCE   317 AA;  36531 MW;  9D04FC9722B78DF0 CRC64;
     MPIKIPDQLP AAEVLGQENI FVMTESRAVT QNIRPLRVLI LNLMPKKIET EIQLMRMLSN
     SPLQVDVDLL RIDDRESKNT PQAHLENFYH DFEQVRGNNY DGMIITGAPL GLVEFEEVVY
     WPRIVEIIEW SHQHVTSTLF LCWAVQAALK ALYGMEKQTH GEKLSGVYRH HRLDEHEPLL
     RGFDDEFVAP HSRYAAFDGD LIRAHTDLQI FAESAEAGVY LAATKDCRQV FVTGHPEYDA
     LTLDGEYQRD LAAGLEPVIP VNYYPDNDPT RTPRASWRSH GHLLFSNWLN YYVYQLTSYR
     VEDIGKVFTY QQNSPSR
//

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