(data stored in ACNUC7421 zone)

SWISSPROT: ENTH_SHISS

ID   ENTH_SHISS              Reviewed;         137 AA.
AC   Q3Z4J6;
DT   16-NOV-2011, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 1.
DT   08-MAY-2019, entry version 80.
DE   RecName: Full=Proofreading thioesterase EntH {ECO:0000255|HAMAP-Rule:MF_00907};
DE            EC=3.1.2.- {ECO:0000255|HAMAP-Rule:MF_00907};
DE   AltName: Full=Enterobactin synthase component H {ECO:0000255|HAMAP-Rule:MF_00907};
GN   Name=entH {ECO:0000255|HAMAP-Rule:MF_00907};
GN   OrderedLocusNames=SSON_0548;
OS   Shigella sonnei (strain Ss046).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=300269;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ss046;
RX   PubMed=16275786; DOI=10.1093/nar/gki954;
RA   Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X.,
RA   Wang J., Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S.,
RA   Nie H., Peng J., Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y.,
RA   Qiang B., Hou Y., Yu J., Jin Q.;
RT   "Genome dynamics and diversity of Shigella species, the etiologic
RT   agents of bacillary dysentery.";
RL   Nucleic Acids Res. 33:6445-6458(2005).
CC   -!- FUNCTION: Required for optimal enterobactin synthesis. Acts as a
CC       proofreading enzyme that prevents EntB misacylation by hydrolyzing
CC       the thioester bound existing between EntB and wrongly charged
CC       molecules. {ECO:0000255|HAMAP-Rule:MF_00907}.
CC   -!- PATHWAY: Siderophore biosynthesis; enterobactin biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00907}.
CC   -!- SUBUNIT: Homotetramer. Dimer of dimers. Interacts specifically
CC       with the aryl carrier protein (ArCP) domain of EntB.
CC       {ECO:0000255|HAMAP-Rule:MF_00907}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00907}.
CC   -!- SIMILARITY: Belongs to the thioesterase PaaI family.
CC       {ECO:0000255|HAMAP-Rule:MF_00907}.
DR   EMBL; CP000038; AAZ87316.1; -; Genomic_DNA.
DR   SMR; Q3Z4J6; -.
DR   EnsemblBacteria; AAZ87316; AAZ87316; SSON_0548.
DR   KEGG; ssn:SSON_0548; -.
DR   HOGENOM; HOG000066991; -.
DR   OMA; HGGVYCS; -.
DR   BioCyc; SSON300269:G1GL2-645-MONOMER; -.
DR   UniPathway; UPA00017; -.
DR   Proteomes; UP000002529; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016790; F:thiolester hydrolase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009239; P:enterobactin biosynthetic process; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00907; Thioesterase_EntH; 1.
DR   InterPro; IPR029069; HotDog_dom_sf.
DR   InterPro; IPR003736; PAAI_dom.
DR   InterPro; IPR026576; Thioesterase_EntH.
DR   InterPro; IPR006683; Thioestr_dom.
DR   Pfam; PF03061; 4HBT; 1.
DR   SUPFAM; SSF54637; SSF54637; 1.
DR   TIGRFAMs; TIGR00369; unchar_dom_1; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q3Z4J6.
DR   SWISS-2DPAGE; Q3Z4J6.
KW   Complete proteome; Cytoplasm; Hydrolase.
FT   CHAIN         1    137       Proofreading thioesterase EntH.
FT                                /FTId=PRO_0000413879.
FT   ACT_SITE     63     63       Nucleophile or proton acceptor.
FT                                {ECO:0000255|HAMAP-Rule:MF_00907}.
SQ   SEQUENCE   137 AA;  15016 MW;  C8DF8DE6321494C1 CRC64;
     MIWKRHLTLD ELNATSDNTM VAHLGIVYTR LGDDVLEAEM PVDTRTHQPF GLLHGGASAA
     LAETLGSMAG FMMTRDGQCV VGTELNATHH RPMSEGKVRG VCQPLHLGRQ NQSWEIIVFD
     EQGRRCCTCR LGTAVLG
//

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