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Database: UniProt
Entry: B7MK77_ECO45
LinkDB: B7MK77_ECO45
Original site: B7MK77_ECO45 
ID   B7MK77_ECO45            Unreviewed;       219 AA.
AC   B7MK77;
DT   24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   24-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 67.
DE   SubName: Full=Isomerase/hydrolase {ECO:0000313|EMBL:CAR02569.1};
DE            EC=3.-.-.- {ECO:0000313|EMBL:CAR02569.1};
GN   Name=ycgM {ECO:0000313|EMBL:CAR02569.1};
GN   OrderedLocusNames=ECS88_1243 {ECO:0000313|EMBL:CAR02569.1};
OS   Escherichia coli O45:K1 (strain S88 / ExPEC).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585035 {ECO:0000313|EMBL:CAR02569.1, ECO:0000313|Proteomes:UP000000747};
RN   [1] {ECO:0000313|Proteomes:UP000000747}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S88 / ExPEC {ECO:0000313|Proteomes:UP000000747};
RX   PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA   Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA   Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA   Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA   Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA   Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA   Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA   Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT   "Organised genome dynamics in the Escherichia coli species results in
RT   highly diverse adaptive paths.";
RL   PLoS Genet. 5:E1000344-E1000344(2009).
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DR   EMBL; CU928161; CAR02569.1; -; Genomic_DNA.
DR   RefSeq; WP_000284277.1; NC_011742.1.
DR   AlphaFoldDB; B7MK77; -.
DR   SMR; B7MK77; -.
DR   GeneID; 75171284; -.
DR   KEGG; ecz:ECS88_1243; -.
DR   HOGENOM; CLU_028458_5_2_6; -.
DR   Proteomes; UP000000747; Chromosome.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.90.850.10; Fumarylacetoacetase-like, C-terminal domain; 1.
DR   InterPro; IPR011234; Fumarylacetoacetase-like_C.
DR   InterPro; IPR036663; Fumarylacetoacetase_C_sf.
DR   PANTHER; PTHR11820; ACYLPYRUVASE; 1.
DR   PANTHER; PTHR11820:SF7; ACYLPYRUVASE FAHD1, MITOCHONDRIAL; 1.
DR   Pfam; PF01557; FAA_hydrolase; 1.
DR   SUPFAM; SSF56529; FAH; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000313|EMBL:CAR02569.1};
KW   Isomerase {ECO:0000313|EMBL:CAR02569.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000747}.
FT   DOMAIN          18..212
FT                   /note="Fumarylacetoacetase-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01557"
SQ   SEQUENCE   219 AA;  23681 MW;  9E20EAC13E0A555C CRC64;
     MYQHHNWQGA LLDYPVSKVV CVGSNYAKHI KEMGSAVPEE PVLFIKPETA LCDLRQPLAI
     PSDFGSVHHE VELAVLIGAT LRQATEEHVR KAIAGYGVAL DLTLRDVQGK MKKAGQPWEK
     AKAFDNSCPL SGFIPAAEFT GDPQNTTLGL SVNGEQRQQG TTADMIHKIV PLIAYMSKFF
     TLKAGDVVLT GTPDGVGPLQ SGDELTVTFD GHSLTTRVL
//
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