Y2424_MYCLE
ID Y2424_MYCLE Reviewed; 300 AA.
AC Q49823;
DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Putative hydrolase ML2424;
DE EC=3.1.-.-;
GN OrderedLocusNames=ML2424; ORFNames=B2168_F1_26;
OS Mycobacterium leprae (strain TN).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=272631;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Smith D.R., Robison K.;
RL Submitted (MAR-1994) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TN;
RX PubMed=11234002; DOI=10.1038/35059006;
RA Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA Barrell B.G.;
RT "Massive gene decay in the leprosy bacillus.";
RL Nature 409:1007-1011(2001).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. SerB family.
CC {ECO:0000305}.
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DR EMBL; U00018; AAA17250.1; -; Genomic_DNA.
DR EMBL; AL583925; CAC31940.1; -; Genomic_DNA.
DR PIR; S72914; S72914.
DR RefSeq; NP_302568.1; NC_002677.1.
DR RefSeq; WP_010908888.1; NC_002677.1.
DR AlphaFoldDB; Q49823; -.
DR SMR; Q49823; -.
DR STRING; 272631.ML2424; -.
DR EnsemblBacteria; CAC31940; CAC31940; CAC31940.
DR KEGG; mle:ML2424; -.
DR PATRIC; fig|272631.5.peg.4662; -.
DR Leproma; ML2424; -.
DR eggNOG; COG0560; Bacteria.
DR HOGENOM; CLU_052657_0_1_11; -.
DR OMA; FGRGLYK; -.
DR Proteomes; UP000000806; Chromosome.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR006385; HAD_hydro_SerB1.
DR InterPro; IPR023214; HAD_sf.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR01490; HAD-SF-IB-hyp1; 1.
PE 3: Inferred from homology;
KW Hydrolase; Magnesium; Metal-binding; Reference proteome.
FT CHAIN 1..300
FT /note="Putative hydrolase ML2424"
FT /id="PRO_0000156892"
FT ACT_SITE 56
FT /note="Nucleophile"
FT /evidence="ECO:0000255"
FT ACT_SITE 58
FT /note="Proton donor"
FT /evidence="ECO:0000255"
FT BINDING 56
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 58
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 231
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 300 AA; 32276 MW; 895887C2EFE567CC CRC64;
MASPDLSNAY NGRIDLGSLA NNASINRALN DMPTAVDDAG VRPQPPIDLT AAAFFDVDNT
LVQGSSAVHF GRGLAARDYF TYRDVLGFIY AQAKFQLLGK ENSQDVAAGQ RKALAFIEGR
SVEQLVALGE EIYDEIIADK IWAGTRQLTQ IHLDAGQQVW LITATPYELA ATIARRLGLT
GALGTVAESV DGIFTGRLVD ELLHGVGKAH AVRSLAIREG LNLKRCTAYS DSYNDVPMLS
LVGTAVAINP DAQLRSLARE RGWEIRDFRT ARKAARIGVP SALALGGALA AAVSRRRDRE
