ID Q7W301_BORPA Unreviewed; 282 AA.
AC Q7W301;
DT 01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2003, sequence version 1.
DT 27-MAR-2024, entry version 93.
DE RecName: Full=S-formylglutathione hydrolase {ECO:0000256|ARBA:ARBA00012479, ECO:0000256|RuleBase:RU363068};
DE EC=3.1.2.12 {ECO:0000256|ARBA:ARBA00012479, ECO:0000256|RuleBase:RU363068};
GN OrderedLocusNames=BPP4250 {ECO:0000313|EMBL:CAE39529.1};
OS Bordetella parapertussis (strain 12822 / ATCC BAA-587 / NCTC 13253).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=257311 {ECO:0000313|EMBL:CAE39529.1, ECO:0000313|Proteomes:UP000001421};
RN [1] {ECO:0000313|Proteomes:UP000001421}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=12822 / ATCC BAA-587 / NCTC 13253
RC {ECO:0000313|Proteomes:UP000001421};
RX PubMed=12910271; DOI=10.1038/ng1227;
RA Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R.,
RA Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L.,
RA Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A.,
RA Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I.,
RA Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T.,
RA Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S.,
RA Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E.,
RA Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M.,
RA Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S.,
RA Barrell B.G., Maskell D.J.;
RT "Comparative analysis of the genome sequences of Bordetella pertussis,
RT Bordetella parapertussis and Bordetella bronchiseptica.";
RL Nat. Genet. 35:32-40(2003).
CC -!- FUNCTION: Serine hydrolase involved in the detoxification of
CC formaldehyde. {ECO:0000256|RuleBase:RU363068}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + S-formylglutathione = formate + glutathione + H(+);
CC Xref=Rhea:RHEA:14961, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15740, ChEBI:CHEBI:57688, ChEBI:CHEBI:57925; EC=3.1.2.12;
CC Evidence={ECO:0000256|ARBA:ARBA00000080,
CC ECO:0000256|RuleBase:RU363068};
CC -!- SIMILARITY: Belongs to the esterase D family.
CC {ECO:0000256|ARBA:ARBA00005622, ECO:0000256|RuleBase:RU363068}.
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DR EMBL; BX640436; CAE39529.1; -; Genomic_DNA.
DR RefSeq; WP_003815759.1; NC_002928.3.
DR AlphaFoldDB; Q7W301; -.
DR ESTHER; borpe-q7vt07; A85-EsteraseD-FGH.
DR MEROPS; S09.940; -.
DR GeneID; 69423635; -.
DR KEGG; bpa:BPP4250; -.
DR HOGENOM; CLU_056472_0_0_4; -.
DR Proteomes; UP000001421; Chromosome.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0018738; F:S-formylglutathione hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0046294; P:formaldehyde catabolic process; IEA:InterPro.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000801; Esterase-like.
DR InterPro; IPR014186; S-formylglutathione_hydrol.
DR NCBIfam; TIGR02821; fghA_ester_D; 1.
DR PANTHER; PTHR10061; S-FORMYLGLUTATHIONE HYDROLASE; 1.
DR PANTHER; PTHR10061:SF0; S-FORMYLGLUTATHIONE HYDROLASE; 1.
DR Pfam; PF00756; Esterase; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU363068, ECO:0000313|EMBL:CAE39529.1};
KW Serine esterase {ECO:0000256|RuleBase:RU363068}.
FT ACT_SITE 150
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR614186-1"
FT ACT_SITE 228
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR614186-1"
FT ACT_SITE 261
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR614186-1"
SQ SEQUENCE 282 AA; 31501 MW; DD7FA909755750CD CRC64;
MAVLELVSQH RCFDGWQRYY RHASKEIGLP MRFSVFVPPQ AARGPVPVLF YLAGLTCTEE
TFMIKAGAQR LAAQHGVMLV APDTSPRGAG FPGEDEHWDF GVGAGFYLDA TAEPWRSHYR
MYSYVVDELH GIVTGELPGD AGRVGIFGHS MGGHGALVLA LRNPDKFRSV SAFAPVVAPA
QVPWGHKAFE RYLGPDRQAW EAYDASALMR TLRQPYPEGI LVDQGLADGF LVEQLRPELF
EAACRHAGQP LTLRRHEGYD HGYYFISTFI EDHIRFHVER LG
//
