ID A9M772_BRUC2 Unreviewed; 278 AA.
AC A9M772;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 67.
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 Name=fghA {ECO:0000313|EMBL:ABX61231.1};
GN OrderedLocusNames=BCAN_A0130 {ECO:0000313|EMBL:ABX61231.1};
OS Brucella canis (strain ATCC 23365 / NCTC 10854).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=483179 {ECO:0000313|EMBL:ABX61231.1, ECO:0000313|Proteomes:UP000001385};
RN [1] {ECO:0000313|EMBL:ABX61231.1, ECO:0000313|Proteomes:UP000001385}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23365 / NCTC 10854 {ECO:0000313|Proteomes:UP000001385};
RA Setubal J.C., Bowns C., Boyle S., Crasta O.R., Czar M.J., Dharmanolla C.,
RA Gillespie J.J., Kenyon R.W., Lu J., Mane S., Mohapatra S., Nagrani S.,
RA Purkayastha A., Rajasimha H.K., Shallom J.M., Shallom S., Shukla M.,
RA Snyder E.E., Sobral B.W., Wattam A.R., Will R., Williams K., Yoo H.,
RA Bruce D., Detter C., Munk C., Brettin T.S.;
RT "Brucella canis ATCC 23365 whole genome shotgun sequencing project.";
RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000872; ABX61231.1; -; Genomic_DNA.
DR RefSeq; WP_002965376.1; NC_010103.1.
DR AlphaFoldDB; A9M772; -.
DR ESTHER; brume-BMEI1822; A85-EsteraseD-FGH.
DR MEROPS; S09.940; -.
DR GeneID; 58776691; -.
DR KEGG; bcs:BCAN_A0130; -.
DR HOGENOM; CLU_056472_0_0_5; -.
DR PhylomeDB; A9M772; -.
DR Proteomes; UP000001385; Chromosome I.
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:ABX61231.1};
KW Serine esterase {ECO:0000256|RuleBase:RU363068}.
FT ACT_SITE 147
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR614186-1"
FT ACT_SITE 223
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR614186-1"
FT ACT_SITE 256
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR614186-1"
SQ SEQUENCE 278 AA; 31131 MW; C2743B6B7D534DBE CRC64;
METISTARCF DGTQGVYRHK SEACQCDMTF ALFLPPQAKD GPVPVLWYLS GLTCTHQNVM
DKGEYRQLAS ELGIAVICPD TSPRGDSIAD EPDNWQFGKG AGFYVDAMQA PFAQNYRMYS
YITQELSALV ARQFPLDMER QAITGHSMGG HGALTIALKN PDRFKSVSAF APIVQPSTAG
WSRPALEKYL GPDEQAWRAY DATLLIEDGH RFPEILVDQG TADGFLDDGL RPWLLEEACR
KAGIALTLNM REGYDHSYFF ISTFMGDHLR WHSERLRS
//
