SFGH_HAEIN
ID SFGH_HAEIN Reviewed; 275 AA.
AC P44556;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=S-formylglutathione hydrolase;
DE Short=FGH;
DE EC=3.1.2.12;
GN OrderedLocusNames=HI_0184;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=10675023;
RX DOI=10.1002/(sici)1522-2683(20000101)21:2<411::aid-elps411>3.0.co;2-4;
RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., Gray C.,
RA Fountoulakis M.;
RT "Two-dimensional map of the proteome of Haemophilus influenzae.";
RL Electrophoresis 21:411-429(2000).
CC -!- FUNCTION: Serine hydrolase involved in the detoxification of
CC formaldehyde. Hydrolyzes S-formylglutathione to glutathione and formate
CC (By similarity). {ECO:0000250}.
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 -!- SIMILARITY: Belongs to the esterase D family. {ECO:0000305}.
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DR EMBL; L42023; AAC21853.1; -; Genomic_DNA.
DR PIR; A64145; A64145.
DR RefSeq; NP_438352.1; NC_000907.1.
DR RefSeq; WP_005694102.1; NC_000907.1.
DR AlphaFoldDB; P44556; -.
DR SMR; P44556; -.
DR STRING; 71421.HI_0184; -.
DR ESTHER; haein-sfgh; A85-EsteraseD-FGH.
DR EnsemblBacteria; AAC21853; AAC21853; HI_0184.
DR KEGG; hin:HI_0184; -.
DR PATRIC; fig|71421.8.peg.188; -.
DR eggNOG; COG0627; Bacteria.
DR HOGENOM; CLU_056472_0_0_6; -.
DR OMA; TFMEDHL; -.
DR PhylomeDB; P44556; -.
DR BioCyc; HINF71421:G1GJ1-194-MON; -.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0018738; F:S-formylglutathione hydrolase activity; IBA:GO_Central.
DR GO; GO:0046294; P:formaldehyde catabolic process; IEA:InterPro.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000801; Esterase-like.
DR InterPro; IPR014186; S-formylglutathione_hydrol.
DR PANTHER; PTHR10061; PTHR10061; 1.
DR Pfam; PF00756; Esterase; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR TIGRFAMs; TIGR02821; fghA_ester_D; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Reference proteome; Serine esterase.
FT CHAIN 1..275
FT /note="S-formylglutathione hydrolase"
FT /id="PRO_0000210344"
FT ACT_SITE 145
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 221
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 254
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
SQ SEQUENCE 275 AA; 31317 MW; 781F5C0411546D3D CRC64;
MKLIEQHQIF GGSQQVWAHN AQTLQCEMKF AVYLPNNPEN RPLGVIYWLS GLTCTEQNFI
TKSGFQRYAA EHQVIVVAPD TSPRGEQVPN DAAYDLGQGA GFYLNATEQP WATNYQMYDY
ILNELPDLIE ANFPTNGKRS IMGHSMGGHG ALVLALRNRE RYQSVSAFSP ILSPSLVPWG
EKAFSAYLGE DREKWQQYDA SSLIQQGYKV QGMRIDQGLE DEFLPTQLRT EDFIETCRVA
NQPVDVRFHK GYDHSYYFIA SFIGEHIAYH AEFLK