ID   Q9JZ43_NEIMB            Unreviewed;       275 AA.
AC   Q9JZ43;
DT   01-OCT-2000, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2000, sequence version 1.
DT   27-MAR-2024, entry version 115.
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=NMB1305 {ECO:0000313|EMBL:AAF41680.1};
OS   Neisseria meningitidis serogroup B (strain MC58).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41680.1, ECO:0000313|Proteomes:UP000000425};
RN   [1] {ECO:0000313|EMBL:AAF41680.1, ECO:0000313|Proteomes:UP000000425}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MC58 {ECO:0000313|EMBL:AAF41680.1,
RC   ECO:0000313|Proteomes:UP000000425};
RX   PubMed=10710307; DOI=10.1126/science.287.5459.1809;
RA   Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E.,
RA   Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., Nelson W.C.,
RA   Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., Haft D.H., Salzberg S.L.,
RA   White O., Fleischmann R.D., Dougherty B.A., Mason T., Ciecko A.,
RA   Parksey D.S., Blair E., Cittone H., Clark E.B., Cotton M.D.,
RA   Utterback T.R., Khouri H., Qin H., Vamathevan J., Gill J., Scarlato V.,
RA   Masignani V., Pizza M., Grandi G., Sun L., Smith H.O., Fraser C.M.,
RA   Moxon E.R., Rappuoli R., Venter J.C.;
RT   "Complete genome sequence of Neisseria meningitidis serogroup B strain
RT   MC58.";
RL   Science 287:1809-1815(2000).
RN   [2] {ECO:0007829|PDB:4B6G}
RP   X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) OF 3-275.
RX   PubMed=22937752; DOI=10.1089/ars.2012.4749;
RA   Chen N.H., Counago R.M., Djoko K.Y., Jennings M.P., Apicella M.A., Kobe B.,
RA   McEwan A.G.;
RT   "A glutathione-dependent detoxification system is required for formaldehyde
RT   resistance and optimal survival of Neisseria meningitidis in biofilms.";
RL   Antioxid. Redox Signal. 18:743-755(2013).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE002098; AAF41680.1; -; Genomic_DNA.
DR   PIR; G81097; G81097.
DR   RefSeq; NP_274324.1; NC_003112.2.
DR   RefSeq; WP_002225169.1; NC_003112.2.
DR   PDB; 4B6G; X-ray; 1.40 A; A/B=3-275.
DR   PDBsum; 4B6G; -.
DR   AlphaFoldDB; Q9JZ43; -.
DR   SMR; Q9JZ43; -.
DR   STRING; 122586.NMB1305; -.
DR   ESTHER; neime-ESD; A85-EsteraseD-FGH.
DR   MEROPS; S09.940; -.
DR   PaxDb; 122586-NMB1305; -.
DR   KEGG; nme:NMB1305; -.
DR   PATRIC; fig|122586.8.peg.1637; -.
DR   HOGENOM; CLU_056472_0_0_4; -.
DR   InParanoid; Q9JZ43; -.
DR   OrthoDB; 9782200at2; -.
DR   Proteomes; UP000000425; 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; 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   1: Evidence at protein level;
KW   3D-structure {ECO:0007829|PDB:4B6G};
KW   Hydrolase {ECO:0000256|RuleBase:RU363068};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000425};
KW   Serine esterase {ECO:0000256|RuleBase:RU363068}.
FT   ACT_SITE        145
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR614186-1"
FT   ACT_SITE        221
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR614186-1"
FT   ACT_SITE        254
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR614186-1"
SQ   SEQUENCE   275 AA;  31431 MW;  5D3AE8477A35775E CRC64;
     MKLIEQHQIF GGSQQVWAHH AQTLQCEMKF AVYLPNNPEN RPLGVIYWLS GLTCTEQNFI
     TKSGFQRYAA EHQVIVVAPD TSPRGEQVPN DDAYDLGQSA GFYLNATEQP WAANYQMYDY
     ILNELPRLIE KHFPTNGKRS IMGHSMGGHG ALVLALRNQE RYQSVSAFSP ILSPSLVPWG
     EKAFTAYLGK DREKWQQYDA NSLIQQGYKV QGMRIDQGLE DEFLPTQLRT EDFIETCRAA
     NQPVDVRFHK GYDHSYYFIA SFIGEHIAYH AAFLK
//