ID A0A147HZ96_9SPHN Unreviewed; 276 AA.
AC A0A147HZ96;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 17.
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 ORFNames=NS334_12700 {ECO:0000313|EMBL:KTT70333.1};
OS Sphingomonas endophytica.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=869719 {ECO:0000313|EMBL:KTT70333.1, ECO:0000313|Proteomes:UP000074310};
RN [1] {ECO:0000313|EMBL:KTT70333.1, ECO:0000313|Proteomes:UP000074310}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NS334 {ECO:0000313|EMBL:KTT70333.1,
RC ECO:0000313|Proteomes:UP000074310};
RX PubMed=26793183;
RA Midha S., Bansal K., Sharma S., Kumar N., Patil P.P., Chaudhry V.,
RA Patil P.B.;
RT "Genomic Resource of Rice Seed Associated Bacteria.";
RL Front. Microbiol. 6:1551-1551(2016).
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KTT70333.1}.
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; LDTB01000054; KTT70333.1; -; Genomic_DNA.
DR RefSeq; WP_058756340.1; NZ_LDTB01000054.1.
DR AlphaFoldDB; A0A147HZ96; -.
DR PATRIC; fig|869719.3.peg.2524; -.
DR OrthoDB; 9782200at2; -.
DR Proteomes; UP000074310; Unassembled WGS sequence.
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:KTT70333.1};
KW Serine esterase {ECO:0000256|RuleBase:RU363068}.
FT ACT_SITE 146
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 276 AA; 29998 MW; 6B2988E6871867A1 CRC64;
METVSTAKAH GGTQGVYRHA STATGTDMTF SVYVPDHAPG AKLPVVWYLS GLTCTHANVT
DKGEYRRACA EHGLIFVAPD TSPRGDDVPD EDRWDFGKGA GFYVDATQAP WSAYYRMWSY
VTGELPALIA SAFPADMARQ SIMGHSMGGH GALTTALRHP DRFRAVSAFA PIVAPTQVPW
GGALDRYLGD DMAAKRRHDA VALIEDGARV KELLVDQGDA DSFLAEQLRP ELLAEACAAA
GIDLTLRMRS GYDHSYHFIS TFMADHLAWH AARLRA
//
