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Database: UniProt
Entry: A9CJ11_AGRFC
LinkDB: A9CJ11_AGRFC
Original site: A9CJ11_AGRFC 
ID   A9CJ11_AGRFC            Unreviewed;       277 AA.
AC   A9CJ11;
DT   15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT   15-JAN-2008, sequence version 1.
DT   27-MAR-2024, entry version 88.
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=Atu1476 {ECO:0000313|EMBL:AAK87266.1};
OS   Agrobacterium fabrum (strain C58 / ATCC 33970) (Agrobacterium tumefaciens
OS   (strain C58)).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium;
OC   Agrobacterium tumefaciens complex.
OX   NCBI_TaxID=176299 {ECO:0000313|EMBL:AAK87266.1, ECO:0000313|Proteomes:UP000000813};
RN   [1] {ECO:0000313|EMBL:AAK87266.1, ECO:0000313|Proteomes:UP000000813}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C58 / ATCC 33970 {ECO:0000313|Proteomes:UP000000813};
RX   PubMed=11743193; DOI=10.1126/science.1066804;
RA   Wood D.W., Setubal J.C., Kaul R., Monks D.E., Kitajima J.P., Okura V.K.,
RA   Zhou Y., Chen L., Wood G.E., Almeida N.F.Jr., Woo L., Chen Y.,
RA   Paulsen I.T., Eisen J.A., Karp P.D., Bovee D.Sr., Chapman P.,
RA   Clendenning J., Deatherage G., Gillet W., Grant C., Kutyavin T., Levy R.,
RA   Li M.J., McClelland E., Palmieri A., Raymond C., Rouse G.,
RA   Saenphimmachak C., Wu Z., Romero P., Gordon D., Zhang S., Yoo H., Tao Y.,
RA   Biddle P., Jung M., Krespan W., Perry M., Gordon-Kamm B., Liao L., Kim S.,
RA   Hendrick C., Zhao Z.Y., Dolan M., Chumley F., Tingey S.V., Tomb J.F.,
RA   Gordon M.P., Olson M.V., Nester E.W.;
RT   "The genome of the natural genetic engineer Agrobacterium tumefaciens
RT   C58.";
RL   Science 294:2317-2323(2001).
RN   [2] {ECO:0000313|EMBL:AAK87266.1, ECO:0000313|Proteomes:UP000000813}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C58 / ATCC 33970 {ECO:0000313|Proteomes:UP000000813};
RX   PubMed=11743194; DOI=10.1126/science.1066803;
RA   Goodner B., Hinkle G., Gattung S., Miller N., Blanchard M., Qurollo B.,
RA   Goldman B.S., Cao Y., Askenazi M., Halling C., Mullin L., Houmiel K.,
RA   Gordon J., Vaudin M., Iartchouk O., Epp A., Liu F., Wollam C., Allinger M.,
RA   Doughty D., Scott C., Lappas C., Markelz B., Flanagan C., Crowell C.,
RA   Gurson J., Lomo C., Sear C., Strub G., Cielo C., Slater S.;
RT   "Genome sequence of the plant pathogen and biotechnology agent
RT   Agrobacterium tumefaciens C58.";
RL   Science 294:2323-2328(2001).
RN   [3] {ECO:0007829|PDB:3E4D}
RP   X-RAY CRYSTALLOGRAPHY (2.01 ANGSTROMS) IN COMPLEX WITH MAGNESIUM.
RX   PubMed=19653299; DOI=10.1002/pro.216;
RA   van Straaten K.E., Gonzalez C.F., Valladares R.B., Xu X., Savchenko A.V.,
RA   Sanders D.A.;
RT   "The structure of a putative S-formylglutathione hydrolase from
RT   Agrobacterium tumefaciens.";
RL   Protein Sci. 18:2196-2202(2009).
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; AE007869; AAK87266.1; -; Genomic_DNA.
DR   PIR; A97539; A97539.
DR   PIR; AD2758; AD2758.
DR   RefSeq; NP_354481.1; NC_003062.2.
DR   RefSeq; WP_010971651.1; NC_003062.2.
DR   PDB; 3E4D; X-ray; 2.01 A; A/B/C/D/E/F=1-277.
DR   PDBsum; 3E4D; -.
DR   AlphaFoldDB; A9CJ11; -.
DR   SMR; A9CJ11; -.
DR   STRING; 176299.Atu1476; -.
DR   ESTHER; agrt5-a9cj11; A85-EsteraseD-FGH.
DR   MEROPS; S09.940; -.
DR   EnsemblBacteria; AAK87266; AAK87266; Atu1476.
DR   GeneID; 66221685; -.
DR   KEGG; atu:Atu1476; -.
DR   PATRIC; fig|176299.10.peg.1500; -.
DR   eggNOG; COG0627; Bacteria.
DR   HOGENOM; CLU_056472_0_0_5; -.
DR   OrthoDB; 9782200at2; -.
DR   PhylomeDB; A9CJ11; -.
DR   BioCyc; AGRO:ATU1476-MONOMER; -.
DR   EvolutionaryTrace; A9CJ11; -.
DR   Proteomes; UP000000813; Chromosome circular.
DR   GO; GO:0052689; F:carboxylic ester hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; 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   1: Evidence at protein level;
KW   3D-structure {ECO:0007829|PDB:3E4D};
KW   Hydrolase {ECO:0000256|RuleBase:RU363068};
KW   Metal-binding {ECO:0007829|PDB:3E4D};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000813};
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"
FT   BINDING         90
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0007829|PDB:3E4D"
FT   BINDING         91
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0007829|PDB:3E4D"
FT   BINDING         94
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0007829|PDB:3E4D"
FT   BINDING         97
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0007829|PDB:3E4D"
SQ   SEQUENCE   277 AA;  31268 MW;  F3010875E9C8FE9B CRC64;
     MNIISQNTAF GGMQGVFSHQ SETLKSEMTF AVYVPPKAIH EPCPVVWYLS GLTCTHANVM
     EKGEYRRMAS ELGLVVVCPD TSPRGNDVPD ELTNWQMGKG AGFYLDATEE PWSEHYQMYS
     YVTEELPALI GQHFRADMSR QSIFGHSMGG HGAMTIALKN PERFKSCSAF APIVAPSSAD
     WSEPALEKYL GADRAAWRRY DACSLVEDGA RFPEFLIDQG KADSFLEKGL RPWLFEEAIK
     GTDIGLTLRM HDRYDHSYYF ISTFMDDHLK WHAERLG
//
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