ID A0A167INR3_CALVF Unreviewed; 301 AA.
AC A0A167INR3;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=S-formylglutathione hydrolase {ECO:0000256|ARBA:ARBA00016774};
DE EC=3.1.2.12 {ECO:0000256|ARBA:ARBA00012479};
GN ORFNames=CALVIDRAFT_487004 {ECO:0000313|EMBL:KZO92812.1};
OS Calocera viscosa (strain TUFC12733).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Dacrymycetes;
OC Dacrymycetales; Dacrymycetaceae; Calocera.
OX NCBI_TaxID=1330018 {ECO:0000313|EMBL:KZO92812.1, ECO:0000313|Proteomes:UP000076738};
RN [1] {ECO:0000313|EMBL:KZO92812.1, ECO:0000313|Proteomes:UP000076738}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TUFC12733 {ECO:0000313|EMBL:KZO92812.1,
RC ECO:0000313|Proteomes:UP000076738};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
CC -!- SIMILARITY: Belongs to the esterase D family.
CC {ECO:0000256|ARBA:ARBA00005622}.
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DR EMBL; KV417307; KZO92812.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A167INR3; -.
DR STRING; 1330018.A0A167INR3; -.
DR OrthoDB; 630at2759; -.
DR Proteomes; UP000076738; Unassembled WGS sequence.
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 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 Reference proteome {ECO:0000313|Proteomes:UP000076738}.
FT ACT_SITE 149
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR614186-1"
FT ACT_SITE 229
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR614186-1"
FT ACT_SITE 264
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR614186-1"
SQ SEQUENCE 301 AA; 32299 MW; 503C64BA5A61279C CRC64;
MSVSTIKSNK CFGGQLIKLS AKAESYNGLE TKFNVFVPEG KGPFPVLYYL AGLTCDEDTG
ATKGMFEGPA AAHGIALVFP DTSPRGAGIA GEDADWDFGT GAGFYLDATA PAYASHYRGF
TYLTQELPEL LKKSGLPLDL NRQSIMGHSM GGHGALVLYL KTLALGKYAS CSAFAPITNP
TLCPWGTKAF AGYLKGGVEE GKEWDATELL RSGQAKGELR IRFDWGSADN FFQAGQLLPE
NFLGEVKSLG VGGVVGTQRE GYDHSYYFIM SFAAEHVACE SEFFACCLIQ CSQRSQSTQS
T
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