ID A0A0D2DII7_9EURO Unreviewed; 190 AA.
AC A0A0D2DII7;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Putative glutathione-dependent formaldehyde-activating enzyme {ECO:0000256|HAMAP-Rule:MF_03142};
DE EC=4.4.1.22 {ECO:0000256|HAMAP-Rule:MF_03142};
DE AltName: Full=S-(hydroxymethyl)glutathione synthase {ECO:0000256|HAMAP-Rule:MF_03142};
GN ORFNames=PV04_10353 {ECO:0000313|EMBL:KIW62152.1};
OS Phialophora macrospora.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Phialophora.
OX NCBI_TaxID=1851006 {ECO:0000313|EMBL:KIW62152.1, ECO:0000313|Proteomes:UP000054266};
RN [1] {ECO:0000313|EMBL:KIW62152.1, ECO:0000313|Proteomes:UP000054266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 27337 {ECO:0000313|EMBL:KIW62152.1,
RC ECO:0000313|Proteomes:UP000054266};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Capronia semiimmersa CBS27337.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the condensation of formaldehyde and glutathione to
CC S-hydroxymethylglutathione. {ECO:0000256|HAMAP-Rule:MF_03142}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-(hydroxymethyl)glutathione = formaldehyde + glutathione;
CC Xref=Rhea:RHEA:22488, ChEBI:CHEBI:16842, ChEBI:CHEBI:57925,
CC ChEBI:CHEBI:58758; EC=4.4.1.22; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_03142};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_03142};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000256|HAMAP-
CC Rule:MF_03142};
CC -!- PATHWAY: One-carbon metabolism; formaldehyde degradation; formate from
CC formaldehyde (glutathione route): step 1/3. {ECO:0000256|HAMAP-
CC Rule:MF_03142}.
CC -!- SIMILARITY: Belongs to the Gfa family. {ECO:0000256|ARBA:ARBA00005495,
CC ECO:0000256|HAMAP-Rule:MF_03142}.
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DR EMBL; KN846963; KIW62152.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D2DII7; -.
DR STRING; 5601.A0A0D2DII7; -.
DR HOGENOM; CLU_090716_0_0_1; -.
DR OrthoDB; 2405678at2759; -.
DR UniPathway; UPA00562; UER00621.
DR Proteomes; UP000054266; Unassembled WGS sequence.
DR GO; GO:0051907; F:S-(hydroxymethyl)glutathione synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046294; P:formaldehyde catabolic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.90.1590.10; glutathione-dependent formaldehyde- activating enzyme (gfa); 1.
DR HAMAP; MF_00723; Formald_GSH; 1.
DR InterPro; IPR006913; CENP-V/GFA.
DR InterPro; IPR014185; Formald_GSH.
DR InterPro; IPR011057; Mss4-like_sf.
DR NCBIfam; TIGR02820; formald_GSH; 1.
DR PANTHER; PTHR33337:SF40; CENP-V_GFA DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR33337; GFA DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF04828; GFA; 1.
DR PIRSF; PIRSF033318; Formald_GSH; 1.
DR SUPFAM; SSF51316; Mss4-like; 1.
DR PROSITE; PS51891; CENP_V_GFA; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_03142};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_03142};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_03142}.
FT DOMAIN 20..166
FT /note="CENP-V/GFA"
FT /evidence="ECO:0000259|PROSITE:PS51891"
FT BINDING 27
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="structural"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03142"
FT BINDING 29
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="structural"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03142"
FT BINDING 48
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03142"
FT BINDING 50
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03142"
FT BINDING 53
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03142"
FT BINDING 95
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="structural"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03142"
FT BINDING 98
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="structural"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03142"
SQ SEQUENCE 190 AA; 20638 MW; 8233F55E8EA82F7E CRC64;
MAPKLHPLID NGLVKGQPNF PGGTLRCRCK SNPVEVELKG NVLHNHACGC SQCWKPEGAL
FSIVAVIPDA NVKVTKNGDK LAVVNPEATI LRYACKDCGV HMYGPIEKDH AFKGLSFVHV
ELSDDKGWQE PQFAAFVSSL IEQGYPPEKM GEVRQRLKEI GLEPYDALSP PLMDALATFA
AEKAGKGSKL
//
