GFA_PODAN
ID GFA_PODAN Reviewed; 213 AA.
AC B2ACV0; A0A090CNE2;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 13-APR-2016, sequence version 3.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Putative glutathione-dependent formaldehyde-activating enzyme {ECO:0000255|HAMAP-Rule:MF_03142};
DE EC=4.4.1.22 {ECO:0000255|HAMAP-Rule:MF_03142};
DE AltName: Full=S-(hydroxymethyl)glutathione synthase {ECO:0000255|HAMAP-Rule:MF_03142};
GN OrderedLocusNames=Pa_3_11350; ORFNames=PODANS_3_11350;
OS Podospora anserina (strain S / ATCC MYA-4624 / DSM 980 / FGSC 10383)
OS (Pleurage anserina).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Podosporaceae; Podospora;
OC Podospora anserina.
OX NCBI_TaxID=515849;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383;
RX PubMed=18460219; DOI=10.1186/gb-2008-9-5-r77;
RA Espagne E., Lespinet O., Malagnac F., Da Silva C., Jaillon O., Porcel B.M.,
RA Couloux A., Aury J.-M., Segurens B., Poulain J., Anthouard V.,
RA Grossetete S., Khalili H., Coppin E., Dequard-Chablat M., Picard M.,
RA Contamine V., Arnaise S., Bourdais A., Berteaux-Lecellier V., Gautheret D.,
RA de Vries R.P., Battaglia E., Coutinho P.M., Danchin E.G.J., Henrissat B.,
RA El Khoury R., Sainsard-Chanet A., Boivin A., Pinan-Lucarre B., Sellem C.H.,
RA Debuchy R., Wincker P., Weissenbach J., Silar P.;
RT "The genome sequence of the model ascomycete fungus Podospora anserina.";
RL Genome Biol. 9:R77.1-R77.22(2008).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383;
RX PubMed=24558260; DOI=10.1534/genetics.113.159988;
RA Grognet P., Bidard F., Kuchly C., Tong L.C.H., Coppin E., Benkhali J.A.,
RA Couloux A., Wincker P., Debuchy R., Silar P.;
RT "Maintaining two mating types: Structure of the mating type locus and its
RT role in heterokaryosis in Podospora anserina.";
RL Genetics 197:421-432(2014).
CC -!- FUNCTION: Catalyzes the condensation of formaldehyde and glutathione to
CC S-hydroxymethylglutathione. {ECO:0000255|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:0000255|HAMAP-
CC Rule:MF_03142};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03142,
CC ECO:0000255|PROSITE-ProRule:PRU01239};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000255|HAMAP-Rule:MF_03142,
CC ECO:0000255|PROSITE-ProRule:PRU01239};
CC -!- PATHWAY: One-carbon metabolism; formaldehyde degradation; formate from
CC formaldehyde (glutathione route): step 1/3. {ECO:0000255|HAMAP-
CC Rule:MF_03142}.
CC -!- SIMILARITY: Belongs to the Gfa family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAP61265.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAP61265.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CDP27619.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CU633453; CAP61265.1; ALT_SEQ; Genomic_DNA.
DR EMBL; FO904938; CDP27619.1; ALT_INIT; Genomic_DNA.
DR RefSeq; XP_001903490.1; XM_001903455.1.
DR AlphaFoldDB; B2ACV0; -.
DR SMR; B2ACV0; -.
DR STRING; 5145.XP_001903490.1; -.
DR EnsemblFungi; CAP61265; CAP61265; PODANS_3_11350.
DR GeneID; 6187609; -.
DR KEGG; pan:PODANSg505; -.
DR eggNOG; ENOG502SKH9; Eukaryota.
DR HOGENOM; CLU_090716_0_0_1; -.
DR OrthoDB; 1326510at2759; -.
DR UniPathway; UPA00562; UER00621.
DR Proteomes; UP000001197; Chromosome 3.
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 HAMAP; MF_00723; Formald_GSH; 1.
DR InterPro; IPR006913; CENP-V/GFA.
DR InterPro; IPR014185; Formald_GSH.
DR InterPro; IPR011057; Mss4-like_sf.
DR Pfam; PF04828; GFA; 1.
DR PIRSF; PIRSF033318; Formald_GSH; 1.
DR SUPFAM; SSF51316; SSF51316; 1.
DR TIGRFAMs; TIGR02820; formald_GSH; 1.
DR PROSITE; PS51891; CENP_V_GFA; 1.
PE 3: Inferred from homology;
KW Lyase; Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..213
FT /note="Putative glutathione-dependent formaldehyde-
FT activating enzyme"
FT /id="PRO_0000406163"
FT DOMAIN 19..165
FT /note="CENP-V/GFA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01239"
FT BINDING 26
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="structural"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03142,
FT ECO:0000255|PROSITE-ProRule:PRU01239"
FT BINDING 28
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="structural"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03142,
FT ECO:0000255|PROSITE-ProRule:PRU01239"
FT BINDING 47
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03142,
FT ECO:0000255|PROSITE-ProRule:PRU01239"
FT BINDING 49
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03142,
FT ECO:0000255|PROSITE-ProRule:PRU01239"
FT BINDING 52
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03142,
FT ECO:0000255|PROSITE-ProRule:PRU01239"
FT BINDING 94
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="structural"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03142,
FT ECO:0000255|PROSITE-ProRule:PRU01239"
FT BINDING 97
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="structural"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03142,
FT ECO:0000255|PROSITE-ProRule:PRU01239"
SQ SEQUENCE 213 AA; 23150 MW; 1BFC52896DD673B8 CRC64;
MVSLHPLLDN GITPGSDSFP GGTLKCLCPS FPVEITLTTN VAHNHACGCS KCWKPAGALF
SIVGVVPRDE LSVTANGDKL AIVDESAVIQ RYACKECGTH LYRRIEKEHP FYGLDFVHAE
LSEEEGWQEP QFAAFVSSVI EQGFDPAKIG EVRARFRELG LETYDSLSPP LMDAIAAWTG
RKNGKYDLHS WLDCERRKGG GGGGQPGGVV CRL
