GFA_COLGM
ID GFA_COLGM Reviewed; 191 AA.
AC E3QRY8;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 1.
DT 03-AUG-2022, entry version 43.
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 ORFNames=GLRG_08555;
OS Colletotrichum graminicola (strain M1.001 / M2 / FGSC 10212) (Maize
OS anthracnose fungus) (Glomerella graminicola).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum graminicola species complex.
OX NCBI_TaxID=645133;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M1.001 / M2 / FGSC 10212;
RX PubMed=22885923; DOI=10.1038/ng.2372;
RA O'Connell R.J., Thon M.R., Hacquard S., Amyotte S.G., Kleemann J.,
RA Torres M.F., Damm U., Buiate E.A., Epstein L., Alkan N., Altmueller J.,
RA Alvarado-Balderrama L., Bauser C.A., Becker C., Birren B.W., Chen Z.,
RA Choi J., Crouch J.A., Duvick J.P., Farman M.A., Gan P., Heiman D.,
RA Henrissat B., Howard R.J., Kabbage M., Koch C., Kracher B., Kubo Y.,
RA Law A.D., Lebrun M.-H., Lee Y.-H., Miyara I., Moore N., Neumann U.,
RA Nordstroem K., Panaccione D.G., Panstruga R., Place M., Proctor R.H.,
RA Prusky D., Rech G., Reinhardt R., Rollins J.A., Rounsley S., Schardl C.L.,
RA Schwartz D.C., Shenoy N., Shirasu K., Sikhakolli U.R., Stueber K.,
RA Sukno S.A., Sweigard J.A., Takano Y., Takahara H., Trail F.,
RA van der Does H.C., Voll L.M., Will I., Young S., Zeng Q., Zhang J.,
RA Zhou S., Dickman M.B., Schulze-Lefert P., Ver Loren van Themaat E.,
RA Ma L.-J., Vaillancourt L.J.;
RT "Lifestyle transitions in plant pathogenic Colletotrichum fungi deciphered
RT by genome and transcriptome analyses.";
RL Nat. Genet. 44:1060-1065(2012).
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}.
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DR EMBL; GG697372; EFQ33626.1; -; Genomic_DNA.
DR RefSeq; XP_008097646.1; XM_008099455.1.
DR AlphaFoldDB; E3QRY8; -.
DR SMR; E3QRY8; -.
DR STRING; 645133.E3QRY8; -.
DR EnsemblFungi; EFQ33626; EFQ33626; GLRG_08555.
DR GeneID; 24413920; -.
DR VEuPathDB; FungiDB:GLRG_08555; -.
DR eggNOG; ENOG502SKH9; Eukaryota.
DR HOGENOM; CLU_090716_0_0_1; -.
DR OrthoDB; 1326510at2759; -.
DR UniPathway; UPA00562; UER00621.
DR Proteomes; UP000008782; 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 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..191
FT /note="Putative glutathione-dependent formaldehyde-
FT activating enzyme"
FT /id="PRO_0000406158"
FT DOMAIN 20..166
FT /note="CENP-V/GFA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01239"
FT BINDING 27
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 29
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 48
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 50
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 53
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 95
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 98
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 191 AA; 20901 MW; F0BC9194866BA9B4 CRC64;
MAPTLHPLID NGITKGDPNF SGGTLRCHCR SKPVEVLLGG NVAHNHACGC SKCWKPAGSL
FSVVGVIPRE QVKVTANEEK LHIIDDSAVI LRNACKECGV HMYGRIEKPH PFKGLDFVHV
ELSDQKGWQE PQFAAFVSSI IEQGFNPKGT DGVRRKFKSV GLETYDTLSP TLVDLISTWT
AQQNGRLPAK L
