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GFA_PYRTT
ID   GFA_PYRTT               Reviewed;         190 AA.
AC   E3S405;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2011, sequence version 1.
DT   03-AUG-2022, entry version 44.
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=PTT_17259;
OS   Pyrenophora teres f. teres (strain 0-1) (Barley net blotch fungus)
OS   (Drechslera teres f. teres).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC   Pyrenophora.
OX   NCBI_TaxID=861557;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=0-1;
RX   PubMed=21067574; DOI=10.1186/gb-2010-11-11-r109;
RA   Ellwood S.R., Liu Z., Syme R.A., Lai Z., Hane J.K., Keiper F., Moffat C.S.,
RA   Oliver R.P., Friesen T.L.;
RT   "A first genome assembly of the barley fungal pathogen Pyrenophora teres f.
RT   teres.";
RL   Genome Biol. 11:R109.1-R109.14(2010).
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; GL537081; EFQ87295.1; -; Genomic_DNA.
DR   RefSeq; XP_003304610.1; XM_003304562.1.
DR   AlphaFoldDB; E3S405; -.
DR   SMR; E3S405; -.
DR   STRING; 861557.E3S405; -.
DR   EnsemblFungi; EFQ87295; EFQ87295; PTT_17259.
DR   KEGG; pte:PTT_17259; -.
DR   eggNOG; ENOG502SKH9; Eukaryota.
DR   HOGENOM; CLU_090716_0_0_1; -.
DR   OrthoDB; 1326510at2759; -.
DR   UniPathway; UPA00562; UER00621.
DR   Proteomes; UP000001067; 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..190
FT                   /note="Putative glutathione-dependent formaldehyde-
FT                   activating enzyme"
FT                   /id="PRO_0000406164"
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   190 AA;  20652 MW;  315C8CFA240EE454 CRC64;
     MPSIHPSIDN GITKGDPNFK GGKLYCHCPT RKVEVTLAGN VAHNHACGCS KCWKPEGALF
     SVVGVISKDA VSVTANGDKL HIVDESAAIQ RNACKECGVH LFGRIIVDHP FKGLDFVHAE
     LSPQKGWQEP QFAAFVSSII EQGFHPSEMD AIREKFRKVG LQPYDVLSPT LMDLIATYTA
     QKSGKLPAKL
 
 
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