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GFA_PENRW
ID   GFA_PENRW               Reviewed;         191 AA.
AC   B6HE56;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 1.
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   ORFNames=Pc20g15670;
OS   Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin
OS   54-1255) (Penicillium chrysogenum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC   Penicillium chrysogenum species complex.
OX   NCBI_TaxID=500485;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255;
RX   PubMed=18820685; DOI=10.1038/nbt.1498;
RA   van den Berg M.A., Albang R., Albermann K., Badger J.H., Daran J.-M.,
RA   Driessen A.J.M., Garcia-Estrada C., Fedorova N.D., Harris D.M.,
RA   Heijne W.H.M., Joardar V.S., Kiel J.A.K.W., Kovalchuk A., Martin J.F.,
RA   Nierman W.C., Nijland J.G., Pronk J.T., Roubos J.A., van der Klei I.J.,
RA   van Peij N.N.M.E., Veenhuis M., von Doehren H., Wagner C., Wortman J.R.,
RA   Bovenberg R.A.L.;
RT   "Genome sequencing and analysis of the filamentous fungus Penicillium
RT   chrysogenum.";
RL   Nat. Biotechnol. 26:1161-1168(2008).
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; AM920435; CAP86896.1; -; Genomic_DNA.
DR   RefSeq; XP_002564039.1; XM_002563993.1.
DR   AlphaFoldDB; B6HE56; -.
DR   SMR; B6HE56; -.
DR   STRING; 1108849.XP_002564039.1; -.
DR   EnsemblFungi; CAP86896; CAP86896; PCH_Pc20g15670.
DR   GeneID; 8303824; -.
DR   KEGG; pcs:Pc20g15670; -.
DR   VEuPathDB; FungiDB:PCH_Pc20g15670; -.
DR   eggNOG; ENOG502SKH9; Eukaryota.
DR   HOGENOM; CLU_090716_0_0_1; -.
DR   OMA; ECGTHMY; -.
DR   OrthoDB; 1326510at2759; -.
DR   BioCyc; PCHR:PC20G15670-MON; -.
DR   UniPathway; UPA00562; UER00621.
DR   Proteomes; UP000000724; Contig Pc00c20.
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_0000406160"
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;  20587 MW;  9A42224AC773B8D4 CRC64;
     MAPSLHPLID NGITPGSGSF AGGKLRCHCA SDRVEVTLNS NVAHNHACGC SKCWKPSGSL
     FSIVGVVPRD AVSVTANASK LSVVDKEATI QRYGCKDCGV HLFGRIEKDH PFRGLDFVHV
     ELSDEKGWQE PQFAGFVSSI IEQGSHPKEM DEVRAKFKAL GLQTYDVLSP ALMDLISTFT
     AQASGIRFAN L
 
 
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