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GFA_EMENI
ID   GFA_EMENI               Reviewed;         197 AA.
AC   C8VDQ3; Q5AV96;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   03-NOV-2009, sequence version 1.
DT   03-AUG-2022, entry version 64.
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=AN11015, AN7784;
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS   M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Nidulantes.
OX   NCBI_TaxID=227321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA   Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA   Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA   Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA   Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA   Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA   Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA   Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA   Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA   Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA   Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA   Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA   Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA   Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA   van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA   Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA   Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA   Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA   Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA   Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA   van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA   Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA   Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT   effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
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=EAA61572.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AACD01000132; EAA61572.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; BN001304; CBF80099.1; -; Genomic_DNA.
DR   AlphaFoldDB; C8VDQ3; -.
DR   SMR; C8VDQ3; -.
DR   STRING; 227321.C8VDQ3; -.
DR   EnsemblFungi; CBF80099; CBF80099; ANIA_11015.
DR   EnsemblFungi; EAA61572; EAA61572; AN7784.2.
DR   VEuPathDB; FungiDB:AN11015; -.
DR   eggNOG; ENOG502SKH9; Eukaryota.
DR   HOGENOM; CLU_003538_1_0_1; -.
DR   OMA; ECGTHMY; -.
DR   OrthoDB; 1326510at2759; -.
DR   UniPathway; UPA00562; UER00621.
DR   Proteomes; UP000000560; Chromosome IV.
DR   Proteomes; UP000005890; 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..197
FT                   /note="Putative glutathione-dependent formaldehyde-
FT                   activating enzyme"
FT                   /id="PRO_0000406157"
FT   DOMAIN          22..171
FT                   /note="CENP-V/GFA"
FT                   /evidence="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         31
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         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         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         55
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         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"
FT   BINDING         100
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   197 AA;  21100 MW;  6CEF1F1D71CA66BD CRC64;
     MSSSLPLHPL LDNGISQGKP NFPGGKLYCH CASNKVEITL TSDVLHNHAC GCSKCWKPKG
     SIFSVVGVVP TSALSVTANA SKLAIIDKNA PIQRYACKEC GVHLYGRIEV EHPFKGLDFV
     HVELSEGGGK EGWQGVQFAG FVSSLIGQGL DPELVPGVRE RLKSLGLENY DALSPPLMDA
     IATWNAKRDG VVFRSSL
 
 
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