GFA_PARDP
ID GFA_PARDP Reviewed; 194 AA.
AC A1AXY8;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Glutathione-dependent formaldehyde-activating enzyme {ECO:0000255|HAMAP-Rule:MF_00723};
DE EC=4.4.1.22 {ECO:0000255|HAMAP-Rule:MF_00723};
DE AltName: Full=S-(hydroxymethyl)glutathione synthase {ECO:0000255|HAMAP-Rule:MF_00723};
GN Name=gfa {ECO:0000255|HAMAP-Rule:MF_00723}; OrderedLocusNames=Pden_0015;
OS Paracoccus denitrificans (strain Pd 1222).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Paracoccus.
OX NCBI_TaxID=318586;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pd 1222;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Spiro S.,
RA Richardson D.J., Moir J.W.B., Ferguson S.J., van Spanning R.J.M.,
RA Richardson P.;
RT "Complete sequence of chromosome 1 of Paracoccus denitrificans PD1222.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the condensation of formaldehyde and glutathione to
CC S-hydroxymethylglutathione. {ECO:0000255|HAMAP-Rule:MF_00723}.
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_00723};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00723,
CC ECO:0000255|PROSITE-ProRule:PRU01239};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000255|HAMAP-Rule:MF_00723,
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_00723}.
CC -!- SIMILARITY: Belongs to the Gfa family. {ECO:0000255|HAMAP-
CC Rule:MF_00723}.
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DR EMBL; CP000489; ABL68132.1; -; Genomic_DNA.
DR RefSeq; WP_011746365.1; NC_008686.1.
DR AlphaFoldDB; A1AXY8; -.
DR SMR; A1AXY8; -.
DR STRING; 318586.Pden_0015; -.
DR PRIDE; A1AXY8; -.
DR EnsemblBacteria; ABL68132; ABL68132; Pden_0015.
DR KEGG; pde:Pden_0015; -.
DR eggNOG; COG3791; Bacteria.
DR HOGENOM; CLU_090716_0_0_5; -.
DR OMA; ECGTHMY; -.
DR UniPathway; UPA00562; UER00621.
DR Proteomes; UP000000361; Chromosome 1.
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..194
FT /note="Glutathione-dependent formaldehyde-activating
FT enzyme"
FT /id="PRO_1000045838"
FT DOMAIN 24..171
FT /note="CENP-V/GFA"
FT /evidence="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_00723,
FT ECO:0000255|PROSITE-ProRule:PRU01239"
FT BINDING 33
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_00723,
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_00723,
FT ECO:0000255|PROSITE-ProRule:PRU01239"
FT BINDING 54
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_00723,
FT ECO:0000255|PROSITE-ProRule:PRU01239"
FT BINDING 57
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_00723,
FT ECO:0000255|PROSITE-ProRule:PRU01239"
FT BINDING 99
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_00723,
FT ECO:0000255|PROSITE-ProRule:PRU01239"
FT BINDING 102
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_00723,
FT ECO:0000255|PROSITE-ProRule:PRU01239"
SQ SEQUENCE 194 AA; 20967 MW; 95B6E386B1756619 CRC64;
MVDTSGVKIH PAVDNGIKPA QPGFAGGTLH CKCSTNPVRV AVRAQTAHNH VCGCTKCWKP
EGAIFSQVAV VGRDALEVLE GAEKLEIVNA EAPIQRHRCR DCGVHMYGRI ENRDHPFYGL
DFVHTELSDE DGWSAPEFAA FVSSIIESGV DPSRMEAIRA RLRELGLEPY DALSPPLMDA
IATHIAKRSG ALAA
