ID A0A369U1T8_PARVE Unreviewed; 194 AA. AC A0A369U1T8; DT 07-NOV-2018, integrated into UniProtKB/TrEMBL. DT 07-NOV-2018, sequence version 1. DT 03-MAY-2023, entry version 12. DE RecName: Full=Glutathione-dependent formaldehyde-activating enzyme {ECO:0000256|HAMAP-Rule:MF_00723}; DE EC=4.4.1.22 {ECO:0000256|HAMAP-Rule:MF_00723}; DE AltName: Full=S-(hydroxymethyl)glutathione synthase {ECO:0000256|HAMAP-Rule:MF_00723}; GN Name=gfa {ECO:0000256|HAMAP-Rule:MF_00723, GN ECO:0000313|EMBL:RDD71393.1}; GN ORFNames=DVR11_11165 {ECO:0000313|EMBL:RDD71393.1}; OS Paracoccus versutus (Thiobacillus versutus). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales; OC Paracoccaceae; Paracoccus. OX NCBI_TaxID=34007 {ECO:0000313|EMBL:RDD71393.1, ECO:0000313|Proteomes:UP000253839}; RN [1] {ECO:0000313|EMBL:RDD71393.1, ECO:0000313|Proteomes:UP000253839} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MAL 1HM19 {ECO:0000313|EMBL:RDD71393.1, RC ECO:0000313|Proteomes:UP000253839}; RA Chulalaksananukul W.; RT "Whole Genome Sequencing of Paracoccus versutus strain MAL 1HM19."; RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the condensation of formaldehyde and glutathione to CC S-hydroxymethylglutathione. {ECO:0000256|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:0000256|HAMAP- CC Rule:MF_00723}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00723}; CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000256|HAMAP- CC Rule:MF_00723}; CC -!- PATHWAY: One-carbon metabolism; formaldehyde degradation; formate from CC formaldehyde (glutathione route): step 1/3. {ECO:0000256|HAMAP- CC Rule:MF_00723}. CC -!- SIMILARITY: Belongs to the Gfa family. {ECO:0000256|ARBA:ARBA00005495, CC ECO:0000256|HAMAP-Rule:MF_00723}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:RDD71393.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; QPML01000046; RDD71393.1; -; Genomic_DNA. DR AlphaFoldDB; A0A369U1T8; -. DR EnsemblBacteria; RDD71393; RDD71393; DVR11_11165. DR UniPathway; UPA00562; UER00621. DR Proteomes; UP000253839; 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 Gene3D; 3.90.1590.10; glutathione-dependent formaldehyde- activating enzyme (gfa); 1. 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 PANTHER; PTHR33337:SF40; CENP-V/GFA DOMAIN-CONTAINING PROTEIN-RELATED; 1. DR PANTHER; PTHR33337; GFA DOMAIN-CONTAINING PROTEIN; 1. DR Pfam; PF04828; GFA; 1. DR PIRSF; PIRSF033318; Formald_GSH; 1. DR SUPFAM; SSF51316; Mss4-like; 1. DR TIGRFAMs; TIGR02820; formald_GSH; 1. DR PROSITE; PS51891; CENP_V_GFA; 1. PE 3: Inferred from homology; KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00723}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_00723}; Zinc {ECO:0000256|HAMAP-Rule:MF_00723}. FT DOMAIN 24..171 FT /note="CENP-V/GFA" FT /evidence="ECO:0000259|PROSITE:PS51891" FT BINDING 31 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /ligand_note="structural" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00723" FT BINDING 33 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /ligand_note="structural" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00723" FT BINDING 52 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00723" FT BINDING 54 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00723" FT BINDING 57 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00723" FT BINDING 99 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /ligand_note="structural" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00723" FT BINDING 102 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /ligand_note="structural" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00723" SQ SEQUENCE 194 AA; 20951 MW; 010F29E75667733D CRC64; MVDTSGVKIH PAVDNGIKPA QPGFAGGTLH CKCSTNPVRV AIRAQTAHNH VCGCTKCWKP EGAIFSQVAV VGRDAVEVLE GAEKLEIVNA EAPIQRHRCR DCGVHMYGRI ENRDHPFYGL DFVHTELSDE DGWAAPEFAA FVSSIIESGV DPSRMEAIRA RLRELGLEPY DALSPPLMDA IATHIAKRSG ALAA //