ID A0A1G9LF90_9RHOB Unreviewed; 243 AA.
AC A0A1G9LF90;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
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 ORFNames=SAMN04487971_11472 {ECO:0000313|EMBL:SDL60534.1};
OS Paracoccus chinensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Paracoccus.
OX NCBI_TaxID=525640 {ECO:0000313|EMBL:SDL60534.1, ECO:0000313|Proteomes:UP000199555};
RN [1] {ECO:0000313|EMBL:SDL60534.1, ECO:0000313|Proteomes:UP000199555}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.7655 {ECO:0000313|EMBL:SDL60534.1,
RC ECO:0000313|Proteomes:UP000199555};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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 ---------------------------------------------------------------------------
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; FNGE01000014; SDL60534.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G9LF90; -.
DR STRING; 525640.SAMN04487971_11472; -.
DR OrthoDB; 7765631at2; -.
DR UniPathway; UPA00562; UER00621.
DR Proteomes; UP000199555; 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 NCBIfam; TIGR02820; formald_GSH; 1.
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 SUPFAM; SSF51316; Mss4-like; 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};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00723}.
FT DOMAIN 24..171
FT /note="CENP-V/GFA"
FT /evidence="ECO:0000259|PROSITE:PS51891"
FT REGION 188..232
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 243 AA; 26360 MW; AAE2E0AFADF95D1A CRC64;
MATNQRVRIH PAVDNGVKQG NPEFSGGVLT CHCTNRLVKI RVGAQTAHNH VCGCTKCWKP
EGAIFSQVAV VSRDAIKVLE NGDKLQIVDK DAAIQRYACR DCGVHMYGRI ENRDHPFYGL
DFVHTELSEE EGWSAPEFAA FVSSVIESGV NPDRMDAIRA RLRELGLPPY DTLSPPLMDL
IATHAANRQA KPAPAAARQN ASPAPVQAAP KASPLPQRSS VPTPPASEGR SIIGRLMSRL
LGR
//
