GFA_RHOP5
ID GFA_RHOP5 Reviewed; 189 AA.
AC Q07HI5;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, 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=RPE_4679;
OS Rhodopseudomonas palustris (strain BisA53).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Rhodopseudomonas.
OX NCBI_TaxID=316055;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BisA53;
RG US DOE Joint Genome Institute;
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 Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Pelletier D.A., Kyrpides N., Kim E., Harwood C.S., Oda Y.,
RA Richardson P.;
RT "Complete sequence of Rhodopseudomonas palustris BisA53.";
RL Submitted (SEP-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; CP000463; ABJ08599.1; -; Genomic_DNA.
DR RefSeq; WP_011666054.1; NC_008435.1.
DR AlphaFoldDB; Q07HI5; -.
DR SMR; Q07HI5; -.
DR STRING; 316055.RPE_4679; -.
DR EnsemblBacteria; ABJ08599; ABJ08599; RPE_4679.
DR KEGG; rpe:RPE_4679; -.
DR eggNOG; COG3791; Bacteria.
DR HOGENOM; CLU_090716_0_0_5; -.
DR OMA; ECGTHMY; -.
DR OrthoDB; 1555973at2; -.
DR UniPathway; UPA00562; UER00621.
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; Zinc.
FT CHAIN 1..189
FT /note="Glutathione-dependent formaldehyde-activating
FT enzyme"
FT /id="PRO_1000045839"
FT DOMAIN 20..167
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_00723,
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_00723,
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_00723,
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_00723,
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_00723,
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_00723,
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_00723,
FT ECO:0000255|PROSITE-ProRule:PRU01239"
SQ SEQUENCE 189 AA; 20117 MW; 858B0B557F13BD13 CRC64;
MTVHIHPAVD NGVKKGTGSF AGGTLVCKCS DRPVKVGIKG DVAHNHACGC TKCWKPDGAT
FSVVAVVPRG NVTVLENGDK LQIVDTSATI QRHACKVCGT HMFGRIENTG HPFYGLDFIH
PELFYEQGSA APEFAAFVSS IIESGVDPAQ MPEIRSRLKE LGLEPYDCLS PALMDAIAGH
IAKTSRKAA
