GFA_XANC5
ID GFA_XANC5 Reviewed; 191 AA.
AC Q3BXJ3;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 98.
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=XCV0789;
OS Xanthomonas campestris pv. vesicatoria (strain 85-10).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=316273;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=85-10;
RX PubMed=16237009; DOI=10.1128/jb.187.21.7254-7266.2005;
RA Thieme F., Koebnik R., Bekel T., Berger C., Boch J., Buettner D.,
RA Caldana C., Gaigalat L., Goesmann A., Kay S., Kirchner O., Lanz C.,
RA Linke B., McHardy A.C., Meyer F., Mittenhuber G., Nies D.H.,
RA Niesbach-Kloesgen U., Patschkowski T., Rueckert C., Rupp O., Schneiker S.,
RA Schuster S.C., Vorhoelter F.J., Weber E., Puehler A., Bonas U., Bartels D.,
RA Kaiser O.;
RT "Insights into genome plasticity and pathogenicity of the plant pathogenic
RT Bacterium Xanthomonas campestris pv. vesicatoria revealed by the complete
RT genome sequence.";
RL J. Bacteriol. 187:7254-7266(2005).
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; AM039952; CAJ22420.1; -; Genomic_DNA.
DR RefSeq; WP_011346393.1; NZ_CP017190.1.
DR AlphaFoldDB; Q3BXJ3; -.
DR SMR; Q3BXJ3; -.
DR STRING; 456327.BJD11_18865; -.
DR EnsemblBacteria; CAJ22420; CAJ22420; XCV0789.
DR KEGG; xcv:XCV0789; -.
DR eggNOG; COG3791; Bacteria.
DR HOGENOM; CLU_090716_0_0_6; -.
DR OMA; ECGTHMY; -.
DR UniPathway; UPA00562; UER00621.
DR Proteomes; UP000007069; Chromosome.
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..191
FT /note="Glutathione-dependent formaldehyde-activating
FT enzyme"
FT /id="PRO_1000045841"
FT DOMAIN 22..169
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_00723,
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_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 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 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_00723,
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_00723,
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_00723,
FT ECO:0000255|PROSITE-ProRule:PRU01239"
SQ SEQUENCE 191 AA; 20446 MW; 93F304A61FB178C0 CRC64;
MTNVSIHPSV DDGVARGGAE DFQGGTLECH CASDKVTVEV SAQTAHNHAC GCSKCWKPDG
AKFSVVAVVP RDNVKVTAHP EKLKIVDEGA TIQRHACTGC GVHLYGRIEN KDHAFYGLDF
VHTELSKQQG WSAPGFAAFV SSIIETGTPP EQMDGIRTRL TELGLPPYDC LSPALMDALS
AHVARKKGLL H
