GFA_RHILO
ID GFA_RHILO Reviewed; 189 AA.
AC Q98LU4;
DT 07-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 07-NOV-2003, sequence version 2.
DT 03-AUG-2022, entry version 101.
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=mlr0874;
OS Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
OS (Mesorhizobium loti (strain MAFF 303099)).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Phyllobacteriaceae; Mesorhizobium.
OX NCBI_TaxID=266835;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 29417 / CECT 9101 / MAFF 303099;
RX PubMed=11214968; DOI=10.1093/dnares/7.6.331;
RA Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S.,
RA Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y.,
RA Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y.,
RA Nakayama S., Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M.,
RA Tabata S.;
RT "Complete genome structure of the nitrogen-fixing symbiotic bacterium
RT Mesorhizobium loti.";
RL DNA Res. 7:331-338(2000).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB48369.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BA000012; BAB48369.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_032930445.1; NC_002678.2.
DR AlphaFoldDB; Q98LU4; -.
DR SMR; Q98LU4; -.
DR STRING; 266835.14021758; -.
DR EnsemblBacteria; BAB48369; BAB48369; BAB48369.
DR GeneID; 66683808; -.
DR KEGG; mlo:mlr0874; -.
DR eggNOG; COG3791; Bacteria.
DR HOGENOM; CLU_090716_0_0_5; -.
DR OrthoDB; 1555973at2; -.
DR UniPathway; UPA00562; UER00621.
DR Proteomes; UP000000552; 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..189
FT /note="Glutathione-dependent formaldehyde-activating
FT enzyme"
FT /id="PRO_0000220322"
FT DOMAIN 20..166
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; 20125 MW; 39BB5DF9208FB4CE CRC64;
MAEKLHPRID NGLPKESASF AGGTLVCACT SKPVKVKVKG QIAHNHACGC TKCWKPEGAI
FSVVAVAGTG DVTVTENGDK LKVVDASALI QRHACTGCGV HMHGPVERDH AFKGLTFIHP
ERFVEDGWSP PGFTAFVSSI IESGVDPKRM DGIRAQLRTI GLEPYDCLNP GLMDYIATWT
AKKSGALPA
