(data stored in ACNUC7421 zone)

SWISSPROT: 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   11-DEC-2019, entry version 90.
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; Rhizobiales;
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};
DR   EMBL; BA000012; BAB48369.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_032930445.1; NC_002678.2.
DR   SMR; Q98LU4; -.
DR   STRING; 266835.14021758; -.
DR   PRIDE; Q98LU4; -.
DR   EnsemblBacteria; BAB48369; BAB48369; BAB48369.
DR   KEGG; mlo:mlr0874; -.
DR   eggNOG; ENOG4108QBQ; Bacteria.
DR   eggNOG; COG3791; LUCA.
DR   HOGENOM; HOG000230144; -.
DR   KO; K03396; -.
DR   OrthoDB; 1555973at2; -.
DR   BioCyc; MLOT266835:G1G20-711-MONOMER; -.
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; IPR014185; Formald_GSH.
DR   InterPro; IPR006913; GFA/CENP-V.
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;
DR   PRODOM; Q98LU4.
DR   SWISS-2DPAGE; Q98LU4.
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   METAL           27
FT                   /note="Zinc 1; structural"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00723,
FT                   ECO:0000255|PROSITE-ProRule:PRU01239"
FT   METAL           29
FT                   /note="Zinc 1; structural"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00723,
FT                   ECO:0000255|PROSITE-ProRule:PRU01239"
FT   METAL           48
FT                   /note="Zinc 2; catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00723,
FT                   ECO:0000255|PROSITE-ProRule:PRU01239"
FT   METAL           50
FT                   /note="Zinc 2; catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00723,
FT                   ECO:0000255|PROSITE-ProRule:PRU01239"
FT   METAL           53
FT                   /note="Zinc 2; catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00723,
FT                   ECO:0000255|PROSITE-ProRule:PRU01239"
FT   METAL           95
FT                   /note="Zinc 1; structural"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00723,
FT                   ECO:0000255|PROSITE-ProRule:PRU01239"
FT   METAL           98
FT                   /note="Zinc 1; 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
//

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