GFAL_HALED
ID GFAL_HALED Reviewed; 157 AA.
AC E1VBT6; Q2WBH8;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 1.
DT 03-AUG-2022, entry version 50.
DE RecName: Full=Putative glutathione-dependent formaldehyde-activating enzyme;
DE EC=4.4.1.22;
GN OrderedLocusNames=HELO_2322;
OS Halomonas elongata (strain ATCC 33173 / DSM 2581 / NBRC 15536 / NCIMB 2198
OS / 1H9).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=768066;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 33173 / DSM 2581 / NBRC 15536 / NCIMB 2198 / 1H9;
RX PubMed=16872527; DOI=10.1186/1746-1448-2-10;
RA Kurz M., Brunig A.N., Galinski E.A.;
RT "NhaD type sodium/proton-antiporter of Halomonas elongata: a salt stress
RT response mechanism in marine habitats?";
RL Saline Syst. 2:10-10(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33173 / DSM 2581 / NBRC 15536 / NCIMB 2198 / 1H9;
RX PubMed=20849449; DOI=10.1111/j.1462-2920.2010.02336.x;
RA Schwibbert K., Marin-Sanguino A., Bagyan I., Heidrich G., Lentzen G.,
RA Seitz H., Rampp M., Schuster S.C., Klenk H.P., Pfeiffer F., Oesterhelt D.,
RA Kunte H.J.;
RT "A blueprint of ectoine metabolism from the genome of the industrial
RT producer Halomonas elongata DSM 2581(T).";
RL Environ. Microbiol. 13:1973-1994(2011).
CC -!- FUNCTION: Catalyzes the condensation of formaldehyde and glutathione to
CC S-hydroxymethylglutathione. {ECO:0000250}.
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;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU01239};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000255|PROSITE-
CC ProRule:PRU01239};
CC -!- PATHWAY: One-carbon metabolism; formaldehyde degradation; formate from
CC formaldehyde (glutathione route): step 1/3.
CC -!- SIMILARITY: Belongs to the Gfa family. {ECO:0000305}.
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DR EMBL; AM167899; CAJ44470.1; -; Genomic_DNA.
DR EMBL; FN869568; CBV42206.1; -; Genomic_DNA.
DR AlphaFoldDB; E1VBT6; -.
DR STRING; 768066.HELO_2322; -.
DR EnsemblBacteria; CBV42206; CBV42206; HELO_2322.
DR KEGG; hel:HELO_2322; -.
DR eggNOG; COG3791; Bacteria.
DR HOGENOM; CLU_116419_0_0_6; -.
DR OMA; LEGSCQC; -.
DR UniPathway; UPA00562; UER00621.
DR Proteomes; UP000008707; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051907; F:S-(hydroxymethyl)glutathione synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0046294; P:formaldehyde catabolic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR006913; CENP-V/GFA.
DR InterPro; IPR011057; Mss4-like_sf.
DR Pfam; PF04828; GFA; 1.
DR SUPFAM; SSF51316; SSF51316; 1.
DR PROSITE; PS51891; CENP_V_GFA; 1.
PE 3: Inferred from homology;
KW Lyase; Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..157
FT /note="Putative glutathione-dependent formaldehyde-
FT activating enzyme"
FT /id="PRO_0000423825"
FT DOMAIN 3..134
FT /note="CENP-V/GFA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01239"
FT BINDING 7
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="structural"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01239"
FT BINDING 9
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="structural"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01239"
FT BINDING 27
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01239"
FT BINDING 29
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01239"
FT BINDING 32
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01239"
FT BINDING 79
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="structural"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01239"
FT BINDING 82
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="structural"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01239"
SQ SEQUENCE 157 AA; 17542 MW; C4C0E989E9F214D4 CRC64;
MLLEGSCHCG AVRFRVVSPH PYPFNRCYCS ICRKTAGGGG YAINLSGDAD TLVVHGAEHT
SIYQAEIDGL TSPGERHFCS RCASALWVFD PRWPELVHPF ASAIDSDLPR PPERVHLMLE
NKPDWVEIES REQDRCFAGY PDESIAEWHA RLGLEEG
