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GFA_BRASB
ID   GFA_BRASB               Reviewed;         187 AA.
AC   A5EP16;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   03-AUG-2022, entry version 82.
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=BBta_5971;
OS   Bradyrhizobium sp. (strain BTAi1 / ATCC BAA-1182).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Bradyrhizobium; unclassified Bradyrhizobium.
OX   NCBI_TaxID=288000;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BTAi1 / ATCC BAA-1182;
RX   PubMed=17540897; DOI=10.1126/science.1139548;
RA   Giraud E., Moulin L., Vallenet D., Barbe V., Cytryn E., Avarre J.-C.,
RA   Jaubert M., Simon D., Cartieaux F., Prin Y., Bena G., Hannibal L.,
RA   Fardoux J., Kojadinovic M., Vuillet L., Lajus A., Cruveiller S., Rouy Z.,
RA   Mangenot S., Segurens B., Dossat C., Franck W.L., Chang W.-S., Saunders E.,
RA   Bruce D., Richardson P., Normand P., Dreyfus B., Pignol D., Stacey G.,
RA   Emerich D., Vermeglio A., Medigue C., Sadowsky M.;
RT   "Legumes symbioses: absence of nod genes in photosynthetic bradyrhizobia.";
RL   Science 316:1307-1312(2007).
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; CP000494; ABQ37910.1; -; Genomic_DNA.
DR   RefSeq; WP_012045861.1; NC_009485.1.
DR   AlphaFoldDB; A5EP16; -.
DR   SMR; A5EP16; -.
DR   STRING; 288000.BBta_5971; -.
DR   EnsemblBacteria; ABQ37910; ABQ37910; BBta_5971.
DR   KEGG; bbt:BBta_5971; -.
DR   eggNOG; COG3791; Bacteria.
DR   HOGENOM; CLU_090716_0_0_5; -.
DR   OMA; ECGTHMY; -.
DR   OrthoDB; 1555973at2; -.
DR   UniPathway; UPA00562; UER00621.
DR   Proteomes; UP000000246; 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..187
FT                   /note="Glutathione-dependent formaldehyde-activating
FT                   enzyme"
FT                   /id="PRO_1000045836"
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   187 AA;  19984 MW;  8097A5B205AD70D6 CRC64;
     MTVHIHPYVD NGVKQGSGHF AGGTLVCKCH DRPVKVAVKG DVAHNHACGC TKCWKPSGAT
     FSVIAVVPRQ NVTVLENGDK LKIVDPSAVI QRYACTGCGT HMYGRIENTG HPFYGLDFIH
     PELFQEQGSA APAFAAFVSS VIESGVKPEQ MGEIRARLKE LGLEPYDCLS PALMDAIATH
     VAKAKAA
 
 
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