位置:首页 > 蛋白库 > GFA_BRASO
GFA_BRASO
ID   GFA_BRASO               Reviewed;         187 AA.
AC   A4YZ37;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 86.
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=BRADO5487;
OS   Bradyrhizobium sp. (strain ORS 278).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Bradyrhizobium; unclassified Bradyrhizobium.
OX   NCBI_TaxID=114615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ORS 278;
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CU234118; CAL79163.1; -; Genomic_DNA.
DR   RefSeq; WP_012029076.1; NC_009445.1.
DR   AlphaFoldDB; A4YZ37; -.
DR   SMR; A4YZ37; -.
DR   STRING; 114615.BRADO5487; -.
DR   EnsemblBacteria; CAL79163; CAL79163; BRADO5487.
DR   KEGG; bra:BRADO5487; -.
DR   eggNOG; COG3791; Bacteria.
DR   HOGENOM; CLU_090716_0_0_5; -.
DR   OMA; ECGTHMY; -.
DR   OrthoDB; 1555973at2; -.
DR   BioCyc; BSP114615:BRADO_RS25505-MON; -.
DR   UniPathway; UPA00562; UER00621.
DR   Proteomes; UP000001994; 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; Reference proteome; Zinc.
FT   CHAIN           1..187
FT                   /note="Glutathione-dependent formaldehyde-activating
FT                   enzyme"
FT                   /id="PRO_1000045837"
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;  19877 MW;  532ED70E612DA2E8 CRC64;
     MTVHIHPSVD HGVKQGSGHF AGGTLVCKCH DRPVKVGIKG DVAHNHACGC TKCWKPSGAT
     FSVVAVVPRQ NVTVLENGDK LKIVDASAVI QRYACTGCGT HMYGRIENTG HPFYGLDFIH
     PELFQEQGSA APGFAAFVSS VIESGVKPEQ MGEIRARLKE LGLEPYDCLS PALMDAIATH
     VAKAKAA
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024