UniProt: A0A0Q6ZHW1

Database: UniProt
Entry: A0A0Q6ZHW1_9BRAD

LinkDB:  A0A0Q6ZHW1_9BRAD 
Original site:  A0A0Q6ZHW1_9BRAD

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Ontology (4)   
   GO (4)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (9)   
   InterPro (6)   
   Pfam (2)   
   PROSITE (1)   
All databases (16)   

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ID   A0A0Q6ZHW1_9BRAD        Unreviewed;       375 AA.
AC   A0A0Q6ZHW1;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=S-(hydroxymethyl)glutathione dehydrogenase {ECO:0000256|ARBA:ARBA00012309, ECO:0000256|RuleBase:RU362016};
DE            EC=1.1.1.284 {ECO:0000256|ARBA:ARBA00012309, ECO:0000256|RuleBase:RU362016};
GN   ORFNames=ASC80_04730 {ECO:0000313|EMBL:KQW22663.1};
OS   Afipia sp. Root123D2.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Afipia.
OX   NCBI_TaxID=1736436 {ECO:0000313|EMBL:KQW22663.1, ECO:0000313|Proteomes:UP000051348};
RN   [1] {ECO:0000313|EMBL:KQW22663.1, ECO:0000313|Proteomes:UP000051348}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root123D2 {ECO:0000313|EMBL:KQW22663.1,
RC   ECO:0000313|Proteomes:UP000051348};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQW22663.1, ECO:0000313|Proteomes:UP000051348}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root123D2 {ECO:0000313|EMBL:KQW22663.1,
RC   ECO:0000313|Proteomes:UP000051348};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NAD(+) + S-(hydroxymethyl)glutathione = H(+) + NADH + S-
CC         formylglutathione; Xref=Rhea:RHEA:19985, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57688, ChEBI:CHEBI:57945,
CC         ChEBI:CHEBI:58758; EC=1.1.1.284;
CC         Evidence={ECO:0000256|ARBA:ARBA00001030,
CC         ECO:0000256|RuleBase:RU362016};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NADP(+) + S-(hydroxymethyl)glutathione = H(+) + NADPH + S-
CC         formylglutathione; Xref=Rhea:RHEA:19981, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57688, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:58758; EC=1.1.1.284;
CC         Evidence={ECO:0000256|ARBA:ARBA00001646};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU362016};
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. Class-III subfamily. {ECO:0000256|ARBA:ARBA00010902,
CC       ECO:0000256|RuleBase:RU362016}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KQW22663.1}.
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DR   EMBL; LMDP01000001; KQW22663.1; -; Genomic_DNA.
DR   RefSeq; WP_056293297.1; NZ_LMDP01000001.1.
DR   AlphaFoldDB; A0A0Q6ZHW1; -.
DR   STRING; 1736436.ASC80_04730; -.
DR   OrthoDB; 9770544at2; -.
DR   Proteomes; UP000051348; Unassembled WGS sequence.
DR   GO; GO:0106322; F:S-(hydroxymethyl)glutathione dehydrogenase NAD activity; IEA:UniProtKB-EC.
DR   GO; GO:0106321; F:S-(hydroxymethyl)glutathione dehydrogenase NADP activity; IEA:UniProtKB-EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006069; P:ethanol oxidation; IEA:InterPro.
DR   CDD; cd08300; alcohol_DH_class_III; 1.
DR   Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR013149; ADH-like_C.
DR   InterPro; IPR013154; ADH-like_N.
DR   InterPro; IPR014183; ADH_3.
DR   InterPro; IPR002328; ADH_Zn_CS.
DR   InterPro; IPR011032; GroES-like_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   NCBIfam; TIGR02818; adh_III_F_hyde; 1.
DR   PANTHER; PTHR43880; ALCOHOL DEHYDROGENASE; 1.
DR   PANTHER; PTHR43880:SF12; ALCOHOL DEHYDROGENASE CLASS-3; 1.
DR   Pfam; PF08240; ADH_N; 1.
DR   Pfam; PF00107; ADH_zinc_N; 1.
DR   SUPFAM; SSF50129; GroES-like; 2.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00059; ADH_ZINC; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|RuleBase:RU362016};
KW   NAD {ECO:0000256|RuleBase:RU362016};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU362016};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051348};
KW   Zinc {ECO:0000256|RuleBase:RU362016}.
FT   DOMAIN          28..120
FT                   /note="Alcohol dehydrogenase-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08240"
FT   DOMAIN          197..335
FT                   /note="Alcohol dehydrogenase-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00107"
SQ   SEQUENCE   375 AA;  39908 MW;  5B0830FE5097D795 CRC64;
     MDVRAAVAIA AGKPLEITTV QLEGPREGEV MVEIKATGVC HTDEFSLSGA DPEGLFPAIL
     GHEGAGVVVE TGPGVTSVKK GDHVIPLYTP ECRQCPSCLS RKTNLCTAIR ATQGQGLMPD
     GTSRFSMGGK PIHHYMGTST FANYTVLPEI AVAKIREDAP FDKVCYIGCG VTTGIGAVIN
     TAKVEQGAKA IVFGLGGIGL NVLQGLRLAG ADMIIGVDIN NDRKAWGERF GMTHFVNPKE
     VGKDLVPYLV DMTKSGADQI GGADYTFDCT GNVTVMRQAL EACHRGWGQS IVIGVAPSGA
     EISTRPFQLV TGRVWKGTAF GGARGRTDVP KIVDWYMQGK IQIDPMITHV MPLNDINKAF
     DLMKRGESIR GVVTF
//

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