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Database: UniProt
Entry: H0TX19_9BRAD
LinkDB: H0TX19_9BRAD
Original site: H0TX19_9BRAD 
ID   H0TX19_9BRAD            Unreviewed;       391 AA.
AC   H0TX19;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   SubName: Full=S-(Hydroxymethyl)glutathione dehydrogenase (Glutathione-dependent formaldehyde dehydrogenase) (Fdh) {ECO:0000313|EMBL:CCE11007.1};
DE            EC=1.1.1.284 {ECO:0000313|EMBL:CCE11007.1};
GN   Name=fdh {ECO:0000313|EMBL:CCE11007.1};
GN   ORFNames=BRAS3843_570063 {ECO:0000313|EMBL:CCE11007.1};
OS   Bradyrhizobium sp. STM 3843.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Bradyrhizobium.
OX   NCBI_TaxID=551947 {ECO:0000313|EMBL:CCE11007.1, ECO:0000313|Proteomes:UP000002686};
RN   [1] {ECO:0000313|Proteomes:UP000002686}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=STM3843 {ECO:0000313|Proteomes:UP000002686};
RX   PubMed=24704842; DOI=10.3390/genes3010035;
RA   Mornico D., Miche L., Bena G., Nouwen N., Vermeglio A., Vallenet D.,
RA   Smith A.A., Giraud E., Medigue C., Moulin L.;
RT   "Comparative genomics of aeschynomene symbionts: insights into the
RT   ecological lifestyle of nod-independent photosynthetic bradyrhizobia.";
RL   Genes (Basel) 3:35-61(2011).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947,
CC         ECO:0000256|RuleBase:RU361277};
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. {ECO:0000256|RuleBase:RU361277}.
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:CCE11007.1}.
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DR   EMBL; CAFK01000304; CCE11007.1; -; Genomic_DNA.
DR   RefSeq; WP_008973517.1; NZ_CAFK01000304.1.
DR   AlphaFoldDB; H0TX19; -.
DR   OrthoDB; 9773078at2; -.
DR   Proteomes; UP000002686; 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   CDD; cd08283; FDH_like_1; 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; IPR002328; ADH_Zn_CS.
DR   InterPro; IPR011032; GroES-like_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR42813:SF2; DEHYDROGENASE, ZINC-CONTAINING, PUTATIVE (AFU_ORTHOLOGUE AFUA_2G02810)-RELATED; 1.
DR   PANTHER; PTHR42813; ZINC-TYPE ALCOHOL DEHYDROGENASE-LIKE; 1.
DR   Pfam; PF08240; ADH_N; 1.
DR   Pfam; PF00107; ADH_zinc_N; 1.
DR   SUPFAM; SSF50129; GroES-like; 1.
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|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU361277};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:CCE11007.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002686};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          26..150
FT                   /note="Alcohol dehydrogenase-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08240"
FT   DOMAIN          197..266
FT                   /note="Alcohol dehydrogenase-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00107"
SQ   SEQUENCE   391 AA;  43027 MW;  CDF5CE8FE4D0DDD9 CRC64;
     MKALVWHGKE DIRCDTVTDP EIEHERDAII KVTSCAICGS DLHLFHNYIP AMMPGDIMGH
     ETMGEVVEVG SGVNGKLKKG DRIVVPFTII CGECEQCRRG NFSVCETTNR NKKIAEKVFG
     HTTAGLFGYT HLTGGYPGGQ AEYLRVPFAD KTHIKVPDSL SDEQALFLSD ILPTGWQAAV
     QCDIEPDDTV AVWGCGPVGQ MAIRSAILLG AKQVIAIDRL PERLSMAEAA GAITINFEKE
     SVVGRLNELT DSKGPEKCID AVGFESHVSV AQPDSVLDRA KQMFMMENDR PHALREAIYV
     CRPGGIISIP GVYGGFSDKI PMGMLMNKGL TIRTGQTHVN RWTDDLLQRI EDGQIDPSFV
     ITHTMPLERG PEMYRVFRDK QDSCVKVVLK P
//
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