ID Q7UVY0_RHOBA Unreviewed; 402 AA.
AC Q7UVY0;
DT 01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2003, sequence version 1.
DT 24-JAN-2024, entry version 125.
DE SubName: Full=Probable formaldehyde dehydrogenase {ECO:0000313|EMBL:CAD72591.1};
GN Name=fdh {ECO:0000313|EMBL:CAD72591.1};
GN OrderedLocusNames=RB2373 {ECO:0000313|EMBL:CAD72591.1};
OS Rhodopirellula baltica (strain DSM 10527 / NCIMB 13988 / SH1).
OC Bacteria; Planctomycetota; Planctomycetia; Pirellulales; Pirellulaceae;
OC Rhodopirellula.
OX NCBI_TaxID=243090 {ECO:0000313|EMBL:CAD72591.1, ECO:0000313|Proteomes:UP000001025};
RN [1] {ECO:0000313|EMBL:CAD72591.1, ECO:0000313|Proteomes:UP000001025}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10527 / NCIMB 13988 / SH1
RC {ECO:0000313|Proteomes:UP000001025};
RX PubMed=12835416; DOI=10.1073/pnas.1431443100;
RA Gloeckner F.O., Kube M., Bauer M., Teeling H., Lombardot T., Ludwig W.,
RA Gade D., Beck A., Borzym K., Heitmann K., Rabus R., Schlesner H., Amann R.,
RA Reinhardt R.;
RT "Complete genome sequence of the marine planctomycete Pirellula sp. strain
RT 1.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:8298-8303(2003).
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}.
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DR EMBL; BX294137; CAD72591.1; -; Genomic_DNA.
DR RefSeq; NP_864907.1; NC_005027.1.
DR RefSeq; WP_011118811.1; NC_005027.1.
DR AlphaFoldDB; Q7UVY0; -.
DR STRING; 243090.RB2373; -.
DR EnsemblBacteria; CAD72591; CAD72591; RB2373.
DR KEGG; rba:RB2373; -.
DR PATRIC; fig|243090.15.peg.1083; -.
DR eggNOG; COG1063; Bacteria.
DR HOGENOM; CLU_026673_11_3_0; -.
DR InParanoid; Q7UVY0; -.
DR OMA; CETVDVS; -.
DR OrthoDB; 9769198at2; -.
DR Proteomes; UP000001025; Chromosome.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd08282; PFDH_like; 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; IPR014184; HCHO_DH_non_GSH.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR NCBIfam; TIGR02819; fdhA_non_GSH; 1.
DR PANTHER; PTHR42813:SF3; GLUTATHIONE-INDEPENDENT FORMALDEHYDE DEHYDROGENASE; 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|RuleBase:RU361277};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000001025};
KW Zinc {ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 38..147
FT /note="Alcohol dehydrogenase-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08240"
FT DOMAIN 200..267
FT /note="Alcohol dehydrogenase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00107"
SQ SEQUENCE 402 AA; 42456 MW; 696177F5F2903538 CRC64;
MSDNKGVVYL GAGKVDVQSI DDPKLELSYR GKTRQCHHGV ILKVISTNIC GSDQHMVRGR
TTAPAGMVLG HEITGEVIEV GRDVEFIKKG DICSVPFNIA CGRCRCCKEG DTGVCENVNP
DRPGAAYGYV DMGGWIGGQS RYVMVPYADW NLLAFPDRDQ ALAKIRDLTM LSDIFPTGYH
GAYTAGVTTG STVYVAGAGP VGLACAHAAQ LLGAAVVIVG DMVEERLAQA RSFGCETVDL
KTDASLPDMI EQILGSREVD CAVDCVGFEA RGHGGDSGVE KPATVLNQVM EVTRVGGGVG
IPGLYVTDDP GGVDEAARTG NLSLRIGLGW AKSLHFTTGQ CPVMKYNRGL MMAILHDRCQ
IAKAVNATVI SLDDAPQGYA DFDQGAAKKF VLDPHGVLAA ST
//