ID A1B197_PARDP Unreviewed; 394 AA.
AC A1B197;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 106.
DE SubName: Full=Glutathione-independent formaldehyde dehydrogenase {ECO:0000313|EMBL:ABL69291.1};
GN OrderedLocusNames=Pden_1186 {ECO:0000313|EMBL:ABL69291.1};
OS Paracoccus denitrificans (strain Pd 1222).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Paracoccus.
OX NCBI_TaxID=318586 {ECO:0000313|EMBL:ABL69291.1, ECO:0000313|Proteomes:UP000000361};
RN [1] {ECO:0000313|Proteomes:UP000000361}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pd 1222 {ECO:0000313|Proteomes:UP000000361};
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Spiro S.,
RA Richardson D.J., Moir J.W.B., Ferguson S.J., van Spanning R.J.M.,
RA Richardson P.;
RT "Complete sequence of chromosome 1 of Paracoccus denitrificans PD1222.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000489; ABL69291.1; -; Genomic_DNA.
DR RefSeq; WP_011747511.1; NC_008686.1.
DR AlphaFoldDB; A1B197; -.
DR STRING; 318586.Pden_1186; -.
DR EnsemblBacteria; ABL69291; ABL69291; Pden_1186.
DR GeneID; 75500707; -.
DR KEGG; pde:Pden_1186; -.
DR eggNOG; COG1063; Bacteria.
DR HOGENOM; CLU_026673_11_3_5; -.
DR OrthoDB; 5295340at2; -.
DR Proteomes; UP000000361; Chromosome 1.
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:UP000000361};
KW Zinc {ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 35..144
FT /note="Alcohol dehydrogenase-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08240"
FT DOMAIN 197..265
FT /note="Alcohol dehydrogenase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00107"
SQ SEQUENCE 394 AA; 41796 MW; 740FDED57C5AF796 CRC64;
MSSNRGVVYI GPGKVEVQDI ADPKLEAPDR RKIAHGVILK VVSTNICGSD QHMVRGRTTA
EPGLILGHEI TGEVIEKGAD VEMLEIGDIV SVPFNVACGR CRCCREGDTG VCLTVNPSRA
GGAYGYVDMG GWIGGQARYV MVPYADFNLL KFPDRDRAMA KIRDLTMLSD ILPTGFHGAW
KAGVGVGSVV YVAGAGPVGL AAAASARILG AAVVMVGDFN KERLEHARKV GFEPVDLSKG
DDLPEMIAQI TGTPEVDAAI DAVGFEARGH SGGEQPAIVL NQMMQITRAA GQIGIPGLYV
TEDPGAVDDA ARHGSLSMRF GLGWAKAQSF HTGQTPVLKY NRQLMQAILH DRLPIADIVN
ATVIPLDQAV QGYESFDRGV AKKFVLDPHG MLAA
//
