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Database: UniProt
Entry: A0A1M3BM44_9ACTN
LinkDB: A0A1M3BM44_9ACTN
Original site: A0A1M3BM44_9ACTN 
ID   A0A1M3BM44_9ACTN        Unreviewed;       404 AA.
AC   A0A1M3BM44;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   SubName: Full=Formaldehyde dehydrogenase, glutathione-independent {ECO:0000313|EMBL:OJU85386.1};
GN   ORFNames=BGO11_07000 {ECO:0000313|EMBL:OJU85386.1};
OS   Solirubrobacterales bacterium 70-9.
OC   Bacteria; Actinomycetota; Thermoleophilia; Solirubrobacterales.
OX   NCBI_TaxID=1895833 {ECO:0000313|EMBL:OJU85386.1, ECO:0000313|Proteomes:UP000184118};
RN   [1] {ECO:0000313|EMBL:OJU85386.1, ECO:0000313|Proteomes:UP000184118}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=70-9 {ECO:0000313|EMBL:OJU85386.1};
RA   Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA   Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT   "Genome-resolved meta-omics ties microbial dynamics to process performance
RT   in biotechnology for thiocyanate degradation.";
RL   Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
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:OJU85386.1}.
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DR   EMBL; MKSH01000037; OJU85386.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1M3BM44; -.
DR   Proteomes; UP000184118; Unassembled WGS sequence.
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; IPR013154; ADH-like_N.
DR   InterPro; IPR002328; ADH_Zn_CS.
DR   InterPro; IPR007698; AlaDH/PNT_NAD(H)-bd.
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; PF01262; AlaDh_PNT_C; 1.
DR   SUPFAM; SSF50129; GroES-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00059; ADH_ZINC; 1.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          44..153
FT                   /note="Alcohol dehydrogenase-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08240"
FT   DOMAIN          192..246
FT                   /note="Alanine dehydrogenase/pyridine nucleotide
FT                   transhydrogenase NAD(H)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01262"
SQ   SEQUENCE   404 AA;  42344 MW;  D6A28F5FA329333F CRC64;
     MADNRGVAYM GTGKVEVQDI DYPAWEIKEG PGVPTESVGR ELPHGAIVKL VATNICGSDQ
     HMVRGRTTAP EGLILGHEIT GEVVEVGPGV EFIEVGDLVS TPFNIACGRC RNCKERNTGV
     CLNVNPAQPG GAYGYVDMGG WIGGQAEYVM VPYADWNLLK FPDKDQAMEK ILDLTMLSDI
     FPTGYHGAVS AGVGTGSTVY VAGAGPVGLA AAHAAQLLGA AVVIVGDANE ERLEQARSFG
     CETLNIDKGE IPDQIEGILG VPEVDCGVDA VGFEAKGHGP DAGEEPAVVL NALMDVTRAA
     GRLGIPGLYV VEDPGAESDE AKEGSLALKL GAGWAKSLSF VTGQCPVMKY HRELMNAILN
     DRCEIAKAVN ATVIRLDDAP EGYEDFDKGA AKKFVIDPHG LVAA
//
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