ID A0A1Q3TPG5_9CHLR Unreviewed; 394 AA.
AC A0A1Q3TPG5;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Glutathione-dependent formaldehyde dehydrogenase {ECO:0000313|EMBL:OJW04341.1};
GN ORFNames=BGO39_11310 {ECO:0000313|EMBL:OJW04341.1};
OS Chloroflexi bacterium 54-19.
OC Bacteria; Chloroflexota.
OX NCBI_TaxID=1895928 {ECO:0000313|EMBL:OJW04341.1, ECO:0000313|Proteomes:UP000186384};
RN [1] {ECO:0000313|EMBL:OJW04341.1, ECO:0000313|Proteomes:UP000186384}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=54-19 {ECO:0000313|EMBL:OJW04341.1};
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 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:OJW04341.1}.
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DR EMBL; MKTJ01000013; OJW04341.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q3TPG5; -.
DR STRING; 1895928.BGO39_11310; -.
DR Proteomes; UP000186384; 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; 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 InterPro; IPR020843; PKS_ER.
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 SMART; SM00829; PKS_ER; 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 Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 8..387
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 394 AA; 42601 MW; E99D5F08940D0F71 CRC64;
MRALCWFGKE DVRVEAVPDP QILNPRDAIV KITTTAICGS DLHLYDGVIP TMEKGDILGH
EFMGEIVEVG KEVHNLKVGD RVVVPFTIAC GNCFFCKKGL WASCDNSNPN AWMLEKLYGY
SGSGLFGYSH MMGGYAGGQA EFARVPFADI GPVKVPDGLA DEQVLFLSDI FPTGYQAAEN
ANIAAGDTVA IWGCGPVGQF AIQSAWMLGA GRVIAIDRVP ERLELAATKG KAEIINSDTE
NVVEKLRSMT GGRGPDSCID CVGMESTGHT PDALYDKVKM AMKLETDRPT ALREVITACR
KGGTVSIPGV YGGLLDKFPM GAAFGKGLIF KMGQTNMHNY LKPLMDRIEK GEIDPSFVIT
HRLGLEDAPA AYKTFRDKQD GCIKVVLKPH EVTA
//
