ID A0A1Q7UQF1_9CHLR Unreviewed; 328 AA.
AC A0A1Q7UQF1;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 28-JUN-2023, entry version 13.
DE SubName: Full=Alcohol dehydrogenase {ECO:0000313|EMBL:OLE03970.1};
GN ORFNames=AUG82_06215 {ECO:0000313|EMBL:OLE03970.1};
OS Ktedonobacter sp. 13_1_20CM_4_53_11.
OC Bacteria; Chloroflexota; Ktedonobacteria; Ktedonobacterales;
OC Ktedonobacteraceae; Ktedonobacter.
OX NCBI_TaxID=1805225 {ECO:0000313|EMBL:OLE03970.1, ECO:0000313|Proteomes:UP000186213};
RN [1] {ECO:0000313|EMBL:OLE03970.1, ECO:0000313|Proteomes:UP000186213}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27843720;
RA Butterfield C.N., Li Z., Andeer P.F., Spaulding S., Thomas B.C., Singh A.,
RA Hettich R.L., Suttle K.B., Probst A.J., Tringe S.G., Northen T., Pan C.,
RA Banfield J.F.;
RT "Proteogenomic analyses indicate bacterial methylotrophy and archaeal
RT heterotrophy are prevalent below the grass root zone.";
RL PeerJ 4:E2687-E2687(2016).
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:OLE03970.1}.
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DR EMBL; MNIY01000119; OLE03970.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q7UQF1; -.
DR STRING; 1805225.AUG82_06215; -.
DR Proteomes; UP000186213; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd08267; MDR1; 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; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR InterPro; IPR002364; Quin_OxRdtase/zeta-crystal_CS.
DR PANTHER; PTHR44013; ZINC-TYPE ALCOHOL DEHYDROGENASE-LIKE PROTEIN C16A3.02C; 1.
DR PANTHER; PTHR44013:SF1; ZINC-TYPE ALCOHOL DEHYDROGENASE-LIKE PROTEIN C16A3.02C; 1.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF13602; ADH_zinc_N_2; 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; PS01162; QOR_ZETA_CRYSTAL; 1.
PE 4: Predicted;
FT DOMAIN 10..320
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 328 AA; 35502 MW; BC94664B3E8FA12C CRC64;
MKAIVNTHYG SPDVLQLKEV EKPAPSDHEV LVKVLAASAA AGDWHLLRAQ PFLMRFTSGL
LKPKHQILGA AFAGRVETVG RNVTQFQPGD EVFGDVSACG FGAFAEYVSV PEKAVALKPT
RLTFEEAATV PVSAVTALQG LRDQGHIQPG QKVLINGASG GVGTFAVQIA KAFGAEVTGV
CSTRNVDMVR SIGADYVIDY MQEDFTKNGQ RYDLILAVNG YHPISAYQRA LSQEGMYVMT
GGSMAQMFQA MLLGPWLSKN GSQKMGNLLA KPNQKDLVFV KELLEAGKVV PVIERRYPLR
EVPEAIRYVE EGHAKGKVVI TVDQNNLT
//
