ID D9T3X9_MICAI Unreviewed; 318 AA.
AC D9T3X9;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 24-JAN-2024, entry version 63.
DE SubName: Full=Alcohol dehydrogenase zinc-binding domain protein {ECO:0000313|EMBL:ADL49727.1};
GN OrderedLocusNames=Micau_6234 {ECO:0000313|EMBL:ADL49727.1};
OS Micromonospora aurantiaca (strain ATCC 27029 / DSM 43813 / BCRC 12538 / CBS
OS 129.76 / JCM 10878 / NBRC 16125 / NRRL B-16091 / INA 9442).
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=644283 {ECO:0000313|EMBL:ADL49727.1, ECO:0000313|Proteomes:UP000001908};
RN [1] {ECO:0000313|EMBL:ADL49727.1, ECO:0000313|Proteomes:UP000001908}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27029 / DSM 43813 / JCM 10878 / NBRC 16125 / INA 9442
RC {ECO:0000313|Proteomes:UP000001908};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Chang Y.-J., Jeffries C., Kyrpides N., Ivanova N., Ovchinnikova G.,
RA Hirsch A.M., Woyke T.;
RT "Complete sequence of Micromonospora aurantiaca ATCC 27029.";
RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP002162; ADL49727.1; -; Genomic_DNA.
DR RefSeq; WP_013289324.1; NC_014391.1.
DR AlphaFoldDB; D9T3X9; -.
DR STRING; 644283.Micau_6234; -.
DR KEGG; mau:Micau_6234; -.
DR eggNOG; COG0604; Bacteria.
DR HOGENOM; CLU_026673_3_1_11; -.
DR OMA; GSMECLM; -.
DR OrthoDB; 5195079at2; -.
DR Proteomes; UP000001908; Chromosome.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
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; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR PANTHER; PTHR43677:SF4; QUINONE OXIDOREDUCTASE-LIKE PROTEIN 2; 1.
DR PANTHER; PTHR43677; SHORT-CHAIN DEHYDROGENASE/REDUCTASE; 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.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000001908}.
FT DOMAIN 10..315
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 318 AA; 32066 MW; 48535F362B1E3557 CRC64;
MRAVWLREFG GPEVLVPGTA PDPAPGPGQV LVDVAHANIT FVETMFRASG FGPFGTELPV
IPGNGVGGTI TALGPDADPA LAGRVVVTTT GGTGGYAERV VVDQGAPVPV PPGLPLDAAV
ALMADGRTAL MLARAAGLRR GDRVLVEAAA GGVGSLLVQL AARAGATVVA AVGGSRKVAV
LRAAGLDVVV DYRRAGWTDR VRDSVGAVDV VFDGVGGPLA REAFDLLAPG GRMLSFGLAG
GTWADIPAES AAARGVTLLS PRPGPDELRA LTEAALAEGA AGRLRPLIGQ RFPLERAAAA
HAAIEARETL GKTLLDVR
//