ID E6TMD8_MYCSR Unreviewed; 324 AA.
AC E6TMD8;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE SubName: Full=Zn-dependent oxidoreductase, NADPH:quinone reductase {ECO:0000313|EMBL:ADU00494.1};
GN OrderedLocusNames=Mspyr1_39020 {ECO:0000313|EMBL:ADU00494.1};
OS Mycolicibacterium gilvum (strain DSM 45189 / LMG 24558 / Spyr1)
OS (Mycobacterium gilvum).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=278137 {ECO:0000313|EMBL:ADU00494.1, ECO:0000313|Proteomes:UP000008916};
RN [1] {ECO:0000313|Proteomes:UP000008916}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45189 / LMG 24558 / Spyr1
RC {ECO:0000313|Proteomes:UP000008916};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., LaButti K., Ivanova N.M., Mikhailova N.M., Land M., Hauser L.,
RA Koukkou A.I., Drainas C., Kyrpides N., Woyke T.;
RT "Complete sequence of chromosome of Mycobacterium sp. Spyr1.";
RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADU00494.1, ECO:0000313|Proteomes:UP000008916}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45189 / LMG 24558 / Spyr1
RC {ECO:0000313|Proteomes:UP000008916};
RX PubMed=22180818;
RA Kallimanis A., Karabika E., Mavromatis K., Lapidus A., Labutti K.M.,
RA Liolios K., Ivanova N., Goodwin L., Woyke T., Velentzas A.D.,
RA Perisynakis A., Ouzounis C.C., Kyrpides N.C., Koukkou A.I., Drainas C.;
RT "Complete genome sequence of Mycobacterium sp. strain (Spyr1) and
RT reclassification to Mycobacterium gilvum Spyr1.";
RL Stand. Genomic Sci. 5:144-153(2011).
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DR EMBL; CP002385; ADU00494.1; -; Genomic_DNA.
DR RefSeq; WP_011895346.1; NC_014814.1.
DR AlphaFoldDB; E6TMD8; -.
DR KEGG; msp:Mspyr1_39020; -.
DR HOGENOM; CLU_026673_3_1_11; -.
DR Proteomes; UP000008916; Chromosome.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR CDD; cd08241; QOR1; 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; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR PANTHER; PTHR43677:SF3; PROSTAGLANDIN REDUCTASE 3; 1.
DR PANTHER; PTHR43677; SHORT-CHAIN DEHYDROGENASE/REDUCTASE; 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.
PE 4: Predicted;
FT DOMAIN 10..321
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 324 AA; 33390 MW; AD8324A0D860ACC0 CRC64;
MRAIQIAELS GPGAARLVEI DEPAADDGTV LVEVHAAGVA FPDALQSRGL YQYKPEMPYT
PGAEVAGVVR SAPAGAHVKA GDRVAGLTML CGAMAEVVAL QPERVFALPD SVSFEAGAGI
LFNDLTVQFA LRTRGRLAAG ETVLVHGAAG GIGTSTLRLA PAFGASRTIA VVSTEEKADV
ARAAGATDVV LADGFKDAVK ELTGGRGVDI VVDPVGGDRF TDSLRSLAPG GRLLVVGFTG
GDIPTVKVNR LLLNNVDAVG VGWGAWTMTH PGYLQEQWAE LEPLLASGTV PAPEPVVYPL
ERAAEAIASL EDRSARGKVV VAVR
//
