ID K9DBX5_9BURK Unreviewed; 329 AA.
AC K9DBX5;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Enoyl reductase (ER) domain-containing protein {ECO:0000259|SMART:SM00829};
GN ORFNames=HMPREF9710_03938 {ECO:0000313|EMBL:EKU80771.1};
OS Massilia timonae CCUG 45783.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Massilia.
OX NCBI_TaxID=883126 {ECO:0000313|EMBL:EKU80771.1, ECO:0000313|Proteomes:UP000009874};
RN [1] {ECO:0000313|EMBL:EKU80771.1, ECO:0000313|Proteomes:UP000009874}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCUG 45783 {ECO:0000313|EMBL:EKU80771.1,
RC ECO:0000313|Proteomes:UP000009874};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Huys G., Walker B., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Goldberg J., Griggs A., Gujja S.,
RA Hansen M., Howarth C., Imamovic A., Larimer J., McCowen C., Montmayeur A.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Massilia timonae CCUG 45783.";
RL Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
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:EKU80771.1}.
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DR EMBL; AGZI01000049; EKU80771.1; -; Genomic_DNA.
DR RefSeq; WP_005669273.1; NZ_JH992924.1.
DR AlphaFoldDB; K9DBX5; -.
DR STRING; 47229.LO55_5083; -.
DR PATRIC; fig|883126.3.peg.3965; -.
DR eggNOG; COG0604; Bacteria.
DR HOGENOM; CLU_026673_3_3_4; -.
DR OrthoDB; 9787435at2; -.
DR Proteomes; UP000009874; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd08272; MDR6; 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; PTHR44154; QUINONE OXIDOREDUCTASE; 1.
DR PANTHER; PTHR44154:SF1; QUINONE OXIDOREDUCTASE; 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;
KW Reference proteome {ECO:0000313|Proteomes:UP000009874};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT DOMAIN 10..316
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 329 AA; 34989 MW; 92E09ABFD7B723C3 CRC64;
MKAQLLSSFG GPESFELRDV PKPVPQAGQV LVRVQATSIN PLDYQVRRGD YADLVPLPGI
TGHDVSGVVE EVGPGVTAFA PGDEVWYTPQ IFDGPGSYAE YHVAFENIVG RKPASLTHLE
AASLTLVGGT AWEALAVRAQ LKAGESILIH GGAGGVGHVV IQVAKAIGAR VFTTVKEENF
EFARSLGADV VIDYTKEDYV EAVGRETGGH GVDVVFDTIG GDTLTRSPDV LAQLGRVVSI
VDIAQPQNLI QAWGKNASYH FVFTRQNRGK LDELSALIER GQLKPHVGAV YSLADIPLAH
ARLESRDNGL RGKIAIAVGP LADRTSAQV
//