ID A0A0J1G6T8_9FIRM Unreviewed; 359 AA.
AC A0A0J1G6T8;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Enoyl reductase (ER) domain-containing protein {ECO:0000259|SMART:SM00829};
GN ORFNames=RHS_3167 {ECO:0000313|EMBL:KLU71058.1};
OS Robinsoniella sp. RHS.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Robinsoniella.
OX NCBI_TaxID=1504536 {ECO:0000313|EMBL:KLU71058.1, ECO:0000313|Proteomes:UP000036477};
RN [1] {ECO:0000313|EMBL:KLU71058.1, ECO:0000313|Proteomes:UP000036477}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RHS {ECO:0000313|EMBL:KLU71058.1};
RX PubMed=25284151; DOI=10.1016/j.cell.2014.09.008;
RA Seedorf H., Griffin N.W., Ridaura V.K., Reyes A., Cheng J., Rey F.E.,
RA Smith M.I., Simon G.M., Scheffrahn R.H., Woebken D., Spormann A.M.,
RA Van Treuren W., Ursell L.K., Pirrung M., Robbins-Pianka A., Cantarel B.L.,
RA Lombard V., Henrissat B., Knight R., Gordon J.I.;
RT "Bacteria from diverse habitats colonize and compete in the mouse gut.";
RL Cell 159:253-266(2014).
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:KLU71058.1}.
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DR EMBL; JNGB01000030; KLU71058.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0J1G6T8; -.
DR PATRIC; fig|1504536.3.peg.4059; -.
DR Proteomes; UP000036477; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0044238; P:primary metabolic process; IEA:UniProt.
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; PTHR43401; L-THREONINE 3-DEHYDROGENASE; 1.
DR PANTHER; PTHR43401:SF2; L-THREONINE 3-DEHYDROGENASE; 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;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000036477};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 15..357
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 359 AA; 39666 MW; 377B72D55FB01F82 CRC64;
MAKTVKTMKA LVVYGKNDYR LESDYPVPEL KKGEVLIKVE ACGVCASDIK NWHGAEGYWG
DGKSEPWVKT PFIPGHEFVG EVVEVAEGYQ GCAKAGDRIT GEQIVPCGEC MFCRTGHYWM
CDQADIFGFR AHVNGAMAEY MILPEKTRIY QIPKDLELEK AILIEPYSCA KHAVDRADIS
NTDVVVISGV GTLGLAMVNY ARLRRPKKLI AIDMKEDRLA IAKSFGADIC LNPSECDVVK
EIQSMTNGYG CDIYIEATGH PSSVQQGLDA IRKLGRFIEF SVFGQKVSVD WSVIGDGKEL
DILGAHLGPY CFDVVTEWIA DNTIYTDGVV THTFSLDQWQ QAFEQNAKGD GSLKVVIKP
//
