ID A0A0R2CT27_9LACO Unreviewed; 373 AA.
AC A0A0R2CT27;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Oxidoreductase zinc-binding protein {ECO:0000313|EMBL:KRM94194.1};
GN ORFNames=FC56_GL001142 {ECO:0000313|EMBL:KRM94194.1};
OS Lentilactobacillus senioris DSM 24302 = JCM 17472.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lentilactobacillus.
OX NCBI_TaxID=1423802 {ECO:0000313|EMBL:KRM94194.1, ECO:0000313|Proteomes:UP000051256};
RN [1] {ECO:0000313|EMBL:KRM94194.1, ECO:0000313|Proteomes:UP000051256}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 24302 {ECO:0000313|EMBL:KRM94194.1,
RC ECO:0000313|Proteomes:UP000051256};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
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:KRM94194.1}.
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DR EMBL; AYZR01000004; KRM94194.1; -; Genomic_DNA.
DR RefSeq; WP_056977283.1; NZ_AYZR01000004.1.
DR AlphaFoldDB; A0A0R2CT27; -.
DR STRING; 1423802.FC56_GL001142; -.
DR PATRIC; fig|1423802.4.peg.1158; -.
DR Proteomes; UP000051256; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR CDD; cd05289; MDR_like_2; 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 PANTHER; PTHR11695; ALCOHOL DEHYDROGENASE RELATED; 1.
DR PANTHER; PTHR11695:SF294; RETICULON-4-INTERACTING PROTEIN 1, MITOCHONDRIAL; 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.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000051256}.
FT DOMAIN 15..331
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
FT REGION 333..373
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 341..356
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 373 AA; 41497 MW; C3EDD98A4F3810EB CRC64;
MKAAQIKRYT HRIKANIVDV DIPALRLNEI LVKVVCAGVN PLDVMDMTGQ FKLIQKFPMP
LKLGNEFSGV VEKVGQQVTD FKKGDNVYGL LPMNRLGSFA EYVVINERDL APMPANVTFQ
HAATVPLDAM TAVQAVMEEM SAQAGQKLFM PLGNDGLINL VLPLAKRLGV EVNVAGDSRL
KEPLLAAGVT QFIDMAEENY WEVAPKSDMI IDTIGSSEFR HELAVVKAGG QIVSLRMNPN
ENFAVEHGMR PDKRVLFSVM GAKYDRLAKE QNARYRFLFV RSDGKRLREI TKRIQREGFN
PIIDPHEFDL DHINDALQLV AKGTTLGKVL VNVSQPKPKD NPPKETMEEE KPVVESEEPV
VVTPDSATEL PEK
//