ID C4LLI7_CORK4 Unreviewed; 358 AA.
AC C4LLI7;
DT 07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 07-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE SubName: Full=Putative oxidoreductase {ECO:0000313|EMBL:ACR18692.1};
GN OrderedLocusNames=ckrop_1984 {ECO:0000313|EMBL:ACR18692.1};
OS Corynebacterium kroppenstedtii (strain DSM 44385 / JCM 11950 / CIP 105744 /
OS CCUG 35717).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=645127 {ECO:0000313|EMBL:ACR18692.1, ECO:0000313|Proteomes:UP000001473};
RN [1] {ECO:0000313|EMBL:ACR18692.1, ECO:0000313|Proteomes:UP000001473}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44385 / JCM 11950 / CIP 105744 / CCUG 35717
RC {ECO:0000313|Proteomes:UP000001473};
RX PubMed=18430482; DOI=10.1016/j.jbiotec.2008.03.004;
RA Tauch A., Schneider J., Szczepanowski R., Tilker A., Viehoever P.,
RA Gartemann K.-H., Arnold W., Blom J., Brinkrolf K., Brune I., Goetker S.,
RA Weisshaar B., Goesmann A., Droege M., Puehler A.;
RT "Ultrafast pyrosequencing of Corynebacterium kroppenstedtii DSM44385
RT revealed insights into the physiology of a lipophilic corynebacterium that
RT lacks mycolic acids.";
RL J. Biotechnol. 136:22-30(2008).
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DR EMBL; CP001620; ACR18692.1; -; Genomic_DNA.
DR AlphaFoldDB; C4LLI7; -.
DR STRING; 645127.ckrop_1984; -.
DR KEGG; ckp:ckrop_1984; -.
DR eggNOG; COG0604; Bacteria.
DR HOGENOM; CLU_026673_3_3_11; -.
DR OrthoDB; 3613651at2; -.
DR Proteomes; UP000001473; Chromosome.
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:UP000001473}.
FT DOMAIN 36..354
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 358 AA; 38310 MW; EA2571F5A165FDB2 CRC64;
MNDSVNNSKI PDSNTPAPNT PDSDVMHDVW VATGYGKQLT QKNMPVPQPD PHDVVINVRA
ASLNPVDQKI LDGQMRALMS FEFPLIPGSD GAGIVSQVGS EVTRFKPGDL VFFRAQSDRL
GAFAPFFATH EDTVALAPQG MSFTDAASLP LVGLTAWQAL TEKAELKPGD RVLIHAGSGG
VGSLAVQMAH HLGAYVIATV SGKNADFVRS LGADEVIDYR TQRFEEHVSD LDVVFDPIGG
PQLKRSISVT KPGGIVVGIS TDPTPQLARE QELNPALRLL FGAISLSTRR AAEKAGVRYE
FLLMHPSGGQ LAHLAKLCED GVLKPLVGRI INYVDIPHEL ENMSGNGIRG KVVVDIQG
//
