ID A0A0B6WV77_9BACT Unreviewed; 312 AA.
AC A0A0B6WV77;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Zn-dependent oxidoreductase, NADPH:quinone reductase {ECO:0000313|EMBL:CDM64159.1};
GN ORFNames=PYK22_00151 {ECO:0000313|EMBL:CDM64159.1};
OS Pyrinomonas methylaliphatogenes.
OC Bacteria; Acidobacteriota; Blastocatellia; Blastocatellales;
OC Pyrinomonadaceae; Pyrinomonas.
OX NCBI_TaxID=454194 {ECO:0000313|EMBL:CDM64159.1, ECO:0000313|Proteomes:UP000031518};
RN [1] {ECO:0000313|EMBL:CDM64159.1, ECO:0000313|Proteomes:UP000031518}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K22 {ECO:0000313|EMBL:CDM64159.1,
RC ECO:0000313|Proteomes:UP000031518};
RA Stott M.;
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CDM64159.1, ECO:0000313|Proteomes:UP000031518}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K22 {ECO:0000313|EMBL:CDM64159.1,
RC ECO:0000313|Proteomes:UP000031518};
RA Lee K.C.Y., Power J.F., Dunfield P.F., Morgan X.C., Huttenhower C.,
RA Stott M.B.;
RT "Complete genome sequence of Pyrinomonas methylaliphatogenes type strain
RT K22T.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CBXV010000001; CDM64159.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B6WV77; -.
DR STRING; 454194.PYK22_00151; -.
DR Proteomes; UP000031518; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; 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 InterPro; IPR002364; Quin_OxRdtase/zeta-crystal_CS.
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.
DR PROSITE; PS01162; QOR_ZETA_CRYSTAL; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000031518}.
FT DOMAIN 13..309
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 312 AA; 34368 MW; DE230DDAC0DBF7F3 CRC64;
MEMMKAVRIH RFGGPEVLTY EDAPRPQIAS DELLVRVHGA GVNPVDWKIR EGRLQQFLQH
KLPLILGWDF SGVVEEVGSA VEGFKVGDEV YARPDIRRDG AYAEFIAVRA REVALKPKTL
DHIHAAAVPL ASITAWDALI KTARLEAGQR VLIHAAAGGV GHFAVQFARW RGAYVIGTAS
AANHDLVREL GANEMIDYRA ERFEEKVKDV DVVFDTVGGD VQRRSWGVLK KGGMLVSIVD
RPSEKTAEEY GVRAAYVFIE PDAEVLKQVA ELIDAGVVKP VVENIFALSE ARRAHELSQS
GHVRGKIVLR VA
//
