ID F7RP13_9GAMM Unreviewed; 335 AA.
AC F7RP13;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE SubName: Full=Quinone oxidoreductase (NADPH:quinone reductase) / putative arginate lyase {ECO:0000313|EMBL:EGM69882.1};
DE EC=1.1.1.- {ECO:0000313|EMBL:EGM69882.1};
GN ORFNames=SOHN41_02143 {ECO:0000313|EMBL:EGM69882.1};
OS Shewanella sp. HN-41.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=327275 {ECO:0000313|EMBL:EGM69882.1, ECO:0000313|Proteomes:UP000002956};
RN [1] {ECO:0000313|EMBL:EGM69882.1, ECO:0000313|Proteomes:UP000002956}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HN-41 {ECO:0000313|EMBL:EGM69882.1,
RC ECO:0000313|Proteomes:UP000002956};
RX PubMed=21868804; DOI=10.1128/JB.05578-11;
RA Kim D.H., Jiang S., Lee J.H., Cho Y.J., Chun J., Choi S.H., Park H.S.,
RA Hur H.G.;
RT "Draft Genome Sequence of Shewanella sp. Strain HN-41, Which Produces
RT Arsenic-Sulfide Nanotubes.";
RL J. Bacteriol. 193:5039-5040(2011).
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. Quinone oxidoreductase subfamily.
CC {ECO:0000256|ARBA:ARBA00010371}.
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:EGM69882.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AFOZ01000025; EGM69882.1; -; Genomic_DNA.
DR AlphaFoldDB; F7RP13; -.
DR STRING; 327275.SOHN41_02143; -.
DR Proteomes; UP000002956; Unassembled WGS sequence.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; 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; 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 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; 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.
DR PROSITE; PS01162; QOR_ZETA_CRYSTAL; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000313|EMBL:EGM69882.1}; NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000313|EMBL:EGM69882.1};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 14..330
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 335 AA; 35304 MW; 572529267BB34E7F CRC64;
MHTPMTMQAL EITETNGNFI LTDHVVTQPK SGQVLVKVIA SGINPLDLKI RAGQAAHAKQ
PFPAVLGIDM AGEIISIGPD VSNFKVSDLV YGMTGGVAGQ QGSLAQYQVA DARLLAKAPT
NISLLQAAAM PLVVITAWEG LVDRAKVAAG HKVLVQGGAG GVGHVVIQLA KAFGAEVFAT
AAAKDADYIR SLGAIYIDYQ STSVEQYLEE LTDNEGFDII YNTIGGVSLD QAFQSVKSYT
GHVVSCLGWG THSIAPLSFK AATYSGVFTL MPLLTGKSRE HHGKILSQAS LLTEQGLLNV
RLDPQQFDFG SIEQAYHKAA SATNIGKVVV TVSKA
//