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Database: UniProt
Entry: A0A1H9U685_9LACT
LinkDB: A0A1H9U685_9LACT
Original site: A0A1H9U685_9LACT 
ID   A0A1H9U685_9LACT        Unreviewed;       672 AA.
AC   A0A1H9U685;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   SubName: Full=2,4-dienoyl-CoA reductase {ECO:0000313|EMBL:SES04986.1};
GN   ORFNames=SAMN04488559_12222 {ECO:0000313|EMBL:SES04986.1};
OS   Isobaculum melis.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC   Isobaculum.
OX   NCBI_TaxID=142588 {ECO:0000313|EMBL:SES04986.1, ECO:0000313|Proteomes:UP000198948};
RN   [1] {ECO:0000313|EMBL:SES04986.1, ECO:0000313|Proteomes:UP000198948}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 13760 {ECO:0000313|EMBL:SES04986.1,
RC   ECO:0000313|Proteomes:UP000198948};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000256|ARBA:ARBA00001917};
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DR   EMBL; FOHA01000022; SES04986.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H9U685; -.
DR   STRING; 142588.SAMN04488559_12222; -.
DR   OrthoDB; 9772736at2; -.
DR   Proteomes; UP000198948; Unassembled WGS sequence.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   CDD; cd02803; OYE_like_FMN_family; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR001155; OxRdtase_FMN_N.
DR   PANTHER; PTHR42917; 2,4-DIENOYL-COA REDUCTASE; 1.
DR   PANTHER; PTHR42917:SF2; 2,4-DIENOYL-COA REDUCTASE [(2E)-ENOYL-COA-PRODUCING]; 1.
DR   Pfam; PF12831; FAD_oxidored; 1.
DR   Pfam; PF00724; Oxidored_FMN; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00469; PNDRDTASEII.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   SUPFAM; SSF51395; FMN-linked oxidoreductases; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000198948}.
FT   DOMAIN          6..336
FT                   /note="NADH:flavin oxidoreductase/NADH oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00724"
FT   DOMAIN          467..622
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
SQ   SEQUENCE   672 AA;  74220 MW;  CD9843F147B3A4A9 CRC64;
     MNQYPEIFKP LTIKRMTLKN RVIMPPMGTN FANMDGSFNN EHIEYYRQRA KGGTGLITLE
     NACVDFPMGT NGTTQLRIDN DQYIPGLWKF NETMHAYGAC TSVQINHAGA SAYGLRLEGN
     QPVSASNIPS KKGNAVPRPL EKEEILAIVK KYGEAANRAQ RAGFDCIEIH AGHSYLVSQF
     LSPLYNVRTD EFGGSPENRA RFAKLIVEEV RQAVGPFFPI CLRFSADEML EGGNTLEETM
     DLLSYFADEV DILNVSAALN DSIQYQIDQM NLADGWRSYM AKAVKERFGK VTVTSGNIRS
     PKVANDILAR GDADLLAMGR GLIAEPNWVN KVAQNQEHLL RKCISCNIGC ADHRIAKSRP
     VRCTVNPDVI HEDAYKEEQI KHDLQMVVIG GGTTALEAAT SAAEIGATVT LFEEKPYLGG
     LAREIARLPD KKRIDDYVTY LEARAKECPS LTIHLNTRAD LATIQQLNPD LVVNATGAKP
     LLPPISGLHE TLALPDRQVY SIFDLLHNME DFQEFEGKHI AVIGGGAVGL DVVEYYAERG
     AASVSIVEMQ PALGKDLDMI TRISMLDIIE KHGVNVYTNT ALTEVTNDHF KVMRDGEEMA
     IPFDLGFVCL GMKADNPLME QLTAFGAETG ATIANIGDSK LARRIYEGAR EARDILTTVH
     QVDAQKNMQE QF
//
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