ID N8W2Z8_9GAMM Unreviewed; 676 AA.
AC N8W2Z8;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=2,4-dienoyl-CoA reductase [NADPH] {ECO:0008006|Google:ProtNLM};
GN ORFNames=F967_01377 {ECO:0000313|EMBL:ENV06406.1};
OS Acinetobacter sp. CIP 102637.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1144669 {ECO:0000313|EMBL:ENV06406.1, ECO:0000313|Proteomes:UP000023788};
RN [1] {ECO:0000313|EMBL:ENV06406.1, ECO:0000313|Proteomes:UP000023788}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIP 102637 {ECO:0000313|EMBL:ENV06406.1,
RC ECO:0000313|Proteomes:UP000023788};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Cerqueira G., Feldgarden M., Courvalin P., Perichon B.,
RA Grillot-Courvalin C., Clermont D., Rocha E., Yoon E.-J., Nemec A.,
RA Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B.,
RA Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Larimer J., McCowan C., Murphy C., Neiman D., Pearson M.,
RA Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Acinetobacter sp. CIP 102637.";
RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|ARBA:ARBA00001917};
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:ENV06406.1}.
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DR EMBL; APPG01000030; ENV06406.1; -; Genomic_DNA.
DR RefSeq; WP_004798969.1; NZ_KB849435.1.
DR AlphaFoldDB; N8W2Z8; -.
DR PATRIC; fig|1144669.3.peg.1366; -.
DR HOGENOM; CLU_012153_1_0_6; -.
DR Proteomes; UP000023788; Unassembled WGS sequence.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR CDD; cd02930; DCR_FMN; 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; PF00724; Oxidored_FMN; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR PRINTS; PR00368; FADPNR.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF51395; FMN-linked oxidoreductases; 1.
DR SUPFAM; SSF51971; Nucleotide-binding domain; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000023788}.
FT DOMAIN 7..331
FT /note="NADH:flavin oxidoreductase/NADH oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00724"
FT DOMAIN 377..639
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
SQ SEQUENCE 676 AA; 74212 MW; 6387F2A33202B4C2 CRC64;
MTSYANILKP LHLGFTTIKN RVVMGSMHSG LEDRFFNYPK LAAYFGERAK GGVGLIITGG
ISPNRQGWLL PAGGTMNTLA DIPHHRLVTH AVHKHGAKIL MQILHSGRYG YHPFSVSSSP
IQAPINPFKP RQMSDSQILA TIEDYARCAS LAKKAGYDGV EIMGSEGYLI NQFLSNHVNK
RTDRWGGDIE NRMRFPVEIV KAIRAKVGEK FIICFRLSML DLVHDGNTMQ EVIIIAKALE
KAGITLLNTG IGWHEARIPT IVTSVPRAAF VDYTAVVKQH VSVPVIASNR INMPDVAEEI
VASGQADMVQ MARPFLADPY WVNKTATNRV DEINTCIACN QACLDHAFKN ERVSCLVNPQ
ACFETELVYI KTKKPKRVAV VGGGVAGMSA ATVAASRGHA VTLFEANNDV GGQFNLAKVV
PGKEEFHETI RYFKVQLKQT GVDVRLNTKV NREQLEREGF DEVVIATGVV PRALKIQGSD
APQVLSYAEV LKGAKVGHKV AVIGAGGIGF DVSEFLLKPP HQPQPQPLAE WQREWGVDPN
PNYISEGGTQ RPEVEMPVRQ IYLLQRKTTP LGIGLGKTSG WVHRAQLKKH GVRMLRGVQY
KAVTDEGLWV EHNGHDQLLR VDTIVVCAGQ ESVKDLVPRE NETTLAKYHV IGGAKLAGEL
DAKRAIREGA ELAAKL
//