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Database: UniProt
Entry: A0A067NFX6_PLEOS
LinkDB: A0A067NFX6_PLEOS
Original site: A0A067NFX6_PLEOS 
ID   A0A067NFX6_PLEOS        Unreviewed;      1088 AA.
AC   A0A067NFX6;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=enoyl-[acyl-carrier-protein] reductase {ECO:0000256|ARBA:ARBA00038963};
DE            EC=1.3.1.104 {ECO:0000256|ARBA:ARBA00038963};
GN   ORFNames=PLEOSDRAFT_1093851 {ECO:0000313|EMBL:KDQ26938.1};
OS   Pleurotus ostreatus PC15.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Pleurotineae; Pleurotaceae; Pleurotus.
OX   NCBI_TaxID=1137138 {ECO:0000313|EMBL:KDQ26938.1, ECO:0000313|Proteomes:UP000027073};
RN   [1] {ECO:0000313|Proteomes:UP000027073}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PC15 {ECO:0000313|Proteomes:UP000027073};
RX   PubMed=24958869; DOI=10.1073/pnas.1400592111;
RA   Riley R., Salamov A.A., Brown D.W., Nagy L.G., Floudas D., Held B.W.,
RA   Levasseur A., Lombard V., Morin E., Otillar R., Lindquist E.A., Sun H.,
RA   LaButti K.M., Schmutz J., Jabbour D., Luo H., Baker S.E., Pisabarro A.G.,
RA   Walton J.D., Blanchette R.A., Henrissat B., Martin F., Cullen D.,
RA   Hibbett D.S., Grigoriev I.V.;
RT   "Extensive sampling of basidiomycete genomes demonstrates inadequacy of the
RT   white-rot/brown-rot paradigm for wood decay fungi.";
RL   Proc. Natl. Acad. Sci. U.S.A. 111:9923-9928(2014).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2,3-saturated acyl-[ACP] + NADP(+) = a (2E)-enoyl-[ACP] +
CC         H(+) + NADPH; Xref=Rhea:RHEA:22564, Rhea:RHEA-COMP:9925, Rhea:RHEA-
CC         COMP:9926, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:78784, ChEBI:CHEBI:78785; EC=1.3.1.104;
CC         Evidence={ECO:0000256|ARBA:ARBA00035831};
CC   -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
CC       {ECO:0000256|ARBA:ARBA00007572}.
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. Quinone oxidoreductase subfamily.
CC       {ECO:0000256|ARBA:ARBA00010371}.
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DR   EMBL; KL198009; KDQ26938.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A067NFX6; -.
DR   STRING; 1137138.A0A067NFX6; -.
DR   VEuPathDB; FungiDB:PLEOSDRAFT_1093851; -.
DR   HOGENOM; CLU_285117_0_0_1; -.
DR   InParanoid; A0A067NFX6; -.
DR   OrthoDB; 2788069at2759; -.
DR   Proteomes; UP000027073; Unassembled WGS sequence.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003910; F:DNA ligase (ATP) activity; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006310; P:DNA recombination; IEA:InterPro.
DR   GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR   CDD; cd08290; ETR; 1.
DR   Gene3D; 1.10.3260.10; DNA ligase, ATP-dependent, N-terminal domain; 1.
DR   Gene3D; 3.30.470.30; DNA ligase/mRNA capping enzyme; 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   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR   InterPro; IPR013149; ADH-like_C.
DR   InterPro; IPR012310; DNA_ligase_ATP-dep_cent.
DR   InterPro; IPR016059; DNA_ligase_ATP-dep_CS.
DR   InterPro; IPR012308; DNA_ligase_ATP-dep_N.
DR   InterPro; IPR036599; DNA_ligase_N_sf.
DR   InterPro; IPR011032; GroES-like_sf.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020843; PKS_ER.
DR   PANTHER; PTHR43981; ENOYL-[ACYL-CARRIER-PROTEIN] REDUCTASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43981:SF2; ENOYL-[ACYL-CARRIER-PROTEIN] REDUCTASE, MITOCHONDRIAL; 1.
DR   Pfam; PF00107; ADH_zinc_N; 1.
DR   Pfam; PF01068; DNA_ligase_A_M; 1.
DR   Pfam; PF04675; DNA_ligase_A_N; 1.
DR   SMART; SM00829; PKS_ER; 1.
DR   SUPFAM; SSF56091; DNA ligase/mRNA capping enzyme, catalytic domain; 1.
DR   SUPFAM; SSF50129; GroES-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00697; DNA_LIGASE_A1; 1.
DR   PROSITE; PS50160; DNA_LIGASE_A3; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160};
KW   Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW   NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027073};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT   DOMAIN          408..525
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
SQ   SEQUENCE   1088 AA;  120783 MW;  DEF879EE8E4DF741 CRC64;
     MSEPVVVEGV PFSLQDPHIH PARGTFRRWL AALRRQFNPL PPNTVSILLR LLFPEEDKKR
     KYELQETKFI PLLANCFGFS STSLEKWDAE GNSGCLGCEL RRILEETHAD PSESISSLSI
     AQVDELLDEL AASSSFTDNS IRRKYLKASR RPRSAVIRCL FRPLTPLDAA CAVQIILRDM
     RPLLYPQTEK HYTAALKNIN SRSYTTLTKE DVMFELDPPG SLYRMSKVVA RLDEAVEAYE
     QSLKPGQPRI GIAIQIPKSS KAQSCGHGLK FLQGAKKVYA ETKYDGERAQ IHVEVPSDGT
     KVRITIFSKS TRDSSLDRVG VFPIIRQALG LEEGQTPRIS QNVILDAEMV AYQNDHIDEF
     WRIRGLVETT AYGVRGSCRI SGAGKPSNIA NSQCSLASSV NEGCHLALVF FDILYLDSQS
     TLHRPYDERR DLLERTVQPI PHHALFSKRT LLEPRRESLT AHLCEVFADA ISNHEEGLVL
     KASNSRYNDT LLPWVKVKRD YIPGLGDCLD MVILGADWEK DRGRGLYAPT GTLTTFYVGI
     LENSSEIESS PGTKPAFHIY YTSSYGLDRE TLEETNFLIK NSDPVEYDKK HPPQGLPYAY
     TLYPGIKPPG ILFSTPLLGE LYGDRFTKAA QSKYYELRFP RLIKIYRPKE RSWQGGVTPE
     VLLSTAREIL GVDDEDKDVR DVCKGLFGQP PSPGVRSGKK RMKQQVHWVS SALRAASNRA
     VVYTKNGDPT SVLTALTHPQ LPSPSPSTLN IKFLLAPINP ADINVVEGVY PAKPQLTSSL
     TQSGLGSADT PVYVGGNEGL AEVTEVGSGV EGLKKGDWVI MTRPQAGTWS SNKNVSPREL
     LKVPRELDGF KLDEVSGATI TVNPATAYNM IHDFTTLQEG DWLVQNGANS AVGQAVIQIA
     AAKGIKTLNF VRNRDNFSEL KAQLTSLGAT TVLTYDELAD KSLRGKVKEW TDGKGIRLGL
     NCVGGKDTTL MTQLLGQDGH LVTYGAMSKQ PLSLPTPMFI FKNLQAHGFW QSRWYKQRGP
     AEQGELMKKL VQFMSKGQLS PPEHEIVTIA GHESDETATQ KVREIMSKLA AGRFGKKVLL
     RMEEVTSD
//
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