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Database: UniProt
Entry: W1P6H1_AMBTC
LinkDB: W1P6H1_AMBTC
Original site: W1P6H1_AMBTC 
ID   W1P6H1_AMBTC            Unreviewed;       824 AA.
AC   W1P6H1;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   24-JAN-2024, entry version 47.
DE   RecName: Full=Acyl-CoA dehydrogenase IBR3 {ECO:0008006|Google:ProtNLM};
GN   ORFNames=AMTR_s00003p00122400 {ECO:0000313|EMBL:ERN03166.1};
OS   Amborella trichopoda.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Amborellales; Amborellaceae; Amborella.
OX   NCBI_TaxID=13333 {ECO:0000313|EMBL:ERN03166.1, ECO:0000313|Proteomes:UP000017836};
RN   [1] {ECO:0000313|Proteomes:UP000017836}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=24357323;
RG   Amborella Genome Project;
RT   "The Amborella genome and the evolution of flowering plants.";
RL   Science 342:1241089-1241089(2013).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR   EMBL; KI394358; ERN03166.1; -; Genomic_DNA.
DR   RefSeq; XP_006841491.1; XM_006841428.2.
DR   AlphaFoldDB; W1P6H1; -.
DR   STRING; 13333.W1P6H1; -.
DR   EnsemblPlants; ERN03166; ERN03166; AMTR_s00003p00122400.
DR   GeneID; 18431303; -.
DR   Gramene; ERN03166; ERN03166; AMTR_s00003p00122400.
DR   KEGG; atr:18431303; -.
DR   eggNOG; KOG1469; Eukaryota.
DR   HOGENOM; CLU_007526_3_0_1; -.
DR   OMA; LHGGHFE; -.
DR   OrthoDB; 276350at2759; -.
DR   Proteomes; UP000017836; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IBA:GO_Central.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0033539; P:fatty acid beta-oxidation using acyl-CoA dehydrogenase; IBA:GO_Central.
DR   GO; GO:0048767; P:root hair elongation; IEA:EnsemblPlants.
DR   CDD; cd05154; ACAD10_11_N-like; 1.
DR   Gene3D; 3.90.1200.10; -; 1.
DR   Gene3D; 1.10.540.10; Acyl-CoA dehydrogenase/oxidase, N-terminal domain; 1.
DR   Gene3D; 2.40.110.10; Butyryl-CoA Dehydrogenase, subunit A, domain 2; 1.
DR   Gene3D; 1.20.140.10; Butyryl-CoA Dehydrogenase, subunit A, domain 3; 1.
DR   InterPro; IPR041726; ACAD10_11_N.
DR   InterPro; IPR006091; Acyl-CoA_Oxase/DH_mid-dom.
DR   InterPro; IPR046373; Acyl-CoA_Oxase/DH_mid-dom_sf.
DR   InterPro; IPR036250; AcylCo_DH-like_C.
DR   InterPro; IPR009075; AcylCo_DH/oxidase_C.
DR   InterPro; IPR037069; AcylCoA_DH/ox_N_sf.
DR   InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom_sf.
DR   InterPro; IPR002575; Aminoglycoside_PTrfase.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   PANTHER; PTHR48083:SF13; ACYL-COA DEHYDROGENASE FAMILY MEMBER 11; 1.
DR   PANTHER; PTHR48083; MEDIUM-CHAIN SPECIFIC ACYL-COA DEHYDROGENASE, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR   Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR   Pfam; PF01636; APH; 1.
DR   SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
DR   SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
PE   4: Predicted;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017836}.
FT   DOMAIN          44..270
FT                   /note="Aminoglycoside phosphotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF01636"
FT   DOMAIN          555..653
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          668..816
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   824 AA;  92096 MW;  DE1C255CDDA6DF97 CRC64;
     MASRARDLLG DVQAAHQFDE NALLRYCQEN VEGFPVELIT FRVLQFRHGQ SNPTYCLEVQ
     STSSVKRYVL RKKPPGRLLE TAHAVEREFQ VLKALGDNTR VPVPKAFCLC SDVSVIGTAF
     YIMEYLEGRI FLDPKLPGLN PTVRKSIYLS SAKALAALHS VDVDSVGLRK YGRRDNYCRR
     QIERWAKQYL SATGEGKLER NPKMLNLVDW LNYHIPPEDS SGASGTGLVH GDYRIDNLVF
     HPSEERVIGI LDWELSTLGN QMSDVAYTCM PYILDLTSND AISGVEYVNI PEGIPSQAEY
     LAEYCSAAGR PWPYKHWKFY IAFSMFRGAS IYAGVYHRWN QGNATGGERA QNTGRLANNL
     IETAWAFIAR DDVLPSRPPS ALGGAHVPLE REGVAGDMDR GRYVLRPDVQ ELRSKLLKFI
     DNHIYPLEEE FNKLANSSMR WTVHPEEERL KEMARMEGLW NLWIPEDTAK RARLLLGGSM
     GDSLEYGKAQ LLGAGLSNLE YAYLCEIMGR SNWAPQIFNC NAPDTGNMEV LLQYGTREQQ
     LEWLVPLLEG RIRSGFAMTE PQVASSDATN IECSITRQGD HYIINGNKWW TSGAMDPRCK
     LLIVMGKTDQ TAPRHWQQSM ILVDIQSPGV CVKRPLKVFG FDDAPHGHAE VSFTSVCVPI
     TNLLLGEGRG FEIAQGRLGP GRLHHCMRLI GAAERGLSMM VERAQKRKVF GKLIAEQGSF
     LSDLAKCRVE LEKTRLLVLE AADQLDRFGN KKARGIIAMA KVAAPNMALQ VLDRAIQVHG
     AAGVSSDTVL AHLWATARTL RIADGPDEVH LGTIAKLELQ RAKL
//
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