ID A0A1S3XEN9_TOBAC Unreviewed; 820 AA.
AC A0A1S3XEN9;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Probable acyl-CoA dehydrogenase IBR3 {ECO:0000313|RefSeq:XP_016438330.1};
GN Name=LOC107764289 {ECO:0000313|RefSeq:XP_016438330.1};
OS Nicotiana tabacum (Common tobacco).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC Nicotiana.
OX NCBI_TaxID=4097 {ECO:0000313|Proteomes:UP000084051, ECO:0000313|RefSeq:XP_016438330.1};
RN [1] {ECO:0000313|Proteomes:UP000084051}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. TN90 {ECO:0000313|Proteomes:UP000084051};
RX PubMed=24807620; DOI=10.1038/ncomms4833;
RA Sierro N., Battey J.N., Ouadi S., Bakaher N., Bovet L., Willig A.,
RA Goepfert S., Peitsch M.C., Ivanov N.V.;
RT "The tobacco genome sequence and its comparison with those of tomato and
RT potato.";
RL Nat. Commun. 5:3833-3833(2014).
RN [2] {ECO:0000313|RefSeq:XP_016438330.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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 RefSeq; XP_016438330.1; XM_016582844.1.
DR AlphaFoldDB; A0A1S3XEN9; -.
DR SMR; A0A1S3XEN9; -.
DR STRING; 4097.A0A1S3XEN9; -.
DR PaxDb; 4097-A0A1S3XEN9; -.
DR GeneID; 107764289; -.
DR KEGG; nta:107764289; -.
DR OMA; LHGGHFE; -.
DR OrthoDB; 276350at2759; -.
DR Proteomes; UP000084051; Unplaced.
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 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 Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Reference proteome {ECO:0000313|Proteomes:UP000084051}.
FT DOMAIN 42..268
FT /note="Aminoglycoside phosphotransferase"
FT /evidence="ECO:0000259|Pfam:PF01636"
FT DOMAIN 551..652
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 664..812
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT REGION 376..398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 376..391
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 820 AA; 91137 MW; 303B7F56BB0315DA CRC64;
MANKTSDLVG RVDPAQSFNT EALLRYASAN VVGFPTNPSQ FTVSQFGHGQ SNPTFLIEVH
SGTLAKRYVL RKKPHGTLLT SAHAVEREYK VLHAMSTHTV VPVPKVFCLC TDSSVIGTPF
YIMEYLEGRI FIDPKLPDVQ PERRRVIYRA VAQALAVLHS ADVDAIGLGN YGKRTDYCKR
QVERWAKQYL LSTGEGKSRR NPKMLELADW LRQHIPLEDS SGATAGLVHG DFRIDNVVFH
PIEDRVIGIL DWELSTLGNQ MCDVAYSCLG HIVNIASEDI EENNGFELTS FPEGVPSLAN
YLADYCSAAG RPWPVDQWKF YIAFSLFRGA SIYAGVHSRW IMGNASGGER ARSTGEKADS
FIRTAWSFIQ RKSVLPQHPP TETSSEHSPN QGMPVGGRFV PSEKVQKLRQ KLIKFMEDHI
YPRENEFSKL AQSNMRWTIH PDEEKLKELA KKEGLWNLWI PFDSAARARE LIYGSRNGLS
NNDSDRLLGA GLSNLEYGYL CEIMGRSVWA PQIFNCGAPD TGNMEVLLRY GNEVQMKEWL
VPLLEGKIRS GFAMTEPQVA SSDATNIECS IKRHGDSYIV NGTKWWTSGA MDPRCKILIV
MGKTDLAAPK HKQQSMILVD VNSPGITVKR PLTVFGFDDA PHGHAEILFE NVRVPANNIL
LGEGRGFEIA QGRLGPGRLH HCMRLIGAAD RGMQMMVQRA LQRRAFGKLI AQQGSFLSDV
ARCRIDLEKT RLLVLEAAEQ LDRLGNKKAR GTIAMAKVAA PDMALKVLDT AMQVHGAAGL
SGDTVLAHLW ATARTLRIAD GPDEVHLGTI AKMELQRARL
//