ID A0A0D2PNG1_GOSRA Unreviewed; 814 AA.
AC A0A0D2PNG1;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Acyl-CoA dehydrogenase IBR3 {ECO:0008006|Google:ProtNLM};
GN ORFNames=B456_005G061800 {ECO:0000313|EMBL:KJB28673.1};
OS Gossypium raimondii (New World cotton).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX NCBI_TaxID=29730 {ECO:0000313|EMBL:KJB28673.1, ECO:0000313|Proteomes:UP000032304};
RN [1] {ECO:0000313|EMBL:KJB28673.1, ECO:0000313|Proteomes:UP000032304}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23257886; DOI=10.1038/nature11798;
RA Paterson A.H., Wendel J.F., Gundlach H., Guo H., Jenkins J., Jin D.,
RA Llewellyn D., Showmaker K.C., Shu S., Udall J., Yoo M.J., Byers R.,
RA Chen W., Doron-Faigenboim A., Duke M.V., Gong L., Grimwood J., Grover C.,
RA Grupp K., Hu G., Lee T.H., Li J., Lin L., Liu T., Marler B.S., Page J.T.,
RA Roberts A.W., Romanel E., Sanders W.S., Szadkowski E., Tan X., Tang H.,
RA Xu C., Wang J., Wang Z., Zhang D., Zhang L., Ashrafi H., Bedon F.,
RA Bowers J.E., Brubaker C.L., Chee P.W., Das S., Gingle A.R., Haigler C.H.,
RA Harker D., Hoffmann L.V., Hovav R., Jones D.C., Lemke C., Mansoor S.,
RA ur Rahman M., Rainville L.N., Rambani A., Reddy U.K., Rong J.K.,
RA Saranga Y., Scheffler B.E., Scheffler J.A., Stelly D.M., Triplett B.A.,
RA Van Deynze A., Vaslin M.F., Waghmare V.N., Walford S.A., Wright R.J.,
RA Zaki E.A., Zhang T., Dennis E.S., Mayer K.F., Peterson D.G., Rokhsar D.S.,
RA Wang X., Schmutz J.;
RT "Repeated polyploidization of Gossypium genomes and the evolution of
RT spinnable cotton fibres.";
RL Nature 492:423-427(2012).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; CM001744; KJB28673.1; -; Genomic_DNA.
DR RefSeq; XP_012482135.1; XM_012626681.1.
DR AlphaFoldDB; A0A0D2PNG1; -.
DR EnsemblPlants; KJB28673; KJB28673; B456_005G061800.
DR Gramene; KJB28673; KJB28673; B456_005G061800.
DR OrthoDB; 276350at2759; -.
DR Proteomes; UP000032304; Chromosome 5.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro.
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:UP000032304}.
FT DOMAIN 43..271
FT /note="Aminoglycoside phosphotransferase"
FT /evidence="ECO:0000259|Pfam:PF01636"
FT DOMAIN 545..646
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 658..806
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT REGION 376..403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 377..396
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 814 AA; 90327 MW; 24426F9999F643D9 CRC64;
MANRTGDLVE AVQEAHKIDV KALFGYASAN VPGFPLSPSK FNLSQFGHGQ SNPTYLMEVE
TGSGTVKRYV LRKKPPGKLL QSAHAVEREF QVLKALGDNT NVPVPKVFCL CNDPTVIGTA
FYIMEYLEGR IFVDPSLPGV PPERRRAIYQ ATAKVLASLH SANIDAIGLG SYGRRDNYCK
RQIERWFKQY LASTSEGKPE RYPKMFELVD WLRKNIPPED ASGATGGLVH GDFRVDNVVF
HPTEDRVIGI LDWELSTIGN QMCDVAYSCM PYITQAGLGS DELVKGFEII GIPEGIPTQA
EFLAEYCLES GKAWPVSEWK FYVAFSLFRG ASIYTGVYNR WLMGNASGGK RAEHAGRHAK
SLVDSALDFI SKKTVLPEQP PSVSRGSRQY GTENKAQGLP EGSGRFVPSK KIQELRNKLI
QFMEVHIYPL ENEFNKLARS DLRWTVHPEE ERLKELAKKE GLWNLWIPFD SAARAKELIF
NGSAHCTHDR LLGAGLSNLE YGYLCEIMGR SLWAPQIFNC GAPDTGNMEL NEWLVPLLEG
KIRSAFAMTE PQVASSDATN IECSIKRQGD SYIINGTKWW TSGAMDPRCR ILILMGKTDF
TAPKHKQQSM ILVDIKTPGI CVKRPLTVFG FDDAPHGHAE VSFENVRVPA KNILLGEGRG
FEIAQGRLGP GRLHHCMRLI GTAERGMQLM AERALNRKTF GKYIAQHGSF LSDFAKCRIE
LEQTRLLVLE AADQLDRLGN KKARGTIAMA KVAAPNMALK VLDRAIQVHG GAGVSSDTVL
AHLWASARTL RIADGPDEVH LGTIAQLELR RAKL
//
