ID A0A340XXH5_LIPVE Unreviewed; 1059 AA.
AC A0A340XXH5;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=LOW QUALITY PROTEIN: acyl-CoA dehydrogenase family member 10 {ECO:0000313|RefSeq:XP_007464937.1};
GN Name=ACAD10 {ECO:0000313|RefSeq:XP_007464937.1};
OS Lipotes vexillifer (Yangtze river dolphin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Lipotidae; Lipotes.
OX NCBI_TaxID=118797 {ECO:0000313|Proteomes:UP000265300, ECO:0000313|RefSeq:XP_007464937.1};
RN [1] {ECO:0000313|RefSeq:XP_007464937.1}
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 -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00009347}.
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DR RefSeq; XP_007464937.1; XM_007464875.1.
DR STRING; 118797.A0A340XXH5; -.
DR GeneID; 103088053; -.
DR KEGG; lve:103088053; -.
DR CTD; 80724; -.
DR InParanoid; A0A340XXH5; -.
DR OrthoDB; 276350at2759; -.
DR Proteomes; UP000265300; Unplaced.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW.
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 CDD; cd02603; HAD_sEH-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 Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 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; IPR013786; AcylCoA_DH/ox_N.
DR InterPro; IPR037069; AcylCoA_DH/ox_N_sf.
DR InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom_sf.
DR InterPro; IPR002575; Aminoglycoside_PTrfase.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR006439; HAD-SF_hydro_IA.
DR InterPro; IPR011945; HAD-SF_ppase_IA/epoxid_hydro_N.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR023198; PGP-like_dom2.
DR NCBIfam; TIGR02247; HAD-1A3-hyp; 1.
DR NCBIfam; TIGR01509; HAD-SF-IA-v3; 1.
DR PANTHER; PTHR47829:SF1; AMINOGLYCOSIDE PHOSPHOTRANSFERASE DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR47829; HYDROLASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G12880)-RELATED; 1.
DR Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR Pfam; PF02771; Acyl-CoA_dh_N; 1.
DR Pfam; PF01636; APH; 1.
DR Pfam; PF00702; Hydrolase; 1.
DR PRINTS; PR00413; HADHALOGNASE.
DR SFLD; SFLDG01129; C1.5:_HAD__Beta-PGM__Phosphata; 1.
DR SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
PE 3: Inferred from homology;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000265300}.
FT DOMAIN 288..502
FT /note="Aminoglycoside phosphotransferase"
FT /evidence="ECO:0000259|Pfam:PF01636"
FT DOMAIN 686..786
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 791..892
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 904..1052
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT REGION 614..640
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1059 AA; 117900 MW; B14947FFAC78D0E1 CRC64;
MCLRQLLQSA QLQRAWRAVF VKHGQGRHQG AWRWTHSGGG TYRAVIFDMG GVLIPSPGRV
AAEWEVQNHI PSGTILKALI SGGENGPWMK FMRAEITTED FLQEFGRLCS EISKTSVPLD
SFFSLLTSER VAKQFPVMTE AITQIRAKGL QTAVLSNNFY LPNGKSFLPL DRKQFDVVVE
SCLEGVCKPD ARMYKLCLER LGRQPSESIF LDDLGPNLKA AASLGIHTIK VHDPETAVKE
LETLLGFPLR MAVPNTRPVR KTMEIPKDSL EKHLKDLLGT QATGPLELLQ FDHGXSNPTY
YIKLAKHQLV LRKKPPGTLL PSAHAVEREF RIMKALANAG VPVPKVLDLC EDSRVIGTPF
YLMEYCPGLI YKDPSLPGLE PSQRRAIYTA MNRVLCKIHS VDLKAAGLED YGKHGDYVAC
QVQTWIKQYR ASETSTIPPM ERLIEWLPLH LPRQQQTTVV HGDFRLDNLL FHPETAEVLA
VLDWELSTLG DPLADVAYSC LAHYLPSSSP VQPGLSDSDL SELGIPTAEE YFRMYCLHMG
IHPAENWNFY MAFSFFRIAV ILQGVYKHTL TGHASSATGE QTGKLTEFMS NLAWDFAVKE
GFRIFKEMPA TKPLTRPHHT RARPQSLPRT PGMRSYVTST DSSPAHVSKG ALVFSPEGLS
PPVRELYQRL KQSMERHVYP AEPELQHYQA SAEKWAPSPL VEDLKEKAKA EGLWNLFLPV
ETDPEKKYGA GLTNVEYAHL CEVMGTSLYA PEIFNCSAPD TGNMELLVRY GTKEQKARWL
ILLLEGKARS CFAMTEPQVA SSDATNIDSS IQEEDGFYVI NGHEWWISGI LDPRCQLCVF
MGKTDPHAPR HQQQSMLLVP VDTPGIKIIR PLTVYALEDA PGGHGQVLFE QVCVPKENMV
LGPGRGFEIA QGRLGPGRIH HCMRLIGYSE RALALTKARA KSRVAFGKPL VEQGTVLADI
AQSRVEIEQA QLLVLKAAHV MDVEGNKAAA LDIAMIKMVA LSMAYRVTDR AIQAFGAAGL
SSDYPLSQFF TRARALHFAD GPDEVHRAAV AKMELKRCS
//
