ID K7G7J7_PELSI Unreviewed; 437 AA.
AC K7G7J7;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=medium-chain acyl-CoA dehydrogenase {ECO:0000256|ARBA:ARBA00012033};
DE EC=1.3.8.7 {ECO:0000256|ARBA:ARBA00012033};
OS Pelodiscus sinensis (Chinese softshell turtle) (Trionyx sinensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Trionychia;
OC Trionychidae; Pelodiscus.
OX NCBI_TaxID=13735 {ECO:0000313|Ensembl:ENSPSIP00000016258.1, ECO:0000313|Proteomes:UP000007267};
RN [1] {ECO:0000313|Proteomes:UP000007267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Daiwa-1 {ECO:0000313|Proteomes:UP000007267};
RG Soft-shell Turtle Genome Consortium;
RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000007267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Daiwa-1 {ECO:0000313|Proteomes:UP000007267};
RX PubMed=23624526; DOI=10.1038/ng.2615;
RA Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT into the development and evolution of the turtle-specific body plan.";
RL Nat. Genet. 45:701-706(2013).
RN [3] {ECO:0000313|Ensembl:ENSPSIP00000016258.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|RuleBase:RU362125};
CC -!- PATHWAY: Lipid metabolism; mitochondrial fatty acid beta-oxidation.
CC {ECO:0000256|ARBA:ARBA00005198}.
CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00009347, ECO:0000256|RuleBase:RU362125}.
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DR EMBL; AGCU01028967; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01028968; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01028969; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01028970; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01028971; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_006114550.2; XM_006114488.2.
DR AlphaFoldDB; K7G7J7; -.
DR STRING; 13735.ENSPSIP00000016258; -.
DR Ensembl; ENSPSIT00000016334.1; ENSPSIP00000016258.1; ENSPSIG00000014499.1.
DR GeneID; 102456845; -.
DR KEGG; pss:102456845; -.
DR eggNOG; KOG0139; Eukaryota.
DR GeneTree; ENSGT00940000164410; -.
DR HOGENOM; CLU_018204_0_3_1; -.
DR OMA; YQCEKMG; -.
DR OrthoDB; 1820620at2759; -.
DR TreeFam; TF105054; -.
DR Proteomes; UP000007267; Unassembled WGS sequence.
DR GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IEA:InterPro.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
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; IPR006089; Acyl-CoA_DH_CS.
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 PANTHER; PTHR48083; MEDIUM-CHAIN SPECIFIC ACYL-COA DEHYDROGENASE, MITOCHONDRIAL-RELATED; 1.
DR PANTHER; PTHR48083:SF6; ZGC:85777; 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 SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1.
DR PROSITE; PS00072; ACYL_COA_DH_1; 1.
DR PROSITE; PS00073; ACYL_COA_DH_2; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|RuleBase:RU362125};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU362125};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU362125};
KW Reference proteome {ECO:0000313|Proteomes:UP000007267};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..437
FT /note="medium-chain acyl-CoA dehydrogenase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003906229"
FT DOMAIN 57..171
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 175..270
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 282..428
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 437 AA; 47796 MW; 6D7F60E260B78E51 CRC64;
MRVASSSTAL AMARCWFGLR ARGAWGQGLS VLCGPARPGS SSCASAASGE GAHLLYTREH
YAVRASLRKI IDKEINPFVD KWEEEGQFPA HKVFKTLGQA GFLGVNKPKE YGGMGLDFSY
SIAVAEELGN IRCGGIPMAI GVQTDMATPA LTRFGSDELK RQFLVPTIAG EVVACLGVSE
PGAGSDVASI KTTAVRKGDD YVINGGKMWI TSGCQADWMC LLANSSEGPP HQNKSLICLP
MNLPGVHVAK KIDKMGMRSS DTAQIFFEDV RVPSKYLIGE EGMGFTYQML QFQEERLWAV
ANILAPMENV IQETIDYTRQ RKIYSQPVLH NQTVHFRLAE LATEVELVRS LLYQAVALYL
RGNDVTKLAS MAKLKAGRLA RELTDNCLQF WGGMGFTNEV LVSKLYRDSR LLSIGAGADE
VMLSIICKYM GTLPQKK
//
