ACDSB_DICDI
ID ACDSB_DICDI Reviewed; 413 AA.
AC Q54RR5;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Probable short/branched chain specific acyl-CoA dehydrogenase {ECO:0000250|UniProtKB:P70584};
DE Short=SBCAD {ECO:0000250|UniProtKB:P70584};
DE EC=1.3.8.5 {ECO:0000250|UniProtKB:P70584};
GN Name=acadsb; ORFNames=DDB_G0282967;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: Probable short and branched chain specific acyl-CoA
CC dehydrogenase that catalyzes the removal of one hydrogen from C-2 and
CC C-3 of the fatty acyl-CoA thioester, resulting in the formation of
CC trans-2-enoyl-CoA. {ECO:0000250|UniProtKB:P70584}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-methylbutanoyl-CoA + H(+) + oxidized [electron-transfer
CC flavoprotein] = (2E)-2-methylbut-2-enoyl-CoA + reduced [electron-
CC transfer flavoprotein]; Xref=Rhea:RHEA:43780, Rhea:RHEA-COMP:10685,
CC Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57336,
CC ChEBI:CHEBI:57337, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307; EC=1.3.8.5;
CC Evidence={ECO:0000250|UniProtKB:P70584};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43781;
CC Evidence={ECO:0000250|UniProtKB:P70584};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:P45954};
CC -!- PATHWAY: Lipid metabolism; mitochondrial fatty acid beta-oxidation.
CC {ECO:0000250|UniProtKB:P45954}.
CC -!- PATHWAY: Amino-acid degradation; L-isoleucine degradation.
CC {ECO:0000250|UniProtKB:P45954}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P45954}.
CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; AAFI02000049; EAL65927.1; -; Genomic_DNA.
DR RefSeq; XP_639286.1; XM_634194.1.
DR AlphaFoldDB; Q54RR5; -.
DR SMR; Q54RR5; -.
DR STRING; 44689.DDB0237707; -.
DR PaxDb; Q54RR5; -.
DR PRIDE; Q54RR5; -.
DR EnsemblProtists; EAL65927; EAL65927; DDB_G0282967.
DR GeneID; 8623855; -.
DR KEGG; ddi:DDB_G0282967; -.
DR dictyBase; DDB_G0282967; acadsb.
DR eggNOG; KOG0139; Eukaryota.
DR HOGENOM; CLU_018204_0_0_1; -.
DR InParanoid; Q54RR5; -.
DR OMA; LYREAPM; -.
DR PhylomeDB; Q54RR5; -.
DR Reactome; R-DDI-70895; Branched-chain amino acid catabolism.
DR UniPathway; UPA00364; -.
DR UniPathway; UPA00660; -.
DR PRO; PR:Q54RR5; -.
DR Proteomes; UP000002195; Chromosome 4.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0047119; F:2-methyl-branched-chain-enoyl-CoA reductase activity; IEA:UniProtKB-EC.
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:0102035; F:isobutyryl-CoA:FAD oxidoreductase activity; IEA:UniProtKB-EC.
DR GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006550; P:isoleucine catabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.10.540.10; -; 1.
DR Gene3D; 2.40.110.10; -; 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.
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; SSF47203; 1.
DR SUPFAM; SSF56645; SSF56645; 1.
DR PROSITE; PS00072; ACYL_COA_DH_1; 1.
PE 3: Inferred from homology;
KW FAD; Fatty acid metabolism; Flavoprotein; Lipid metabolism; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..413
FT /note="Probable short/branched chain specific acyl-CoA
FT dehydrogenase"
FT /id="PRO_0000330466"
FT ACT_SITE 393
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P45954"
FT BINDING 152..161
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P45954"
FT BINDING 161
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P45954"
FT BINDING 186..188
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P45954"
FT BINDING 208
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P45954"
FT BINDING 262
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P45954"
FT BINDING 270..273
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P45954"
FT BINDING 298
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250|UniProtKB:P45954"
FT BINDING 309
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250|UniProtKB:P45954"
FT BINDING 366..370
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250|UniProtKB:P45954"
FT BINDING 395..397
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P45954"
SQ SEQUENCE 413 AA; 45030 MW; 918A06E0D0A89692 CRC64;
MIKKLILDPK NVSIIKNGIR NYSKSKSFIQ PITTLSEEET LLKETVANFA NEKVRPLVKV
MDETSELNKG LLKDLFDMNL MGIDISDSYG GANMNFMGSI IAIEELAKVD PAISVIVDVQ
NTLVNNCINR YGSIQQREKY LSMLATNTVG SFCLSESGSG SDAFALATRA VRQSDGTFVL
NGTKQWITNA KEAGVFIVMA NVDPSQGYKG ITAFIVESNN PGLRIGKKED KLGIRASSTC
EVILDNCVVK PTDILGELGR GYKIAIEGLN EGRIGIAAQM LGLAQGVFDS TIPYLMERKQ
FGKPIATFQG MQFTYADLAV DIEAGRLLTY NAARIKEAGL PFVFQASMAK LHCSRVAEKA
ASACISMLGG VGFTKEFPAE KFFRDSKVGQ IYEGTSNIQL QTIAKEIVKN FNK
