ID ACADV_RAT Reviewed; 655 AA.
AC P45953;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-APR-2013, entry version 108.
DE RecName: Full=Very long-chain specific acyl-CoA dehydrogenase, mitochondrial;
DE Short=VLCAD;
DE EC=1.3.8.9;
DE Flags: Precursor;
GN Name=Acadvl; Synonyms=Vlcad;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC Muroidea; Muridae; Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=Wistar; TISSUE=Liver;
RX PubMed=8034667;
RA Aoyama T., Ueno I., Kamijo T., Hashimoto T.;
RT "Rat very-long-chain acyl-CoA dehydrogenase, a novel mitochondrial
RT acyl-CoA dehydrogenase gene product, is a rate-limiting enzyme in
RT long-chain fatty acid beta-oxidation system. cDNA and deduced amino
RT acid sequence and distinct specificities of the cDNA-expressed
RT protein.";
RL J. Biol. Chem. 269:19088-19094(1994).
CC -!- FUNCTION: Active toward esters of long-chain and very long chain
CC fatty acids such as palmitoyl-CoA, mysritoyl-CoA and stearoyl-CoA.
CC Can accommodate substrate acyl chain lengths as long as 24
CC carbons, but shows little activity for substrates of less than 12
CC carbons.
CC -!- CATALYTIC ACTIVITY: A very-long-chain acyl-CoA + electron-transfer
CC flavoprotein = a very-long-chain trans-2,3-dehydroacyl-CoA +
CC reduced electron-transfer flavoprotein.
CC -!- COFACTOR: FAD.
CC -!- PATHWAY: Lipid metabolism; mitochondrial fatty acid beta-
CC oxidation.
CC -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane.
CC -!- PTM: S-nitrosylation at Cys-237 in liver improves catalytic
CC efficiency (By similarity).
CC -!- MISCELLANEOUS: A number of straight-chain acyl-CoA dehydrogenases
CC of different substrate specificities are present in mammalian
CC tissues.
CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
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DR EMBL; D30647; BAA06331.1; -; mRNA.
DR IPI; IPI00213057; -.
DR PIR; A54872; A54872.
DR RefSeq; NP_037023.1; NM_012891.2.
DR UniGene; Rn.33319; -.
DR ProteinModelPortal; P45953; -.
DR SMR; P45953; 69-653.
DR STRING; 10116.ENSRNOP00000024973; -.
DR PaxDb; P45953; -.
DR PRIDE; P45953; -.
DR GeneID; 25363; -.
DR KEGG; rno:25363; -.
DR UCSC; RGD:2014; rat.
DR CTD; 37; -.
DR RGD; 2014; Acadvl.
DR eggNOG; COG1960; -.
DR HOGENOM; HOG000131665; -.
DR HOVERGEN; HBG050448; -.
DR InParanoid; P45953; -.
DR KO; K09479; -.
DR OrthoDB; EOG4P5K8R; -.
DR UniPathway; UPA00660; -.
DR NextBio; 606351; -.
DR ArrayExpress; P45953; -.
DR Genevestigator; P45953; -.
DR GermOnline; ENSRNOG00000018114; Rattus norvegicus.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:RGD.
DR GO; GO:0000062; F:fatty-acyl-CoA binding; IDA:RGD.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IDA:RGD.
DR GO; GO:0017099; F:very-long-chain-acyl-CoA dehydrogenase activity; IDA:RGD.
DR GO; GO:0033539; P:fatty acid beta-oxidation using acyl-CoA dehydrogenase; IMP:RGD.
DR GO; GO:0042760; P:very long-chain fatty acid catabolic process; IMP:RGD.
DR Gene3D; 1.10.540.10; -; 1.
DR Gene3D; 2.40.110.10; -; 1.
DR InterPro; IPR006089; Acyl-CoA_DH_CS.
DR InterPro; IPR006092; Acyl-CoA_DH_N.
DR InterPro; IPR006090; Acyl-CoA_Oxase/DH_1.
DR InterPro; IPR006091; Acyl-CoA_Oxase/DH_cen-dom.
DR InterPro; IPR009075; AcylCo_DH/oxidase_C.
DR InterPro; IPR013786; AcylCoA_DH/ox_N.
DR InterPro; IPR009100; AcylCoA_DH/oxidase.
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; SSF56645; AcylCoA_dehyd_NM; 1.
DR SUPFAM; SSF47203; AcylCoADH_C_like; 1.
DR PROSITE; PS00072; ACYL_COA_DH_1; 1.
DR PROSITE; PS00073; ACYL_COA_DH_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Complete proteome; Direct protein sequencing; FAD;
KW Fatty acid metabolism; Flavoprotein; Isopeptide bond;
KW Lipid metabolism; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Oxidoreductase; Reference proteome;
KW S-nitrosylation; Transit peptide; Ubl conjugation.
FT TRANSIT 1 40 Mitochondrion.
FT CHAIN 41 655 Very long-chain specific acyl-CoA
FT dehydrogenase, mitochondrial.
FT /FTId=PRO_0000000518.
FT NP_BIND 214 223 FAD (By similarity).
FT NP_BIND 249 251 FAD (By similarity).
FT NP_BIND 435 439 FAD (By similarity).
FT NP_BIND 464 466 FAD (By similarity).
FT REGION 41 482 Catalytic.
FT REGION 338 341 Substrate binding (By similarity).
FT REGION 462 463 Substrate binding (By similarity).
FT REGION 483 516 Membrane-anchoring (Probable).
FT ACT_SITE 462 462 Proton acceptor (By similarity).
FT BINDING 223 223 Substrate; via carbonyl oxygen (By
FT similarity).
FT BINDING 366 366 FAD (By similarity).
FT BINDING 463 463 Substrate; via amide nitrogen (By
FT similarity).
FT MOD_RES 237 237 S-nitrosocysteine (By similarity).
FT MOD_RES 239 239 N6-acetyllysine (By similarity).
FT MOD_RES 276 276 N6-acetyllysine (By similarity).
FT MOD_RES 331 331 N6-acetyllysine (By similarity).
FT CROSSLNK 331 331 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in ubiquitin) (By
FT similarity).
SQ SEQUENCE 655 AA; 70749 MW; E808EDEB0E4595D7 CRC64;
MQSARMTPSV GRQLLRLGAR SSRSAALQGQ PRPTSAQRLY ASEATQAVLE KPETLSSDAS
TREKPARAES KSFAVGMFKG QLTTDQVFPY PSVLNEGQTQ FLKELVGPVA RFFEEVNDPA
KNDSLEKVEE DTLQGLKELG AFGLQVPSEL GGLGLSNTQY ARLAEIVGMH DLGVSVTLGA
HQSIGFKGIL LYGTKAQKEK YLPRVASGQA LAAFCLTEPS SGSDVASIRS SAVPSPCGKY
YTLNGSKIWI SNGGLADIFT VFAKTPIKDA ATGAVKEKIT AFVVERSFGG VTHGLPEKKM
GIKASNTSEV YFDGVKVPAE NVLGEVGDGF KVAVNILNNG RFGMAATLAG TMKAIIAKAV
DHATNRTQFG DKIHNFGVIQ EKLARMAILQ YVTESMAYML SANMDQGFKD FQIEAAISKI
FGSEAAWKVT DECIQIMGGM GFMKEPGVER VLRDIRIFRI FEGTNDILRL FVALQGCMDK
GKELTGLGNA LKNPLGNVGL LIGEASKQLR RRTGIGSGLS LSGIVHPELS RSGELAVQAL
EQFATVVEAK LMKHKKGIVN EQFLLQRLAD GAIDLYAMVV VLSRASRSLS EGYPTAQHEK
MLCDSWCIEA ATRIRENMAS LQSNPQQQEL FRNFRSISKA MVENGGLVTS NPLRV
//
