| Tag | Content |
|---|
| CPLM ID | CPLM-009982 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Short/branched chain specific acyl-CoA dehydrogenase, mitochondrial |
Protein Synonyms/Alias | SBCAD; 2-methyl branched chain acyl-CoA dehydrogenase; 2-MEBCAD; 2-methylbutyryl-coenzyme A dehydrogenase; 2-methylbutyryl-CoA dehydrogenase |
Gene Name | Acadsb |
Gene Synonyms/Alias | |
Created Date | July 27, 2013 |
Organism | Rattus norvegicus (Rat) |
NCBI Taxa ID | 10116 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 70 | MMQKAVKKFAQEQIA | acetylation | [1] | | 88 | STMDENSKMEKSVIQ | acetylation | [1] | | 278 | PETSVLGKIGHGYKY | acetylation | [1] | | 284 | GKIGHGYKYAIGSLN | acetylation | [1] | | 324 | KERMQFGKRIFDFQG | acetylation | [1] |
|
Reference | [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns. Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV. Cell Rep. 2012 Aug 30;2(2):419-31. [ PMID: 22902405] |
Functional Description | Has greatest activity toward short branched chain acyl- CoA derivative such as (s)-2-methylbutyryl-CoA, isobutyryl-CoA, and 2-methylhexanoyl-CoA as well as toward short straight chain acyl-CoAs such as butyryl-CoA and hexanoyl-CoA. Can use valproyl- CoA as substrate and may play a role in controlling the metabolic flux of valproic acid in the development of toxicity of this agent. |
Sequence Annotation | NP_BIND 174 183 FAD (By similarity).
NP_BIND 207 209 FAD (By similarity).
NP_BIND 387 391 FAD; shared with dimeric partner (By
NP_BIND 416 418 FAD (By similarity).
REGION 229 230 Substrate binding (By similarity).
REGION 291 294 Substrate binding (By similarity).
ACT_SITE 414 414 Proton acceptor (By similarity).
BINDING 183 183 Substrate; via carbonyl oxygen (By
BINDING 283 283 Substrate (By similarity).
BINDING 319 319 FAD; shared with dimeric partner (By
BINDING 330 330 FAD; shared with dimeric partner (By
BINDING 415 415 Substrate; via amide nitrogen (By
MOD_RES 284 284 N6-acetyllysine (By similarity). |
Keyword | Acetylation; Complete proteome; Direct protein sequencing; FAD; Fatty acid metabolism; Flavoprotein; Lipid metabolism; Mitochondrion; Oxidoreductase; Reference proteome; Transit peptide. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 432 AA |
Protein Sequence | MAVSAFQLWR AGGLLRRNFL THSSSWKIPP RVLKSSQPEA LLSVTNNALC FAPLQTFTDE 60
DIMMQKAVKK FAQEQIAPLV STMDENSKME KSVIQGLFQQ GMMGIEVEAK YGGTEASFLC 120
SVLVIEELAK VDASVALLCD IQNTVINKLF RKHGTEEQKA TYLPKLVTEK LGSFCLSEAG 180
AGSDSFALKT RADKSGNYYV INGSKMWISN AEHAELFLVF ANVDPPSGYR GITCFLVDRD 240
TEGFQIGRRE NKMGIRASST CQLTFENVKV PETSVLGKIG HGYKYAIGSL NEGRIGIAAQ 300
MLGLAQGCFD YTIPYIKERM QFGKRIFDFQ GLQHQVAHVA TQLEAARLLT YNAARLVEAG 360
RPFIKEASMA KYYASEVAGL TTSKCIEWMG GVGYTKDYPV EKFFRDAKIG TIYEGTSNIQ 420
LNTIAKHIDA EY 432 |
Gene Ontology | GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell. GO:0005739; C:mitochondrion; TAS:RGD. GO:0009055; F:electron carrier activity; IDA:RGD. GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. GO:0016937; F:short-branched-chain-acyl-CoA dehydrogenase activity; IDA:MGI. GO:0006637; P:acyl-CoA metabolic process; IDA:MGI. GO:0006635; P:fatty acid beta-oxidation; TAS:RGD. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |