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8SGS

human liver mitochondrial Short-chain specific acyl-CoA dehydrogenase

Functional Information from GO Data
ChainGOidnamespacecontents
A0003995molecular_functionacyl-CoA dehydrogenase activity
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005739cellular_componentmitochondrion
A0005759cellular_componentmitochondrial matrix
A0006629biological_processlipid metabolic process
A0006631biological_processfatty acid metabolic process
A0006635biological_processfatty acid beta-oxidation
A0016491molecular_functionoxidoreductase activity
A0016627molecular_functionoxidoreductase activity, acting on the CH-CH group of donors
A0016937molecular_functionshort-chain fatty acyl-CoA dehydrogenase activity
A0033539biological_processfatty acid beta-oxidation using acyl-CoA dehydrogenase
A0046359biological_processbutyrate catabolic process
A0050660molecular_functionflavin adenine dinucleotide binding
B0003995molecular_functionacyl-CoA dehydrogenase activity
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005739cellular_componentmitochondrion
B0005759cellular_componentmitochondrial matrix
B0006629biological_processlipid metabolic process
B0006631biological_processfatty acid metabolic process
B0006635biological_processfatty acid beta-oxidation
B0016491molecular_functionoxidoreductase activity
B0016627molecular_functionoxidoreductase activity, acting on the CH-CH group of donors
B0016937molecular_functionshort-chain fatty acyl-CoA dehydrogenase activity
B0033539biological_processfatty acid beta-oxidation using acyl-CoA dehydrogenase
B0046359biological_processbutyrate catabolic process
B0050660molecular_functionflavin adenine dinucleotide binding
C0003995molecular_functionacyl-CoA dehydrogenase activity
C0005515molecular_functionprotein binding
C0005634cellular_componentnucleus
C0005739cellular_componentmitochondrion
C0005759cellular_componentmitochondrial matrix
C0006629biological_processlipid metabolic process
C0006631biological_processfatty acid metabolic process
C0006635biological_processfatty acid beta-oxidation
C0016491molecular_functionoxidoreductase activity
C0016627molecular_functionoxidoreductase activity, acting on the CH-CH group of donors
C0016937molecular_functionshort-chain fatty acyl-CoA dehydrogenase activity
C0033539biological_processfatty acid beta-oxidation using acyl-CoA dehydrogenase
C0046359biological_processbutyrate catabolic process
C0050660molecular_functionflavin adenine dinucleotide binding
D0003995molecular_functionacyl-CoA dehydrogenase activity
D0005515molecular_functionprotein binding
D0005634cellular_componentnucleus
D0005739cellular_componentmitochondrion
D0005759cellular_componentmitochondrial matrix
D0006629biological_processlipid metabolic process
D0006631biological_processfatty acid metabolic process
D0006635biological_processfatty acid beta-oxidation
D0016491molecular_functionoxidoreductase activity
D0016627molecular_functionoxidoreductase activity, acting on the CH-CH group of donors
D0016937molecular_functionshort-chain fatty acyl-CoA dehydrogenase activity
D0033539biological_processfatty acid beta-oxidation using acyl-CoA dehydrogenase
D0046359biological_processbutyrate catabolic process
D0050660molecular_functionflavin adenine dinucleotide binding
Functional Information from PROSITE/UniProt
site_idPS00072
Number of Residues13
DetailsACYL_COA_DH_1 Acyl-CoA dehydrogenases signature 1. ALSEpgNGSDagA
ChainResidueDetails
AALA153-ALA165

site_idPS00073
Number of Residues20
DetailsACYL_COA_DH_2 Acyl-CoA dehydrogenases signature 2. QiLGGmGYvtEmpaeRhyrD
ChainResidueDetails
AGLN365-ASP384

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"UniProtKB","id":"P15651","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues56
DetailsBinding site: {"description":"in other chain","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"FEB-2009","submissionDatabase":"PDB data bank","title":"Crystal structure of human RAB14.","authoringGroup":["Structural genomics consortium (SGC)"]}}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues20
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues20
DetailsBinding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"FEB-2009","submissionDatabase":"PDB data bank","title":"Crystal structure of human RAB14.","authoringGroup":["Structural genomics consortium (SGC)"]}}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues16
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q07417","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues8
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q07417","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

242199

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