GCDH_PIG
ID GCDH_PIG Reviewed; 408 AA.
AC P81140;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Glutaryl-CoA dehydrogenase, mitochondrial;
DE Short=GCD;
DE EC=1.3.8.6;
DE Flags: Precursor; Fragment;
GN Name=GCDH;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE, PROTEIN SEQUENCE OF 14-38 AND 375-407, AND FUNCTION.
RC TISSUE=Liver;
RX PubMed=1438360;
RA Goodman S.I., Kratz L.E., Frerman F.E.;
RT "Pork and human cDNAs encoding glutaryl-CoA dehydrogenase.";
RL Prog. Clin. Biol. Res. 375:169-173(1992).
CC -!- FUNCTION: Catalyzes the oxidative decarboxylation of glutaryl-CoA to
CC crotonyl-CoA and CO(2) in the degradative pathway of L-lysine, L-
CC hydroxylysine, and L-tryptophan metabolism. It uses electron transfer
CC flavoprotein as its electron acceptor. {ECO:0000269|PubMed:1438360}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glutaryl-CoA + 2 H(+) + oxidized [electron-transfer
CC flavoprotein] = (2E)-butenoyl-CoA + CO2 + reduced [electron-transfer
CC flavoprotein]; Xref=Rhea:RHEA:13389, Rhea:RHEA-COMP:10685, Rhea:RHEA-
CC COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57332,
CC ChEBI:CHEBI:57378, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307; EC=1.3.8.6;
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC -!- PATHWAY: Amino-acid metabolism; lysine degradation.
CC -!- PATHWAY: Amino-acid metabolism; tryptophan metabolism.
CC -!- SUBUNIT: Homotetramer.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC {ECO:0000305}.
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DR AlphaFoldDB; P81140; -.
DR SMR; P81140; -.
DR STRING; 9823.ENSSSCP00000014599; -.
DR PeptideAtlas; P81140; -.
DR eggNOG; KOG0138; Eukaryota.
DR InParanoid; P81140; -.
DR SABIO-RK; P81140; -.
DR UniPathway; UPA00224; -.
DR UniPathway; UPA00225; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0000062; F:fatty-acyl-CoA binding; IBA:GO_Central.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
DR GO; GO:0004361; F:glutaryl-CoA dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0033539; P:fatty acid beta-oxidation using acyl-CoA dehydrogenase; ISS:UniProtKB.
DR GO; GO:0046949; P:fatty-acyl-CoA biosynthetic process; IBA:GO_Central.
DR GO; GO:0006568; P:tryptophan metabolic 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; PS00073; ACYL_COA_DH_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Direct protein sequencing; FAD; Flavoprotein; Mitochondrion;
KW Oxidoreductase; Reference proteome; Transit peptide.
FT TRANSIT <1..13
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:1438360"
FT CHAIN 14..408
FT /note="Glutaryl-CoA dehydrogenase, mitochondrial"
FT /id="PRO_0000000529"
FT ACT_SITE 384
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 107..108
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 147..156
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 156
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 156
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 182..184
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 257..264
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 289
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 300
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 357..361
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 385
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 386..388
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 386
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 404
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT MOD_RES 210
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q60759"
FT NON_TER 1
SQ SEQUENCE 408 AA; 45123 MW; E517D565A193E146 CRC64;
KGGKTQGRSA KSSRPEFDWR DPLVLEEQLT ADEILIRDTF RTYCQEHLMP RIVLANRNEV
FHREIISEMG ELGVLGPTIK GYGCAGVSSV AYGLLARELE RVDSGYRSAM SVQSSLVMHP
IYAYGSEEQQ QQKYLPRLAK GELLGCFGLT EPNHGSDPGS METRALHNPS NRSYTLNGAK
TWITNSPVAD LFVVWARCED NCIRGFLLEK GMRGLSAPKI EGKFSLRASA TGMIIMDDVE
VPEENVLPKA SSLAVPFGCL NNARYGISWG VLGAAEFCLH TARQYTLDRI QFGVPLAKNQ
LIQRKLADML TEITLGLHAC LQLGRLKDQD KVTPEMVSLL KRNNCGKALD IARQARDMLG
GNGISDEYHV IRHAMNLEAV NTYEGTHDIH ALILGRAITG IQAFTTDK
