GCDH_BOVIN
ID GCDH_BOVIN Reviewed; 438 AA.
AC Q2KHZ9;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Glutaryl-CoA dehydrogenase, mitochondrial;
DE Short=GCD;
DE EC=1.3.8.6;
DE Flags: Precursor;
GN Name=GCDH;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Heart ventricle;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). {ECO:0000250}.
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; Evidence={ECO:0000250};
CC -!- PATHWAY: Amino-acid metabolism; lysine degradation.
CC -!- PATHWAY: Amino-acid metabolism; tryptophan metabolism.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; BC112822; AAI12823.1; -; mRNA.
DR RefSeq; NP_001039404.1; NM_001045939.2.
DR AlphaFoldDB; Q2KHZ9; -.
DR SMR; Q2KHZ9; -.
DR STRING; 9913.ENSBTAP00000043333; -.
DR PaxDb; Q2KHZ9; -.
DR PeptideAtlas; Q2KHZ9; -.
DR PRIDE; Q2KHZ9; -.
DR Ensembl; ENSBTAT00000045996; ENSBTAP00000043333; ENSBTAG00000016211.
DR GeneID; 506310; -.
DR KEGG; bta:506310; -.
DR CTD; 2639; -.
DR VEuPathDB; HostDB:ENSBTAG00000016211; -.
DR VGNC; VGNC:29282; GCDH.
DR eggNOG; KOG0138; Eukaryota.
DR GeneTree; ENSGT00940000158116; -.
DR HOGENOM; CLU_018204_8_0_1; -.
DR InParanoid; Q2KHZ9; -.
DR OMA; AAMDCYD; -.
DR OrthoDB; 589058at2759; -.
DR TreeFam; TF105051; -.
DR UniPathway; UPA00224; -.
DR UniPathway; UPA00225; -.
DR Proteomes; UP000009136; Chromosome 7.
DR Bgee; ENSBTAG00000016211; Expressed in cortex of kidney and 105 other tissues.
DR ExpressionAtlas; Q2KHZ9; baseline and differential.
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 2: Evidence at transcript level;
KW Acetylation; FAD; Flavoprotein; Mitochondrion; Oxidoreductase;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..44
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 45..438
FT /note="Glutaryl-CoA dehydrogenase, mitochondrial"
FT /id="PRO_0000281992"
FT ACT_SITE 414
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 138..139
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 177..186
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 186
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 186
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 212..214
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 287..294
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 319
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 330
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 387..391
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 415
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 416..418
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 416
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 434
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT MOD_RES 240
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q60759"
SQ SEQUENCE 438 AA; 48472 MW; C420C9901292CDEC CRC64;
MALRGVYAQL LNRGPGLRVF RSWSSATAQT EKGEKTQSRS AKPSRPEFDW RDPLLLEEQL
TADEILIRDT FRTYCQERLM PRILLANRNE VFHREIISEM GELGMLGPTI QGYSCAGVSS
VAYGLLAREL ERVDSGYRSA MSVQSSLVMY PIYAYGSEEQ KQKYLPRLAK GELLGCFGLT
EPNHGSDPSG METRARHNPS SRSYILSGSK TWITNSPVAD LLIVWARCED SCIRGFLLEK
GMRGLSTPRI EGKFSLRASS TGMIIMDDVE VPEENVLPGV SGLAGPFGCL NNARYGITWG
VLGAAEFCLH TARQYTLDRI QFGVPLAKNQ LIQKKLADML TEITLGLHAC LQLGRLKDQD
KAAPEMVSLL KRNNCGKALD IARQARDMLG GNGISDEYHV IRHVMNLESV NTYEGTHDIH
ALILGRAITG IQAFVAGK
