ACD_DESML
ID ACD_DESML Reviewed; 389 AA.
AC C3UVB0;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 1.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=Glutaryl-CoA dehydrogenase;
DE Short=GDH(Des);
DE EC=1.3.99.32;
GN Name=Acd;
OS Desulfococcus multivorans.
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfobacterales;
OC Desulfobacteraceae; Desulfococcus.
OX NCBI_TaxID=897;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, SUBUNIT,
RP PATHWAY, COFACTOR, AND ACTIVITY REGULATION.
RC STRAIN=ATCC 33890 / DSM 2059 / Goettingen / 1be1;
RX PubMed=19395484; DOI=10.1128/jb.00205-09;
RA Wischgoll S., Taubert M., Peters F., Jehmlich N., von Bergen M., Boll M.;
RT "Decarboxylating and nondecarboxylating glutaryl-coenzyme A dehydrogenases
RT in the aromatic metabolism of obligately anaerobic bacteria.";
RL J. Bacteriol. 191:4401-4409(2009).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) IN COMPLEX WITH FAD AND SUBSTRATE,
RP COFACTOR, AND MUTAGENESIS OF ALA-80; VAL-88 AND VAL-366.
RC STRAIN=ATCC 33890 / DSM 2059 / Goettingen / 1be1;
RX PubMed=20486657; DOI=10.1021/bi100317m;
RA Wischgoll S., Demmer U., Warkentin E., Gunther R., Boll M., Ermler U.;
RT "Structural basis for promoting and preventing decarboxylation in glutaryl-
RT coenzyme A dehydrogenases.";
RL Biochemistry 49:5350-5357(2010).
CC -!- FUNCTION: Catalyzes the dehydrogenation of Glutaryl-CoA to glutaconyl-
CC CoA. {ECO:0000269|PubMed:19395484}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=A + glutaryl-CoA = (2E)-glutaconyl-CoA + AH2;
CC Xref=Rhea:RHEA:47420, ChEBI:CHEBI:13193, ChEBI:CHEBI:17499,
CC ChEBI:CHEBI:57353, ChEBI:CHEBI:57378; EC=1.3.99.32;
CC Evidence={ECO:0000269|PubMed:19395484};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:19395484, ECO:0000269|PubMed:20486657};
CC -!- ACTIVITY REGULATION: Inhibited by glutaconyl-CoA.
CC {ECO:0000269|PubMed:19395484}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=25 uM for glutaryl-CoA;
CC Vmax=11 mmol/min/mg enzyme;
CC -!- PATHWAY: Aromatic compound metabolism; benzoyl-CoA degradation.
CC {ECO:0000269|PubMed:19395484}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:19395484,
CC ECO:0000269|PubMed:20486657}.
CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; FJ688103; ACP50614.1; -; Genomic_DNA.
DR RefSeq; WP_070962329.1; NZ_CP019913.2.
DR PDB; 3MPI; X-ray; 2.05 A; A/B/C/D=1-389.
DR PDB; 3MPJ; X-ray; 2.10 A; A/B/D/E/F/G=1-389.
DR PDBsum; 3MPI; -.
DR PDBsum; 3MPJ; -.
DR AlphaFoldDB; C3UVB0; -.
DR SMR; C3UVB0; -.
DR KEGG; ag:ACP50614; -.
DR KEGG; dml:Dmul_25030; -.
DR KEGG; dml:Dmul_34900; -.
DR PATRIC; fig|897.4.peg.2846; -.
DR OrthoDB; 760677at2; -.
DR BRENDA; 1.3.99.32; 1889.
DR UniPathway; UPA00739; -.
DR EvolutionaryTrace; C3UVB0; -.
DR GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IEA:InterPro.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
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; PS00072; ACYL_COA_DH_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aromatic hydrocarbons catabolism; FAD; Flavoprotein;
KW Nucleotide-binding; Oxidoreductase.
FT CHAIN 1..389
FT /note="Glutaryl-CoA dehydrogenase"
FT /id="PRO_0000418764"
FT ACT_SITE 367
FT /note="Proton acceptor"
FT /evidence="ECO:0000305"
FT BINDING 87
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:20486657"
FT BINDING 91
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:20486657"
FT BINDING 126..129
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:20486657"
FT BINDING 135
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:20486657"
FT BINDING 135
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:20486657"
FT BINDING 159..161
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:20486657"
FT BINDING 181
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:20486657"
FT BINDING 271
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:20486657"
FT BINDING 281..284
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:20486657"
FT BINDING 340
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:20486657"
FT BINDING 344
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:20486657"
FT BINDING 367..371
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:20486657"
FT BINDING 385
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:20486657"
FT MUTAGEN 80
FT /note="A->E: Loses the FAD cofactor and dehydrogenase
FT activity."
FT /evidence="ECO:0000269|PubMed:20486657"
FT MUTAGEN 88
FT /note="V->S: A residual dehydrogenase activity is
FT observed."
FT /evidence="ECO:0000269|PubMed:20486657"
FT MUTAGEN 366
FT /note="V->Y: Loses the FAD cofactor but a residual
FT dehydrogenase activity is observed."
FT /evidence="ECO:0000269|PubMed:20486657"
FT HELIX 7..23
FT /evidence="ECO:0007829|PDB:3MPI"
FT TURN 24..27
FT /evidence="ECO:0007829|PDB:3MPI"
FT HELIX 28..34
FT /evidence="ECO:0007829|PDB:3MPI"
FT TURN 39..42
FT /evidence="ECO:0007829|PDB:3MPI"
FT HELIX 43..48
FT /evidence="ECO:0007829|PDB:3MPI"
FT TURN 49..52
FT /evidence="ECO:0007829|PDB:3MPI"
FT STRAND 54..56
FT /evidence="ECO:0007829|PDB:3MPJ"
FT HELIX 58..60
FT /evidence="ECO:0007829|PDB:3MPI"
FT HELIX 68..82
FT /evidence="ECO:0007829|PDB:3MPI"
FT HELIX 84..93
FT /evidence="ECO:0007829|PDB:3MPI"
FT TURN 94..97
FT /evidence="ECO:0007829|PDB:3MPI"
FT HELIX 98..104
FT /evidence="ECO:0007829|PDB:3MPI"
FT HELIX 107..118
FT /evidence="ECO:0007829|PDB:3MPI"
FT STRAND 133..135
FT /evidence="ECO:0007829|PDB:3MPI"
FT HELIX 137..139
FT /evidence="ECO:0007829|PDB:3MPI"
FT STRAND 143..146
FT /evidence="ECO:0007829|PDB:3MPI"
FT STRAND 148..161
FT /evidence="ECO:0007829|PDB:3MPI"
FT TURN 162..165
FT /evidence="ECO:0007829|PDB:3MPI"
FT STRAND 167..175
FT /evidence="ECO:0007829|PDB:3MPI"
FT HELIX 177..182
FT /evidence="ECO:0007829|PDB:3MPI"
FT STRAND 183..189
FT /evidence="ECO:0007829|PDB:3MPI"
FT TURN 191..193
FT /evidence="ECO:0007829|PDB:3MPI"
FT STRAND 197..201
FT /evidence="ECO:0007829|PDB:3MPI"
FT STRAND 212..223
FT /evidence="ECO:0007829|PDB:3MPI"
FT HELIX 224..226
FT /evidence="ECO:0007829|PDB:3MPI"
FT STRAND 227..230
FT /evidence="ECO:0007829|PDB:3MPI"
FT TURN 231..233
FT /evidence="ECO:0007829|PDB:3MPJ"
FT HELIX 234..270
FT /evidence="ECO:0007829|PDB:3MPI"
FT HELIX 278..280
FT /evidence="ECO:0007829|PDB:3MPI"
FT HELIX 282..310
FT /evidence="ECO:0007829|PDB:3MPI"
FT HELIX 317..342
FT /evidence="ECO:0007829|PDB:3MPI"
FT HELIX 343..347
FT /evidence="ECO:0007829|PDB:3MPI"
FT HELIX 352..359
FT /evidence="ECO:0007829|PDB:3MPI"
FT HELIX 362..365
FT /evidence="ECO:0007829|PDB:3MPI"
FT STRAND 366..368
FT /evidence="ECO:0007829|PDB:3MPI"
FT HELIX 370..381
FT /evidence="ECO:0007829|PDB:3MPI"
SQ SEQUENCE 389 AA; 42382 MW; F479601F35A96975 CRC64;
MDFNLSKELQ MLQKEVRNFV NKKIVPFADQ WDNENHFPYE EAVRPMGELG FFGTVIPEEY
GGEGMDQGWL AAMIVTEEIA RGSSALRVQL NMEVLGCAYT ILTYGSEALK KKYVPKLSSA
EFLGGFGITE PDAGSDVMAM SSTAEDKGDH WLLNGSKTWI SNAAQADVLI YYAYTDKAAG
SRGLSAFVIE PRNFPGIKTS NLEKLGSHAS PTGELFLDNV KVPKENILGK PGDGARIVFG
SLNHTRLSAA AGGVGLAQAC LDAAIKYCNE RRQFGKPIGD FQMNQDMIAQ MAVEVEAARL
LAYKAAAAKD EGRLNNGLDV AMAKYAAGEA VSKCANYAMR ILGAYGYSTE YPVARFYRDA
PTYYMVEGSA NICKMIIALD QLGVRKANR
