ID A9WLR0_RENSM Unreviewed; 387 AA.
AC A9WLR0;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 84.
DE SubName: Full=Glutaryl-CoA dehydrogenase {ECO:0000313|EMBL:ABY21840.1};
DE EC=1.3.8.6 {ECO:0000313|EMBL:ABY21840.1};
GN OrderedLocusNames=RSal33209_0084 {ECO:0000313|EMBL:ABY21840.1};
OS Renibacterium salmoninarum (strain ATCC 33209 / DSM 20767 / JCM 11484 /
OS NBRC 15589 / NCIMB 2235).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Renibacterium.
OX NCBI_TaxID=288705 {ECO:0000313|EMBL:ABY21840.1, ECO:0000313|Proteomes:UP000002007};
RN [1] {ECO:0000313|Proteomes:UP000002007}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33209 / DSM 20767 / JCM 11484 / NBRC 15589 / NCIMB 2235
RC {ECO:0000313|Proteomes:UP000002007};
RX PubMed=18723615; DOI=10.1128/JB.00721-08;
RA Wiens G.D., Rockey D.D., Wu Z., Chang J., Levy R., Crane S., Chen D.S.,
RA Capri G.R., Burnett J.R., Sudheesh P.S., Schipma M.J., Burd H.,
RA Bhattacharyya A., Rhodes L.D., Kaul R., Strom M.S.;
RT "Genome sequence of the fish pathogen Renibacterium salmoninarum suggests
RT reductive evolution away from an environmental Arthrobacter ancestor.";
RL J. Bacteriol. 190:6970-6982(2008).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|RuleBase:RU362125};
CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00009347, ECO:0000256|RuleBase:RU362125}.
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DR EMBL; CP000910; ABY21840.1; -; Genomic_DNA.
DR RefSeq; WP_012243548.1; NC_010168.1.
DR AlphaFoldDB; A9WLR0; -.
DR STRING; 288705.RSal33209_0084; -.
DR KEGG; rsa:RSal33209_0084; -.
DR eggNOG; COG1960; Bacteria.
DR HOGENOM; CLU_018204_8_2_11; -.
DR Proteomes; UP000002007; Chromosome.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004361; F:glutaryl-CoA dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0006635; P:fatty acid beta-oxidation; IEA:InterPro.
DR Gene3D; 1.10.540.10; Acyl-CoA dehydrogenase/oxidase, N-terminal domain; 1.
DR Gene3D; 2.40.110.10; Butyryl-CoA Dehydrogenase, subunit A, domain 2; 1.
DR Gene3D; 1.20.140.10; Butyryl-CoA Dehydrogenase, subunit A, domain 3; 1.
DR InterPro; IPR045008; ACX4-like.
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_sf.
DR PANTHER; PTHR43188; ACYL-COENZYME A OXIDASE; 1.
DR PANTHER; PTHR43188:SF1; ACYL-COENZYME A OXIDASE 4, PEROXISOMAL; 1.
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; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|RuleBase:RU362125};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU362125};
KW Oxidoreductase {ECO:0000256|RuleBase:RU362125,
KW ECO:0000313|EMBL:ABY21840.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002007}.
FT DOMAIN 28..123
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 131..224
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 245..380
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 387 AA; 42694 MW; 19C6A8BB98B5D4F5 CRC64;
MSVPERSLPS ADFYHLESRL TGFEQQKLAQ LREFLTEQVA PYCVQWWNDA EFPAHILPDL
AKLGLSTVIQ QGYSPLFAGL VIVEITKVDT SLATFFLVHH DLFVESLYLF GTDDQRSRYL
ADALALRTTG AFALTEPEHG SDVAGGMTTT ALRDGDEWVI NGAKRWIGNG TFCDYMLLWT
KDAESGGVRG FILDTSLPGV SRVKIDNKIA LRTVQNAHIE LDKVRVSEAD RFAGINSFQD
TNVLLQGSRV MVAWQAVGQQ LGAFEIARKY AVEREQFGRP IGSFQLVQAQ LVKMLGNATA
SLSMMTQLTS LPFMSMDQVA LAKAFTTERM RETVALGRSI LGGNGIVSDY RMSKCFADAE
AIFTYEGSFE INTLIVGRSI TGLSAIV
//
