ID A0A0N1NDQ3_9ACTN Unreviewed; 425 AA.
AC A0A0N1NDQ3;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=(R)-benzylsuccinyl-CoA dehydrogenase {ECO:0000313|EMBL:KPI02225.1};
DE EC=1.3.8.3 {ECO:0000313|EMBL:KPI02225.1};
GN ORFNames=OK006_7724 {ECO:0000313|EMBL:KPI02225.1};
OS Actinobacteria bacterium OK006.
OC Bacteria; Actinomycetota; Actinomycetes.
OX NCBI_TaxID=1592326 {ECO:0000313|EMBL:KPI02225.1, ECO:0000313|Proteomes:UP000037912};
RN [1] {ECO:0000313|EMBL:KPI02225.1, ECO:0000313|Proteomes:UP000037912}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OK006 {ECO:0000313|EMBL:KPI02225.1,
RC ECO:0000313|Proteomes:UP000037912};
RA Brown S.D., Utturkar S.M., Klingeman D.M., Pelletier D.;
RT "Draft genome sequences for four Actinobacteria strains OK006 OK074 OV450
RT and OV320.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KPI02225.1}.
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DR EMBL; LJCU01000253; KPI02225.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N1NDQ3; -.
DR PATRIC; fig|1592326.3.peg.9631; -.
DR Proteomes; UP000037912; Unassembled WGS sequence.
DR GO; GO:0033734; F:(R)-benzylsuccinyl-CoA dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
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; 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; PTHR48083:SF13; ACYL-COA DEHYDROGENASE FAMILY MEMBER 11; 1.
DR PANTHER; PTHR48083; MEDIUM-CHAIN SPECIFIC ACYL-COA DEHYDROGENASE, MITOCHONDRIAL-RELATED; 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:KPI02225.1}.
FT DOMAIN 44..130
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 134..212
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 247..395
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 425 AA; 47702 MW; 7CCB67D06395D4DE CRC64;
MAWDFSTEPE FERKLEWIRW FRAERVDPLD LVYPDRAFHP LDEETGPVVR ALKQQVRDQG
LWAPHLGPEL GGRGFGQLKL ALINEILGES SWAPVIFGTA APDTGNAEII ARYGTEEQKE
RYLKPLLEGE CFSCFSMTEP QAGADPKMFT TRAERDGDDW VITGRKFFSS NARTSKFVIV
MAVTDPDVSA YRGMSMFLVP SDTPGIRMER HLGLMSEAPD EGMHALIEYD GVRVPGDALL
GGEGQAFAIA QTRLGGGRVH HAMRVVGQCQ KALDMMAERA LSRETQGSRL ADKQLVQADL
ADSYAQLQQF RLFVLHTAWQ IDQYQDYKRV RKDISAIKFL TPKVLHDIVY RSMHLHGALG
VSNEMPFADM WTGAAVMAVV DGPSEIHKVT VAKDLLRGYE AASGPWPSQH LPARREWARK
QLENM
//
