ID A0A0D8HLU8_9ACTN Unreviewed; 403 AA.
AC A0A0D8HLU8;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=(R)-benzylsuccinyl-CoA dehydrogenase {ECO:0000313|EMBL:KJF18737.1};
DE EC=1.3.8.3 {ECO:0000313|EMBL:KJF18737.1};
GN Name=bbsG {ECO:0000313|EMBL:KJF18737.1};
GN ORFNames=AXFE_03460 {ECO:0000313|EMBL:KJF18737.1};
OS Acidithrix ferrooxidans.
OC Bacteria; Actinomycetota; Acidimicrobiia; Acidimicrobiales;
OC Acidimicrobiaceae; Acidithrix.
OX NCBI_TaxID=1280514 {ECO:0000313|EMBL:KJF18737.1, ECO:0000313|Proteomes:UP000032360};
RN [1] {ECO:0000313|EMBL:KJF18737.1, ECO:0000313|Proteomes:UP000032360}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Py-F3 {ECO:0000313|EMBL:KJF18737.1,
RC ECO:0000313|Proteomes:UP000032360};
RA Poehlein A., Eisen S., Schloemann M., Johnson B.D., Daniel R., Muehling M.;
RT "Draft genome of the acidophilic iron oxidizer Acidithrix ferrooxidans
RT strain Py-F3.";
RL Submitted (JAN-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:KJF18737.1}.
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DR EMBL; JXYS01000007; KJF18737.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D8HLU8; -.
DR STRING; 1280514.AXFE_03460; -.
DR PATRIC; fig|1280514.3.peg.478; -.
DR OrthoDB; 142556at2; -.
DR Proteomes; UP000032360; 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:KJF18737.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000032360}.
FT DOMAIN 10..132
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 136..236
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 248..398
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 403 AA; 44880 MW; D3D81AE35E54DEC8 CRC64;
MTMDFEYSPK AKDLQNRLLA FMDEAVYPAE EVYEEQMRSS GDPHFYPPII EDLKSQARSR
GLWNLFLPHK TEWTEGLSNL DYAPLAEISG RSHLAPEAIN CAAPDTGNME ILTMFGTEEQ
KEEWLRPLLH GEIRSCFSMT EPAVASSDAS NIECSITRDG DEYVINGRKW WSSGASSSRC
KVAIVMGKTD PKASPYQQQS MILVPLDTPG VKLIRDLTVF GYTDREGHGE IHYDNVRVPI
SNLLGEEGSG FAIAQARLGP GRIHHTMRSI GAAERALALM CKRARSRVAF GKTLAEQGTI
QTWIADSRIE IDQARLLTLY AAWLMDTVGN KGARTEVSEI KVVAPNVALR VIDRAIQVYG
GAGVSEDTPL ARMYAGQRTL RLADGPDEVH RMTIARRELR KHE
//
