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Database: UniProt
Entry: G7WCV9_DESOD
LinkDB: G7WCV9_DESOD
Original site: G7WCV9_DESOD 
ID   G7WCV9_DESOD            Unreviewed;       385 AA.
AC   G7WCV9;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   27-MAR-2024, entry version 57.
DE   SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:AET66865.1};
GN   OrderedLocusNames=Desor_1198 {ECO:0000313|EMBL:AET66865.1};
OS   Desulfosporosinus orientis (strain ATCC 19365 / DSM 765 / NCIMB 8382 / VKM
OS   B-1628 / Singapore I) (Desulfotomaculum orientis).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC   Desulfosporosinus.
OX   NCBI_TaxID=768706 {ECO:0000313|EMBL:AET66865.1, ECO:0000313|Proteomes:UP000006346};
RN   [1] {ECO:0000313|Proteomes:UP000006346}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19365 / DSM 765 / NCIMB 8382 / VKM B-1628
RC   {ECO:0000313|Proteomes:UP000006346};
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Ovchinnikova G., Teshima H., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Pester M.,
RA   Spring S., Ollivier B., Rattei T., Klenk H.-P., Wagner M., Loy A.,
RA   Woyke T.;
RT   "Complete sequence of Desulfosporosinus orientis DSM 765.";
RL   Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AET66865.1, ECO:0000313|Proteomes:UP000006346}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19365 / DSM 765 / NCIMB 8382 / VKM B-1628
RC   {ECO:0000313|Proteomes:UP000006346};
RX   PubMed=23105050; DOI=10.1128/JB.01392-12;
RA   Pester M., Brambilla E., Alazard D., Rattei T., Weinmaier T., Han J.,
RA   Lucas S., Lapidus A., Cheng J.F., Goodwin L., Pitluck S., Peters L.,
RA   Ovchinnikova G., Teshima H., Detter J.C., Han C.S., Tapia R., Land M.L.,
RA   Hauser L., Kyrpides N.C., Ivanova N.N., Pagani I., Huntmann M., Wei C.L.,
RA   Davenport K.W., Daligault H., Chain P.S., Chen A., Mavromatis K.,
RA   Markowitz V., Szeto E., Mikhailova N., Pati A., Wagner M., Woyke T.,
RA   Ollivier B., Klenk H.P., Spring S., Loy A.;
RT   "Complete genome sequences of Desulfosporosinus orientis DSM765T,
RT   Desulfosporosinus youngiae DSM17734T, Desulfosporosinus meridiei DSM13257T,
RT   and Desulfosporosinus acidiphilus DSM22704T.";
RL   J. Bacteriol. 194:6300-6301(2012).
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; CP003108; AET66865.1; -; Genomic_DNA.
DR   RefSeq; WP_014183686.1; NC_016584.1.
DR   AlphaFoldDB; G7WCV9; -.
DR   STRING; 768706.Desor_1198; -.
DR   KEGG; dor:Desor_1198; -.
DR   PATRIC; fig|768706.3.peg.1180; -.
DR   eggNOG; COG1960; Bacteria.
DR   HOGENOM; CLU_018204_0_2_9; -.
DR   OrthoDB; 9802447at2; -.
DR   Proteomes; UP000006346; Chromosome.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; 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; 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; PTHR43884; ACYL-COA DEHYDROGENASE; 1.
DR   PANTHER; PTHR43884:SF12; COMPLEX I ASSEMBLY FACTOR ACAD9, 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   PIRSF; PIRSF016578; HsaA; 3.
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   Reference proteome {ECO:0000313|Proteomes:UP000006346}.
FT   DOMAIN          6..118
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          122..217
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          230..376
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   385 AA;  42896 MW;  151E280BE1C742AE CRC64;
     MDFGLTEEQR MVQEMARDFA EKEIGPYVEE DEENHYYRRE ILSKMGKLGL LGWSIPEEYG
     GNGMGWMEAV TALYEIAKVH TSWRLSISGN VWGPAMTINE WGTKEQKQTY IPRLVSGDSV
     GSFAMTEANT GSDVASMKTL AEDKGDHWLI NGSKMWISGG HTCDIGLLYA VTEKGAGAKG
     ISCFIIDYNK TPGVTRIPIL KKVGMWPAPT SELVFENAMI PKENLLGPLN KGFQICMWML
     NNTRMGCATG SAALSAACLE GSVQYANERT QFGKQIGKYQ MIQQQIAEMK LEDEAAKYLV
     YRAAWLKENK LPSQQATSMA KLYGSIAAVH AANIAMKIYG SYGYSTEYPC GRWLRDAKQF
     ETLEGTSNIH MQIISKIELG YQPNR
//
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