ID   A0A177H4D0_9RHOB        Unreviewed;       549 AA.
AC   A0A177H4D0;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=Putative acyl-CoA dehydrogenase AidB {ECO:0000313|EMBL:OAH05805.1};
DE            EC=1.3.99.- {ECO:0000313|EMBL:OAH05805.1};
GN   Name=aidB {ECO:0000313|EMBL:OAH05805.1};
GN   ORFNames=pfor_37c3566 {ECO:0000313|EMBL:OAH05805.1};
OS   Rhodobacteraceae bacterium SB2.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae.
OX   NCBI_TaxID=1689867 {ECO:0000313|EMBL:OAH05805.1, ECO:0000313|Proteomes:UP000077333};
RN   [1] {ECO:0000313|EMBL:OAH05805.1, ECO:0000313|Proteomes:UP000077333}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SB2 {ECO:0000313|EMBL:OAH05805.1,
RC   ECO:0000313|Proteomes:UP000077333};
RA   Poehlein A., Billerbeck S., Voget S., Wemheuer B., Giebel H.-A.,
RA   Brinkhoff T., Daniel R., Simon M.;
RT   "A new prominent pelagic Roseobacter clade subcluster - CHAB-I-5:
RT   biogeography and genomic comparison to other roseobacters.";
RL   Submitted (MAY-2016) 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:OAH05805.1}.
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DR   EMBL; LGRT01000038; OAH05805.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A177H4D0; -.
DR   STRING; 1689867.pfor_37c3566; -.
DR   PATRIC; fig|1689867.3.peg.3615; -.
DR   OrthoDB; 9771038at2; -.
DR   Proteomes; UP000077333; Unassembled WGS sequence.
DR   GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IEA:InterPro.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
DR   Gene3D; 2.40.110.20; -; 1.
DR   Gene3D; 6.10.250.600; -; 1.
DR   Gene3D; 1.20.140.10; Butyryl-CoA Dehydrogenase, subunit A, domain 3; 1.
DR   InterPro; IPR006089; Acyl-CoA_DH_CS.
DR   InterPro; IPR006091; Acyl-CoA_Oxase/DH_mid-dom.
DR   InterPro; IPR036250; AcylCo_DH-like_C.
DR   InterPro; IPR009075; AcylCo_DH/oxidase_C.
DR   InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom_sf.
DR   InterPro; IPR041504; AidB_N.
DR   PANTHER; PTHR42707; ACYL-COA DEHYDROGENASE; 1.
DR   PANTHER; PTHR42707:SF3; ACYL-COA DEHYDROGENASE AIDB-RELATED; 1.
DR   Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR   Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR   Pfam; PF18158; AidB_N; 1.
DR   SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
DR   SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1.
DR   PROSITE; PS00073; ACYL_COA_DH_2; 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:OAH05805.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077333}.
FT   DOMAIN          17..171
FT                   /note="Adaptive response protein AidB N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF18158"
FT   DOMAIN          186..280
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          290..444
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   549 AA;  60634 MW;  9EFE300A90C39612 CRC64;
     MTPRDPISHL PTHQVINMPP HMGDQDLWGN DRALRHWASH MGGAGHAGHF AHVGHLTGLD
     ETFEKANQAN RHGPELRAFD RYGMRINAVE FHPAYHDLMH LAISNKVHNF AWHNEDNAGH
     VGQSVLTYMF SQPEGGVMCP MAMTYSVVPS LRMAPYLAEE WMPRLLSTQY DRRDIPAAEK
     TGAMIGMFMT EKQGGSDVRA NSTVARPIGD GYLLTGHKFF CSAPMCDAFL VLANTEVMGI
     SCFLVPRWRP DGTRNTLFIQ RMKDKLGNHS NASTEMEFQD TYGVMVGEEG RGIRTIIEMV
     TGNRLYCAMS SAGIMRQALV QALHHTSHRS AFQKRLIQQP LMQNVLADMA VEVEAALALG
     LRVAQAMDRM DDPAEAALAR IGTAVAKYWN TKRCPSLVVE ALECHGGPGY VEESIMPRLY
     REAPLNSIWE GSGNVMGLDV LRAMGREAEA IPAVMAELEK ARGNHPNLDR AIDDLRDELA
     DPEGLEARMR MVTEMMALTL QAALLTRHGD SPVADAFCAS RLAPRYRGAF GTLPKGLDLD
     AIISRALPG
//