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Database: UniProt
Entry: U3BDS5_PSEA4
LinkDB: U3BDS5_PSEA4
Original site: U3BDS5_PSEA4 
ID   U3BDS5_PSEA4            Unreviewed;       409 AA.
AC   U3BDS5;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   SubName: Full=Putative acyl-CoA dehydrogenase {ECO:0000313|EMBL:GAD64923.1};
GN   ORFNames=PA6_054_00070 {ECO:0000313|EMBL:GAD64923.1};
OS   Pseudomonas alcaligenes (strain ATCC 14909 / DSM 50342 / JCM 20561 / NBRC
OS   14159 / NCIMB 9945 / NCTC 10367 / 1577).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1215092 {ECO:0000313|EMBL:GAD64923.1, ECO:0000313|Proteomes:UP000016560};
RN   [1] {ECO:0000313|EMBL:GAD64923.1, ECO:0000313|Proteomes:UP000016560}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14909 / DSM 50342 / JCM 20561 / NBRC 14159 / NCIMB 9945 /
RC   NCTC 10367 / 1577 {ECO:0000313|Proteomes:UP000016560};
RA   Yoshida I., Hosoyama A., Tsuchikane K., Noguchi M., Hirakata S., Ando Y.,
RA   Ohji S., Yamazoe A., Yamazaki S., Fujita N.;
RT   "Whole genome shotgun sequence of Pseudomonas alcaligenes NBRC 14159.";
RL   Submitted (SEP-2013) 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:GAD64923.1}.
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DR   EMBL; BATI01000054; GAD64923.1; -; Genomic_DNA.
DR   RefSeq; WP_021702986.1; NZ_BATI01000054.1.
DR   AlphaFoldDB; U3BDS5; -.
DR   STRING; 43263.A0T30_12615; -.
DR   eggNOG; COG1960; Bacteria.
DR   OrthoDB; 9769473at2; -.
DR   Proteomes; UP000016560; Unassembled WGS sequence.
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   CDD; cd01155; ACAD_FadE2; 1.
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   Reference proteome {ECO:0000313|Proteomes:UP000016560}.
FT   DOMAIN          8..128
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          132..233
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          245..393
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   409 AA;  45219 MW;  A96810428062602C CRC64;
     MDFAYSPKVQ ELRERVTAFM EAYVYPAEAV FEEQVNEGDR WQPTAIMEEL KAKAKAEGLW
     NLFLPESEYG AGLTNMEYAP LAEIMGRSLI GAEPFNCSAP DTGNMETLVR YASEAQKKQW
     LEPLLSGEIR SAFAMTEPGV ASSDATNMQA NARREGDEWV INGRKWWTSG ACDPRCKIMI
     FMGLTNPDAP RHQQHSMILV PSDTPGVKIV RPLPVFGYDD APHGHAEVIF DNVRVPYDNV
     LLGEGRGFEI AQGRLGPGRI HHCMRSIGMA ERALELMCKR AVSRTAFGKP LARLGGNIDH
     IANSRIEINQ ARLLTLNAAY MMDTVGNKVA ASEIAQIKVV APNVALNVID RAIQIHGGAG
     VSNDFPLAYW YAMQRTLRLA DGPDEVHRAA VGKFEVGKYV PREAMKASR
//
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