ID Q6LI98_PHOPR Unreviewed; 396 AA.
AC Q6LI98;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 112.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:CAG22982.1};
GN Name=CAIA {ECO:0000313|EMBL:CAG22982.1};
GN OrderedLocusNames=PBPRB1110 {ECO:0000313|EMBL:CAG22982.1};
OS Photobacterium profundum (strain SS9).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=298386 {ECO:0000313|EMBL:CAG22982.1, ECO:0000313|Proteomes:UP000000593};
RN [1] {ECO:0000313|Proteomes:UP000000593}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1253 / SS9 {ECO:0000313|Proteomes:UP000000593};
RX PubMed=15746425; DOI=10.1126/science.1103341;
RA Vezzi A., Campanaro S., D'Angelo M., Simonato F., Vitulo N., Lauro F.M.,
RA Cestaro A., Malacrida G., Simionati B., Cannata N., Romualdi C.,
RA Bartlett D.H., Valle G.;
RT "Life at depth: Photobacterium profundum genome sequence and expression
RT analysis.";
RL Science 307:1459-1461(2005).
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; CR378678; CAG22982.1; -; Genomic_DNA.
DR RefSeq; WP_011221172.1; NC_006371.1.
DR AlphaFoldDB; Q6LI98; -.
DR STRING; 298386.PBPRB1110; -.
DR KEGG; ppr:PBPRB1110; -.
DR eggNOG; COG1960; Bacteria.
DR HOGENOM; CLU_018204_0_2_6; -.
DR Proteomes; UP000000593; Chromosome 2.
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; 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; IPR006089; Acyl-CoA_DH_CS.
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; PTHR43831; ISOBUTYRYL-COA DEHYDROGENASE; 1.
DR PANTHER; PTHR43831:SF1; ISOBUTYRYL-COA DEHYDROGENASE, MITOCHONDRIAL; 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.
DR PROSITE; PS00072; ACYL_COA_DH_1; 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 Reference proteome {ECO:0000313|Proteomes:UP000000593}.
FT DOMAIN 6..116
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 122..227
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 239..389
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 396 AA; 43643 MW; D580FF979BAFCB35 CRC64;
MDFELNEDQR AFAETARQFA LERLSPMAAE WDEKHIFPKG VLKEAGELGF LSLYTPEEQG
GLALSRLDSS IIFEQLAMGC TSTTAFMTIH NMVTWMIASF ATDEAKAEYC PQLIIGDWLG
SYCLTEPNAG SDAAALTTSA KKIKDQYILN GAKTFISGAG ETDVLVVMAR TVNDEQGRNK
KAEHKSGAKG ISAFIVPADA TGITYGRKEP KMGWNSQPTR SITFDNVAIP ARNLLGQEGE
GFTFAMKGLD GGRINIATCS VGTAQQALNQ ATQYMNERKQ FGKSLAQFQG LQFKLADMAT
ELVAARQLVR YAASKLDRQD PEATAYCAMA KRFATDTGFT VCDQALQLYG GYGYIKEYPL
ERYFRDVRVH QILEGTNEIM RLIIARRLLA EGTEIL
//
