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Database: UniProt
Entry: A0A0P0NYG0_9CAUL
LinkDB: A0A0P0NYG0_9CAUL
Original site: A0A0P0NYG0_9CAUL 
ID   A0A0P0NYG0_9CAUL        Unreviewed;       393 AA.
AC   A0A0P0NYG0;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:ALL12753.1};
GN   ORFNames=AQ619_04935 {ECO:0000313|EMBL:ALL12753.1};
OS   Caulobacter henricii.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Caulobacter.
OX   NCBI_TaxID=69395 {ECO:0000313|EMBL:ALL12753.1, ECO:0000313|Proteomes:UP000056905};
RN   [1] {ECO:0000313|EMBL:ALL12753.1, ECO:0000313|Proteomes:UP000056905}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CB4 {ECO:0000313|EMBL:ALL12753.1,
RC   ECO:0000313|Proteomes:UP000056905};
RA   Scott D., Ely B.;
RT   "Conservation of the essential genome among Caulobacter and Brevundimonas
RT   species.";
RL   Submitted (OCT-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}.
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DR   EMBL; CP013002; ALL12753.1; -; Genomic_DNA.
DR   RefSeq; WP_062145079.1; NZ_CP013002.1.
DR   AlphaFoldDB; A0A0P0NYG0; -.
DR   STRING; 69395.AQ619_04935; -.
DR   KEGG; chq:AQ619_04935; -.
DR   eggNOG; COG1960; Bacteria.
DR   OrthoDB; 9780544at2; -.
DR   Proteomes; UP000056905; Chromosome.
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; PTHR48083:SF1; DEHYDROGENASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_7G06510)-RELATED; 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   PIRSF; PIRSF016578; HsaA; 2.
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}.
FT   DOMAIN          16..121
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          127..225
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          238..385
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   393 AA;  42582 MW;  99182277646E312D CRC64;
     MSSNPAATAT DPQLLEALRD TVRALCRDFP GSYWRGLDRE KAYPTDFVQA MTRAGLLGVL
     IPEAYGGSGL GLTAAATILE EVHANGGNAA ALHAQMYTMG TVLRHGSAAQ KAQWLPAVAD
     GSIRLQAFGV TEPTAGTDTT SISTFARREG NTYVIKGQKV WTSRAEHSDL MVLLARTTPK
     EQVAKKSEGL SVFLVDMRAA RGHGLTIKPI ATMLNHATTE IFFDDLVIPA DSLIGEEGKG
     FKYILDGMNA ERILIAAECL GDSSWLIGKA RDYANERRVF NRPIGQNQGV QFPIARAYAQ
     GHAARLTVYD AAARYEAGLP CGEHANIAKL LASEASWAAA DMCLQTHGGF GFAEEYDIER
     KFRETRLYQV APISTNMILA YVAEHVLGLP RSY
//
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