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Database: UniProt
Entry: A0A248JW77_9PROT
LinkDB: A0A248JW77_9PROT
Original site: A0A248JW77_9PROT 
ID   A0A248JW77_9PROT        Unreviewed;       375 AA.
AC   A0A248JW77;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:ASG22967.1};
GN   ORFNames=Y958_19000 {ECO:0000313|EMBL:ASG22967.1};
OS   Nitrospirillum amazonense CBAmc.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Azospirillaceae; Nitrospirillum.
OX   NCBI_TaxID=1441467 {ECO:0000313|EMBL:ASG22967.1, ECO:0000313|Proteomes:UP000197153};
RN   [1] {ECO:0000313|EMBL:ASG22967.1, ECO:0000313|Proteomes:UP000197153}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBAmC {ECO:0000313|EMBL:ASG22967.1,
RC   ECO:0000313|Proteomes:UP000197153};
RA   Schwab S., dos Santos Teixeira K.R., Simoes Araujo J.L., Soares Vidal M.,
RA   Borges de Freitas H.R., Rivello Crivelaro A.L., Bueno de Camargo Nunes A.,
RA   dos Santos C.M., Palmeira da Silva Rosa D., da Silva Padilha D.,
RA   da Silva E., Araujo Terra L., Soares Mendes V., Farinelli L.,
RA   Magalhaes Cruz L., Baldani J.I.;
RT   "Complete genome sequence of Nitrospirillum amazonense strain CBAmC, an
RT   endophytic nitrogen-fixing and plant growth-promoting bacterium, isolated
RT   from sugarcane.";
RL   Submitted (JUN-2017) 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; CP022111; ASG22967.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A248JW77; -.
DR   KEGG; nao:Y958_19000; -.
DR   Proteomes; UP000197153; 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   CDD; cd01158; SCAD_SBCAD; 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; 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; 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; 1.
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|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU362125};
KW   Reference proteome {ECO:0000313|Proteomes:UP000197153}.
FT   DOMAIN          4..116
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          120..215
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          227..375
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   375 AA;  40221 MW;  D227B9905276B4D0 CRC64;
     MLITEEQAMV RDMARAFARE RLAPGAAERD RTSAFPADEL KAMGELGLMG MLVPEEWGGA
     GTDILSYVLA IEEIAAGDGA ISTIMSVHNS VGCAPILKFG TPAQKERYLR AMASGQMLGA
     FCLTEPQAGS DASALKTRAV RDGDHWVING AKQFITNGQN AGVALVFAVT DPAAGKKGIS
     AFLVPTDTPG YTVARLEHKL GQRCSDTAQI VFDNVRVPHE AMLGEPGQGY RIALANLEGG
     RIGIAAQSVG MAQAAFNAAR DYARERTSMG VAIIEHQAVA FRLADMATRI EAARQLMLHA
     ASLRQAGQPC LKEASMAKLF ASEMAERVCS DAIQTFGGYG YVDDFPVERI YRDVRVCQIY
     EGTSDIQKLV ISRNL
//
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