ID A0A120HNR0_9BRAD Unreviewed; 409 AA.
AC A0A120HNR0;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:AMA59365.1};
GN ORFNames=BCCGELA001_25895 {ECO:0000313|EMBL:AMA59365.1};
OS Bradyrhizobium sp. CCGE-LA001.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=1223566 {ECO:0000313|EMBL:AMA59365.1, ECO:0000313|Proteomes:UP000019052};
RN [1] {ECO:0000313|EMBL:AMA59365.1, ECO:0000313|Proteomes:UP000019052}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCGE-LA001 {ECO:0000313|EMBL:AMA59365.1,
RC ECO:0000313|Proteomes:UP000019052};
RX PubMed=24952318; DOI=10.1016/j.ympev.2014.06.006;
RA Servin-Garciduenas L.E., Zayas-Del Moral A., Ormeno-Orrillo E., Rogel M.A.,
RA Delgado-Salinas A., Sanchez F., Martinez-Romero E.;
RT "Symbiont shift towards Rhizobium nodulation in a group of phylogenetically
RT related Phaseolus species.";
RL Mol. Phylogenet. Evol. 79:1-11(2014).
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DR EMBL; CP013949; AMA59365.1; -; Genomic_DNA.
DR RefSeq; WP_008555593.1; NZ_CP013949.1.
DR AlphaFoldDB; A0A120HNR0; -.
DR STRING; 1223566.BCCGELA001_25895; -.
DR KEGG; brc:BCCGELA001_25895; -.
DR Proteomes; UP000019052; Chromosome.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro.
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; IPR013107; Acyl-CoA_DH_C.
DR InterPro; IPR046373; Acyl-CoA_Oxase/DH_mid-dom_sf.
DR InterPro; IPR036250; AcylCo_DH-like_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; PF08028; Acyl-CoA_dh_2; 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.
PE 4: Predicted;
FT DOMAIN 35..99
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 256..387
FT /note="Acyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08028"
SQ SEQUENCE 409 AA; 44526 MW; 519E89E8676456AE CRC64;
MAPGREPSIS EPARLEAGEL AYAAMMAKAR ALLPRLRERA ARTEELRHLP PETERDLHDT
GLFRMLQPSR IGGAELDYVS LIDCADLLGQ ADASVAWNLA NLASHHWMLG MFEPKAQDLV
WSRDPDALIA SSFIFPAGRA TRVEGGYRLH GSWPFSSGVA SCEWNMLASV VYSDDEADGI
EYRIFLLPKD DYKVLDTWNV AGLRGTGSCD VEVRDAFVAN HMTVAVGDLA GGPTPGSKVN
PNPLYALPVF SLFPYVLSGV ALGNAQACLD DYAEVARHRI STYNRAKLSD FQSTQIKIAE
ASAKIDAARL IMRSACLDAM ANARRGHIPD MATKTRYRRD GAFSVNLCTE AVSMLFAASG
ARGLFTTGVL QRQFRDAHAI NSHLAFNFDA AGTNYGRVAL GLPSENLTL
//
