ID A0A089YSV9_9PSED Unreviewed; 401 AA.
AC A0A089YSV9;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:AIS18724.1};
GN ORFNames=LT40_15550 {ECO:0000313|EMBL:AIS18724.1};
OS Pseudomonas rhizosphaerae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=216142 {ECO:0000313|EMBL:AIS18724.1, ECO:0000313|Proteomes:UP000029499};
RN [1] {ECO:0000313|EMBL:AIS18724.1, ECO:0000313|Proteomes:UP000029499}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16299 {ECO:0000313|EMBL:AIS18724.1};
RX PubMed=25483321; DOI=10.1016/j.jbiotec.2014.11.031;
RA Kwak Y., Jung B.K., Shin J.H.;
RT "Complete genome sequence of Pseudomonas rhizosphaerae IH5T (=DSM 16299T),
RT a phosphate-solubilizing rhizobacterium for bacterial biofertilizer.";
RL J. Biotechnol. 193:137-138(2015).
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DR EMBL; CP009533; AIS18724.1; -; Genomic_DNA.
DR RefSeq; WP_043191784.1; NZ_CP009533.1.
DR AlphaFoldDB; A0A089YSV9; -.
DR STRING; 216142.LT40_15550; -.
DR KEGG; prh:LT40_15550; -.
DR eggNOG; COG1960; Bacteria.
DR HOGENOM; CLU_018204_10_0_6; -.
DR OrthoDB; 6502068at2; -.
DR Proteomes; UP000029499; 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; 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; IPR013786; AcylCoA_DH/ox_N.
DR InterPro; IPR037069; AcylCoA_DH/ox_N_sf.
DR InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom_sf.
DR InterPro; IPR023922; S04_starv_induced_SfnB.
DR NCBIfam; TIGR04022; sulfur_SfnB; 1.
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; PF08028; Acyl-CoA_dh_2; 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.
PE 4: Predicted;
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Reference proteome {ECO:0000313|Proteomes:UP000029499}.
FT DOMAIN 36..123
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 134..217
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 244..376
FT /note="Acyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08028"
SQ SEQUENCE 401 AA; 43183 MW; B8678CFD8B879931 CRC64;
MSSLLHPLDG VARIANDQQA LDVARQLAPL LQRDSALRDR ERHLPHAELA LFSRSGLGGI
SVPKAFGGAG VSNVTLAQVI ALLAAADGSL GQIPQNHFYA LEVLRINGSP AQQQRLYSDV
LAGQRLGNAL AELGTRTAHD RTTRLTRDGD GFRIHGRKFY ATGALYAQCI PTSVIDEQGV
QQLAFVPADS AGVEVIDDWS GFGQRTTGSG SVVFDNVWVS VDAIVPFQSA FERPTTVGPF
AQILHAAIDT GIARGAFEDA LQFVRTRTRP WIDATSDKAV EDPLSLKSFG HLAIRLHAAE
ALLERAGEIL DKAQAEPTAE HVGAASIAVA EARALSTEIS LAAGSTLFEL AGSQATLAEH
GLDRHWRNAR VHTLHDPVRW KYHAIGNYYL NDQLPPRRGT I
//
