ID A0A0B5E8W3_9RHOB Unreviewed; 412 AA.
AC A0A0B5E8W3;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:AJE48752.1};
GN ORFNames=P73_4037 {ECO:0000313|EMBL:AJE48752.1};
OS Celeribacter indicus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Celeribacter.
OX NCBI_TaxID=1208324 {ECO:0000313|EMBL:AJE48752.1, ECO:0000313|Proteomes:UP000031521};
RN [1] {ECO:0000313|EMBL:AJE48752.1, ECO:0000313|Proteomes:UP000031521}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P73 {ECO:0000313|EMBL:AJE48752.1};
RX PubMed=25256706; DOI=10.1099/ijs.0.069039-0;
RA Lai Q., Cao J., Yuan J., Li F., Shao Z.;
RT "Celeribacter indicus sp. nov., a polycyclic aromatic hydrocarbon-degrading
RT bacterium from deep-sea sediment and reclassification of Huaishuia
RT halophila as Celeribacter halophilus comb. nov.";
RL Int. J. Syst. Evol. Microbiol. 64:4160-4167(2014).
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DR EMBL; CP004393; AJE48752.1; -; Genomic_DNA.
DR RefSeq; WP_052453463.1; NZ_FNNW01000014.1.
DR AlphaFoldDB; A0A0B5E8W3; -.
DR STRING; 1208324.P73_4037; -.
DR KEGG; cid:P73_4037; -.
DR HOGENOM; CLU_018204_10_0_5; -.
DR OrthoDB; 6184213at2; -.
DR Proteomes; UP000031521; 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 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:UP000031521}.
FT DOMAIN 25..121
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 129..215
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 241..382
FT /note="Acyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08028"
SQ SEQUENCE 412 AA; 44381 MW; 3EBADA9150F6577E CRC64;
MTTTLKTVPV LDNAAEAFHV ARDYAESIRE GAGLRDRKGT PPYDELRALA QTGLLGINIP
RAYGGAGVAI SEVIDVIRIL ASVDSSIAQT VQSHFTSIDR LRVMGPEHLR RRLYPRILAG
ERLSNASAER GGKSAASFVT RINRQTDGSY LIEGRKYYTT GALTSQWIAV RALSDDNRLA
TAYVPRDTPG IQIDDDWHGF GQRSTTSGTA TFTAVRVPAE LVDFLPYHGP ESDINKALAF
LTHGAIETGI AENALHDGTD FVRTKARPHA EIITEGGADV VAEDLLVQAQ LGRLATSTHA
ARAMVLRAAE IIDAVHATGD YNVDNVGEAL IAVSEAKAFA AEVALETSTA VIGLVGASAT
DLKHALDRHW RNARTHSVHD SLTWKYVQAG RYLLTGEAPN WAPFTAPEAQ AK
//
