ID A0A0Q9KPX1_9MICO Unreviewed; 393 AA.
AC A0A0Q9KPX1;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=Acyl-CoA dehydrogenase C-terminal domain-containing protein {ECO:0000259|Pfam:PF08028};
GN ORFNames=ASG73_01510 {ECO:0000313|EMBL:KRE39065.1};
OS Janibacter sp. Soil728.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC Janibacter.
OX NCBI_TaxID=1736393 {ECO:0000313|EMBL:KRE39065.1, ECO:0000313|Proteomes:UP000051572};
RN [1] {ECO:0000313|EMBL:KRE39065.1, ECO:0000313|Proteomes:UP000051572}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil728 {ECO:0000313|EMBL:KRE39065.1,
RC ECO:0000313|Proteomes:UP000051572};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRE39065.1, ECO:0000313|Proteomes:UP000051572}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil728 {ECO:0000313|EMBL:KRE39065.1,
RC ECO:0000313|Proteomes:UP000051572};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRE39065.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LMRZ01000001; KRE39065.1; -; Genomic_DNA.
DR RefSeq; WP_055989776.1; NZ_LMRZ01000001.1.
DR AlphaFoldDB; A0A0Q9KPX1; -.
DR STRING; 1736393.ASG73_01510; -.
DR OrthoDB; 3404950at2; -.
DR Proteomes; UP000051572; Unassembled WGS sequence.
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; IPR037069; AcylCoA_DH/ox_N_sf.
DR InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom_sf.
DR Pfam; PF08028; Acyl-CoA_dh_2; 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 240..368
FT /note="Acyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08028"
SQ SEQUENCE 393 AA; 43210 MW; 40BA83990E044D13 CRC64;
MNAPLQYIRE HAEELRAEAR PSDRLGRLTD KSVEIIRASE GMKILHSKDH GGFEGHPNDF
FDWVVEVGRH HPSAGWVAGV VGIHPWELGI WGPQAEDDVY GAKGERAEDW VSSPYAPFGR
LVPTEGGYRF TGRWPFATGS DHVEWSILGG MIAGDDGEAL MPPTVVHVLV PMSDIEIIPE
SWNVMGLAGT GSNDITVDAF VPEHRVLVAD DVRANVYTDR HRPDNPLFHM QFGLMFPFAI
SAGTFGIARG AVDAAYAHIA KRVSTQGTAS KTDPFTMEAL ARAESDVEAG IAHLRQLVAT
HFDRVSEGRG HISIEDRLRF RIDQVRATDR AVTAVGDLYR LMGSSAIQQA SPLEPYWRDL
QVAASHVCNV REICYTAWGA HLFGGQVPPS ALY
//