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Database: UniProt
Entry: A0A0Q9KPX1_9MICO
LinkDB: A0A0Q9KPX1_9MICO
Original site: A0A0Q9KPX1_9MICO 
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}.
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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
//
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