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Database: UniProt
Entry: A0A0Q8QUJ7_9SPHN
LinkDB: A0A0Q8QUJ7_9SPHN
Original site: A0A0Q8QUJ7_9SPHN 
ID   A0A0Q8QUJ7_9SPHN        Unreviewed;       430 AA.
AC   A0A0Q8QUJ7;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Acyl-CoA dehydrogenase C-terminal domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=ASE00_00890 {ECO:0000313|EMBL:KRB85390.1};
OS   Sphingomonas sp. Root710.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=1736594 {ECO:0000313|EMBL:KRB85390.1, ECO:0000313|Proteomes:UP000051854};
RN   [1] {ECO:0000313|EMBL:KRB85390.1, ECO:0000313|Proteomes:UP000051854}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root710 {ECO:0000313|EMBL:KRB85390.1,
RC   ECO:0000313|Proteomes:UP000051854};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KRB85390.1, ECO:0000313|Proteomes:UP000051854}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root710 {ECO:0000313|EMBL:KRB85390.1,
RC   ECO:0000313|Proteomes:UP000051854};
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:KRB85390.1}.
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DR   EMBL; LMIB01000001; KRB85390.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0Q8QUJ7; -.
DR   STRING; 1736594.ASE00_00890; -.
DR   OrthoDB; 7316074at2; -.
DR   Proteomes; UP000051854; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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   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;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051854};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        269..290
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          57..140
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          278..407
FT                   /note="Acyl-CoA dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08028"
SQ   SEQUENCE   430 AA;  47374 MW;  7AB2D01A26021F9B CRC64;
     MLFREKDFMA DLGLASLEPP VAQVDLPKPE DYLPREEVAA LTPAILRERT LALKPMIAAK
     ARETELARRP LPDVWSALAR AGIFYHFVPK RYGGLEFGFE DMVDIMMPVA EACASTGWAA
     TFCVEHNYIF SQFPKEAQDE VYAKLPYMIA PGTASPPGKA RKAPGGLRVS GHWKWGSGIM
     NSDWVMAQVV IEDGTPMNGM PDMAFVAFPI EDCTVLDTWH MSGMCGTGSN DFVVNDIFVP
     EHRVLPSRHF INCDGPGALS QENIMYRGAM VPFTAVACAI PALGAARAAV DYYRDKSRTR
     ILMGTQTKAM DTQAVQIRLG RADMLARTAE LLVRDGCRTM QREVEAGNQF DSVWRRRVRA
     QISEGVHLCR DAIVLAMDGS GASAHALDVP IQRYQRDCSV VVTHALYEPD ANHEAHGRAL
     LDLAPAGPMF
//
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