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Database: UniProt
Entry: A0A0Q9CAZ2_9CELL
LinkDB: A0A0Q9CAZ2_9CELL
Original site: A0A0Q9CAZ2_9CELL 
ID   A0A0Q9CAZ2_9CELL        Unreviewed;       390 AA.
AC   A0A0Q9CAZ2;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:KRD40283.1};
GN   ORFNames=ASE27_04895 {ECO:0000313|EMBL:KRD40283.1};
OS   Oerskovia sp. Root918.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC   Oerskovia.
OX   NCBI_TaxID=1736607 {ECO:0000313|EMBL:KRD40283.1, ECO:0000313|Proteomes:UP000051694};
RN   [1] {ECO:0000313|EMBL:KRD40283.1, ECO:0000313|Proteomes:UP000051694}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root918 {ECO:0000313|EMBL:KRD40283.1,
RC   ECO:0000313|Proteomes:UP000051694};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KRD40283.1, ECO:0000313|Proteomes:UP000051694}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root918 {ECO:0000313|EMBL:KRD40283.1,
RC   ECO:0000313|Proteomes:UP000051694};
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:KRD40283.1}.
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DR   EMBL; LMJG01000011; KRD40283.1; -; Genomic_DNA.
DR   RefSeq; WP_056648443.1; NZ_LMJG01000011.1.
DR   AlphaFoldDB; A0A0Q9CAZ2; -.
DR   Proteomes; UP000051694; 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   PANTHER; PTHR43884; ACYL-COA DEHYDROGENASE; 1.
DR   PANTHER; PTHR43884:SF12; COMPLEX I ASSEMBLY FACTOR ACAD9, MITOCHONDRIAL-RELATED; 1.
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;
KW   Reference proteome {ECO:0000313|Proteomes:UP000051694}.
FT   DOMAIN          246..369
FT                   /note="Acyl-CoA dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08028"
SQ   SEQUENCE   390 AA;  41791 MW;  87D2122EA9962397 CRC64;
     MSLPLLTDDL LDRIRSRAAG YDRENAFFTE DLEELTAAGY LRAFVPTAMG GPGLGLRDVA
     HEQIRLAGAA PATALAVNMH HVWTGVARYL YERGDHSLDF VLEEAARGEV FAFGYSEPGN
     DLVLFGSRTQ ARPDGEGGYS FHGRKIFTSL SPAWTRLGVL GIETAPEDGP GLDGAPRLVH
     AFVTREGGGV DVLDDWDTVG MRASQSRTTM LAGAHAPADR VVRRLAPGPS TDPLVLAIFT
     TFEVLLASVY TGIGKRALEL AVENAHRRTS MKNGGRPLSQ DPDIRWRVAD AGIAMDGIYP
     QIDQVAGEID ALVDRGAGWF TAVAGLKVRA TETARVVVDQ AIRVSGGSSY FASSELGRLY
     RDVLAGIFHP SDDESAHSTF ASALLGPVED
//
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