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Database: UniProt
Entry: A0A0Q5ZLR1_9BRAD
LinkDB: A0A0Q5ZLR1_9BRAD
Original site: A0A0Q5ZLR1_9BRAD 
ID   A0A0Q5ZLR1_9BRAD        Unreviewed;       429 AA.
AC   A0A0Q5ZLR1;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   SubName: Full=BEC protein {ECO:0000313|EMBL:KQT18947.1};
GN   ORFNames=ASG57_29705 {ECO:0000313|EMBL:KQT18947.1};
OS   Bradyrhizobium sp. Leaf396.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Bradyrhizobium.
OX   NCBI_TaxID=1736363 {ECO:0000313|EMBL:KQT18947.1, ECO:0000313|Proteomes:UP000051536};
RN   [1] {ECO:0000313|EMBL:KQT18947.1, ECO:0000313|Proteomes:UP000051536}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf396 {ECO:0000313|EMBL:KQT18947.1,
RC   ECO:0000313|Proteomes:UP000051536};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQT18947.1, ECO:0000313|Proteomes:UP000051536}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf396 {ECO:0000313|EMBL:KQT18947.1,
RC   ECO:0000313|Proteomes:UP000051536};
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:KQT18947.1}.
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DR   EMBL; LMQJ01000017; KQT18947.1; -; Genomic_DNA.
DR   RefSeq; WP_024342377.1; NZ_LMQJ01000017.1.
DR   AlphaFoldDB; A0A0Q5ZLR1; -.
DR   OrthoDB; 2986495at2; -.
DR   Proteomes; UP000051536; 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   CDD; cd00567; ACAD; 1.
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; PTHR43884; ACYL-COA DEHYDROGENASE; 1.
DR   PANTHER; PTHR43884:SF41; ACYL-COA DEHYDROGENASE YDBM-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; 2.
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}.
FT   DOMAIN          30..115
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          175..256
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          283..399
FT                   /note="Acyl-CoA dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08028"
SQ   SEQUENCE   429 AA;  47031 MW;  1482091D51C5913E CRC64;
     MTMQVSKTLD TTNKVALDAP IFDPIAFRLS DEQAGIIARA REIGQTVFAG RAATYDREAT
     FPTENYRDLH RVGLLGIAVP KKHGGLGANY QTYALAAAEI GRYCGATALT WNMHVCSTLW
     SGPLADDLDM DAETRAEHER RRAVHYKRIV ADGAIYSQPF SEGGAAAAGG VAFGTEARPV
     AGGWIVNGKK IFASLSGHAD YYGVLCTEIE EGEKASRRNT LYLAISAKSD GVSVVGDWDP
     LGMRGTVSRT LLFKDVFVPE DSALMPRGVY FQAAMRWPHM FLTLSPTYMG LAQAAYDFTV
     HYLRGEVPGM PPVKRRMYPT KQIAVAQMQI KLEQIKGIWF QAVTEACANP SKEQVLRAYA
     AQYSVMEGAN ELAALAIRTC GGQAMLRSLP LERIYRDSRC GSLMLPWTAE LCLDRIGREA
     LYEAGETDD
//
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