ID A0A120FJD3_9BRAD Unreviewed; 590 AA.
AC A0A120FJD3;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=DNA alkylation response protein {ECO:0000313|EMBL:KWV48889.1};
GN ORFNames=AS156_17690 {ECO:0000313|EMBL:KWV48889.1};
OS Bradyrhizobium macuxiense.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=1755647 {ECO:0000313|EMBL:KWV48889.1, ECO:0000313|Proteomes:UP000057737};
RN [1] {ECO:0000313|EMBL:KWV48889.1, ECO:0000313|Proteomes:UP000057737}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BR 10303 {ECO:0000313|EMBL:KWV48889.1,
RC ECO:0000313|Proteomes:UP000057737};
RA Zelli J.E., Simoes-Araujo J.L., Barauna A.C., Silva K.;
RT "Draft Genome Sequence of the Strain BR 10303 (Bradyrhizobium sp.) isolated
RT from nodules of Centrolobium paraense.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|RuleBase:RU362125};
CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00009347, ECO:0000256|RuleBase:RU362125}.
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:KWV48889.1}.
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DR EMBL; LNCU01000106; KWV48889.1; -; Genomic_DNA.
DR RefSeq; WP_066513309.1; NZ_LNCU01000106.1.
DR AlphaFoldDB; A0A120FJD3; -.
DR OrthoDB; 9771038at2; -.
DR Proteomes; UP000057737; Unassembled WGS sequence.
DR GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IEA:InterPro.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
DR Gene3D; 2.40.110.20; -; 1.
DR Gene3D; 6.10.250.600; -; 1.
DR Gene3D; 1.20.140.10; Butyryl-CoA Dehydrogenase, subunit A, domain 3; 1.
DR InterPro; IPR006089; Acyl-CoA_DH_CS.
DR InterPro; IPR006091; Acyl-CoA_Oxase/DH_mid-dom.
DR InterPro; IPR036250; AcylCo_DH-like_C.
DR InterPro; IPR009075; AcylCo_DH/oxidase_C.
DR InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom_sf.
DR InterPro; IPR041504; AidB_N.
DR PANTHER; PTHR42707; ACYL-COA DEHYDROGENASE; 1.
DR PANTHER; PTHR42707:SF2; ACYL-COA DEHYDROGENASE FAMILY MEMBER 11; 1.
DR Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR Pfam; PF18158; AidB_N; 1.
DR SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1.
DR PROSITE; PS00073; ACYL_COA_DH_2; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|RuleBase:RU362125};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU362125};
KW Oxidoreductase {ECO:0000256|RuleBase:RU362125}.
FT DOMAIN 18..177
FT /note="Adaptive response protein AidB N-terminal"
FT /evidence="ECO:0000259|Pfam:PF18158"
FT DOMAIN 188..285
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 295..444
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 590 AA; 65136 MW; 94BBD43C0051AFE1 CRC64;
MQQDLKPSSA SQPGLLAPDT TGMNFYRADP ALTDLLKLHL PDALFRHIEP HLDRLGGLAG
GYLDECARLA DRHTPVLHQR DKFGRDVQHI EYHPAYREIE KAAFGEFGIH ALSIRKGIMG
WPDKYPVVAK HAFTFLFNQT EFGMGCPINV TDGCAKLLNN FGSEALKAKY LDGLTQTDVS
KLTQGGQFMT EKEGGSDVGT LTTRAVQEGD HWRLYGEKWF CSNADAKVVM LLARPEGAGP
GTRGVGLFLM PRFLDDGSQN HYRIVRLKDK LGTRSMASGE IKFDGAVAYA VGKLDRGFVQ
MAEMVNSSRL SNGVKSTSLM RRAWHDAIMV ARGRVVFGQR IIDLPLARRQ LMKIMLPTEQ
ALSMSFLTAD ALDRAEAGSQ DAAALLRILT PTLKFRATRD ARKVCGDAME MRGGIGYIEE
FVTPRLLRDA HLGSIWEGTG NIVAIDALKR AVGRHGADSA LAADLHARLD DSTNVPQAWR
NRLRGLSDRA VAFAREVASR MDNEGDARRA TSLLYHVASA VALAWEGGRI HEMRGDARRL
LLSRMVIDHR VMPGDPFRLT ENTLQRRMTE HLLGDRAIGM AEVGELLVAA
//
