ID A0A142M8V1_AMIAI Unreviewed; 542 AA.
AC A0A142M8V1;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Putative acyl-CoA dehydrogenase {ECO:0000313|EMBL:MBB3704619.1};
GN ORFNames=FHS67_000922 {ECO:0000313|EMBL:MBB3704619.1};
OS Aminobacter aminovorans (Chelatobacter heintzii).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Phyllobacteriaceae; Aminobacter.
OX NCBI_TaxID=83263 {ECO:0000313|EMBL:MBB3704619.1, ECO:0000313|Proteomes:UP000577697};
RN [1] {ECO:0000313|EMBL:MBB3704619.1, ECO:0000313|Proteomes:UP000577697}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10368 {ECO:0000313|EMBL:MBB3704619.1,
RC ECO:0000313|Proteomes:UP000577697};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (AUG-2020) 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:MBB3704619.1}.
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DR EMBL; JACICB010000003; MBB3704619.1; -; Genomic_DNA.
DR RefSeq; WP_067966629.1; NZ_JACICB010000003.1.
DR AlphaFoldDB; A0A142M8V1; -.
DR STRING; 83263.AA2016_3852; -.
DR OrthoDB; 9771038at2; -.
DR Proteomes; UP000577697; 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:SF3; ACYL-COA DEHYDROGENASE AIDB-RELATED; 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; PS00072; ACYL_COA_DH_1; 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 7..164
FT /note="Adaptive response protein AidB N-terminal"
FT /evidence="ECO:0000259|Pfam:PF18158"
FT DOMAIN 178..271
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 282..437
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 542 AA; 58873 MW; 79992E099D9D5793 CRC64;
MTQDVPNQPP PLTGSNAWRG DPLLIQIAEG FSDPVRRDLD GLGRFVLTHE AQDLARLANS
EVPKLRTHDR QGRRIDQVEF HPAYHALMRR SIAGGLHSSV WENGGTETGR RHQVRAARFY
LTAQLECGHL CPITMTNASL AALMASPKLF REWAPRVTTR KYDQAQKPPV EKTGLTLGMG
MTEKQGGTDV RANTTKAERA GGSFYRLTGH KWFMSAPMSD AFLMLAQAPE GLSCFLVPRI
LSDGSANGLQ FQRLKDKLGN RSNASSEVEI QGAIGDLVGE PGGGIKTIMD MVTLTRLDCA
VASSAIMRAG LAEAVHHTRH RQVFGANLVD QPLMQRVLAD MALDVAGATA LAFRLARSFD
EAASDRGEAA FARAMTPVVK YWVCKIAPAL LYEAMECLGG NGYVEEAPLA RYYREAPVNA
IWEGSGNVMA LDVLRVLQRA PGLFEDVLAA LERDLGPGGR SVLGVLRAAM QVASSDEGSA
RILTEQLAIS AAAAELRRMG AGRIADAFIE TRLAGQWRGT YGMIDARHDS RLIIDTLYPQ
VG
//
