ID A0A0Q5AT21_9MICO Unreviewed; 390 AA.
AC A0A0Q5AT21;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:KQQ01551.1};
GN ORFNames=ASF42_13975 {ECO:0000313|EMBL:KQQ01551.1};
OS Rathayibacter sp. Leaf294.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Rathayibacter.
OX NCBI_TaxID=1736326 {ECO:0000313|EMBL:KQQ01551.1, ECO:0000313|Proteomes:UP000051858};
RN [1] {ECO:0000313|Proteomes:UP000051858}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf294 {ECO:0000313|Proteomes:UP000051858};
RA Garrido-Oter R., Mueller D.B.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000051858}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf294 {ECO:0000313|Proteomes:UP000051858};
RA Vorholt J.;
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:KQQ01551.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LMNO01000004; KQQ01551.1; -; Genomic_DNA.
DR RefSeq; WP_056043337.1; NZ_LMNO01000004.1.
DR AlphaFoldDB; A0A0Q5AT21; -.
DR Proteomes; UP000051858; 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; PTHR43831; ISOBUTYRYL-COA DEHYDROGENASE; 1.
DR PANTHER; PTHR43831:SF1; ISOBUTYRYL-COA DEHYDROGENASE, MITOCHONDRIAL; 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; 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 Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Reference proteome {ECO:0000313|Proteomes:UP000051858}.
FT DOMAIN 21..91
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 130..223
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 251..371
FT /note="Acyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08028"
SQ SEQUENCE 390 AA; 41540 MW; 031BE40610CBCD37 CRC64;
MTLLDAPARL VPDLSDRALA RLTARLAETA EHYDRTAEFP WEGIRAVHEA GLLTVAVGSR
YGGTPPSTVD LVRIFGALGQ GDPAVALISA MTVLQHAAHD RGATWPDELY RRVLADSAER
PVLLNAVRAE PEWGAPARGG LPATTIRRDG DEWVLEGRKG FATGSEGLAY HLVWAVDLQG
PSGEPELAHA IVPGDAPGVR VEKTWDHLGQ RASSTHDVVY EQVRLPLEYF RGVPRSQLAP
EAGAGGGFGL AVAALYVGIG RAAQSFFVRF ANERIPTSLG RPIATTERIR SVAGEIEAQL
VQAEEVLLSL AARVDAGDPR AAERLVVGKL LATRSAIAAV ETAVAALGNP GLTRHHPLER
HLRDVLASRV HPPQDDAALL IAGTRTLAAF
//