ID A0A2T6B0I3_9RHOB Unreviewed; 448 AA.
AC A0A2T6B0I3;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Alkylation response protein AidB-like acyl-CoA dehydrogenase {ECO:0008006|Google:ProtNLM};
GN ORFNames=C8N34_107229 {ECO:0000313|EMBL:PTX49581.1};
OS Gemmobacter caeni.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Gemmobacter.
OX NCBI_TaxID=589035 {ECO:0000313|EMBL:PTX49581.1, ECO:0000313|Proteomes:UP000244224};
RN [1] {ECO:0000313|EMBL:PTX49581.1, ECO:0000313|Proteomes:UP000244224}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21823 {ECO:0000313|EMBL:PTX49581.1,
RC ECO:0000313|Proteomes:UP000244224};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (APR-2018) 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:PTX49581.1}.
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DR EMBL; QBKP01000007; PTX49581.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T6B0I3; -.
DR Proteomes; UP000244224; 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 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 35..116
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 168..251
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 279..395
FT /note="Acyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08028"
SQ SEQUENCE 448 AA; 50386 MW; 13D46D7AA88ACFAB CRC64;
MTDQSAITAH PPMSDPADYY DISRIRPVVL EKLRRVNELG ATKFAARARA VDDEASFPVE
NYRDLAEEGF LGLCIPEEYG GWGFSMWEYA MVGAEIAKYC GATALTFNMH NSSMAWSRFM
FDMPNLTPEE KAAFAPLRDR QFRRAIAERA IFSQPISEGG QNWTSKPNQT QCRKVDGGWR
INGFKKFASL AGYCDYYTIV CTEVFEGVEP RHEDTMLFVV HKDAPGLSVK GEWDPLGMRG
TNSRDLILKD VFVTGDDLLM PRGIFGKTLP NWPHMMATLS PTYMGVAQGA FDFTVAYLKG
KVPGQPPIDR RMYATKRIAV GKMYARLANM RALWWQAFTE AKGFPTKGEV MRMYAAQYNV
MEGAAEMTSM AIRTCGGQSM LRSLPLERMY RDSRCGALML PYTSEIMEDY LSILTLYDMD
EIDTAPGDEG GARNSLWRGD SGTLRALR
//