ID I0RF68_MYCXE Unreviewed; 736 AA.
AC I0RF68;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE SubName: Full=FadE6 {ECO:0000313|EMBL:EID09771.1};
GN ORFNames=MXEN_19765 {ECO:0000313|EMBL:EID09771.1};
OS Mycobacterium xenopi RIVM700367.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1150591 {ECO:0000313|EMBL:EID09771.1, ECO:0000313|Proteomes:UP000003584};
RN [1] {ECO:0000313|EMBL:EID09771.1, ECO:0000313|Proteomes:UP000003584}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RIVM700367 {ECO:0000313|EMBL:EID09771.1,
RC ECO:0000313|Proteomes:UP000003584};
RX PubMed=22628510; DOI=10.1128/JB.00482-12;
RA Abdallah A.M., Rashid M., Adroub S.A., Elabdalaoui H., Ali S.,
RA van Soolingen D., Bitter W., Pain A.;
RT "Complete Genome Sequence of Mycobacterium xenopi Type Strain RIVM700367.";
RL J. Bacteriol. 194:3282-3283(2012).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00009347}.
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:EID09771.1}.
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DR EMBL; AJFI01000097; EID09771.1; -; Genomic_DNA.
DR RefSeq; WP_003922924.1; NZ_AJFI01000097.1.
DR AlphaFoldDB; I0RF68; -.
DR PATRIC; fig|1150591.3.peg.3982; -.
DR OrthoDB; 2431337at2; -.
DR Proteomes; UP000003584; 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; 2.
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; 2.
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; IPR009075; AcylCo_DH/oxidase_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; PTHR43292; ACYL-COA DEHYDROGENASE; 1.
DR PANTHER; PTHR43292:SF4; ACYL-COA DEHYDROGENASE FADE34; 1.
DR Pfam; PF00441; Acyl-CoA_dh_1; 2.
DR Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR Pfam; PF02771; Acyl-CoA_dh_N; 2.
DR SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 2.
DR SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 2.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Reference proteome {ECO:0000313|Proteomes:UP000003584}.
FT DOMAIN 6..100
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 222..347
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT DOMAIN 384..474
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 478..568
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 584..730
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 736 AA; 78736 MW; 19737309863CB090 CRC64;
MPIAITPEHR DLADSVRSLV ARVAPSEVLH AAMETGPETP IENPPPYWRA AAEQGLQGVH
LAESVGGQGF GILELAIVLA EFGYGAVPGP FVPSAIASAL ISAHDPHAKV LAELSSGAAI
AAYALGPGLT ATRHGDGLVI RGEVRAVPAA AEASVLVLPV AIDSGEEWIV LHAEQLEIER
VKSIDPLRPI AHVRANAVEV GDDALLSNLS MAAAHALIST LLSAEAIGVA RWATDAASQY
AKIREQFGRP IGQFQAVKHK CAEMIADTER ATAAVWDAAR AIDEARESNW DTASSAVEFA
AAVAGTLAPA AAQRCTQDCI QVHGGIGFTW EHDTNVYYRR ALILAASFGR RTDYPQRVVD
TATSTGMRQL NIDLDPETEK LRAEIRAEVA ALKAMPREER KAAIAEGGWV LPYLPKPWGR
AASPVEQIII EQEFTVGRVK RPQIGIASWI IPSIVAFGTE EQKQRFIPPT FRGEMTWCQL
FSEPGAGSDL AGLATKATRT EGGWRITGQK IWTTAAQFSD WGALLARTDP SAPKHNGITY
FLLDMKSEGV QVKPLRELTG GAMFNTVFID DVFVPDDCVL GEVNRGWEVS RNTLTAERVS
IGSSEAPFLA NLDEFVGFLR DGQFDQVAQN RGGQLIAEGH AAKVLNMRST LLTLAGGDAM
PSAAISKLLS MRTAQGYAEF AVSTFGTDAA IGDPEELAGK WGQYLLASRA TTIYGGTSEV
QLNIIAERLL GLPRDP
//
