ID Q73TK2_MYCPA Unreviewed; 733 AA.
AC Q73TK2;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 107.
DE SubName: Full=FadE6 {ECO:0000313|EMBL:AAS06266.1};
GN Name=fadE6 {ECO:0000313|EMBL:AAS06266.1};
GN OrderedLocusNames=MAP_3716c {ECO:0000313|EMBL:AAS06266.1};
OS Mycolicibacterium paratuberculosis (strain ATCC BAA-968 / K-10)
OS (Mycobacterium paratuberculosis).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium avium complex (MAC).
OX NCBI_TaxID=262316 {ECO:0000313|EMBL:AAS06266.1, ECO:0000313|Proteomes:UP000000580};
RN [1] {ECO:0000313|EMBL:AAS06266.1, ECO:0000313|Proteomes:UP000000580}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-968 / K-10 {ECO:0000313|Proteomes:UP000000580};
RX PubMed=16116077; DOI=10.1073/pnas.0505662102;
RA Li L., Bannantine J.P., Zhang Q., Amonsin A., May B.J., Alt D., Banerji N.,
RA Kanjilal S., Kapur V.;
RT "The complete genome sequence of Mycobacterium avium subspecies
RT paratuberculosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:12344-12349(2005).
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}.
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DR EMBL; AE016958; AAS06266.1; -; Genomic_DNA.
DR RefSeq; WP_003874014.1; NZ_CP106873.1.
DR AlphaFoldDB; Q73TK2; -.
DR STRING; 262316.MAP_3716c; -.
DR KEGG; mpa:MAP_3716c; -.
DR PATRIC; fig|262316.17.peg.3959; -.
DR eggNOG; COG1960; Bacteria.
DR HOGENOM; CLU_018204_9_3_11; -.
DR Proteomes; UP000000580; Chromosome.
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 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:UP000000580}.
FT DOMAIN 7..97
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 218..346
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT DOMAIN 383..471
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 475..567
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 581..727
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 733 AA; 78361 MW; 906C4ADF6C1313B9 CRC64;
MPIAINPEHQ ELADSVRALV ARIAPSETLH EAMETEVGNP PPYWQAAAEQ GLQGVHLAES
VGGQGFGVLE LAIVLAEFGY GAVPGPFVPS AIASALISAH DPDAKALAGL ASGAEIAAYG
LNCCALTATR QGSSLVIRGE LRAVPAAAQA SLLVLPVAID SGEAWVVLRA DQLEIEPVKS
LDPLRPIADV RANAVEVGDD VVLTNLSMGT AHALMTTLLS AEAIGVARWA TDTASSYAKI
REQFGRPIGQ FQAIKHKCAE MIADTERATA AVWDAARAID EARENRWDTA GSHVEFAAAV
AATLAPAAAQ RCAQDCIQVH GGIGFTWEHD TNVYYRRALM LAASFGRSSD YPQKVVDTAT
TTGMRAVDID LDPETEKLRA EIRAEVAALK EIEREQRKVA IAEGGWVLPY LPKPWGRAAG
PVEQIIIAQE FASGRVKRPQ TGIATWIVPS IVAFGTEEQK QRFLPPTFRG EMIWCQLFSE
PGAGSDLAGL STKATRTDGG WRITGQKIWT TAAQFSQWGA LLARTDPSAP KHSGITYFLL
DMKSEGVDVK PLRELTGNAM FNTVYIDDVF VPDECVLGEV NRGWEVSRNT LTAERVSIGS
SEANFLATLS QFVEFVRDGQ FDQVAQHRAG QLIAEGHAAK VLNLRSTLLT LAGGDAMPSA
AISKLLSMRT GQGYAEFAVS SFGTDAAIGD TDQLPGKWGE YLLASRATTI YGGTSEVQLN
IIAERLLGLP RDP
//
