ID Q73TM4_MYCPA Unreviewed; 611 AA.
AC Q73TM4;
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=FadE5 {ECO:0000313|EMBL:AAS06244.1};
GN Name=fadE5 {ECO:0000313|EMBL:AAS06244.1};
GN OrderedLocusNames=MAP_3694c {ECO:0000313|EMBL:AAS06244.1};
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:AAS06244.1, ECO:0000313|Proteomes:UP000000580};
RN [1] {ECO:0000313|EMBL:AAS06244.1, 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 ECO:0000256|RuleBase:RU362125};
CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00009347, ECO:0000256|RuleBase:RU362125}.
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DR EMBL; AE016958; AAS06244.1; -; Genomic_DNA.
DR RefSeq; WP_003879144.1; NZ_CP106873.1.
DR AlphaFoldDB; Q73TM4; -.
DR STRING; 262316.MAP_3694c; -.
DR GeneID; 75272445; -.
DR KEGG; mpa:MAP_3694c; -.
DR eggNOG; COG1960; Bacteria.
DR HOGENOM; CLU_018204_12_1_11; -.
DR Proteomes; UP000000580; Chromosome.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro.
DR CDD; cd01153; ACAD_fadE5; 1.
DR Gene3D; 2.40.110.20; -; 1.
DR Gene3D; 1.20.140.10; Butyryl-CoA Dehydrogenase, subunit A, domain 3; 1.
DR InterPro; IPR025878; Acyl-CoA_dh-like_C_dom.
DR InterPro; IPR020953; Acyl-CoA_DH_N_bac.
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; IPR034188; FadE5-like.
DR PANTHER; PTHR42803; ACYL-COA DEHYDROGENASE; 1.
DR PANTHER; PTHR42803:SF1; BROAD-SPECIFICITY LINEAR ACYL-COA DEHYDROGENASE FADE5; 1.
DR Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR Pfam; PF12806; Acyl-CoA_dh_C; 1.
DR Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR Pfam; PF12418; AcylCoA_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 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|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU362125};
KW Reference proteome {ECO:0000313|Proteomes:UP000000580}.
FT DOMAIN 3..34
FT /note="Acyl-CoA dehydrogenase N-terminal bacteria"
FT /evidence="ECO:0000259|Pfam:PF12418"
FT DOMAIN 162..271
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 288..454
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT DOMAIN 475..607
FT /note="Acetyl-CoA dehydrogenase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF12806"
SQ SEQUENCE 611 AA; 66562 MW; F730CA301EAD1EA1 CRC64;
MSHYKSNVRD QEFNLFEVLG VDKALGQGEF SDLDADTARE MLNEISRLAE GPIADSFVEG
DRNPPVFDPK THSVTLPESF KKSVHAVIEA GWDKVGIDEA LGGVAMPKAL LWALHEHILG
ANPAVWMYAG GAGFANILYH LGTDEQKKWA VMAAERGWGS TMVLTEPDAG SDVGAGRTKA
VKQDDGSWHI DGVKRFITSA DSDDLFENIF HLVLARPEGA GPGTKGLSLF FVPKFLFDFE
TGELGERNGV FVTNVEHKMG LKVSATCELS FGQHDVPAKG WLVGEVHNGI AQMFEVIEQA
RMMVGTKAIA TLSTGYLNAL EYAKSRVQGA DMTQMTDKTA PRVTITHHPD VRRSLMTQKA
YAEGLRALYL FTSTYQDAAV AEALYGVDAE LAVKVNDLML PVVKGVGSEQ AYAKLTESLQ
TFGGSGFLQD YPIEQYIRDS KIDSLYEGTT AIQAQDFFFR KIVRDKGVAL AHVSEQIQKF
VDSESGNGRL KSERELLAKA LADVQGMATA LTGYLMAAQE DVTSLYKVGL GSVRFLMSVG
DLIIGWLLQR QAAVAVAALD AGASGEDRSF YEGKIAVASF FAKNFLPMLT STREVIETLD
NDIMELDEAA F
//
