ID O33229_MYCTU Unreviewed; 386 AA.
AC O33229; F2GPJ9; I6YA35;
DT 01-JAN-1998, integrated into UniProtKB/TrEMBL.
DT 01-JAN-1998, sequence version 1.
DT 27-MAR-2024, entry version 147.
DE SubName: Full=Probable acyl-CoA dehydrogenase FadE20 {ECO:0000313|EMBL:CCP45522.1};
GN Name=fadE20 {ECO:0000313|EMBL:CCP45522.1};
GN OrderedLocusNames=Rv2724c {ECO:0000313|EMBL:CCP45522.1};
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332 {ECO:0000313|EMBL:CCP45522.1, ECO:0000313|Proteomes:UP000001584};
RN [1] {ECO:0000313|EMBL:CCP45522.1, ECO:0000313|Proteomes:UP000001584}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv {ECO:0000313|Proteomes:UP000001584};
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C., Harris D.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E.III., Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L., Oliver K., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton J.,
RA Squares R., Squares S., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2] {ECO:0007829|PubMed:21969609}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21969609; DOI=10.1074/mcp.M111.011445;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=A + a 2,3-saturated acyl-CoA = a 2,3-dehydroacyl-CoA + AH2;
CC Xref=Rhea:RHEA:48608, ChEBI:CHEBI:13193, ChEBI:CHEBI:17499,
CC ChEBI:CHEBI:60015, ChEBI:CHEBI:65111;
CC Evidence={ECO:0000256|ARBA:ARBA00043783};
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; AL123456; CCP45522.1; -; Genomic_DNA.
DR RefSeq; NP_217240.1; NC_000962.3.
DR RefSeq; WP_003413981.1; NZ_NVQJ01000017.1.
DR AlphaFoldDB; O33229; -.
DR SMR; O33229; -.
DR STRING; 83332.Rv2724c; -.
DR PaxDb; 83332-Rv2724c; -.
DR DNASU; 887866; -.
DR GeneID; 887866; -.
DR KEGG; mtu:Rv2724c; -.
DR PATRIC; fig|83332.111.peg.3029; -.
DR eggNOG; COG1960; Bacteria.
DR InParanoid; O33229; -.
DR OrthoDB; 8876745at2; -.
DR PhylomeDB; O33229; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
DR GO; GO:0033539; P:fatty acid beta-oxidation using acyl-CoA dehydrogenase; IBA:GO_Central.
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; IPR006089; Acyl-CoA_DH_CS.
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; PTHR43884; ACYL-COA DEHYDROGENASE; 1.
DR PANTHER; PTHR43884:SF12; COMPLEX I ASSEMBLY FACTOR ACAD9, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF00441; Acyl-CoA_dh_1; 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.
DR PROSITE; PS00073; ACYL_COA_DH_2; 1.
PE 1: Evidence at protein level;
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:UP000001584}.
FT DOMAIN 14..125
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 129..224
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 236..384
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 386 AA; 42845 MW; 93303871E24BFC40 CRC64;
MGSATKYQRT LFEPEHELFR ESYRAFLDRH VAPYHDEWEK TKIVDRGVWL EAGKQGFLGM
AVPEEYGGGG NADFRYNTVI TEETCAGRYS GIGFGLHNDI VAPYLLALAT EEQKRRWFPN
FCTGELITAI AMTEPGTGSD LQGITTRAVK HGDHYVLNGS KTFITNGINS DLVIVVAQTD
PEKGAQGFSL LVVERGMAGF ERGRQLDKIG LDAQDTAELS FTDVAVPAEN LLGQEGMGFI
YLMQNLPQER ISIAIMAAAG MESVLEQTLQ YAKERKAFGR SIGSFQNSRF LLAELATEAT
VVRIMVDEFI KLHLAGKLTA EQAAMAKWYA TEKQVYLNDR CLQLHGGYGY MREYPVARAY
LDSRVQTIYG GTTEIMKEII GRGLGV
//
