ID   ACD2_MYCTU              Reviewed;         407 AA.
AC   P96831; F2GLV2; I6Y2X6; L0T2P6;
DT   03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT   03-AUG-2022, sequence version 4.
DT   03-AUG-2022, entry version 140.
DE   RecName: Full=Probable acyl-CoA dehydrogenase FadE2 {ECO:0000303|PubMed:9634230};
DE            EC=1.3.99.-;
GN   Name=fadE2 {ECO:0000312|EMBL:CCP42879.1};
GN   OrderedLocusNames=Rv0154c {ECO:0000312|EMBL:CCP42879.1};
OS   Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83332;
RN   [1] {ECO:0000312|EMBL:CCP42879.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=9634230; DOI=10.1038/31159;
RA   Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
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.M., Devlin K.,
RA   Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA   Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA   Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA   Squares S., Squares R., 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]
RP   PROTEIN SEQUENCE OF 1-8, AND SEQUENCE REVISION TO N-TERMINUS.
RC   STRAIN=H37Rv;
RX   PubMed=34915127; DOI=10.1016/j.ygeno.2021.12.001;
RA   Shi J., Meng S., Wan L., Zhang Z., Jiang S., Zhu H., Dai E., Chang L.,
RA   Gao H., Wan K., Zhang L., Zhao X., Liu H., Lyu Z., Zhang Y., Xu P.;
RT   "Deep N-terminomics of Mycobacterium tuberculosis H37Rv extensively correct
RT   annotated encoding genes.";
RL   Genomics 114:292-304(2022).
RN   [3] {ECO:0007744|PubMed:21969609}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=21969609; DOI=10.1074/mcp.m111.011627;
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; Evidence={ECO:0000305};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000305};
CC   -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CCP42879.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000269|PubMed:34915127};
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DR   EMBL; AL123456; CCP42879.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_214668.1; NC_000962.3.
DR   RefSeq; WP_003401015.1; NZ_NVQJ01000001.1.
DR   SMR; P96831; -.
DR   STRING; 83332.Rv0154c; -.
DR   PaxDb; P96831; -.
DR   PRIDE; P96831; -.
DR   DNASU; 886836; -.
DR   GeneID; 886836; -.
DR   KEGG; mtu:Rv0154c; -.
DR   PATRIC; fig|83332.111.peg.179; -.
DR   TubercuList; Rv0154c; -.
DR   eggNOG; COG1960; Bacteria.
DR   OMA; HRMLTVY; -.
DR   PhylomeDB; P96831; -.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR   GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IBA:GO_Central.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0033539; P:fatty acid beta-oxidation using acyl-CoA dehydrogenase; IBA:GO_Central.
DR   Gene3D; 1.10.540.10; -; 1.
DR   Gene3D; 2.40.110.10; -; 1.
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.
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; SSF47203; 1.
DR   SUPFAM; SSF56645; SSF56645; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; FAD; Flavoprotein; Oxidoreductase;
KW   Reference proteome.
FT   CHAIN           1..407
FT                   /note="Probable acyl-CoA dehydrogenase FadE2"
FT                   /id="PRO_0000455761"
SQ   SEQUENCE   407 AA;  44808 MW;  CD5C83166632CCD0 CRC64;
     MDFAMSAKAI DYRTRLSDFM TEHVFGAEAD YDDYRRAAGP ADHTAPPIIE ELKTKAKDRG
     LWNLFLSAES GLTNLEYAPL AEMTGWSMEI APEALNCAAP DTGNMEILHM FGTEQQRAQW
     LRPLLDGKIR SAFSMTEPAV ASSDARNIET TISRDGADYV INGRKWWTSG AADPRCKILI
     VMGRTNPDAA AHQQQSMVLV PIDTPGVTIV RSTPVFGWQD RHGHCEIDYH NVRVPATNLL
     GEEGSGFAIA QARLGPGRIH HCMRALGAAE RALALMVNRV RNRVAFGRPL AEQGVVQQAI
     AQSRNEIDQA RLLCEKAAWT IDQHGNKEAR HLVAMIKAVA PRVACDVIDR AIQVHGAAGV
     SDDTPLARLY GWHRAMRIFD GPDEVHLRSI ARAELSREKS TFAAAVT