ID O53158_MYCTU Unreviewed; 609 AA.
AC O53158; F2GET3; I6XBJ6; Q7D8E4;
DT 01-JUN-1998, integrated into UniProtKB/TrEMBL.
DT 01-JUN-1998, sequence version 1.
DT 27-MAR-2024, entry version 157.
DE SubName: Full=Probable acyl-CoA dehydrogenase FadE15 {ECO:0000313|EMBL:CCP44226.1};
GN Name=fadE15 {ECO:0000313|EMBL:CCP44226.1};
GN OrderedLocusNames=Rv1467c {ECO:0000313|EMBL:CCP44226.1};
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:CCP44226.1, ECO:0000313|Proteomes:UP000001584};
RN [1] {ECO:0000313|EMBL:CCP44226.1, 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 -!- 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; CCP44226.1; -; Genomic_DNA.
DR RefSeq; NP_215983.1; NC_000962.3.
DR RefSeq; WP_003900343.1; NZ_NVQJ01000004.1.
DR AlphaFoldDB; O53158; -.
DR SMR; O53158; -.
DR STRING; 83332.Rv1467c; -.
DR PaxDb; 83332-Rv1467c; -.
DR DNASU; 886562; -.
DR GeneID; 886562; -.
DR KEGG; mtu:Rv1467c; -.
DR PATRIC; fig|83332.111.peg.1633; -.
DR TubercuList; Rv1467c; -.
DR eggNOG; COG1960; Bacteria.
DR InParanoid; O53158; -.
DR OrthoDB; 9807883at2; -.
DR PhylomeDB; O53158; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
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 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 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 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 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..455
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT DOMAIN 474..604
FT /note="Acetyl-CoA dehydrogenase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF12806"
SQ SEQUENCE 609 AA; 65924 MW; 7BBB17958D31F01F CRC64;
MGHYIANVRD LEFNLLEVLD IGAVLGTGRY SDLDVDTVRT ILAEAARLAE GPIAESFGYA
DRNPPVFDPN THSISVPDEL AKTVQAIKEA GWWRLGLAEE IGGMPAPPPL AWAVNEMIYC
ANPSACFFNL GPVLAQSLYI EGNDEQRRWA AEGVQRGWQA TMVLTEPDAG SDVGAGRTKA
FEQPDGTWHI EGVKRFISGG DVGNTAENIF HLVLARPEGA GPGTKGLSLF YVPNYLFDPD
TFELGARNGV YVTGLEHKMG LKSSPTCELT FGGADVPAVG YLVGGVHNGI AQMFTVIEHA
RMTIGVKSAG TLSTGYLNAL AFAKERVQGA DLTQMTDKTA PRVTIMHHPD VRRSLMTQKA
YAEGLRALYL YAAAHQDDAV AQRVSGADHD MAHRVDDLLL PIVKGVGSER AYEILTESLQ
TLGGSGFLVD YPLEQYIRDA KIDSLYEGTT AIQALDFFFR KIVRDHGKAL QFVLAQVTHT
VENIDPSLKP QAELLRTALD DITAMTGALT GYLMSAAQHS SDIYKVGLGS VRYLLAVGDL
LIGWRLLVLA GVAHAALADG PSQNDEAFYR GKIAVAAFFA KNMLPKLTGV RSVIENIDDD
IMRVPEDAF
//
