FADE_SALTI
ID FADE_SALTI Reviewed; 814 AA.
AC Q8Z937;
DT 01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Acyl-coenzyme A dehydrogenase {ECO:0000250|UniProtKB:Q8ZRJ7};
DE Short=ACDH {ECO:0000250|UniProtKB:Q8ZRJ7};
DE Short=Acyl-CoA dehydrogenase {ECO:0000250|UniProtKB:Q8ZRJ7};
DE EC=1.3.8.7 {ECO:0000250|UniProtKB:Q8ZRJ7};
DE EC=1.3.8.8 {ECO:0000250|UniProtKB:Q8ZRJ7};
DE AltName: Full=Medium-/long-chain fatty acyl-CoA dehydrogenase {ECO:0000250|UniProtKB:Q8ZRJ7};
GN Name=fadE; OrderedLocusNames=STY0354, t2541;
OS Salmonella typhi.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=90370;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CT18;
RX PubMed=11677608; DOI=10.1038/35101607;
RA Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA Barrell B.G.;
RT "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT serovar Typhi CT18.";
RL Nature 413:848-852(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700931 / Ty2;
RX PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT CT18.";
RL J. Bacteriol. 185:2330-2337(2003).
CC -!- FUNCTION: Catalyzes the dehydrogenation of acyl-coenzymes A (acyl-CoAs)
CC to 2-enoyl-CoAs, the first step of the beta-oxidation cycle of fatty
CC acid degradation. Is required for the utilization of medium- and long-
CC chain fatty acids as sole carbon sources for growth. Is needed for
CC bacterial survival during carbone-source starvation.
CC {ECO:0000250|UniProtKB:Q8ZRJ7}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a medium-chain 2,3-saturated fatty acyl-CoA + H(+) + oxidized
CC [electron-transfer flavoprotein] = a medium-chain (2E)-enoyl-CoA +
CC reduced [electron-transfer flavoprotein]; Xref=Rhea:RHEA:14477,
CC Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:83723,
CC ChEBI:CHEBI:83726; EC=1.3.8.7;
CC Evidence={ECO:0000250|UniProtKB:Q8ZRJ7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a long-chain 2,3-saturated fatty acyl-CoA + H(+) + oxidized
CC [electron-transfer flavoprotein] = a long-chain (2E)-enoyl-CoA +
CC reduced [electron-transfer flavoprotein]; Xref=Rhea:RHEA:17721,
CC Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:83721,
CC ChEBI:CHEBI:83727; EC=1.3.8.8;
CC Evidence={ECO:0000250|UniProtKB:Q8ZRJ7};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:P15651};
CC -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC {ECO:0000250|UniProtKB:Q8ZRJ7}.
CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; AL513382; CAD08779.1; -; Genomic_DNA.
DR EMBL; AE014613; AAO70125.1; -; Genomic_DNA.
DR RefSeq; NP_454921.1; NC_003198.1.
DR RefSeq; WP_000973055.1; NZ_WSUR01000017.1.
DR AlphaFoldDB; Q8Z937; -.
DR SMR; Q8Z937; -.
DR STRING; 220341.16501595; -.
DR EnsemblBacteria; AAO70125; AAO70125; t2541.
DR KEGG; stt:t2541; -.
DR KEGG; sty:STY0354; -.
DR PATRIC; fig|220341.7.peg.348; -.
DR eggNOG; COG1960; Bacteria.
DR HOGENOM; CLU_012192_0_0_6; -.
DR OMA; SAYAHSQ; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000000541; Chromosome.
DR Proteomes; UP000002670; Chromosome.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0004466; F:long-chain-acyl-CoA dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0033539; P:fatty acid beta-oxidation using acyl-CoA dehydrogenase; IEA:InterPro.
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 InterPro; IPR015396; DUF1974.
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 Pfam; PF09317; DUF1974; 1.
DR SUPFAM; SSF47203; SSF47203; 1.
DR SUPFAM; SSF56645; SSF56645; 1.
PE 3: Inferred from homology;
KW FAD; Fatty acid metabolism; Flavoprotein; Lipid metabolism; Oxidoreductase.
FT CHAIN 1..814
FT /note="Acyl-coenzyme A dehydrogenase"
FT /id="PRO_0000201202"
FT ACT_SITE 497
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P15651"
SQ SEQUENCE 814 AA; 89274 MW; 425C6195436B2E07 CRC64;
MMILSIIATV VLLGALFYHR VSLFLSSLIL LAWTAALGVA GLWSIWLLVP LAIILVPFNL
TPMRKSMISA PVFRGFRKVM PPMSRTEKEA IDAGTTWWEG DLFQGKPDWK KLHNYPQPQL
TAEEQAFLDG PVEEACRMAN DFQITHELAD LPPELWAYLK EHRFFAMIIK KEYGGLEFSA
YVQSRVLQKL SGVSGILAIT VGVPNSLGPG ELLQHYGTEE QKNHYLPRLA RGQEIPCFAL
TSPEAGSDAG AIPDTGVVCM GEWQGQQVLG MRLTWNKRYI TLAPIATVLG LAFKLSDPDR
LLGGEEELGI TCALIPTSTP GVEIGRRHFP LNVPFQNGPT RGNDIFVPID YIIGGPKMAG
QGWRMLVECL SVGRGITLPS NSTGGVKSVA LATGAYAHIR RQFKISIGKM EGIEEPLARI
AGNAYVMDAA ASLITYGIML GEKPAVLSAI VKYHCTHRGQ QSIIDAMDIT GGKGIMLGES
NFLARAYQGA PIAITVEGAN ILTRSMMIFG QGAIRCHPYV LEEMAAAQNN DVNAFDKLLF
KHIGHVGSNT VRSFWLGLTR GLTSHTPTGD ATKRYYQHLN RLSANLALLS DVSMAVLGGS
LKRRERISTR LGDVLSQLYL ASAVLKRYDD EGRHEADLPL VHWGVQDALY RAEQAMDDLL
QNFPNRVVAG LLTAMIFPTG RHYLAPSDKL DHAVAKILQV PNATRSRIGR GQYLTPAEHN
PVGLLEEALR DVIAADPIHQ RICKELGKNL PFTRLDELAR NALAKGLIDK DEAAILAKAE
ESRLRSINVD DFEPEALATK PVKLPEKVRK VEAA
