FADE_SALTY
ID FADE_SALTY Reviewed; 814 AA.
AC Q8ZRJ7;
DT 01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Acyl-coenzyme A dehydrogenase {ECO:0000303|PubMed:10206693};
DE Short=ACDH {ECO:0000303|PubMed:10206693};
DE Short=Acyl-CoA dehydrogenase {ECO:0000303|PubMed:10206693};
DE EC=1.3.8.7 {ECO:0000305|PubMed:10206693};
DE EC=1.3.8.8 {ECO:0000305|PubMed:10206693};
DE AltName: Full=Medium-/long-chain fatty acyl-CoA dehydrogenase {ECO:0000303|PubMed:10206693};
GN Name=fadE;
GN Synonyms=fadF {ECO:0000303|PubMed:10206693},
GN yafH {ECO:0000303|PubMed:10206693}; OrderedLocusNames=STM0309;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [2]
RP IDENTIFICATION, FUNCTION, PATHWAY, INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=LT2;
RX PubMed=10206693; DOI=10.1099/13500872-145-1-15;
RA Spector M.P., DiRusso C.C., Pallen M.J., Garcia del Portillo F., Dougan G.,
RA Finlay B.B.;
RT "The medium-/long-chain fatty acyl-CoA dehydrogenase (fadF) gene of
RT Salmonella typhimurium is a phase 1 starvation-stress response (SSR)
RT locus.";
RL Microbiology 145:15-31(1999).
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 S.typhimurium to utilize medium- and
CC long-chain fatty acids as sole carbon sources for growth. Is needed for
CC bacterial survival during carbone-source starvation.
CC {ECO:0000269|PubMed:10206693}.
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:0000305|PubMed:10206693};
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:0000305|PubMed:10206693};
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:0000269|PubMed:10206693}.
CC -!- INDUCTION: Is under the negative control of the global regulator FadR
CC and the positive control of the cAMP:cAMP receptor protein (cAMP:CRP)
CC as well as the alarmone ppGpp. Is induced under carbon-source
CC starvation and in the presence of the long-chain fatty acid oleate.
CC Induction during carbon starvation is cAMP:CRP-dependent and sigma(S)-
CC independent. {ECO:0000269|PubMed:10206693}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene show undetectable in vivo
CC beta-oxidation levels, and are unable to grow on oleate or decanoate as
CC a sole carbon and energy source, in contrast to the wild-type parent
CC strain. {ECO:0000269|PubMed:10206693}.
CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; AE006468; AAL19266.1; -; Genomic_DNA.
DR RefSeq; NP_459307.1; NC_003197.2.
DR RefSeq; WP_000973041.1; NC_003197.2.
DR AlphaFoldDB; Q8ZRJ7; -.
DR SMR; Q8ZRJ7; -.
DR STRING; 99287.STM0309; -.
DR PaxDb; Q8ZRJ7; -.
DR EnsemblBacteria; AAL19266; AAL19266; STM0309.
DR GeneID; 1251828; -.
DR KEGG; stm:STM0309; -.
DR PATRIC; fig|99287.12.peg.328; -.
DR HOGENOM; CLU_012192_0_0_6; -.
DR OMA; SAYAHSQ; -.
DR PhylomeDB; Q8ZRJ7; -.
DR BioCyc; SENT99287:STM0309-MON; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000001014; 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; 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; 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 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 2: Evidence at transcript level;
KW FAD; Fatty acid metabolism; Flavoprotein; Lipid metabolism; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..814
FT /note="Acyl-coenzyme A dehydrogenase"
FT /id="PRO_0000201203"
FT ACT_SITE 497
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P15651"
SQ SEQUENCE 814 AA; 89216 MW; 7C3BD7A7DF61886B CRC64;
MMILSIIATV VLLGALFYHR VSLFLSSLIL LAWTAALGVA GLWSIWLLVP LAIILVPFNL
TPMRKSMISA PVFRGFRKVM PPMSRTEKEA IDAGTTWWEG DLFQGKPDWK KLHNYPQPQL
TAEEQAFLDG PVEEACRMAN DFQITHELAD LPPELWAYLK EHRFFAMIIK KEYGGLEFSA
YAQSRVLQKL 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
LKRRERISAR LGDVLSQLYL ASAVLKRYDD EGRHEADLPL VHWGVQDALY RAEQAMDDLL
QNFPNRVVAG LLTAMIFPTG RHYLAPSDKL DHAVAKILQV PNATRSRIGR GQYLTPAEHN
PVGLLEEALR DVIAADPIHQ RICKELGKNL PFTRLDELAR NALAKGLIDK DEAAILAKAE
ESRLRSINVD DFEPEALATK PVKLPEKVRK VEAA
