ID   A0A5U3EHG6_SALET        Unreviewed;       729 AA.
AC   A0A5U3EHG6;
DT   12-AUG-2020, integrated into UniProtKB/TrEMBL.
DT   12-AUG-2020, sequence version 1.
DT   07-APR-2021, entry version 5.
DE   RecName: Full=Fatty acid oxidation complex subunit alpha {ECO:0000256|HAMAP-Rule:MF_01621};
DE   Includes:
DE     RecName: Full=Enoyl-CoA hydratase/Delta(3)-cis-Delta(2)-trans-enoyl-CoA isomerase/3-hydroxybutyryl-CoA epimerase {ECO:0000256|HAMAP-Rule:MF_01621};
DE              EC=4.2.1.17 {ECO:0000256|HAMAP-Rule:MF_01621};
DE              EC=5.1.2.3 {ECO:0000256|HAMAP-Rule:MF_01621};
DE              EC=5.3.3.8 {ECO:0000256|HAMAP-Rule:MF_01621};
DE   Includes:
DE     RecName: Full=3-hydroxyacyl-CoA dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01621};
DE              EC=1.1.1.35 {ECO:0000256|HAMAP-Rule:MF_01621};
GN   Name=fadB {ECO:0000256|HAMAP-Rule:MF_01621,
GN   ECO:0000313|EMBL:EBP3986417.1};
GN   ORFNames=S308_13495 {ECO:0000313|EMBL:EBP3986417.1};
OS   Salmonella enterica I.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=59201 {ECO:0000313|EMBL:EBP3986417.1};
RN   [1] {ECO:0000313|EMBL:EBP3986417.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CFSAN002857 {ECO:0000313|EMBL:EBP3986417.1};
RG   GenomeTrakr network: Whole genome sequencing for foodborne pathogen traceback;
RL   Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in the aerobic and anaerobic degradation of long-
CC       chain fatty acids via beta-oxidation cycle. Catalyzes the formation of
CC       3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA. It can also use
CC       D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as substrate.
CC       {ECO:0000256|HAMAP-Rule:MF_01621}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(3S)-3-hydroxybutanoyl-CoA = (3R)-3-hydroxybutanoyl-CoA;
CC         Xref=Rhea:RHEA:21760, ChEBI:CHEBI:57315, ChEBI:CHEBI:57316;
CC         EC=5.1.2.3; Evidence={ECO:0000256|HAMAP-Rule:MF_01621};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a (3E)-enoyl-CoA = a 4-saturated (2E)-enoyl-CoA;
CC         Xref=Rhea:RHEA:45228, ChEBI:CHEBI:58521, ChEBI:CHEBI:85097;
CC         EC=5.3.3.8; Evidence={ECO:0000256|HAMAP-Rule:MF_01621};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a (3S)-3-hydroxyacyl-CoA + NAD(+) = a 3-oxoacyl-CoA + H(+) +
CC         NADH; Xref=Rhea:RHEA:22432, ChEBI:CHEBI:15378, ChEBI:CHEBI:57318,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:90726; EC=1.1.1.35;
CC         Evidence={ECO:0000256|ARBA:ARBA00023994, ECO:0000256|HAMAP-
CC         Rule:MF_01621};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a (3S)-3-hydroxyacyl-CoA = a (2E)-enoyl-CoA + H2O;
CC         Xref=Rhea:RHEA:16105, ChEBI:CHEBI:15377, ChEBI:CHEBI:57318,
CC         ChEBI:CHEBI:58856; EC=4.2.1.17; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01621};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a (3Z)-enoyl-CoA = a 4-saturated (2E)-enoyl-CoA;
CC         Xref=Rhea:RHEA:45900, ChEBI:CHEBI:85097, ChEBI:CHEBI:85489;
CC         EC=5.3.3.8; Evidence={ECO:0000256|HAMAP-Rule:MF_01621};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 4-saturated-(3S)-3-hydroxyacyl-CoA = a (3E)-enoyl-CoA + H2O;
CC         Xref=Rhea:RHEA:20724, ChEBI:CHEBI:15377, ChEBI:CHEBI:58521,
CC         ChEBI:CHEBI:137480; EC=4.2.1.17; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01621};
CC   -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC       {ECO:0000256|ARBA:ARBA00005005, ECO:0000256|HAMAP-Rule:MF_01621}.
CC   -!- SUBUNIT: Heterotetramer of two alpha chains (FadB) and two beta chains
CC       (FadA). {ECO:0000256|HAMAP-Rule:MF_01621}.
CC   -!- SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family.
CC       {ECO:0000256|ARBA:ARBA00005254}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the 3-hydroxyacyl-CoA
CC       dehydrogenase family. {ECO:0000256|HAMAP-Rule:MF_01621}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the enoyl-CoA
CC       hydratase/isomerase family. {ECO:0000256|ARBA:ARBA00008750,
CC       ECO:0000256|HAMAP-Rule:MF_01621}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EBP3986417.1}.
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DR   EMBL; AAGLPU010000017; EBP3986417.1; -; Genomic_DNA.
DR   UniPathway; UPA00659; -.
DR   GO; GO:0036125; C:fatty acid beta-oxidation multienzyme complex; IEA:InterPro.
DR   GO; GO:0003857; F:3-hydroxyacyl-CoA dehydrogenase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008692; F:3-hydroxybutyryl-CoA epimerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0004165; F:dodecenoyl-CoA delta-isomerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0004300; F:enoyl-CoA hydratase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0070403; F:NAD+ binding; IEA:InterPro.
DR   GO; GO:0006635; P:fatty acid beta-oxidation; IEA:UniProtKB-UniPathway.
DR   HAMAP; MF_01621; FadB; 1.
DR   InterPro; IPR006180; 3-OHacyl-CoA_DH_CS.
DR   InterPro; IPR006176; 3-OHacyl-CoA_DH_NAD-bd.
DR   InterPro; IPR006108; 3HC_DH_C.
DR   InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR   InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR   InterPro; IPR018376; Enoyl-CoA_hyd/isom_CS.
DR   InterPro; IPR001753; Enoyl-CoA_hydra/iso.
DR   InterPro; IPR012799; FadB.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   Pfam; PF00725; 3HCDH; 2.
DR   Pfam; PF02737; 3HCDH_N; 1.
DR   Pfam; PF00378; ECH_1; 1.
DR   SUPFAM; SSF48179; SSF48179; 2.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   SUPFAM; SSF52096; SSF52096; 1.
DR   TIGRFAMs; TIGR02437; FadB; 1.
DR   PROSITE; PS00067; 3HCDH; 1.
DR   PROSITE; PS00166; ENOYL_COA_HYDRATASE; 1.
PE   3: Inferred from homology;
KW   Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832, ECO:0000256|HAMAP-
KW   Rule:MF_01621};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_01621};
KW   Lipid degradation {ECO:0000256|ARBA:ARBA00022963, ECO:0000256|HAMAP-
KW   Rule:MF_01621};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098, ECO:0000256|HAMAP-
KW   Rule:MF_01621};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_01621};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268, ECO:0000256|HAMAP-
KW   Rule:MF_01621};
KW   NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_01621};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW   Rule:MF_01621}.
FT   DOMAIN          316..494
FT                   /note="3HCDH_N"
FT                   /evidence="ECO:0000259|Pfam:PF02737"
FT   DOMAIN          496..592
FT                   /note="3HCDH"
FT                   /evidence="ECO:0000259|Pfam:PF00725"
FT   DOMAIN          627..690
FT                   /note="3HCDH"
FT                   /evidence="ECO:0000259|Pfam:PF00725"
FT   NP_BIND         400..402
FT                   /note="NAD"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01621"
FT   REGION          1..189
FT                   /note="Enoyl-CoA hydratase/isomerase"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01621"
FT   REGION          311..729
FT                   /note="3-hydroxyacyl-CoA dehydrogenase"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01621"
FT   REGION          708..729
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        450
FT                   /note="For 3-hydroxyacyl-CoA dehydrogenase activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01621"
FT   BINDING         296
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01621"
FT   BINDING         324
FT                   /note="NAD; via amide nitrogen"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01621"
FT   BINDING         343
FT                   /note="NAD"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01621"
FT   BINDING         407
FT                   /note="NAD"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01621"
FT   BINDING         429
FT                   /note="NAD"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01621"
FT   BINDING         453
FT                   /note="NAD"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01621"
FT   BINDING         500
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01621"
FT   BINDING         660
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01621"
FT   SITE            119
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01621"
FT   SITE            139
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01621"
SQ   SEQUENCE   729 AA;  79575 MW;  B2EE6FB80FECC808 CRC64;
     MLYKGDTLYL DWLEDGIAEL VFDATGSVNK LDTATVASLG QALEVLEKQH DLKGLLLRSN
     KAAFIVGADI TEFLSLFLVP EEQLSQWLHF ANSVFNRLED LPVPTLAAVN GYALGGGCEC
     VLATDYRLAT PDLRIGLPET KLGIMPGFGG SVRLPRMLGA DSALEIIAAG KDVGAEHALK
     IGLVDGVVKQ EKLIEGAIAV LRQAIAGDLD WKAKRQPKLE PLKLSKIEAT MSFTIAKGMV
     AQTAGKHYPA PMTAVKTIEA AARFGREEAL NLENKSFVPL AHTNEARALV GIFLNDQYVK
     GKAKKLTKDI ETPKQAAVLG AGIMGGGIAY QSAWKGVPVI MKDINDKSLT LGMTEAAKLL
     NKQLERGKID GLKLAGVIST IHPTLDYAGF DRVDVVVEAV VENPKVKKAV LVETEEKVRP
     DTVLASNTST IPIGELASVL KRPENFCGMH FFNPVHRMPL VEIIRGEKSS DETIAKVVAW
     ASKMGKTPIV VNDCPGFFVN RVLFPYFAGF SQLLRDGADF RKVDKVMEKQ FGWPMGPAYL
     LDVVGIDTAH HAQAVMAAGF PQRMQKDYRD AIDALFDASR FGQKNGLGFW RYKEDSKGKP
     KKEEDAAVDD LLASVSQSKR DFSDDEIIAR MMIPMVNEVV RCLEEGIIAS PAEADMALVY
     GLGFPPFHGG AFRWLDTQGS AKYLDMAQQY QHLGPLYEVP EGLRNKARHN EPYYPPVEPA
     RPVGSLKTA
//