ID   A0A8E6U6I7_SALER        Unreviewed;       729 AA.
AC   A0A8E6U6I7;
DT   19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2022, sequence version 1.
DT   14-DEC-2022, entry version 4.
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:QVT26619.1};
GN   ORFNames=LM45_22920 {ECO:0000313|EMBL:QVT26619.1};
OS   Salmonella enterica (Salmonella choleraesuis).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=28901 {ECO:0000313|EMBL:QVT26619.1};
RN   [1] {ECO:0000313|EMBL:QVT26619.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CFSAN024230 {ECO:0000313|EMBL:QVT26619.1};
RG   GenomeTrakr network: Whole genome sequencing for foodborne pathogen traceback;
RL   Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:QVT26619.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CFSAN024230 {ECO:0000313|EMBL:QVT26619.1};
RA   Hoffmann M., Balkey M., Luo Y.;
RT   "Whole genome PacBio Sequel sequence of Salmonella enterica subsp.
RT   enterica.";
RL   Submitted (MAY-2021) 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:ARBA00023693, 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: 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}.
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DR   EMBL; CP075011; QVT26619.1; -; 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:delta(3)-delta(2)-enoyl-CoA 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; 6-phosphogluconate dehydrogenase C-terminal domain-like; 2.
DR   SUPFAM; SSF52096; ClpP/crotonase; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 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   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                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01621"
FT   BINDING         324
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01621"
FT   BINDING         343
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01621"
FT   BINDING         400..402
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01621"
FT   BINDING         407
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01621"
FT   BINDING         429
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01621"
FT   BINDING         453
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01621"
FT   BINDING         500
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01621"
FT   BINDING         660
FT                   /ligand="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;  79682 MW;  C129D87722D30F44 CRC64;
     MLYKGDTLYL DWLEDGIAEL VFDAPGSVNK LDTATVASLG QALEVLEKQH DLKGLLLRSN
     KAAFIVGADI TEFLSLFLVP EEQLSQWLHF ANSVFNRLED LPVPTLAAVN GYALGGGCEC
     VLATDYRLAT PDLRIGLPET KLGIMPGFGG SVRMPRMLGA DSALEIIAAG KDIGAEQALK
     IGLVDGVVKQ EKLIDGAIAV LRQAITGDLD WRAKRQPKLE PLKLSKIEAA MSFTIAKGMV
     AQTAGKHYPA PMTAVKTIEA AARFGREEAL NLENKSFVPL AHTNEARALV GIFLNDQYVK
     GKAKKLTKDI ETPKQAAVLG AGIMGGGIAY QSAWKGVPVI MKDINDKSLN LGMTEAAKLL
     NKQLERGKID GLKLAGVIST IHPTLDYAGF DRVDVVVEAV VENPKVKKAV LAETEQKVRP
     ETVLASNTST IPIRELASAL ERPENFCGMH FFNPVHRMPL VEIIRGEKSS DETIAKVVAW
     ASKMGKTPIV VNDCPGFFVN RVLFPYFAGF SQLLRDGADF RKVDKVMEKQ FGWPMGPAYL
     LDVVGIDTAH HAQAVMAAGF PQRMQKEYRD AIDALFDASR FGQKNGLGFW RYKEDSKGKP
     KKEEDAAVDD LLASVSQPKR DFSDDEIIAR MMIPMINEVV RCLEEGIIAS PAEADMALVY
     GLGFPPLHGG AFRWLDTQGS AKYLDMAQQY QHLGPLYEVP EGLRNKARHN EPYYPPVEPA
     RPVGSLKTA
//