ID   A0A5Z9QYL0_SALET        Unreviewed;       729 AA.
AC   A0A5Z9QYL0;
DT   22-APR-2020, integrated into UniProtKB/TrEMBL.
DT   22-APR-2020, sequence version 1.
DT   07-APR-2021, entry version 7.
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:ECB5300441.1};
GN   ORFNames=AUA42_21275 {ECO:0000313|EMBL:EBV9836563.1}, D3D97_23335
GN   {ECO:0000313|EMBL:ECV0369698.1}, DBZ74_22095
GN   {ECO:0000313|EMBL:TAD54701.1}, DPD93_17155
GN   {ECO:0000313|EMBL:EBS3628613.1}, EYJ84_22250
GN   {ECO:0000313|EMBL:ECB5300441.1}, H9S94_23545
GN   {ECO:0000313|EMBL:QNN37625.1};
OS   Salmonella enterica subsp. enterica serovar Albany.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=211968 {ECO:0000313|EMBL:ECB5300441.1, ECO:0000313|Proteomes:UP000337743};
RN   [1] {ECO:0000313|EMBL:TAD54701.1, ECO:0000313|Proteomes:UP000293700}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=sg_wb24 {ECO:0000313|Proteomes:UP000293700}, and Sg_wb24
RC   {ECO:0000313|EMBL:TAD54701.1};
RA   Kohli G.S., Zwe Y.H., Ding Y., Givskov M., Liang Y.;
RT   "Comparative genomic analysis of various Salmonella enterica serotypes in
RT   Singapore.";
RL   Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EBS3628613.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=238461 {ECO:0000313|EMBL:EBS3628613.1};
RA   Ashton P.M., Dallman T., Nair S., De Pinna E., Peters T., Grant K.;
RL   Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:ECB5300441.1, ECO:0000313|Proteomes:UP000337743}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CVM-N26076 {ECO:0000313|EMBL:EBV9836563.1}, FSIS11917612
RC   {ECO:0000313|EMBL:ECB5300441.1, ECO:0000313|Proteomes:UP000337743},
RC   and FSIS21822039 {ECO:0000313|EMBL:ECV0369698.1};
RG   GenomeTrakr network: Whole genome sequencing for foodborne pathogen traceback;
RL   Submitted (FEB-2019) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|EMBL:QNN37625.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=R17.5974 {ECO:0000313|EMBL:QNN37625.1};
RA   Chiou C.-S., Hong Y.-P., Wang Y.-W., Chen Y.-S.;
RT   "Salmonella enterica subsp. enterica serovar Albany strain R19.5974.";
RL   Submitted (AUG-2020) 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: 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|HAMAP-Rule:MF_01621}.
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DR   EMBL; AAGVHF010000021; EBS3628613.1; -; Genomic_DNA.
DR   EMBL; AAHGYV010000131; EBV9836563.1; -; Genomic_DNA.
DR   EMBL; AAHXWF010000013; ECB5300441.1; -; Genomic_DNA.
DR   EMBL; AAKSWE010000038; ECV0369698.1; -; Genomic_DNA.
DR   EMBL; CP060730; QNN37625.1; -; Genomic_DNA.
DR   EMBL; QAUU01000104; TAD54701.1; -; Genomic_DNA.
DR   RefSeq; WP_023241747.1; NZ_RQSE01000017.1.
DR   UniPathway; UPA00659; -.
DR   Proteomes; UP000293700; Unassembled WGS sequence.
DR   Proteomes; UP000337743; Unassembled WGS sequence.
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; 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; 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.
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;  79598 MW;  92F9FE07364E13BE CRC64;
     MLYKGDTLYL DWLEDGIAEL VFDASGSVNK LDTATVASLG QALEVLEKQH DLKGLLLRSN
     KAAFIVGADI TEFLSLFLVP EEQLSQWLHF ANSVFNRLED LPVPTLAAVN GYALGGGCEC
     VLATDYRLAT PDLRIGLPET KLGIMPGFGG SVRLPRMLGA DSALEIIAAG KDVGAEHALK
     IGLVDGVVKQ EKLIEGAIAV LRQAITGDLD WRAKRQPKLE PLKLSKIEAA MSFTIAKGMV
     AQTAGKHYPA PMTAVKTIEA AARFGREEAL NLENKSFVPL AHTNEARALV GIFLNDQYVK
     GKAKKLTKDI ETPKQAAVLG AGIMGGGIAY QSAWKGVPVI MKDINDKSLN LGMTEAAKLL
     NKQLERGKID GLKLAGVIST IHPTLDYAGF DRVDVVVEAV VENPKVKKAV LAETEQKVRP
     ETVLASNTST IPIGELASAL ERPENFCGMH FFNPVHRMPL VEIIRGEKSS DETIAKVVAW
     ASKMGKTPIV VNDCPGFFVN RVLFPYFAGF SQLLRDGADF RKVDKVMEKQ FGWPMGPAYL
     LDVVGIDTAH HAQAVMAAGF PQRMQKEYRD AIDALFDASR FGQKNGLGFW RYKEDSKGKP
     KKEEDAAVDD LLASVSQPKR DFSDDEIIAR MMIPMINEVV RCLEEGIIAS PAEADMALVY
     GLGFPPFHGG AFRWLDTQGS AKYLDMAQQY QHLGPLYEVP EGLRNKARHN EPYYPPVEPA
     RPVGSLKTA
//