ID A0A8E6U6I7_SALER Unreviewed; 729 AA. AC A0A8E6U6I7; DT 19-JAN-2022, integrated into UniProtKB/TrEMBL. DT 19-JAN-2022, sequence version 1. DT 22-FEB-2023, 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: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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 CDD; cd06558; crotonase-like; 1. DR Gene3D; 1.10.1040.50; -; 1. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1. 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 PANTHER; PTHR43612; TRIFUNCTIONAL ENZYME SUBUNIT ALPHA; 1. DR PANTHER; PTHR43612:SF3; TRIFUNCTIONAL ENZYME SUBUNIT ALPHA, MITOCHONDRIAL; 1. 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="3-hydroxyacyl-CoA dehydrogenase NAD binding" FT /evidence="ECO:0000259|Pfam:PF02737" FT DOMAIN 496..592 FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal" FT /evidence="ECO:0000259|Pfam:PF00725" FT DOMAIN 627..690 FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal" 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 //