ID FADB_SHESH Reviewed; 716 AA. AC A8FP63; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 13-NOV-2007, sequence version 1. DT 04-NOV-2026, entry version 110. DE RecName: Full=Fatty acid oxidation complex subunit alpha {ECO:0000255|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:0000255|HAMAP-Rule:MF_01621}; DE EC=4.2.1.17 {ECO:0000255|HAMAP-Rule:MF_01621}; DE EC=5.1.2.3 {ECO:0000255|HAMAP-Rule:MF_01621}; DE EC=5.3.3.8 {ECO:0000255|HAMAP-Rule:MF_01621}; DE Includes: DE RecName: Full=3-hydroxyacyl-CoA dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01621}; DE EC=1.1.1.35 {ECO:0000255|HAMAP-Rule:MF_01621}; GN Name=fadB {ECO:0000255|HAMAP-Rule:MF_01621}; GN OrderedLocusNames=Ssed_0023; OS Shewanella sediminis (strain HAW-EB3). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Alteromonadales; Shewanellaceae; Shewanella. OX NCBI_TaxID=425104; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HAW-EB3; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., RA Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Detter J.C., RA Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., RA Zhao J.-S., Richardson P.; RT "Complete sequence of Shewanella sediminis HAW-EB3."; RL Submitted (AUG-2007) 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:0000255|HAMAP-Rule:MF_01621}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a (3S)-3-hydroxyacyl-CoA + NAD(+) = a 3-oxoacyl-CoA + NADH + CC H(+); 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:0000255|HAMAP-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:0000255|HAMAP- CC 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:0000255|HAMAP- CC 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:0000255|HAMAP-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:0000255|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:0000255|HAMAP-Rule:MF_01621}; CC -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation. CC {ECO:0000255|HAMAP-Rule:MF_01621}. CC -!- SUBUNIT: Heterotetramer of two alpha chains (FadB) and two beta chains CC (FadA). {ECO:0000255|HAMAP-Rule:MF_01621}. CC -!- SIMILARITY: In the N-terminal section; belongs to the enoyl-CoA CC hydratase/isomerase family. {ECO:0000255|HAMAP-Rule:MF_01621}. CC -!- SIMILARITY: In the C-terminal section; belongs to the 3-hydroxyacyl-CoA CC dehydrogenase family. {ECO:0000255|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; CP000821; ABV34636.1; -; Genomic_DNA. DR RefSeq; WP_012004162.1; NC_009831.1. DR AlphaFoldDB; A8FP63; -. DR SMR; A8FP63; -. DR STRING; 425104.Ssed_0023; -. DR KEGG; sse:Ssed_0023; -. DR eggNOG; COG1024; Bacteria. DR eggNOG; COG1250; Bacteria. DR HOGENOM; CLU_009834_16_3_6; -. DR OMA; AADKYAH; -. DR OrthoDB; 5389341at2; -. DR UniPathway; UPA00659; -. DR Proteomes; UP000002015; Chromosome. DR GO; GO:0036125; C:fatty acid beta-oxidation multienzyme complex; IEA:InterPro. DR GO; GO:0018812; F:3-hydroxyacyl-CoA dehydratase activity; IEA:RHEA. 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:0016509; F:long-chain (3S)-3-hydroxyacyl-CoA dehydrogenase (NAD+) activity; IEA:TreeGrafter. DR GO; GO:0070403; F:NAD+ binding; IEA:InterPro. DR GO; GO:0006635; P:fatty acid beta-oxidation; IEA:UniProtKB-UniRule. DR CDD; cd06558; crotonase-like; 1. DR FunFam; 1.10.1040.50:FF:000001; Fatty acid oxidation complex subunit alpha; 1. DR FunFam; 3.40.50.720:FF:000009; Fatty oxidation complex, alpha subunit; 1. DR Gene3D; 1.10.1040.50; -; 1. DR Gene3D; 3.90.226.10; 2-enoyl-CoA Hydratase, Chain A, domain 1; 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; IPR050136; FA_oxidation_alpha_subunit. DR InterPro; IPR012799; FadB. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR NCBIfam; TIGR02437; FadB; 1. DR NCBIfam; NF008727; fadB; 1. DR PANTHER; PTHR43612; TRIFUNCTIONAL ENZYME SUBUNIT ALPHA; 1. DR PANTHER; PTHR43612:SF3; TRIFUNCTIONAL ENZYME SUBUNIT ALPHA, MITOCHONDRIAL; 1. DR Pfam; PF00725; 3HCDH; 1. 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 PROSITE; PS00067; 3HCDH; 1. DR PROSITE; PS00166; ENOYL_COA_HYDRATASE; 1. PE 3: Inferred from homology; KW Fatty acid metabolism; Isomerase; Lipid degradation; Lipid metabolism; KW Lyase; Multifunctional enzyme; NAD; Oxidoreductase; Reference proteome. FT CHAIN 1..716 FT /note="Fatty acid oxidation complex subunit alpha" FT /id="PRO_1000088085" FT REGION 1..189 FT /note="Enoyl-CoA hydratase/isomerase" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01621" FT REGION 311..716 FT /note="3-hydroxyacyl-CoA dehydrogenase" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01621" FT ACT_SITE 450 FT /note="For 3-hydroxyacyl-CoA dehydrogenase activity" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01621" FT BINDING 296 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01621" FT BINDING 324 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01621" FT BINDING 343 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01621" FT BINDING 400..402 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01621" FT BINDING 407 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01621" FT BINDING 429 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01621" FT BINDING 453 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01621" FT BINDING 500 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01621" FT SITE 119 FT /note="Important for catalytic activity" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01621" FT SITE 139 FT /note="Important for catalytic activity" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01621" SQ SEQUENCE 716 AA; 77021 MW; AD91C405CB10CF8A CRC64; MIYQSPTIQV ELLEDNIARL CFNASGSVNK LDRETINSLD AALDAIQQDS HIQALVLTSA KGAFIVGADI TEFLGLFAQE DSVLLPWIAE ANVVFNKLED LPFPTISAIN GFALGGGFET VLATDFRIAD TTAKIGLPET KLGLIPGFGG TVRLPRLIGT DNALEWITSG KDQRPEAALK VGAIDAVVAP ENLQASAIKM LKDALAEKLD WQSRRARKQA ALTLPKLEAM MSFATAKGMV FKIAGKHYPA PMAAISVIEQ AARCGRADAL KVEHQAFVKL AKTDVAQALI GIFLNDQLVK GKAKKAGKLA KNIDTAAVLG AGIMGGGIAY QSASKGTPII MKDIAQPALE LGLGEASKLL AAQIKRGRST PQKMAKVLNN ITATLDYTPV KDVDVVVEAV VEHPKVKSMV LAEVEQNVSD DAIITSNTST ISINLLAKSL KKPERFCGMH FFNPVHKMPL VEVIRGENSS EETIASVVAY ASKMGKTPIV VNDCPGFFVN RVLFPYFAGF SGLLADGADF AAIDKVMEKQ FGWPMGPAYL LDVVGIDTGH HAQAVMAEGF PDRMGKNGKD AIDIMFEAER FGQKNSKGFY AYSVDRRGKP KKDVDPTSYE LLGAEFGELK AFESEDIIAR TMIPMIIETV RCLEEGIIAT PAEADMGLVF GLGFPPFRGG VFRYIDTMGV ANFVALADKY AHLGGLYQVT DAMRELAANN GSYYQS //