ID A0A0Q9ZJL6_9GAMM Unreviewed; 719 AA. AC A0A0Q9ZJL6; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 27-MAR-2024, entry version 43. 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:KRG32409.1}; GN ORFNames=AK822_12715 {ECO:0000313|EMBL:KRG32409.1}; OS Psychrobacter sp. P11F6. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae; OC Psychrobacter. OX NCBI_TaxID=1699621 {ECO:0000313|EMBL:KRG32409.1, ECO:0000313|Proteomes:UP000050989}; RN [1] {ECO:0000313|EMBL:KRG32409.1, ECO:0000313|Proteomes:UP000050989} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=P11F6 {ECO:0000313|EMBL:KRG32409.1, RC ECO:0000313|Proteomes:UP000050989}; RA Ruckert C., Albersmeier A., Moghadam M.S., Winkler A., Lale R., RA Kalinowski J.; RT "High quality draft genome sequence of Psychrobacter sp. P11F6, isolated RT from an ascidian tunicate in the Norwegian sea."; RL Submitted (AUG-2015) 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 -!- SIMILARITY: In the central section; belongs to the 3-hydroxyacyl-CoA CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00007005}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {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:KRG32409.1}. 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; LJCE01000002; KRG32409.1; -; Genomic_DNA. DR RefSeq; WP_060491905.1; NZ_CM003594.1. DR AlphaFoldDB; A0A0Q9ZJL6; -. DR PATRIC; fig|1699621.3.peg.2694; -. DR OrthoDB; 5389341at2; -. DR UniPathway; UPA00659; -. DR Proteomes; UP000050989; Chromosome. 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; IPR001753; Enoyl-CoA_hydra/iso. DR InterPro; IPR012799; FadB. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR NCBIfam; TIGR02437; FadB; 1. DR PANTHER; PTHR43612:SF8; FATTY ACID OXIDATION COMPLEX SUBUNIT ALPHA; 1. DR PANTHER; PTHR43612; TRIFUNCTIONAL ENZYME SUBUNIT ALPHA; 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 PROSITE; PS00067; 3HCDH; 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|HAMAP-Rule:MF_01621, ECO:0000313|EMBL:KRG32409.1}; KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963, ECO:0000256|HAMAP- KW Rule:MF_01621}; Lipid metabolism {ECO:0000256|HAMAP-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 318..496 FT /note="3-hydroxyacyl-CoA dehydrogenase NAD binding" FT /evidence="ECO:0000259|Pfam:PF02737" FT DOMAIN 498..593 FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal" FT /evidence="ECO:0000259|Pfam:PF00725" FT DOMAIN 629..712 FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal" FT /evidence="ECO:0000259|Pfam:PF00725" FT REGION 1..190 FT /note="Enoyl-CoA hydratase/isomerase" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01621" FT REGION 313..719 FT /note="3-hydroxyacyl-CoA dehydrogenase" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01621" FT ACT_SITE 452 FT /note="For 3-hydroxyacyl-CoA dehydrogenase activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01621" FT BINDING 298 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01621" FT BINDING 326 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01621" FT BINDING 345 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01621" FT BINDING 402..404 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01621" FT BINDING 409 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01621" FT BINDING 431 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01621" FT BINDING 455 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01621" FT BINDING 502 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01621" FT SITE 120 FT /note="Important for catalytic activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01621" FT SITE 140 FT /note="Important for catalytic activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01621" SQ SEQUENCE 719 AA; 78134 MW; 3E1E632EAE4C89D0 CRC64; MVYQGNRITV TMLEDGIANM QYNAENESVN KFDAETNKQF GEAVTALEKA DDVKGLIVTS GKGVFIAGAD ITEFVGSFKK PESEIKDWVV GINDAFNRFE DLPFPKVAAI NGAALGGGCE MTLVCEYRVM SDKAIIGLPE TQLGIFPGFG GTVRTTRVIG IDNALELIAT GTPKKPLDAL KLGLVDATVA ADDLQDAAID LVKKCISGEL DWKAKREEKL NPVKLNQLEQ AMAFNSAKGM IFAKANPKQY PAPALAIAAM EKHVNLPRDK AIEVEAAGFA KAAKTPQAES LVGLFLSDQL VKKLAKQHSK KAHEINEAAV LGAGIMGGGI AYQAASKGLP IIMKDIKSEQ LDLGMGEASK LLGKMVDRGK MTPAKMGETL SRIRPTLNYG DFAETDIVIE AVVENPNVKR AVLKEVEGLV KDDCILASNT STISITFLAE ALERPENFVG MHFFNPVHRM PLVEVIRGEK SSEEAIATTV ALASKMGKVP VVVNDCPGFL VNRVLFPYFG AFDLLLKQGA DFAHVDKVME KFGWPMGPAY LIDVVGLDTG VHGAEVMAEG FPDRMKPDYK GAIELLYENK RLGQKNGVGF YKYEMDKRGK PKKVADEATY ELLKTTTDSD KQTFEDQAII DRTMLAFCNE TVRCLEDNIV STPSEADMAM IMGVGFPPFR GGPCRYIDQM GLDNYLALCE KYAYLGKAYE APQKIRDMAA AGDTFYATA //