ID A0A068QV47_9GAMM Unreviewed; 728 AA.
AC A0A068QV47;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 56.
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:CDG18882.1};
GN ORFNames=XDD1_3188 {ECO:0000313|EMBL:CDG18882.1};
OS Xenorhabdus doucetiae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Xenorhabdus.
OX NCBI_TaxID=351671 {ECO:0000313|EMBL:CDG18882.1, ECO:0000313|Proteomes:UP000032721};
RN [1] {ECO:0000313|EMBL:CDG18882.1, ECO:0000313|Proteomes:UP000032721}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FRM16 / DSM 17909 {ECO:0000313|Proteomes:UP000032721};
RA Genoscope - CEA;
RL Submitted (JUL-2013) 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}.
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DR EMBL; FO704550; CDG18882.1; -; Genomic_DNA.
DR RefSeq; WP_045972331.1; NZ_VNHN01000049.1.
DR AlphaFoldDB; A0A068QV47; -.
DR STRING; 351671.XDD1_3188; -.
DR KEGG; xdo:XDD1_3188; -.
DR HOGENOM; CLU_009834_16_3_6; -.
DR OrthoDB; 5389341at2; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000032721; 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; 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 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.
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}; 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 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..691
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..728
FT /note="3-hydroxyacyl-CoA dehydrogenase"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01621"
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 728 AA; 78879 MW; CF1CA1FAD76A5966 CRC64;
MLYLSETIQV KWLKDGIAEL IFNAPAAINK LDTKTVTSLD QAVAALEQAI ELKGLLIRSE
KPAFIVGADI TEFLSLFNAP AEKLHELLDL ANNIFNRIED LPVPTLSAIN GYALGGGCEL
VLSTDFRVAS PDLRIGLPET KLGIMPGFGG SVRLPRLIGT DNALEIISAG KDIGAEEALK
NGLVDAVVSA EKLRDSAVSV LEQAIRGDLD WKAARQPKLM PLNLNEIERT MSFTVAKGLV
MKVAGSHYPA PITAVKTIEK AAILGRDEAL KLESASFVSL AHTPVAHALV GIFLNDQYVK
GLAKKHLQAV TTPEHAAVLG AGIMGGGIAY QSARKGIPVL MKDINQKALD LGVNEAAKLL
NKQFERGRLD AMKMAKILAS IQPTLNYAGI EQSQIVVEAV VENPKIKTAV LAEAESYISD
DCILASNTST IPITELAKSL KRPENFCGMH FFNPVHRMPL VEIIRGEKTS DKTISSVVAY
ASKMGKTPIV VNDCPGFFVN RVLFPYLAGF GMLLRDGGDF RQIDKIMEKE FGWPMGPAYL
IDVVGIDTAH HAQAVMAQGF PDRMSRDYRD AIDVLFENQR YGQKNGVGFY QYVQDKKGKP
KKAQDETTDQ LLASISKPKQ AFSGEEIIAR TMIPMINEVV RCLEEGVIAS PAEADMALVY
GLGFPPFHGG VFRYLDTMGT AAYVKLAESY AHLGALYHVP AGLKAKSESN ESYYPAPAEL
AVNPGEKA
//
