ID A0A2N5EI55_9GAMM Unreviewed; 729 AA.
AC A0A2N5EI55;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
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 ORFNames=CYR34_19675 {ECO:0000313|EMBL:PLR44208.1};
OS Chimaeribacter arupi.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Chimaeribacter.
OX NCBI_TaxID=2060066 {ECO:0000313|EMBL:PLR44208.1, ECO:0000313|Proteomes:UP000234626};
RN [1] {ECO:0000313|EMBL:PLR44208.1, ECO:0000313|Proteomes:UP000234626}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2016Iso1 {ECO:0000313|EMBL:PLR44208.1,
RC ECO:0000313|Proteomes:UP000234626};
RA Rossi A., Fisher M.;
RT "Characterization of six clinical isolates of Enterochimera gen. nov., a
RT novel genus of the Yersiniaciae family and the three species Enterochimera
RT arupensis sp. nov., Enterochimera coloradensis sp. nov, and Enterochimera
RT californica sp. nov.";
RL Submitted (DEC-2017) 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: 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:PLR44208.1}.
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DR EMBL; PJZK01000028; PLR44208.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N5EI55; -.
DR OrthoDB; 5389341at2; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000234626; 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: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; 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 {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}; Reference proteome {ECO:0000313|Proteomes:UP000234626}.
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 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 586..605
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; 78597 MW; 98FB4EED9BE1C1FE CRC64;
MLYQGDTLHL HWLENGIAEL VFDAPGSVNK LDTQTVASLG EAVTALENQP DLKGVLLRSN
KAAFIVGADI TEFLSLFDAP PEKLTQWLGF ANQIFNRLED LPVPTISAIT GYALGGGCEC
VLATDFRIAS PETRIGLPET KLGIMPGFGG SVRLPRLLGA DSAMEIITAG KDVSAAEALK
LGLVDAVVAQ EKLVAAALQM LNAAIDGRLD WRAARQPKLL PLKLSALEAA MSFNVAKGLV
LQQAGKHYPA PMAAVTTIEA AAGMGRDEAL KRETASFVPL AGSDQARALV GIFLNDQFVK
GQAKKFAAQA TSPAQAAVLG AGIMGGGIAY QSALKGVPVL MKDISEKSLT LGMNEAGKLL
DKQRERGKID GLKMAQTLAT IQPTLDYAGI GRAQVVVEAV VENPKVKAAV LAEAEALLDE
QAVLASNTST IPISTLARSL KRPENFCGMH FFNPVHRMPL VEVVRGEKTS DRTLATVVAY
ALRMGKTPIV VNDCPGFFIN RVLFPYFSGF SLLMRDGADF RQIDKVMEKQ FGWPMGPAYL
LDVVGIDTAY HAQAVMAQGF PDRMAKSYRD AVDVMFDQQR FGQKNGTGFY RYSEDSKGKP
RKQPDEAVDR LLAEIRPQAH EFSADEIIAR MMVPMINEVV RCLEENIVAS PAEADLALVY
GIGFPPFHGG ALRYLDTLGS RRYVELADRY AHLGALYQVP DGLRAKAESN ARYYPDATPL
AEINTGTPA
//
