ID A3X8D7_9RHOB Unreviewed; 734 AA.
AC A3X8D7;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 88.
DE SubName: Full=Fatty oxidation complex, alpha subunit {ECO:0000313|EMBL:EAQ45915.1};
GN ORFNames=MED193_05969 {ECO:0000313|EMBL:EAQ45915.1};
OS Roseobacter sp. MED193.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseobacter.
OX NCBI_TaxID=314262 {ECO:0000313|EMBL:EAQ45915.1, ECO:0000313|Proteomes:UP000005943};
RN [1] {ECO:0000313|EMBL:EAQ45915.1, ECO:0000313|Proteomes:UP000005943}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MED193 {ECO:0000313|EMBL:EAQ45915.1,
RC ECO:0000313|Proteomes:UP000005943};
RA Pinhassi J., Pedros-Alio C., Ferriera S., Johnson J., Kravitz S.,
RA Halpern A., Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R.,
RA Venter J.C.;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
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};
CC -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC {ECO:0000256|ARBA:ARBA00005005}.
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:EAQ45915.1}.
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DR EMBL; AANB01000003; EAQ45915.1; -; Genomic_DNA.
DR RefSeq; WP_009808716.1; NZ_CH902583.1.
DR AlphaFoldDB; A3X8D7; -.
DR STRING; 314262.MED193_05969; -.
DR eggNOG; COG1024; Bacteria.
DR eggNOG; COG1250; Bacteria.
DR HOGENOM; CLU_009834_15_2_5; -.
DR OrthoDB; 9771883at2; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000005943; Unassembled WGS sequence.
DR GO; GO:0003857; F:3-hydroxyacyl-CoA dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
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 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; 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; 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.
PE 3: Inferred from homology;
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW NAD {ECO:0000256|ARBA:ARBA00023027}.
FT DOMAIN 329..507
FT /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT /evidence="ECO:0000259|Pfam:PF02737"
FT DOMAIN 511..606
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
SQ SEQUENCE 734 AA; 78695 MW; 85D14A592790CE58 CRC64;
MSEFTLSKDA DGVATITWDV PGKTMNVMSF DGLSQLEACI DQALADDEIK GVVITSGKEG
SFAGGMDLNL LAVMKEEAGD DPARGVFEGT MKMHALLRKI ELAGMDLKTK KGGKPIATAL
PGTAAGIGME LPLSTHRIFA AENPKAKYGL PEIMVGIFPG AGGTTRMVRK VGAIAAAPLL
LEGKMLDVKK AKGAGYVDEI AADPVAAAKE WVLNASGADL VKPWDAKGYK MPGGAPYHPA
GFMNFVGASA MVHGKTQGAF PAAKALLSAV YEGALVDFDT ALKIEARWFT SVLMNPSSGA
MIRSLFINKE ALEKGAVRPK DIPDQRVQKL GVLGAGMMGA GIALVSAQAG MEVVLIDRDQ
EAADKGKAYT ESYLDKGMKR GKVTQDKKDA MLARITATPD LDALKGCDLI IEAVFEDPAV
KAEMTKKVEA VIPEDCIFAS NTSTLPITGL AEASSRPEQF IGIHFFSPVE KMFLVEIIKG
KETGPRAVAK ALDYVRQIKK TPIVVNDARF FYANRCIIPY VNEGARMITE GVSPVLIDNA
ARQLGFPVGP IQLTDETSID LGAKIARATK AAMGNEYPDS PADDMIFWME DLGRLGRKSN
AGFFDYDDKG KRTGYWKGMQ DKYPLAEDQP DLIEVQERLM FAQVLEAVRA LEEGVLEDIR
EGDVGAVLAW GFAPWSGGPL SWLDIIGTPY AAERCDQLTA AYGERFACPD LLRDMAAKGQ
TFYGRFNPDA ASAA
//
