ID A0A1M5SK96_9RHOB Unreviewed; 732 AA.
AC A0A1M5SK96;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=3-hydroxyacyl-CoA dehydrogenase / enoyl-CoA hydratase / 3-hydroxybutyryl-CoA epimerase {ECO:0000313|EMBL:SHH38678.1};
GN ORFNames=SAMN05444003_3006 {ECO:0000313|EMBL:SHH38678.1};
OS Cognatiyoonia sediminum.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Cognatiyoonia.
OX NCBI_TaxID=1508389 {ECO:0000313|EMBL:SHH38678.1, ECO:0000313|Proteomes:UP000184074};
RN [1] {ECO:0000313|EMBL:SHH38678.1, ECO:0000313|Proteomes:UP000184074}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 28715 {ECO:0000313|EMBL:SHH38678.1,
RC ECO:0000313|Proteomes:UP000184074};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) 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}.
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DR EMBL; FQXB01000006; SHH38678.1; -; Genomic_DNA.
DR RefSeq; WP_072902447.1; NZ_FQXB01000006.1.
DR AlphaFoldDB; A0A1M5SK96; -.
DR STRING; 1508389.SAMN05444003_3006; -.
DR OrthoDB; 9771883at2; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000184074; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000184074}.
FT DOMAIN 328..506
FT /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT /evidence="ECO:0000259|Pfam:PF02737"
FT DOMAIN 510..605
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
SQ SEQUENCE 732 AA; 78811 MW; B8D76B222AEF11B2 CRC64;
MTDFTMATDA DGVAVITWDT VGKSMNVMNQ QGFVDLNALV NEALVDDAVK GIVITSGKEG
SFAGGMDLNI IAKMKESAGE NPAAGLMDGL MQCHGVLRNI ERAGMDPKTN KGGKPIAAAL
PGTALGIGYE IPLSCHRIFA ADNPKAKIGL PEIMVGIFPG MGGTTRLVRK MGAMAASPFL
LEGKLSDPKK AKAAGLIDEV VPADELLSAA KAWVLSEPTI VKPWDEKGYK MPGGAPYHPA
GFMTYVGASA MINGRTKGVY PAAKALLSAA YEGALVPFDT AIKIEARWFT HVLMNPSSEA
MIRSLFINKE ALEKGANRPD VDDQKVKKVG VLGAGMMGAG ISLVSALAGI EVVLIDRDQD
AADKGKSYTA DYMDKGIKRK KATEEKKEAV LGLINATTDL EALKGCDLIV EAVFEDVGVK
ADMTKKVEAI VGEDCIFATN TSTLPITELA KASVRPEQFI GIHFFSPVDK MMLVEIIKGK
ETGDRAVAKS LDFVRQIRKT PIVVNDERFF YANRCIIPYI NEGIRMVKEG VEPALIENAA
KLVGMPLGPL QLTDETSIDL GVKIAKATKA AMSDDYPNEE VDQVLFWMFD EGRLGRKSNS
GFYAYDEKGK RQGLWEGLAD QYPVADEQPE LLEVQHRLLF AQVLEAVRAL EENVLEDIRE
GDVGAILGWG FAPWSGGPFS WLDIIGAPYA AERCDQLAAT HGERFATPNL LREMADKNVS
FYSIYGAGKA AA
//
