ID A0A2T8HUI2_9RHOB Unreviewed; 730 AA.
AC A0A2T8HUI2;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=3-hydroxyacyl-CoA dehydrogenase {ECO:0000313|EMBL:PVH29058.1};
GN ORFNames=DDE20_08505 {ECO:0000313|EMBL:PVH29058.1};
OS Pararhodobacter oceanensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Pararhodobacter.
OX NCBI_TaxID=2172121 {ECO:0000313|EMBL:PVH29058.1, ECO:0000313|Proteomes:UP000245911};
RN [1] {ECO:0000313|EMBL:PVH29058.1, ECO:0000313|Proteomes:UP000245911}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AM505 {ECO:0000313|EMBL:PVH29058.1,
RC ECO:0000313|Proteomes:UP000245911};
RA Wang X.-L., Du Z.-J.;
RT "Pararhodobacter oceanense sp. nov., isolated from marine intertidal
RT sediment.";
RL Submitted (APR-2018) 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:PVH29058.1}.
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DR EMBL; QDKM01000003; PVH29058.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T8HUI2; -.
DR OrthoDB; 9771883at2; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000245911; 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:UP000245911}.
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 730 AA; 77898 MW; 986943E33F6FDE76 CRC64;
MTELHYKVDA DGVAIITWDV PEKSMNVMSF EGLQELEDGI DKALADDAVK GVVITSAKPD
FAGGMDLNIL AKMREDAGDN PAKGLFDGVM SMHALLRKIE LAGMDRKTQK GGKPIAAALP
GTAMGIGLEI PLACHRIFAA DNPKARIGLP EIKVGIFPGA GGTTRLSWKL GAMAAAPLLL
EGKALAPAKA KAAGVIDEVV PADELLAKAK EWVLGASDAD LVKGWDKKGY KVPGGTPYHP
AGFPTFVGAS AMVHANTWGA YPAAKALLSA VYEGLQVPFD TALKVEARWF THVLMNPSSS
AMIRSLFVNK GALEKGANRP DVPDERVKKV GVLGAGMMGA GIAYVSAAAG IEVVLLDSSV
ESAEKGKAYS TGILDKAIKR GRSTEEKKAA LLGQITTTAD YADLEGCDLI IEAVFEDPKV
KADVTAKAEA VIPETAIFAS NTSTLPITSL AEASSRPEQF IGIHFFSPVD KMLLVEIIKG
AQTGERAVAK SLDYVRQIRK TPIVVNDARF FYANRCIIPY INEGMRMVAE GVAPPLVDNA
ARLLGFPVGP LQLVDETSLD LGAKIAKATK AAMGNDYPDD AVDEVVFWMV DEGRLGRKSN
AGFFDYDEKG KRQGYWSGLG DKFPRAEDQP ELDQVKHRLM MAQVLEAVRA LDEGVLEDIR
EGDVGAILGW GFAPWSGGPF SWLDIIGLKR AVEICDGLEA EFGPRFKATQ SMREMAASGA
TFYGQKVKAA
//
