ID Q5LVD0_RUEPO Unreviewed; 698 AA.
AC Q5LVD0;
DT 01-FEB-2005, integrated into UniProtKB/TrEMBL.
DT 01-FEB-2005, sequence version 1.
DT 27-MAR-2024, entry version 125.
DE SubName: Full=Enoyl-CoA hydratase/isomerase/3-hydroxyacyl-CoA dehydrogenase {ECO:0000313|EMBL:AAV94077.1};
GN OrderedLocusNames=SPO0772 {ECO:0000313|EMBL:AAV94077.1};
OS Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3) (Silicibacter
OS pomeroyi).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Ruegeria.
OX NCBI_TaxID=246200 {ECO:0000313|EMBL:AAV94077.1, ECO:0000313|Proteomes:UP000001023};
RN [1] {ECO:0000313|EMBL:AAV94077.1, ECO:0000313|Proteomes:UP000001023}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700808 / DSM 15171 / DSS-3
RC {ECO:0000313|Proteomes:UP000001023};
RX PubMed=15602564; DOI=10.1038/nature03170;
RA Moran M.A., Buchan A., Gonzalez J.M., Heidelberg J.F., Whitman W.B.,
RA Kiene R.P., Henriksen J.R., King G.M., Belas R., Fuqua C., Brinkac L.,
RA Lewis M., Johri S., Weaver B., Pai G., Eisen J.A., Rahe E., Sheldon W.M.,
RA Ye W., Miller T.R., Carlton J., Rasko D.A., Paulsen I.T., Ren Q.,
RA Daugherty S.C., Deboy R.T., Dodson R.J., Durkin A.S., Madupu R.,
RA Nelson W.C., Sullivan S.A., Rosovitz M.J., Haft D.H., Selengut J., Ward N.;
RT "Genome sequence of Silicibacter pomeroyi reveals adaptations to the marine
RT environment.";
RL Nature 432:910-913(2004).
RN [2] {ECO:0000313|EMBL:AAV94077.1, ECO:0000313|Proteomes:UP000001023}
RP GENOME REANNOTATION.
RC STRAIN=ATCC 700808 / DSM 15171 / DSS-3
RC {ECO:0000313|Proteomes:UP000001023};
RX PubMed=25780504; DOI=10.1186/1944-3277-9-11;
RA Rivers A.R., Smith C.B., Moran M.A.;
RT "An updated genome annotation for the model marine bacterium Ruegeria
RT pomeroyi DSS-3.";
RL Stand. Genomic Sci. 9:11-11(2014).
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: Belongs to the enoyl-CoA hydratase/isomerase family.
CC {ECO:0000256|RuleBase:RU003707}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the enoyl-CoA
CC hydratase/isomerase family. {ECO:0000256|ARBA:ARBA00008750}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000031; AAV94077.1; -; Genomic_DNA.
DR RefSeq; WP_011046521.1; NC_003911.12.
DR AlphaFoldDB; Q5LVD0; -.
DR STRING; 246200.SPO0772; -.
DR PaxDb; 246200-SPO0772; -.
DR KEGG; sil:SPO0772; -.
DR eggNOG; COG1024; Bacteria.
DR eggNOG; COG1250; Bacteria.
DR HOGENOM; CLU_009834_16_3_5; -.
DR OrthoDB; 9771883at2; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000001023; Chromosome.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-KW.
DR GO; GO:0003857; F:3-hydroxyacyl-CoA dehydrogenase activity; IEA:UniProtKB-EC.
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; IPR018376; Enoyl-CoA_hyd/isom_CS.
DR InterPro; IPR001753; Enoyl-CoA_hydra/iso.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR23309; 3-HYDROXYACYL-COA DEHYROGENASE; 1.
DR PANTHER; PTHR23309:SF9; PEROXISOMAL BIFUNCTIONAL ENZYME; 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; PS00166; ENOYL_COA_HYDRATASE; 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 NAD {ECO:0000256|ARBA:ARBA00023027};
KW Peroxisome {ECO:0000256|ARBA:ARBA00023140};
KW Reference proteome {ECO:0000313|Proteomes:UP000001023}.
FT DOMAIN 292..468
FT /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT /evidence="ECO:0000259|Pfam:PF02737"
FT DOMAIN 473..567
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
FT DOMAIN 603..688
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
SQ SEQUENCE 698 AA; 74472 MW; 823A9C465A991197 CRC64;
MPEAIGYERV GDIVILAADN PPVNALGHAV RQGLAVGLDR AEAEGARGVL IYGTGRTFFA
GADIREFGKP PKEPHLPELC NRIEASPLLV VSALHGTALG GGLEVALATH YRIAVPQAKV
GLPEVHLGIL PGAGGTQRLP RVAGVEAALD MITTGRHVRA DEALRLGVID RVAEGEPREI
GLSYLRELLD EGAPRRPVGE MPAPAPVDFD AIYAAVLRKG RGQLSPATAV RAVQAACEAE
SFAAGLKRER ELFMELMNSD QREGLIHAFF ADRAVGKLPE LEGVAPRPLA AIGVIGGGTM
GAGIATAALL SGLSVTMLEM TPEAAEAAKG RIEGNLSGAL KRGKLTAQQF DNLTTKALTL
AIDYDALADA DLVIEAVFED MEVKKQVFTK LDAVCKPGAV LASNTSYLDI NQIAAVTSRP
QDVLGLHFFS PAHVMKLLEV VIADQTAPDV AATGFALGKR LGKVSVRAGV CDGFIGNRIL
SVYRTCADHM ILDGASPYQI DEALEEFGFA MGPFAVADLA GLDIGWAVRK RKRAEGLDPR
ARDSAYADKL CEAGHFGQKT GKGYYDYAAG AKARVPNPEV LPLIEAERAQ QGITPRAFSK
DEIVRRYMAA MVNEAAKVVG EGIARRPLDV DVTLLYGYGF PRYRGGPLKW ADMQGLPELL
ADIKRWAAED AYFWQPAPLL EQLVAEGRTF DDLNKEAV
//
