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Database: UniProt
Entry: A9BSN2_DELAS
LinkDB: A9BSN2_DELAS
Original site: A9BSN2_DELAS 
ID   A9BSN2_DELAS            Unreviewed;       705 AA.
AC   A9BSN2;
DT   15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT   15-JAN-2008, sequence version 1.
DT   24-JAN-2024, entry version 94.
DE   SubName: Full=3-hydroxyacyl-CoA dehydrogenase NAD-binding {ECO:0000313|EMBL:ABX34037.1};
GN   OrderedLocusNames=Daci_1393 {ECO:0000313|EMBL:ABX34037.1};
OS   Delftia acidovorans (strain DSM 14801 / SPH-1).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Delftia.
OX   NCBI_TaxID=398578 {ECO:0000313|EMBL:ABX34037.1, ECO:0000313|Proteomes:UP000000784};
RN   [1] {ECO:0000313|EMBL:ABX34037.1, ECO:0000313|Proteomes:UP000000784}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14801 / SPH-1 {ECO:0000313|Proteomes:UP000000784};
RX   PubMed=15240283; DOI=10.1128/AEM.70.7.4053-4063.2004;
RA   Schleheck D., Knepper T.P., Fischer K., Cook A.M.;
RT   "Mineralization of individual congeners of linear alkylbenzenesulfonate by
RT   defined pairs of heterotrophic bacteria.";
RL   Appl. Environ. Microbiol. 70:4053-4063(2004).
RN   [2] {ECO:0000313|Proteomes:UP000000784}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14801 / SPH-1 {ECO:0000313|Proteomes:UP000000784};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Lowry S., Clum A., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Schleheck D., Richardson P.;
RT   "Complete sequence of Delftia acidovorans DSM 14801 / SPH-1.";
RL   Submitted (NOV-2007) 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: 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}.
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DR   EMBL; CP000884; ABX34037.1; -; Genomic_DNA.
DR   RefSeq; WP_012203323.1; NC_010002.1.
DR   AlphaFoldDB; A9BSN2; -.
DR   STRING; 398578.Daci_1393; -.
DR   GeneID; 24117467; -.
DR   KEGG; dac:Daci_1393; -.
DR   eggNOG; COG1024; Bacteria.
DR   eggNOG; COG1250; Bacteria.
DR   HOGENOM; CLU_009834_16_3_4; -.
DR   OMA; DPLFWKP; -.
DR   UniPathway; UPA00659; -.
DR   Proteomes; UP000000784; Chromosome.
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:SF51; 3-HYDROXYACYL-COA DEHYDROGENASE-RELATED; 1.
DR   PANTHER; PTHR23309; 3-HYDROXYACYL-COA DEHYROGENASE; 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:UP000000784}.
FT   DOMAIN          301..477
FT                   /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF02737"
FT   DOMAIN          482..575
FT                   /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00725"
FT   DOMAIN          612..696
FT                   /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00725"
SQ   SEQUENCE   705 AA;  75091 MW;  E2C88C89230FC07C CRC64;
     MSEQAQASVV QTRLDGAVLV VSINNPPVNA LGQAVRAGLL AAVEQAESDA AVKAVLIVGE
     GKAFIAGADI REFGKPAMPP SLPEVLNRLE ASDKIVVAAI HGPALGGGLE VAMSAHYRLA
     LPAAKLGLPE VNLGLLPGAG GTQRAPRLMG VKAAADLMLS GKHLSAKAAL AAGLVDKLVD
     GTDATAAGLA YTNELLATNT APRRTRDIEI ADKAAALAEL DALAADTAKK SRGLFSPLKI
     VECVRAAVEL PFDEGIAKER ALFVECLNSP QRAGLIHAFF AERETAKIPE AKAAAPRHFA
     KIAVIGGGTM GAGITVSALD AGLTVTMIER DADSIARGQA NVEKVYNGLI AKGRMTEEAK
     AAVMARYTPS TSYDDIKDVD LVIEAVFEDL EVKKAVFKEL DRVCKPGAVL ATNTSYLDID
     AIAAATSRPQ DVIGLHFFSP ANIMKLLEIV VPAKVAPDVV TTAFELAKRM KKVPVRAGVC
     DGFIGNRILA VYKQAADYIM EDGASPYEID EAVRGFGYPM GPFQVTDLAG GDIGWATRKR
     RAATRDPKAR YVEVADRVCE RGWFGQKTGR GFYLYPHGAR VGQPDPEVLA IVDAERAKKG
     VTPRKFTPEE IMRRYMAAMV NEGAKVVEEG IALRPLDVDV TFLSGYGFPR FRGGPMKWAD
     MQGLDKVLAD IREFAKEDAL FWKPAPLLEK LVAEGRDFES LNKAA
//
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