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Database: UniProt
Entry: A0A369THW1_9RHOB
LinkDB: A0A369THW1_9RHOB
Original site: A0A369THW1_9RHOB 
ID   A0A369THW1_9RHOB        Unreviewed;       733 AA.
AC   A0A369THW1;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=3-hydroxyacyl-CoA dehydrogenase {ECO:0000313|EMBL:RDD64939.1};
GN   ORFNames=DU478_17195 {ECO:0000313|EMBL:RDD64939.1};
OS   Thalassococcus profundi.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Thalassococcus.
OX   NCBI_TaxID=2282382 {ECO:0000313|EMBL:RDD64939.1, ECO:0000313|Proteomes:UP000253977};
RN   [1] {ECO:0000313|EMBL:RDD64939.1, ECO:0000313|Proteomes:UP000253977}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WRAS1 {ECO:0000313|EMBL:RDD64939.1,
RC   ECO:0000313|Proteomes:UP000253977};
RA   Yu M.;
RT   "Thalassococcus profundi sp. nov., a marine bacterium isolated from deep
RT   seawater of Okinawa Trough.";
RL   Submitted (JUL-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:RDD64939.1}.
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DR   EMBL; QPMK01000016; RDD64939.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A369THW1; -.
DR   OrthoDB; 9771883at2; -.
DR   UniPathway; UPA00659; -.
DR   Proteomes; UP000253977; 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:UP000253977}.
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   733 AA;  78729 MW;  26BCCFC6A996846F CRC64;
     MTDFTMIKGD DGVAIITWDV PGKSMNVLSM QGLRDLDALM DEALADDAVK GIVITSGKDS
     FAGGMDLNVI AKMKSDAGDE PERGLFEGIM QMHAALRKIE LAGMDPKTLK GGKPVAAALP
     GTALGIGLEI PLATHRIFCS VNPKAKIGLP EIMVGIFPGA GGTTRMVRKL GAMAASPFLL
     EGKLSDPMKA KSAGIIDEVV ADPLEAAKEW VLNAKDADLV KPWDAKGYKM PGGAPYHPAG
     FMTFVGASAM VHGKTQGVYP AAKALLSAVY EGALVPFDTA LKIEARWFTN VLMNPSSGAM
     IRSLFINKEA LEKGAVRPAD VADQRVRKVG VLGAGMMGAG IALVSAQAGI DVVLLDQKQE
     AADKGKAYSA SYMDKGIQRK KATEESKEAL LGRIHATTDY AALRDCDLIV EAVFEDPRIK
     AEVTQNVEKV IPEDCIFATN TSTLPITDLA GASSRPEQFI GIHFFSPVEK MMLVEIIKGK
     ETGDRAVAKA LDFVRQIRKT PIVVNDARFF YANRCIIPYI NEGMRMVAEG VAPALVENAA
     RMVGMPLGPL QLVDETSIDL GAKIARATKA AMGDAYPDGA VDEVIFWMEG QERLGRKSNA
     GFYSYDDKGK RQGLWSGLGE KYAPLDDQPD LIEVQHRLLF AQVLEAVRAL EEGVLMDIRE
     GDVGAILGWG FAPWSGGPFS WLDIIGAPYA AERCDQLTEK FGDRFACPAL LREMADKGQS
     FYGRFGQDAD KAA
//
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