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Database: UniProt
Entry: E7REV3_9BACL
LinkDB: E7REV3_9BACL
Original site: E7REV3_9BACL 
ID   E7REV3_9BACL            Unreviewed;       794 AA.
AC   E7REV3;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   24-JAN-2024, entry version 53.
DE   SubName: Full=3-hydroxyacyl-CoA dehydrogenase/enoyl-CoA hydratase/isomerase family protein {ECO:0000313|EMBL:EGA90489.1};
GN   ORFNames=GPDM_04964 {ECO:0000313|EMBL:EGA90489.1};
OS   Planococcus donghaensis MPA1U2.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Planococcus.
OX   NCBI_TaxID=933115 {ECO:0000313|EMBL:EGA90489.1, ECO:0000313|Proteomes:UP000003052};
RN   [1] {ECO:0000313|EMBL:EGA90489.1, ECO:0000313|Proteomes:UP000003052}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MPA1U2 {ECO:0000313|EMBL:EGA90489.1,
RC   ECO:0000313|Proteomes:UP000003052};
RX   PubMed=21994932; DOI=10.1128/JB.05983-11;
RA   Pearson M.D., Noller H.F.;
RT   "The Draft Genome of Planococcus donghaensis MPA1U2 Reveals Nonsporulation
RT   Pathways Controlled by a Conserved Spo0A Regulon.";
RL   J. Bacteriol. 193:6106-6106(2011).
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   -!- 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:EGA90489.1}.
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DR   EMBL; AEPB01000017; EGA90489.1; -; Genomic_DNA.
DR   RefSeq; WP_008429519.1; NZ_AEPB01000017.1.
DR   AlphaFoldDB; E7REV3; -.
DR   eggNOG; COG1024; Bacteria.
DR   eggNOG; COG1250; Bacteria.
DR   OrthoDB; 9771883at2; -.
DR   UniPathway; UPA00659; -.
DR   Proteomes; UP000003052; Unassembled WGS sequence.
DR   GO; GO:0003857; F:3-hydroxyacyl-CoA dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016853; F:isomerase 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; PTHR48075; 3-HYDROXYACYL-COA DEHYDROGENASE FAMILY PROTEIN; 1.
DR   PANTHER; PTHR48075:SF7; 3-HYDROXYACYL-COA DEHYDROGENASE-RELATED; 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   4: Predicted;
KW   Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW   Isomerase {ECO:0000313|EMBL:EGA90489.1};
KW   Lipid degradation {ECO:0000256|ARBA:ARBA00022963};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW   NAD {ECO:0000256|ARBA:ARBA00023027}.
FT   DOMAIN          7..205
FT                   /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF02737"
FT   DOMAIN          208..305
FT                   /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00725"
SQ   SEQUENCE   794 AA;  87330 MW;  0C85A49FA8562EE8 CRC64;
     MAYQIRKAAV LGSGVMGSGI AAHLANIGIP VMLLDIVPRE LSKEEQAKGL TLEDKVVRNR
     MATGSIQKLL KQKPAPLTAK KNLQLITPGN LEDDLEKLKD VDWIIEVIVE NLDIKKSLYE
     KIDGVRKEGT IISSNTSGIS INAMVEGRSE DFGKHFLGTH FFNPPRYLKL LEIIPAKTTA
     PEVLEFMSTF GEDQLGKGVV VAKDTPNFIA NRIGTYGLLV TLREMMARNY SIGEVDSVTG
     PLIGRPKSAT FRTLDVVGLD TFMHVSKNVY DQTSGEEQKV FDAPEFMKKM VENGWLGAKS
     GQGFFLKKDK EILELDPETL EYRPAGKLKT PSQEMAKQQK GLAAKMKKLV YAEDRTGELL
     WSILSPTLRY SAELNGEIAD DIVAIDNAMK WGFGWQQGPF ETWDAIGVKK SVEKMTQEGH
     AVPAFVQALI DSGNENFYKE QDGDLHFFDG TTYQPVPANE KVIDLKRYKK KHGVIKSNSG
     ASLIDLGDGI ALLEFHSRSN AIGLDIMQMI NFAVDEVDKN YKGLVIGNQG KNFCVGANLG
     MILMEAQDDN IFELDFTIKT FQNAMMKLKY SNKPVVAAPF GMSLGGGAEV TLPAAHIQAS
     METYMGLVEV GVGLIPGGGG NKELYMKQLK GLPNGVTIDY LNIATKVFES IAMAKVSTSA
     EEARENNFLN FVDGISVNSD HLLYDAKQAA LSLYENGYQA PLREKVPVPG EPGYATLLLG
     AEGMFISGYI SEHDLKIAKK LAFVLAGGKV PYGTKVDEQY LLDLERQAFL SLVAEPKTQQ
     RMQHMLVKGK PLRN
//
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