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Database: UniProt
Entry: B8G2Y9_CHLAD
LinkDB: B8G2Y9_CHLAD
Original site: B8G2Y9_CHLAD 
ID   B8G2Y9_CHLAD            Unreviewed;       807 AA.
AC   B8G2Y9;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 82.
DE   SubName: Full=3-hydroxyacyl-CoA dehydrogenase NAD-binding {ECO:0000313|EMBL:ACL23293.1};
GN   OrderedLocusNames=Cagg_0347 {ECO:0000313|EMBL:ACL23293.1};
OS   Chloroflexus aggregans (strain MD-66 / DSM 9485).
OC   Bacteria; Chloroflexota; Chloroflexia; Chloroflexales; Chloroflexineae;
OC   Chloroflexaceae; Chloroflexus.
OX   NCBI_TaxID=326427 {ECO:0000313|EMBL:ACL23293.1, ECO:0000313|Proteomes:UP000002508};
RN   [1] {ECO:0000313|Proteomes:UP000002508}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MD-66 / DSM 9485 {ECO:0000313|Proteomes:UP000002508};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Pitluck S., Foster B., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Bryant D.A., Richardson P.;
RT   "Complete sequence of Chloroflexus aggregans DSM 9485.";
RL   Submitted (DEC-2008) 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};
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DR   EMBL; CP001337; ACL23293.1; -; Genomic_DNA.
DR   RefSeq; WP_012615659.1; NC_011831.1.
DR   AlphaFoldDB; B8G2Y9; -.
DR   STRING; 326427.Cagg_0347; -.
DR   KEGG; cag:Cagg_0347; -.
DR   eggNOG; COG1024; Bacteria.
DR   eggNOG; COG1250; Bacteria.
DR   HOGENOM; CLU_010448_0_0_0; -.
DR   OrthoDB; 9771883at2; -.
DR   UniPathway; UPA00659; -.
DR   Proteomes; UP000002508; Chromosome.
DR   GO; GO:0016020; C:membrane; 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; IPR045004; ECH_dom.
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; PF16113; ECH_2; 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   Membrane {ECO:0000256|SAM:Phobius}; NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          8..204
FT                   /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF02737"
FT   DOMAIN          208..307
FT                   /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00725"
FT   DOMAIN          508..639
FT                   /note="Enoyl-CoA hydratase/isomerase"
FT                   /evidence="ECO:0000259|Pfam:PF16113"
SQ   SEQUENCE   807 AA;  88540 MW;  7FFB881A492FB563 CRC64;
     MTYHIKRVGV IGAGTMGAAI AALVAGTGIP VLLLDVPPRS LTPDEEAKGL TLSHPQVRNR
     IVQQGFERMR KARPSNLYTE RSAELITLGN TEDDFHRLAE CDWIVEAIVE QIGPKQALMA
     RLEEVRKPTA IITTNTSGIP IRIIAEGRSE AFRRHFFGSH FFNPPRYLRL LEIIPGDDAD
     PTVVAAFRQF AEERLGKGVV ICKDRPNFIG NRIFVYAGQV LLNFALQHGY QVEEVDALTG
     PLIGRPNTAS FRLLDQVGID VMAYVAGNLY DAIPDDESRE VYRQNDLTQR MVAAGKLGKK
     VGQGFYKEMK RDGKREFWPI DLQTLEYIPP QGTASVDALI AAARKIKSLP ERLRFILSKA
     ETEHDRGAQL VAAAMYPMMA YAARRLPEIA DSVADVDNAM RWGFAHEQGP FQLWQAMGIA
     ETAARMRTFG ETLPAWVDEL IKAEGRFYGE IDGQPAAYNV ATGKLEPISR DPRAIDLAAL
     KAAGRELFGN DSASVIDLGD GVLCFELHSK ANTIGGPVIE TLIKALDELE QGPWVGMVIG
     NQGPRFSAGL DLNDVGAAVM AGAWDDIDEY AALVQQTFRR MRDSAKPVVS APFGQTLGGG
     VELSMHTAAS VAAAETYMGF VEFGVGVIPA WGGCTEMNRR IIATAARNGH DPLKAFQQVF
     ETIALAKVAT SAHEAKELGL LRPTDRIVFN PDYLIGEAKR EVLRLVADGY TPTISAKPCY
     ALGRDGLAAA RIAIYQMREA GFATPYDAVL AEKLAYVLCG GELSSPQWVD DVYMHSLERI
     TVIELLKDER TQARARHMLE HGKPLRN
//
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