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Database: UniProt
Entry: A0A0G1KUA3_9BACT
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Original site: A0A0G1KUA3_9BACT 
ID   A0A0G1KUA3_9BACT        Unreviewed;       650 AA.
AC   A0A0G1KUA3;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   SubName: Full=3-hydroxyacyl-CoA dehydrogenase NAD-binding protein {ECO:0000313|EMBL:KKT59927.1};
GN   ORFNames=UW53_C0005G0010 {ECO:0000313|EMBL:KKT59927.1};
OS   Candidatus Giovannonibacteria bacterium GW2011_GWA1_44_25.
OC   Bacteria; Candidatus Giovannonibacteria.
OX   NCBI_TaxID=1618645 {ECO:0000313|EMBL:KKT59927.1, ECO:0000313|Proteomes:UP000034087};
RN   [1] {ECO:0000313|EMBL:KKT59927.1, ECO:0000313|Proteomes:UP000034087}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA   Wilkins M.J., Williams K.H., Banfield J.F.;
RT   "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT   radiation of phyla.";
RL   Nature 0:0-0(2015).
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:KKT59927.1}.
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DR   EMBL; LCIR01000005; KKT59927.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G1KUA3; -.
DR   UniPathway; UPA00659; -.
DR   Proteomes; UP000034087; 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; 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; IPR013328; 6PGD_dom2.
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; 1.
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}.
FT   DOMAIN          4..162
FT                   /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF02737"
FT   DOMAIN          301..355
FT                   /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00725"
SQ   SEQUENCE   650 AA;  72441 MW;  0E8CBC6AFD67256A CRC64;
     MKRVAVFGAG VMGSGVAAEL AKAKVGVMLF DSFPGALAKA KETLPAAIFQ TVKNYKFVYR
     SREAVTEVFE RIKFYKTTPE NVKNVASADA VIEAIKENAN LKIALYQELE RFLPPEAPMF
     TNTSTFQIAR LAAGLKHPER FMGLHFFNPV SAMPPVEAIL HKGNLRDNSL DIEKAAIDVA
     RLLGKKLFWA PDLPGFIVNR LLVRMVQASA KLGATADFRK IDKAFGTGAW FSDPVARLIV
     DEFLAAARDL IVKDKGHELL GMSEEKFKEN VDALMKLGTA MPKGPYEMIE LVDSGKDPEV
     RFEMGPYKLI DHVGVDVAAD CCRMLKLQES DRWEVPEILE KMTTEGKLGK KSPLGGFYQD
     RKSVKFEFAP DKSCARIGWS GKTLPLHLVK ELKEKFCLAK QVGAMCVILE INRARGADID
     EFLAAMLSEE AARYAIKTWH SAIHEAMDYP GTVIAAIKGS AFGGAYEWAL ACDYIIAEKS
     AKIGLVELKR GIKPGGGGTQ TLPRRAGLQK ALRMILRGAT LYELGEEVGM PWVDEAVDKI
     TEERLMELVA NADKIGKKKR EPIHYTLWDW ISEFTESWGA WKFWKGKPPE SFRLARQAIW
     KGNENSILLG IGNYEFNAVV AAFQTDDALR MIIEFLEERF KKLKRGGEDE
//
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