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
//