ID A0A1Q7W6T7_9ACTN Unreviewed; 724 AA.
AC A0A1Q7W6T7;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=3-hydroxyacyl-CoA dehydrogenase {ECO:0000313|EMBL:OLE26439.1};
GN ORFNames=AUG49_08130 {ECO:0000313|EMBL:OLE26439.1};
OS Catenulispora sp. 13_1_20CM_3_70_7.
OC Bacteria; Actinomycetota; Actinomycetes; Catenulisporales;
OC Catenulisporaceae; Catenulispora.
OX NCBI_TaxID=1805055 {ECO:0000313|EMBL:OLE26439.1, ECO:0000313|Proteomes:UP000186605};
RN [1] {ECO:0000313|EMBL:OLE26439.1, ECO:0000313|Proteomes:UP000186605}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27843720;
RA Butterfield C.N., Li Z., Andeer P.F., Spaulding S., Thomas B.C., Singh A.,
RA Hettich R.L., Suttle K.B., Probst A.J., Tringe S.G., Northen T., Pan C.,
RA Banfield J.F.;
RT "Proteogenomic analyses indicate bacterial methylotrophy and archaeal
RT heterotrophy are prevalent below the grass root zone.";
RL PeerJ 4:E2687-E2687(2016).
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:OLE26439.1}.
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DR EMBL; MNJN01000125; OLE26439.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q7W6T7; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000186605; 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}.
FT DOMAIN 328..506
FT /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT /evidence="ECO:0000259|Pfam:PF02737"
FT DOMAIN 509..606
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
SQ SEQUENCE 724 AA; 77155 MW; B5555D5B08F43047 CRC64;
MSEQNHIRWE RDSDSVVVLT MDAPGQSANT MNRAFVEALG PVLDRLEAEK EQIAGVVVTS
AKKTFFAGGD LNELIRARPE DAAEVMARNV QIKALLRRLE TLGRPVAAAI NGAALGGGLE
IALACHHRIA LDAKGSEIGL PEVTLGLLPG AGGVVRSVRL LGIADALLKV LLQGQRYEPR
AAREVGLVHE VANTPEELLA TAKAWVLANP EAAQPWDAPG YKIPGGDPKN PKFAANLPAF
PANLRKQLKG ANYPAPRNIL AAAVEGARLD FDNAMTVEAR YFVELVCAGP KSGGQVAKNM
TQAFFFDMQK VTNGASRPSG FEPWRATKVA VLGAGMMGAG IAYVCARGGI EVVLKDVSVE
AAEKGKAYSA GLLDKAVARG KMTREAADEV LARIHPTATA RDAAGADLVI EAVFESPELK
GKVFAEIQDV VAPDALLGSN TSTLPITGLA AAVRRPADFI GLHFFSPVDK MPLLEIIAGS
QTSDAAVAKA FDLAKQIRKT PVIVNDSRGF FTSRVIGRFL DEAVAMVGEG LDSNSIEQAG
SQAGYPAPPL RLMDELTLTL PQKIREEARA AAGPDWVEHG SEAVINRMVD DFGRGGRSSG
AGFYEYVDGE RAGLWPGLAE HFGKPGHRIP FEDMKERMLF AEALDSVRCL DEGVLRSVAE
ANIGSILGIG FPAWTGGVIQ YINGYDGGVT GFVARAKELR EKYGERFEVP ESLALKAERG
ERIE
//
