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Database: UniProt
Entry: A0A1H2DC04_9ACTN
LinkDB: A0A1H2DC04_9ACTN
Original site: A0A1H2DC04_9ACTN 
ID   A0A1H2DC04_9ACTN        Unreviewed;       714 AA.
AC   A0A1H2DC04;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=3-hydroxyacyl-CoA dehydrogenase / enoyl-CoA hydratase / 3-hydroxybutyryl-CoA epimerase {ECO:0000313|EMBL:SDT80022.1};
GN   ORFNames=SAMN04489716_9028 {ECO:0000313|EMBL:SDT80022.1};
OS   Actinoplanes derwentensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Actinoplanes.
OX   NCBI_TaxID=113562 {ECO:0000313|EMBL:SDT80022.1, ECO:0000313|Proteomes:UP000198688};
RN   [1] {ECO:0000313|EMBL:SDT80022.1, ECO:0000313|Proteomes:UP000198688}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 43941 {ECO:0000313|EMBL:SDT80022.1,
RC   ECO:0000313|Proteomes:UP000198688};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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};
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}.
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DR   EMBL; LT629758; SDT80022.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H2DC04; -.
DR   STRING; 113562.SAMN04489716_9028; -.
DR   OrthoDB; 3216872at2; -.
DR   UniPathway; UPA00659; -.
DR   Proteomes; UP000198688; Chromosome i.
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198688}.
FT   DOMAIN          316..494
FT                   /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF02737"
FT   DOMAIN          497..597
FT                   /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00725"
SQ   SEQUENCE   714 AA;  76537 MW;  12DDC4C95AFFDE0D CRC64;
     MSETIRYDRA DDGIVVLTLD DPSRGANTMN DAYVRSMEET VSRLEAERDE ITGVIITSAK
     KSWFAGGDLD QLGSVPADRG GDVFAMSTRV KGQLRRLETL GRPVVAALNG SALGGGLELA
     LATHRRIALS DPRLEIGLPE VTLGLLPAGG GVVRTVRLLG LATALTEVLL KGTRHKLAKA
     VQLGLIDEVV DTPEQLITAA REWIIQNPGA VQPWDTKGYR IPGGSPSTPS LAAMLPAFPA
     NLRKQLKNAP YPAPRNILSA AVEGAQVDVD TALVIETRYF VELVTGQVAK NMIKAFFFDL
     NEVSQRDIGE VPPITKVAVL GAGMMGAAIA YVSARAGLPT VLRDVTLEGA QRGKAYSEKL
     VGKDVSRGRI TPEKGEALLG LITATDQIAD LAGADLVIEA VFEDPALKHK VFAEIETVVA
     PHALLCSNTS TLPITALADG VSRQADFIGL HFFSPVDKMP LVEVIKGEKT SDLTVRRSLD
     VVRRLRKTPI VVNDSRGFFT SRVIGTFTNE GIALLAEGVA PASIEQASSQ AGYPAPVLQL
     MDELTLTLPR KIRDEYRAAA SAAGRERETH PADEVIDRMI DEFGRPGRSG GAGFYEYTDG
     KRTGLWPGLS AFARPDVAIP FEDLKERMLF IEAIETVKCL DEGVLTSVAE ANIGSILGIG
     YPGWTGGVLQ YINQYDGGLP GFAARARQLA DRYGDRFTPP PLLLAKAEAN ETFV
//
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