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Database: UniProt
Entry: D0LWW1_HALO1
LinkDB: D0LWW1_HALO1
Original site: D0LWW1_HALO1 
ID   D0LWW1_HALO1            Unreviewed;       726 AA.
AC   D0LWW1;
DT   15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT   15-DEC-2009, sequence version 1.
DT   24-JAN-2024, entry version 69.
DE   SubName: Full=3-hydroxyacyl-CoA dehydrogenase NAD-binding protein {ECO:0000313|EMBL:ACY14208.1};
GN   OrderedLocusNames=Hoch_1658 {ECO:0000313|EMBL:ACY14208.1};
OS   Haliangium ochraceum (strain DSM 14365 / JCM 11303 / SMP-2).
OC   Bacteria; Myxococcota; Polyangia; Haliangiales; Kofleriaceae; Haliangium.
OX   NCBI_TaxID=502025 {ECO:0000313|EMBL:ACY14208.1, ECO:0000313|Proteomes:UP000001880};
RN   [1] {ECO:0000313|EMBL:ACY14208.1, ECO:0000313|Proteomes:UP000001880}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14365 / CIP 107738 / JCM 11303 / AJ 13395 / SMP-2
RC   {ECO:0000313|Proteomes:UP000001880};
RX   PubMed=21304682; DOI=10.4056/sigs.69.1277;
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Ivanova N., Daum C., Lang E., Abt B., Kopitz M., Saunders E., Lapidus A.,
RA   Lucas S., Glavina Del Rio T., Nolan M., Tice H., Copeland A., Cheng J.F.,
RA   Chen F., Bruce D., Goodwin L., Pitluck S., Mavromatis K., Pati A.,
RA   Mikhailova N., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Detter J.C., Brettin T., Rohde M., Goker M., Bristow J.,
RA   Markowitz V., Eisen J.A., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Haliangium ochraceum type strain (SMP-2).";
RL   Stand. Genomic Sci. 2:96-106(2010).
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; CP001804; ACY14208.1; -; Genomic_DNA.
DR   RefSeq; WP_012826816.1; NC_013440.1.
DR   AlphaFoldDB; D0LWW1; -.
DR   STRING; 502025.Hoch_1658; -.
DR   KEGG; hoh:Hoch_1658; -.
DR   eggNOG; COG1024; Bacteria.
DR   eggNOG; COG1250; Bacteria.
DR   HOGENOM; CLU_009834_16_2_7; -.
DR   OMA; PFRYMDT; -.
DR   OrthoDB; 9771883at2; -.
DR   UniPathway; UPA00659; -.
DR   Proteomes; UP000001880; Chromosome.
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; 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:UP000001880}.
FT   DOMAIN          322..499
FT                   /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF02737"
FT   DOMAIN          503..599
FT                   /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00725"
SQ   SEQUENCE   726 AA;  76790 MW;  D0F8186FE46BC3A7 CRC64;
     MSSDAISVST DENGIAVLVI DRPDSSANYL SGELAMALLA TVERLAADED LRGVVLSSTK
     PGSFVHGSEL REFVGAYESG LGAAGAREIS RAFQHLTRRM ETCGKLFAAA LAGPALGSGL
     ELALACHHRV LADDPAAVLG LPEVCCGLIP GGGGTQRLPR LIGIERALPL LLSGRPVGPA
     EALALGLVHA LAPAGRVVDA ARAWMSEARE ATQPWDRRGF SLPGGNGAES PAVRTAFMVE
     TARVRAKTQG KLPAPLALLS SVYEGTITDF DTGLRIESNY FGQMFATPVA RNLMRTLFIN
     KPAVDALAYR PREVPLSQVR TLGVIGAGAM GAGIACAAAS AGIDVELIDQ SAELAEEGRV
     YAERQLATAV QRGKLGAGAA TAILARIAPS ADYTRLGRCD LAIEAVYENR DLKRSVIARA
     EAELTSTAVL ASSTSSLPIG GLARASRRPT QFLGMHFSAP AERMAMVEVI TSAHTSQESL
     CLALDFAAQL GKTPILVNDG PAFYTTRVFS TFIDEGTCML SEGVAPALIE NAARRAGMPV
     GPLAEFDEVS LELSAKIIAQ ARADGLSAER TRADAAPVIA TMMELGRRGR RYGAGFYEYP
     EAGKKYLWPG LGEHFPVSAE QPSVDELETR FLTIQALEAV RCVEDGVIAS AAEADLGAVL
     GFGYPTWTGG TLSYVDMRGH ARFIADCERF TERYGPRYEP SAWLRAHAET GQLFHPKTPA
     PEALIL
//
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