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Database: UniProt
Entry: A0A0A1VKU4_9BURK
LinkDB: A0A0A1VKU4_9BURK
Original site: A0A0A1VKU4_9BURK 
ID   A0A0A1VKU4_9BURK        Unreviewed;       706 AA.
AC   A0A0A1VKU4;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   24-JAN-2024, entry version 42.
DE   SubName: Full=3-hydroxyacyl-CoA dehydrogenase {ECO:0000313|EMBL:GAD24335.1};
GN   ORFNames=AVS7_04095 {ECO:0000313|EMBL:GAD24335.1};
OS   Acidovorax sp. MR-S7.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Acidovorax.
OX   NCBI_TaxID=1268622 {ECO:0000313|EMBL:GAD24335.1};
RN   [1] {ECO:0000313|EMBL:GAD24335.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MR-S7 {ECO:0000313|EMBL:GAD24335.1};
RX   DOI=10.1128/genomeA.00412-13;
RA   Miura T., Kusada H., Kamagata Y., Hanada S., Kimura N.;
RT   "Genome Sequence of the Multiple-beta-Lactam-Antibiotic-Resistant Bacterium
RT   Acidovorax sp. Strain MR-S7.";
RL   Genome Announc. 1:e00412-13(2013).
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; DF238983; GAD24335.1; -; Genomic_DNA.
DR   RefSeq; WP_020229836.1; NZ_DF238983.1.
DR   AlphaFoldDB; A0A0A1VKU4; -.
DR   STRING; 1268622.AVS7_04095; -.
DR   eggNOG; COG1250; Bacteria.
DR   OrthoDB; 5287258at2; -.
DR   UniPathway; UPA00659; -.
DR   Proteomes; UP000030646; Unassembled WGS sequence.
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:UP000030646}.
FT   DOMAIN          315..490
FT                   /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF02737"
FT   DOMAIN          493..590
FT                   /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00725"
SQ   SEQUENCE   706 AA;  74647 MW;  1AC1EDC407308DC4 CRC64;
     MTDQFPLTLQ EGGIALIRLD AQPGEAGAVC PPQLEALVAA LQTAAERADV QGVLLHASGP
     SWLPEAGAQA WLDLCRAGDA HAIAAVLQRR SGLLRAVERL PNPIAIVIEG ACMDLCLEFA
     LACHARWAVP GARLGLPLVK RGLPPSAGAT QRLPRLAGIP AVLNGLLAGD TWEADAARQM
     GLLSGVQPLA QALQDARAWL LAHPQAQAPW DAKGYRLPGG AGAMAAHAGR SFTDNIARLR
     KPSDTQPAPL ALLSAVYEGT QLPIDAALKV EAQCAAQALA EPATANQIRS LWLHQAQARQ
     LVRRPADVPE QPVRKLGVLG SGLMGAGIAQ VAAAAGIDVV MVDTSAERAQ AAHGKIAAAL
     ARGHGDRAAA IAQRIEPTAD LQRLHGCEFV IEAVFEDRAV KADLMARAAP VLADRPVHFV
     WASNTSTLPI GGLASAWAAP EQVIGMHFFS PVPRMPLLEI ILGARTNPAT VARTLDLAAR
     LGKTPILVND SSGFYTSRIF CAYIDEGMAM LAEGVNPALI ENAARQAGFA TAPLAVTDEV
     SLDLQALVIG QARKDGLEEK FLRTLAQPAV ERMNQLQRLG RKSGGGFYDY PKSGKHLWPG
     LAQQFPQSGE QPDLDTVMGR MLCIEAMESA RCLEEGVLTS AADGDLGALL GLGFPAWTGG
     TFSYIDTVGC AAFVQRCDVL ADRFGERFRP SAWLRDRAAQ GLRFHP
//
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