ID A0A1E4LM09_9BURK Unreviewed; 282 AA. AC A0A1E4LM09; DT 18-JAN-2017, integrated into UniProtKB/TrEMBL. DT 18-JAN-2017, sequence version 1. DT 14-DEC-2022, entry version 17. DE SubName: Full=3-hydroxybutyryl-CoA dehydrogenase {ECO:0000313|EMBL:ODU57133.1}; GN ORFNames=ABT02_18345 {ECO:0000313|EMBL:ODU57133.1}; OS Comamonadaceae bacterium SCN 68-20. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Comamonadaceae. OX NCBI_TaxID=1660161 {ECO:0000313|EMBL:ODU57133.1, ECO:0000313|Proteomes:UP000095151}; RN [1] {ECO:0000313|EMBL:ODU57133.1, ECO:0000313|Proteomes:UP000095151} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=26031303; DOI=10.1111/1462-2920.12936; RA Kantor R.S., van Zyl A.W., van Hille R.P., Thomas B.C., Harrison S.T., RA Banfield J.F.; RT "Bioreactor microbial ecosystems for thiocyanate and cyanide degradation RT unravelled with genome-resolved metagenomics."; RL Environ. Microbiol. 17:4929-4941(2015). CC -!- SIMILARITY: Belongs to the 3-hydroxyacyl-CoA dehydrogenase family. CC {ECO:0000256|ARBA:ARBA00009463}. 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:ODU57133.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; MEFU01000065; ODU57133.1; -; Genomic_DNA. DR AlphaFoldDB; A0A1E4LM09; -. DR STRING; 1660161.ABT02_18345; -. DR EnsemblBacteria; ODU57133; ODU57133; ABT02_18345. DR Proteomes; UP000095151; Unassembled WGS sequence. DR GO; GO:0070403; F:NAD+ binding; IEA:InterPro. DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro. DR GO; GO:0044248; P:cellular catabolic process; IEA:UniProt. DR GO; GO:0006631; P:fatty acid metabolic process; IEA:InterPro. DR GO; GO:1901575; P:organic substance catabolic process; IEA:UniProt. DR Gene3D; 1.10.1040.10; -; 1. DR InterPro; IPR022694; 3-OHacyl-CoA_DH. DR InterPro; IPR006180; 3-OHacyl-CoA_DH_CS. 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; IPR036291; NAD(P)-bd_dom_sf. DR Pfam; PF00725; 3HCDH; 1. DR Pfam; PF02737; 3HCDH_N; 1. DR PIRSF; PIRSF000105; HCDH; 1. DR SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1. DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1. DR PROSITE; PS00067; 3HCDH; 1. PE 3: Inferred from homology; KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|PIRSR:PIRSR000105-2}. FT DOMAIN 5..183 FT /note="3HCDH_N" FT /evidence="ECO:0000259|Pfam:PF02737" FT DOMAIN 186..282 FT /note="3HCDH" FT /evidence="ECO:0000259|Pfam:PF00725" FT BINDING 10..15 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000105-2" FT BINDING 33 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000105-2" FT BINDING 49 FT /ligand="CoA" FT /ligand_id="ChEBI:CHEBI:57287" FT /evidence="ECO:0000256|PIRSR:PIRSR000105-3" FT BINDING 56 FT /ligand="CoA" FT /ligand_id="ChEBI:CHEBI:57287" FT /evidence="ECO:0000256|PIRSR:PIRSR000105-3" FT BINDING 92 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000105-2" FT BINDING 97 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000105-2" FT BINDING 119 FT /ligand="CoA" FT /ligand_id="ChEBI:CHEBI:57287" FT /evidence="ECO:0000256|PIRSR:PIRSR000105-3" FT BINDING 119 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000105-2" FT BINDING 143 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000105-2" FT BINDING 274 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000105-2" FT SITE 140 FT /note="Important for catalytic activity" FT /evidence="ECO:0000256|PIRSR:PIRSR000105-1" SQ SEQUENCE 282 AA; 29667 MW; 75450D6F7207F32E CRC64; MTIQTVGIIG AGTMGNGIAQ ACAVSGINVV MVDISDAAVQ KGIATVAGSL DRLIKKEKIT AADKDAALAR IKASTSYDDL KAAQLVIEAA TENYELKLKI LKQADALLAP EVIIASNTSS ISITKLAAAT SRADKFIGMH FFNPVPMMAL VEIIRGLQTS DATHDAVKAL AEHLGKSPIT VKNAPGFVVN RILVPMINEA FFVLAEGLAT PEDIDAGMKL GCNQPIGPLA LADMVGLDVC LAVMDVYLAE FGDSKYRACP LLKEYVAAGR LGRKTGRGVY SY //