ID A0A101XPN0_9BACL Unreviewed; 287 AA.
AC A0A101XPN0;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=3-hydroxybutyryl-CoA dehydrogenase {ECO:0000313|EMBL:KUO95294.1};
GN ORFNames=ATW55_14285 {ECO:0000313|EMBL:KUO95294.1};
OS Ferroacidibacillus organovorans.
OC Bacteria; Bacillota; Bacilli; Bacillales; Alicyclobacillaceae;
OC Ferroacidibacillus.
OX NCBI_TaxID=1765683 {ECO:0000313|EMBL:KUO95294.1, ECO:0000313|Proteomes:UP000053557};
RN [1] {ECO:0000313|EMBL:KUO95294.1, ECO:0000313|Proteomes:UP000053557}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ITV001 {ECO:0000313|EMBL:KUO95294.1,
RC ECO:0000313|Proteomes:UP000053557};
RA Dall'Agnol H., Nancucheo I., Johnson B., Oliveira R., Leite L., Pylro V.,
RA Nunes G.L., Tzotzos G., Fernandes G.R., Dutra J., Orellana S.C.,
RA Oliveira G.;
RT "Draft genome sequence of Acidibacillus ferrooxidans ITV001, isolated from
RT a chalcopyrite acid mine drainage site in Brazil.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Lipid metabolism; butanoate metabolism.
CC {ECO:0000256|ARBA:ARBA00005086}.
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:KUO95294.1}.
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DR EMBL; LPVJ01000054; KUO95294.1; -; Genomic_DNA.
DR RefSeq; WP_067718051.1; NZ_LPVJ01000054.1.
DR AlphaFoldDB; A0A101XPN0; -.
DR OrthoDB; 9771883at2; -.
DR UniPathway; UPA00863; -.
DR Proteomes; UP000053557; 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:0019605; P:butyrate metabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0044248; P:cellular catabolic process; IEA:UniProt.
DR GO; GO:1901575; P:organic substance catabolic process; IEA:UniProt.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 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 PANTHER; PTHR48075; 3-HYDROXYACYL-COA DEHYDROGENASE FAMILY PROTEIN; 1.
DR PANTHER; PTHR48075:SF5; 3-HYDROXYACYL-COA DEHYDROGENASE FAMILY PROTEIN; 1.
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|PIRSR:PIRSR000105-2};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 5..183
FT /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT /evidence="ECO:0000259|Pfam:PF02737"
FT DOMAIN 186..282
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
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 287 AA; 31311 MW; 319F3D15682945BF CRC64;
MAIQHVMVIG AGQMGSGIAQ VCAMRGMRVT LQDIAPEFVE RGFSRIEESL VRIVKKGGLS
ESASRDTLAS ITLTTTLDAV ASADFVIEAA VEKMDIKKSL FMQLDGLAKP DAILATNTSS
LPITEIAAVT SRPERVIGMH FMNPVPVMQL VEIIRGLQTS EKTYRAVADL AQALGKTPVE
VHDYPGFISN RILLPMINEA IYCLYEGVAD RDAIDTVMKL GMNHPMGPLQ LADFIGLDTC
LSIMEILHDG LGDSKYRPCP LLRKYVAAGW LGKKSGRGFY DYRSESK
//
