ID A0A1F4Q327_9BACT Unreviewed; 334 AA.
AC A0A1F4Q327;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=3-hydroxybutyryl-CoA dehydrogenase {ECO:0008006|Google:ProtNLM};
GN ORFNames=A3H39_03000 {ECO:0000313|EMBL:OGB90423.1};
OS candidate division NC10 bacterium RIFCSPLOWO2_02_FULL_66_22.
OC Bacteria; candidate division NC10.
OX NCBI_TaxID=1801658 {ECO:0000313|EMBL:OGB90423.1, ECO:0000313|Proteomes:UP000177374};
RN [1] {ECO:0000313|EMBL:OGB90423.1, ECO:0000313|Proteomes:UP000177374}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
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:OGB90423.1}.
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; METH01000174; OGB90423.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F4Q327; -.
DR STRING; 1801658.A3H39_03000; -.
DR Proteomes; UP000177374; 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; 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:SF1; LAMBDA-CRYSTALLIN HOMOLOG; 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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 9..189
FT /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT /evidence="ECO:0000259|Pfam:PF02737"
FT DOMAIN 192..290
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
FT SITE 145
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR000105-1"
SQ SEQUENCE 334 AA; 35744 MW; 537AF5892B405120 CRC64;
MLRIDEIRSV AVIGAGVMGS GIAQTFAQAG YAVRLQARHE GTLRAARDRI ARSQDAMVRG
DLLSEEAARD ALARIHPTTI LEEATRECHF VSESVPEDLE LKRQVFAALD RQVPPGAVLS
TDTSGLSISA IASATSRPER VVGFHWMNPP HLMPTVEVIR GAQTADAALD LTCELARRIG
RVPIRVEKDV PGFLWNRLQL ALIREALHVV EQGIASPEAV DLAVTAGLGL RWAAVGPLRL
MDLGGLATFH SVAAYLYQDL SKASEPQHAL ATKVAAGETG ARAGRGFYDY PAGSAEAAIA
ARDARLFELL KLLRLPVFRD RDSAPDPTGA SPGG
//