ID D8GTU3_CLOLD Unreviewed; 313 AA.
AC D8GTU3;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE SubName: Full=3-hydroxybutyryl-CoA dehydrogenase {ECO:0000313|EMBL:ADK16756.1};
DE EC=1.1.1.157 {ECO:0000313|EMBL:ADK16756.1};
GN Name=hbd2 {ECO:0000313|EMBL:ADK16756.1};
GN OrderedLocusNames=CLJU_c37300 {ECO:0000313|EMBL:ADK16756.1};
OS Clostridium ljungdahlii (strain ATCC 55383 / DSM 13528 / PETC).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=748727 {ECO:0000313|EMBL:ADK16756.1, ECO:0000313|Proteomes:UP000001656};
RN [1] {ECO:0000313|EMBL:ADK16756.1, ECO:0000313|Proteomes:UP000001656}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 55383 / DSM 13528 / PETC
RC {ECO:0000313|Proteomes:UP000001656};
RX PubMed=20616070; DOI=10.1073/pnas.1004716107;
RA Kopke M., Held C., Hujer S., Liesegang H., Wiezer A., Wollherr A.,
RA Ehrenreich A., Liebl W., Gottschalk G., Durre P.;
RT "Clostridium ljungdahlii represents a microbial production platform based
RT on syngas.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:13087-13092(2010).
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: Belongs to the 3-hydroxyacyl-CoA dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00009463}.
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DR EMBL; CP001666; ADK16756.1; -; Genomic_DNA.
DR RefSeq; WP_013240334.1; NZ_LITS01000017.1.
DR AlphaFoldDB; D8GTU3; -.
DR SMR; D8GTU3; -.
DR STRING; 748727.CLJU_c37300; -.
DR KEGG; clj:CLJU_c37300; -.
DR PATRIC; fig|748727.19.peg.959; -.
DR eggNOG; COG1250; Bacteria.
DR HOGENOM; CLU_009834_2_0_9; -.
DR OrthoDB; 9815331at2; -.
DR UniPathway; UPA00863; -.
DR Proteomes; UP000001656; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008691; F:3-hydroxybutyryl-CoA dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0070403; F:NAD+ binding; 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: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,
KW ECO:0000313|EMBL:ADK16756.1}.
FT DOMAIN 5..185
FT /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT /evidence="ECO:0000259|Pfam:PF02737"
FT DOMAIN 188..286
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
FT SITE 141
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR000105-1"
SQ SEQUENCE 313 AA; 34638 MW; D2D29BB2C6F0C0F1 CRC64;
MNIKNIAVLG TGTMGHGIAL LSAKAGLNVV MYGRSNASLE RGFNNIKSSL NSLKAAGKLS
DEKCEEILSK IKGVKTIQEA AKDADFVIEA LAENLELKQD IFRQLDEICS PDVVLTSNTS
GLSPTAIAKN TKYPERVAIA HFWNPPQLIP LVEVVPGEKT SQDTMKIIMN WVEFIGKKAV
RMEKECLGFI GNRLQLALLR EALYIVEQGW AKPEEVDKAM EYGHGRRLPV TGPLCSADLG
GLDIFNNISS YLFKDLCNYT KPSKLMQDKV EAGNLGSKSG QGFYNWTPEV LEKKQKERTE
VLLDFLERDS RGK
//
