GenomeNet

Database: UniProt
Entry: D0LTX8_HALO1
LinkDB: D0LTX8_HALO1
Original site: D0LTX8_HALO1 
ID   D0LTX8_HALO1            Unreviewed;       297 AA.
AC   D0LTX8;
DT   15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT   15-DEC-2009, sequence version 1.
DT   27-MAR-2024, entry version 64.
DE   SubName: Full=3-hydroxybutyryl-CoA dehydrogenase {ECO:0000313|EMBL:ACY15822.1};
DE            EC=1.1.1.157 {ECO:0000313|EMBL:ACY15822.1};
GN   OrderedLocusNames=Hoch_3320 {ECO:0000313|EMBL:ACY15822.1};
OS   Haliangium ochraceum (strain DSM 14365 / JCM 11303 / SMP-2).
OC   Bacteria; Myxococcota; Polyangia; Haliangiales; Kofleriaceae; Haliangium.
OX   NCBI_TaxID=502025 {ECO:0000313|EMBL:ACY15822.1, ECO:0000313|Proteomes:UP000001880};
RN   [1] {ECO:0000313|EMBL:ACY15822.1, ECO:0000313|Proteomes:UP000001880}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14365 / CIP 107738 / JCM 11303 / AJ 13395 / SMP-2
RC   {ECO:0000313|Proteomes:UP000001880};
RX   PubMed=21304682; DOI=10.4056/sigs.69.1277;
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Ivanova N., Daum C., Lang E., Abt B., Kopitz M., Saunders E., Lapidus A.,
RA   Lucas S., Glavina Del Rio T., Nolan M., Tice H., Copeland A., Cheng J.F.,
RA   Chen F., Bruce D., Goodwin L., Pitluck S., Mavromatis K., Pati A.,
RA   Mikhailova N., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Detter J.C., Brettin T., Rohde M., Goker M., Bristow J.,
RA   Markowitz V., Eisen J.A., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Haliangium ochraceum type strain (SMP-2).";
RL   Stand. Genomic Sci. 2:96-106(2010).
CC   -!- PATHWAY: Lipid metabolism; butanoate metabolism.
CC       {ECO:0000256|ARBA:ARBA00005086}.
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DR   EMBL; CP001804; ACY15822.1; -; Genomic_DNA.
DR   RefSeq; WP_012828422.1; NC_013440.1.
DR   AlphaFoldDB; D0LTX8; -.
DR   STRING; 502025.Hoch_3320; -.
DR   KEGG; hoh:Hoch_3320; -.
DR   eggNOG; COG1250; Bacteria.
DR   HOGENOM; CLU_009834_2_0_7; -.
DR   OrthoDB; 9771883at2; -.
DR   Proteomes; UP000001880; Chromosome.
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: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; 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; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   4: Predicted;
KW   NAD {ECO:0000256|PIRSR:PIRSR000105-2};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:ACY15822.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001880}.
FT   DOMAIN          12..191
FT                   /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF02737"
FT   DOMAIN          194..287
FT                   /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00725"
FT   BINDING         17..22
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000105-2"
FT   BINDING         40
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000105-2"
FT   BINDING         100
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000105-2"
FT   BINDING         105
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000105-2"
FT   BINDING         127
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000105-2"
FT   BINDING         151
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000105-2"
FT   BINDING         281
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000105-2"
FT   SITE            148
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000105-1"
SQ   SEQUENCE   297 AA;  31492 MW;  03C1BB5EE858686C CRC64;
     MPHFRSAPDV NTVAVLGAGT MGRGIAYVAA LSGCTVRLRD IDHDLVERAL ADIAATMEKG
     VQRGKLDAAA RDAALPRLHG SIDLVQAVAE ADVVIEAAPE ILELKREIFA AADQAAPAHA
     LLASNTSSLA VADIAAAVRE PARVLGMHFF NPVHIMKLLE VVVHEHTADE AAELARGLAA
     RWGKEAITVR DSPGFASSRL GLVLGLEAMR MLESGVASAA DIDTAMRLGY GHPMGPLELT
     DLVGLDVRLK IAEYLATELG PHFAPPAILR DKVEAGELGR KSGQGFFPWQ DGKRSDR
//
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