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Database: UniProt
Entry: C7NGQ2_KYTSD
LinkDB: C7NGQ2_KYTSD
Original site: C7NGQ2_KYTSD 
ID   C7NGQ2_KYTSD            Unreviewed;       299 AA.
AC   C7NGQ2;
DT   13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT   13-OCT-2009, sequence version 1.
DT   27-MAR-2024, entry version 66.
DE   SubName: Full=3-hydroxyacyl-CoA dehydrogenase {ECO:0000313|EMBL:ACV07574.1};
GN   OrderedLocusNames=Ksed_26220 {ECO:0000313|EMBL:ACV07574.1};
OS   Kytococcus sedentarius (strain ATCC 14392 / DSM 20547 / CCM 314 / 541)
OS   (Micrococcus sedentarius).
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Kytococcaceae;
OC   Kytococcus.
OX   NCBI_TaxID=478801 {ECO:0000313|EMBL:ACV07574.1, ECO:0000313|Proteomes:UP000006666};
RN   [1] {ECO:0000313|EMBL:ACV07574.1, ECO:0000313|Proteomes:UP000006666}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14392 / DSM 20547 / CCM 314 / 541
RC   {ECO:0000313|Proteomes:UP000006666};
RX   PubMed=21304632; DOI=10.4056/sigs.761;
RA   Sims D., Brettin T., Detter J.C., Han C., Lapidus A., Copeland A.,
RA   Glavina Del Rio T., Nolan M., Chen F., Lucas S., Tice H., Cheng J.F.,
RA   Bruce D., Goodwin L., Pitluck S., Ovchinnikova G., Pati A., Ivanova N.,
RA   Mavrommatis K., Chen A., Palaniappan K., D'haeseleer P., Chain P.,
RA   Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Schneider S.,
RA   Goker M., Pukall R., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Kytococcus sedentarius type strain (541).";
RL   Stand. Genomic Sci. 1:12-20(2009).
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
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DR   EMBL; CP001686; ACV07574.1; -; Genomic_DNA.
DR   RefSeq; WP_015780495.1; NC_013169.1.
DR   AlphaFoldDB; C7NGQ2; -.
DR   STRING; 478801.Ksed_26220; -.
DR   KEGG; kse:Ksed_26220; -.
DR   eggNOG; COG1250; Bacteria.
DR   HOGENOM; CLU_009834_0_1_11; -.
DR   Proteomes; UP000006666; Chromosome.
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; 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.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          6..181
FT                   /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF02737"
FT   DOMAIN          186..241
FT                   /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00725"
FT   SITE            139
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000105-1"
SQ   SEQUENCE   299 AA;  31251 MW;  773B46EF907BEDFD CRC64;
     MSARRAAVIG AGTIGLGWAG IFAGHGWDVA VFDPRDGLDA ALDDAAAEAA GALTAAGREV
     STQQVRERLA VAGSLEEAAE GAEHVQESGP EDLEWKRRTF AQLEAATGPG TVLATSSSFI
     TSSEISRDNL EQGRMLVGHP FNPVLVLPLV EVVGGSNTHP ETVEAAVETY RAVGKHPVVV
     GAEVQGFIGN RLQFVLLAEA LHLVEQGVAT PEEIDEVVRT SLGPRWAALG PLRASSMGGA
     RGMTGLFELL SPELEKLQPG LPDLATQIRT TGVVDAAYGD NQPTPAEVAR RLRGALSDD
//
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