ID Q2SUT0_BURTA Unreviewed; 388 AA.
AC Q2SUT0;
DT 24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT 24-JAN-2006, sequence version 1.
DT 24-JAN-2024, entry version 99.
DE SubName: Full=3-hydroxyacyl-CoA dehydrogenase family protein {ECO:0000313|EMBL:ABC38229.1};
GN OrderedLocusNames=BTH_I2807 {ECO:0000313|EMBL:ABC38229.1};
OS Burkholderia thailandensis (strain ATCC 700388 / DSM 13276 / CCUG 48851 /
OS CIP 106301 / E264).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=271848 {ECO:0000313|EMBL:ABC38229.1, ECO:0000313|Proteomes:UP000001930};
RN [1] {ECO:0000313|EMBL:ABC38229.1, ECO:0000313|Proteomes:UP000001930}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700388 / DSM 13276 / CIP 106301 / E264
RC {ECO:0000313|Proteomes:UP000001930};
RX PubMed=16336651; DOI=10.1186/1471-2164-6-174;
RA Kim H.S., Schell M.A., Yu Y., Ulrich R.L., Sarria S.H., Nierman W.C.,
RA DeShazer D.;
RT "Bacterial genome adaptation to niches: divergence of the potential
RT virulence genes in three Burkholderia species of different survival
RT strategies.";
RL BMC Genomics 6:174-174(2005).
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DR EMBL; CP000086; ABC38229.1; -; Genomic_DNA.
DR AlphaFoldDB; Q2SUT0; -.
DR KEGG; bte:BTH_I2807; -.
DR HOGENOM; CLU_009834_0_1_4; -.
DR OMA; RDNCLTH; -.
DR Proteomes; UP000001930; Chromosome I.
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; 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 SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 4: Predicted;
FT DOMAIN 89..258
FT /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT /evidence="ECO:0000259|Pfam:PF02737"
FT DOMAIN 262..333
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 48..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..78
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 388 AA; 42057 MW; 48169AC1E039FCFB CRC64;
MSGARRDARD ACRSRRRSPA RSGRANRNSR MTLRHSCGFF APGGCARAAS RIRRRPTDSA
AQRNHGGSMR QSFAHSNTLE TPPMEIQRIA VVGAGVIGAS WTAFYLSKGF DVAVTDPAPD
ARTRLDASLA NFLGERAGTL APRVAFEPTL DAALDGADFV QESGPERLDF KRELYRRIDA
RLPAHVLVAS SSSGLKMSDI QTACDAHPER CLIAHPFNPP HLIPLVELVG GAATSAGAIA
QAKRFYDGLG KVTIVLNKEM AGHVANRLAA ALFREVYHLV GEGVVSVEDA DKAVSWGPGL
RWGLMGQSLI YHLGGGEGGI AHFLEHLSGP MAEWWRDLGS PSFSPDVDRQ LIDALREIQG
AHSMRELGAE RDRLLVELID ARRDSFLP
//