ID B0SKH9_LEPBP Unreviewed; 436 AA.
AC B0SKH9;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE SubName: Full=3-hydroxyacyl-CoA dehydrogenase, NAD binding FadB putative signal peptide {ECO:0000313|EMBL:ABZ96736.1};
DE EC=4.2.1.17 {ECO:0000313|EMBL:ABZ96736.1};
GN Name=fadB2 {ECO:0000313|EMBL:ABZ96736.1};
GN OrderedLocusNames=LEPBI_I0599 {ECO:0000313|EMBL:ABZ96736.1};
OS Leptospira biflexa serovar Patoc (strain Patoc 1 / ATCC 23582 / Paris).
OC Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC Leptospira.
OX NCBI_TaxID=456481 {ECO:0000313|EMBL:ABZ96736.1, ECO:0000313|Proteomes:UP000001847};
RN [1] {ECO:0000313|EMBL:ABZ96736.1, ECO:0000313|Proteomes:UP000001847}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Patoc 1 / ATCC 23582 / Paris
RC {ECO:0000313|Proteomes:UP000001847};
RX PubMed=18270594; DOI=10.1371/journal.pone.0001607;
RA Picardeau M., Bulach D.M., Bouchier C., Zuerner R.L., Zidane N.,
RA Wilson P.J., Creno S., Kuczek E.S., Bommezzadri S., Davis J.C., McGrath A.,
RA Johnson M.J., Boursaux-Eude C., Seemann T., Rouy Z., Coppel R.L.,
RA Rood J.I., Lajus A., Davies J.K., Medigue C., Adler B.;
RT "Genome sequence of the saprophyte Leptospira biflexa provides insights
RT into the evolution of Leptospira and the pathogenesis of leptospirosis.";
RL PLoS ONE 3:E1607-E1607(2008).
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DR EMBL; CP000786; ABZ96736.1; -; Genomic_DNA.
DR RefSeq; WP_012387623.1; NC_010602.1.
DR AlphaFoldDB; B0SKH9; -.
DR STRING; 456481.LEPBI_I0599; -.
DR KEGG; lbi:LEPBI_I0599; -.
DR HOGENOM; CLU_009834_2_0_12; -.
DR OrthoDB; 9771883at2; -.
DR BioCyc; LBIF456481:LEPBI_RS02945-MONOMER; -.
DR Proteomes; UP000001847; Chromosome I.
DR GO; GO:0004300; F:enoyl-CoA hydratase activity; IEA:UniProtKB-EC.
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; 1.10.1040.50; -; 1.
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; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR48075; 3-HYDROXYACYL-COA DEHYDROGENASE FAMILY PROTEIN; 1.
DR PANTHER; PTHR48075:SF7; 3-HYDROXYACYL-COA DEHYDROGENASE-RELATED; 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;
KW Lyase {ECO:0000313|EMBL:ABZ96736.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001847}.
FT DOMAIN 6..181
FT /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT /evidence="ECO:0000259|Pfam:PF02737"
FT DOMAIN 185..283
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
SQ SEQUENCE 436 AA; 47681 MW; B68096F3623EF5D0 CRC64;
MREIKTVTIL GANGAMGSGS AGVIAAFGGA KVHMLARDVE KAKQGIEAAV ASVKTDTIRA
RMIPGSYDAD LEKAVAESDW VFELVAESYE VKEPINTRIA KARRPGTIVS TVSSGLSIGR
LAKAYDEDGQ KHYYGTHFFN PPYKMILCEL VTHSGNDKKV TQALGEYLDK VLGRAVVYTN
DTPAFAGNRI GFQLMNEVAH FAEKYADKGG IALMDEIMSG YTGRAMGPLA TADFVGLDVH
KAIVDNIYDN TKDEAHETFK LPGYFQKLID AGKLGMKSGG GLTKVVKHAD GKREKFVYNI
KTGEYDPYPK FDIPFIKEAR QKIKESNYKG AMDVVKNASG FEAEIARYFI SRYISYSLSL
VGEVVDTKEN TDGAMGFGFN WVPASAFVDF LGGPKETIKL MEASKIPVPK LLKDAKEGKK
FYELGDKLDA RSLFKG
//
