| General Information |
| MoonProt ID | 4026 |
| First appeared in release | 4.0 |
| Name(s) | 3-oxoacyl-[acyl-carrier-protein] reductase (From the FabG gene) |
| UniProt ID | A0A0Z8UQY0 |
| GO terms | "GO:0004316 3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity
GO:0016491 oxidoreductase activity
GO:0051287 NAD binding
GO:0006629 lipid metabolic process
GO:0006631 fatty acid metabolic process
GO:0006633 fatty acid biosynthetic process
GO:0032787 monocarboxylic acid metabolic process" |
| Organisms for which functions have been demonstrated | Streptococcus suis |
| Sequence length | 244.0 |
| FASTA sequence | ">tr|A0A0Z8UQY0|A0A0Z8UQY0_STRSU 3-oxoacyl-[acyl-carrier-protein] reductase OS=Streptococcus suis OX=1307 GN=fabG_1 PE=3 SV=1
MELTNKNVFVTGSSRGIGLAIAHKFASLGANVVLNGRGQLGQDILDSFADYDVKVLAISGDISSAEDAKRMVAEAIETLGSVDILVNNAGITKDGMALRMTEEDFDTVLKVNLTGTFNMTQAVLKPMTKAREGAIINLSSVSGLIGNAGQANYAASKAGVIGFTKAIAREVAGRNVRVNAIAPGFIQSDMTDVLSDKIKEAMTAQIPMKRFGATEEVADVAVFLAKQEYLTGQVIAVDGGLTMQ" |
| Structure Information |
| PDB ID | NA |
| Quaternary structure | NA |
| SCOP | |
| CATH | |
| TM Helix Prediction | no TM helices |
| DisProt Annotation | |
| Predicted Disorder Regions | |
| Connections to Disease |
| OMIM ID | |
| Function 1 |
| Function description | enzyme, 3-ketoacyl-ACP reductase, keto reduction step in elongation step of fatty acid synthesis |
| References for function | _ |
| E.C. number | 1.1.1.100 |
| Location of functional site(s) | |
| Cellular location of function | cytoplasm |
| Comments | |
| Function 2 |
| Function description | adhesin, binds host cells, binds plasminogen, binds complement C3 |
| References for function | Guo G, Zhou Y, Li P, Li Q, Yu Y, Zhang W. FabG moonlights as an extracellular adhesin mediates cytoadhesion of Streptococcus suis via interaction with plasminogen. BMC Microbiol. 2025 Jul 4;25(1):412. doi: 10.1186/s12866-025-04129-7. PMID: 40615777; PMCID: PMC12232145. |
| E.C. number | |
| Location of functional site(s) | |
| Cellular location of function | cell surface |
| Comments | |