ID Q4UN54_RICFE Unreviewed; 241 AA. AC Q4UN54; DT 05-JUL-2005, integrated into UniProtKB/TrEMBL. DT 05-JUL-2005, sequence version 1. DT 27-MAR-2024, entry version 113. DE RecName: Full=3-oxoacyl-[acyl-carrier-protein] reductase FabG {ECO:0000256|ARBA:ARBA00017650}; DE AltName: Full=3-ketoacyl-acyl carrier protein reductase {ECO:0000256|ARBA:ARBA00033040}; DE AltName: Full=Beta-Ketoacyl-acyl carrier protein reductase {ECO:0000256|ARBA:ARBA00029743, ECO:0000256|ARBA:ARBA00032683}; DE AltName: Full=Beta-ketoacyl-ACP reductase {ECO:0000256|ARBA:ARBA00029899}; GN Name=phbB {ECO:0000313|EMBL:AAY61004.1}; GN OrderedLocusNames=RF_0153 {ECO:0000313|EMBL:AAY61004.1}; OS Rickettsia felis (strain ATCC VR-1525 / URRWXCal2) (Rickettsia azadi). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales; OC Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group. OX NCBI_TaxID=315456 {ECO:0000313|EMBL:AAY61004.1, ECO:0000313|Proteomes:UP000008548}; RN [1] {ECO:0000313|EMBL:AAY61004.1, ECO:0000313|Proteomes:UP000008548} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC VR-1525 / URRWXCal2 {ECO:0000313|Proteomes:UP000008548}; RX PubMed=15984913; DOI=10.1371/journal.pbio.0030248; RA Ogata H., Renesto P., Audic S., Robert C., Blanc G., Fournier P.E., RA Parinello H., Claverie J.M., Raoult D.; RT "The genome sequence of Rickettsia felis identifies the first putative RT conjugative plasmid in an obligate intracellular parasite."; RL PLoS Biol. 3:1-12(2005). RN [2] {ECO:0007829|PDB:4KMS} RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS). RX PubMed=33620038; DOI=10.1107/s2053230x21001497; RA Rodarte J.V., Abendroth J., Edwards T.E., Lorimer D.D., Staker B.L., RA Zhang S., Myler P.J., McLaughlin K.J.; RT "Crystal structure of acetoacetyl-CoA reductase from Rickettsia felis."; RL Acta Crystallogr. F Struct. Biol. Commun. 77:54-60(2021). CC -!- FUNCTION: Catalyzes the NADPH-dependent reduction of beta-ketoacyl-ACP CC substrates to beta-hydroxyacyl-ACP products, the first reductive step CC in the elongation cycle of fatty acid biosynthesis. CC {ECO:0000256|ARBA:ARBA00002607}. CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) CC family. {ECO:0000256|ARBA:ARBA00006484}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000053; AAY61004.1; -; Genomic_DNA. DR PDB; 4KMS; X-ray; 2.00 A; A/B=1-241. DR PDBsum; 4KMS; -. DR AlphaFoldDB; Q4UN54; -. DR SMR; Q4UN54; -. DR STRING; 315456.RF_0153; -. DR KEGG; rfe:RF_0153; -. DR eggNOG; COG1028; Bacteria. DR HOGENOM; CLU_010194_1_3_5; -. DR OrthoDB; 9804774at2; -. DR BRENDA; 1.1.1.36; 15352. DR Proteomes; UP000008548; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0018454; F:acetoacetyl-CoA reductase activity; IEA:InterPro. DR GO; GO:0042619; P:poly-hydroxybutyrate biosynthetic process; IEA:InterPro. DR CDD; cd05333; BKR_SDR_c; 1. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1. DR InterPro; IPR011283; Acetoacetyl-CoA_reductase. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR InterPro; IPR020904; Sc_DH/Rdtase_CS. DR InterPro; IPR002347; SDR_fam. DR NCBIfam; TIGR01829; AcAcCoA_reduct; 1. DR PANTHER; PTHR42879; 3-OXOACYL-(ACYL-CARRIER-PROTEIN) REDUCTASE; 1. DR PANTHER; PTHR42879:SF2; 3-OXOACYL-[ACYL-CARRIER-PROTEIN] REDUCTASE FABG; 1. DR Pfam; PF13561; adh_short_C2; 1. DR PRINTS; PR00081; GDHRDH. DR PRINTS; PR00080; SDRFAMILY. DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1. DR PROSITE; PS00061; ADH_SHORT; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0007829|PDB:4KMS}; KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516}; KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098}; KW Oxidoreductase {ECO:0000313|EMBL:AAY61004.1}. SQ SEQUENCE 241 AA; 26252 MW; FB09A2EDA99C0651 CRC64; MSEIAIVTGG TRGIGKATAL ELKNKGLTVV ANFFSNYDAA KEMEEKYGIK TKCWNVADFE ECRQAVKEIE EEFKKPVSIL VNNAGITKDK MLHRMSHQDW NDVINVNLNS CFNMSSSVME QMRNQDYGRI VNISSINAQA GQVGQTNYSA AKAGIIGFTK ALARETASKN ITVNCIAPGY IATEMVGAVP EDVLAKIINS IPKKRLGQPE EIARAVAFLV DENAGFITGE TISINGGHNM I //