ID A0A139ZK01_RICCR Unreviewed; 312 AA. AC A0A139ZK01; DT 11-MAY-2016, integrated into UniProtKB/TrEMBL. DT 11-MAY-2016, sequence version 1. DT 03-MAY-2023, entry version 26. DE SubName: Full=Threonine aldolase {ECO:0000313|EMBL:AJQ52464.1}; GN ORFNames=UQ52_07470 {ECO:0000313|EMBL:AJQ52464.1}; OS Rickettsia conorii subsp. raoultii. OG Plasmid prra2 {ECO:0000313|Proteomes:UP000077462}. OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales; OC Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group. OX NCBI_TaxID=369822 {ECO:0000313|EMBL:AJQ52464.1, ECO:0000313|Proteomes:UP000077462}; RN [1] {ECO:0000313|EMBL:AJQ52464.1, ECO:0000313|Proteomes:UP000077462} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Khabarovsk {ECO:0000313|EMBL:AJQ52464.1, RC ECO:0000313|Proteomes:UP000077462}; RC PLASMID=prra2 {ECO:0000313|Proteomes:UP000077462}; RX PubMed=27103706; RA El Karkouri K., Mediannikov O., Robert C., Raoult D., Fournier P.E.; RT "Genome Sequence of the Tick-Borne Pathogen Rickettsia raoultii."; RL Genome Announc. 4:e00157-16(2016). CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000256|ARBA:ARBA00001933}; CC -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}. CC -!- SIMILARITY: Belongs to the threonine aldolase family. CC {ECO:0000256|ARBA:ARBA00006966}. 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; CP010971; AJQ52464.1; -; Genomic_DNA. DR RefSeq; WP_064464878.1; NZ_CP010971.1. DR AlphaFoldDB; A0A139ZK01; -. DR EnsemblBacteria; AJQ52464; AJQ52464; UQ52_07470. DR PATRIC; fig|369822.3.peg.1688; -. DR Proteomes; UP000077462; Plasmid prra2. DR GO; GO:0016829; F:lyase activity; IEA:InterPro. DR GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro. DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1. DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1. DR InterPro; IPR001597; ArAA_b-elim_lyase/Thr_aldolase. DR InterPro; IPR023603; Low_specificity_L-TA. DR InterPro; IPR015424; PyrdxlP-dep_Trfase. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major. DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small. DR PANTHER; PTHR48097:SF9; L-THREONINE ALDOLASE; 1. DR PANTHER; PTHR48097; L-THREONINE ALDOLASE-RELATED; 1. DR Pfam; PF01212; Beta_elim_lyase; 1. DR PIRSF; PIRSF017617; Thr_aldolase; 2. DR SUPFAM; SSF53383; PLP-dependent transferases; 1. PE 3: Inferred from homology; KW Plasmid {ECO:0000313|EMBL:AJQ52464.1}; KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898}. FT DOMAIN 8..221 FT /note="Aromatic amino acid beta-eliminating lyase/threonine FT aldolase" FT /evidence="ECO:0000259|Pfam:PF01212" FT MOD_RES 206 FT /note="N6-(pyridoxal phosphate)lysine" FT /evidence="ECO:0000256|PIRSR:PIRSR017617-1" SQ SEQUENCE 312 AA; 35226 MW; 346F05C750EAB96A CRC64; MQKVKIIDLR SDTITLQTPE VIQAMHTAVV GDFAYGEDKS CNDLTEYCKR LFKVEDALFV TSGMLANRLA IVSQTNPGDE IITHYNYHIN FFDSAGNAKV SNIVFNCINN TSGILENKDI EHAINSKPRY KIFAQVKLVT IENSINGFNG KIYPFEKQVE LYKYLKSHNI NLHLDGARLF NSHVETNIAL ADYAKYTDTL SVCFSKGLGA PFGSMLLGKN LATLFADGIT EIQYIKLISP YPETNIVTFS IKELNITNDV FLNACQTYGL LLFPWLQYHI RAVIHLGITR SDIVYAIDTI QKVVSFYNHN KK //