LTAE_PSEAE
ID LTAE_PSEAE Reviewed; 346 AA.
AC Q9HTF1;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Low specificity L-threonine aldolase;
DE Short=Low specificity L-TA;
DE EC=4.1.2.48;
GN Name=ltaE; OrderedLocusNames=PA5413;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
CC -!- FUNCTION: Catalyzes the cleavage of L-allo-threonine and L-threonine to
CC glycine and acetaldehyde. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-threonine = acetaldehyde + glycine; Xref=Rhea:RHEA:19625,
CC ChEBI:CHEBI:15343, ChEBI:CHEBI:57305, ChEBI:CHEBI:57926; EC=4.1.2.48;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-allo-threonine = acetaldehyde + glycine;
CC Xref=Rhea:RHEA:26209, ChEBI:CHEBI:15343, ChEBI:CHEBI:57305,
CC ChEBI:CHEBI:58585; EC=4.1.2.48;
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250};
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the threonine aldolase family. {ECO:0000305}.
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DR EMBL; AE004091; AAG08798.1; -; Genomic_DNA.
DR PIR; A82971; A82971.
DR RefSeq; NP_254100.1; NC_002516.2.
DR RefSeq; WP_003105702.1; NZ_QZGE01000031.1.
DR AlphaFoldDB; Q9HTF1; -.
DR SMR; Q9HTF1; -.
DR STRING; 287.DR97_2790; -.
DR PaxDb; Q9HTF1; -.
DR PRIDE; Q9HTF1; -.
DR EnsemblBacteria; AAG08798; AAG08798; PA5413.
DR GeneID; 880064; -.
DR KEGG; pae:PA5413; -.
DR PATRIC; fig|208964.12.peg.5673; -.
DR PseudoCAP; PA5413; -.
DR HOGENOM; CLU_049619_0_0_6; -.
DR InParanoid; Q9HTF1; -.
DR OMA; ETDCEVF; -.
DR PhylomeDB; Q9HTF1; -.
DR BioCyc; PAER208964:G1FZ6-5540-MON; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0008732; F:L-allo-threonine aldolase activity; IEA:RHEA.
DR GO; GO:0006567; P:threonine catabolic process; IEA:InterPro.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR001597; ArAA_b-elim_lyase/Thr_aldolase.
DR InterPro; IPR026273; Low_specificity_L-TA_bact.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR Pfam; PF01212; Beta_elim_lyase; 1.
DR PIRSF; PIRSF038940; Low_specificity_LTA; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
PE 3: Inferred from homology;
KW Lyase; Pyridoxal phosphate; Reference proteome.
FT CHAIN 1..346
FT /note="Low specificity L-threonine aldolase"
FT /id="PRO_0000121577"
FT MOD_RES 207
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 346 AA; 38213 MW; 52129E3422DAC845 CRC64;
MTDHTQQFAS DNYSGICPEA WAAMAEANRG HERAYGDDQW TARASDYFRQ LFETDCEVFF
AFNGTAANSL ALAALCQSYH SVICSETAHV ETDECGAPEF FSNGSKLLLA QTEVGKLTPA
SIRDIALKRQ DIHYPKPRVV TLTQATEVGT VYRPDELKAI SATCKELGLH LHMDGARFSN
ACAFLGCSPA ELSWKAGVDV LCFGGTKNGM AVGEAILFFN RDLAEDFDYR CKQAGQLASK
MRFLAAPWVG VLQDDAWLRY ADHANRCARL LAELVADVPG VSLMFPVEAN GVFLQLSEPA
IEALRARGWR FYTFIGEGGA RFMCSWDTDI ERVRELARDI RLVMGA