LTAE_PSEUN
ID LTAE_PSEUN Reviewed; 346 AA.
AC O50584;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Low specificity L-threonine aldolase;
DE Short=Low specificity L-TA;
DE EC=4.1.2.48;
GN Name=ltaE; Synonyms=ltaP;
OS Pseudomonas sp. (strain NCIMB 10558).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=268808;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF N-TERMINUS,
RP MUTAGENESIS OF LYS-207, AND CHARACTERIZATION.
RX PubMed=9464392; DOI=10.1128/aem.64.2.549-554.1998;
RA Liu J.-Q., Ito S., Dairi T., Itoh N., Kataoka M., Shimizu S., Yamada H.;
RT "Gene cloning, nucleotide sequencing, and purification and characterization
RT of the low-specificity L-threonine aldolase from Pseudomonas sp. strain
RT NCIMB 10558.";
RL Appl. Environ. Microbiol. 64:549-554(1998).
CC -!- FUNCTION: Catalyzes the cleavage of L-allo-threonine and L-threonine to
CC glycine and acetaldehyde. Can also act on L-erythro-phenylserine, L-
CC threo-phenylserine, L-beta-3,4-methylenedioxyphenylserine and L-beta-
CC 3,4-dihydroxyphenylserine.
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 8.0-8.5.;
CC Temperature dependence:
CC Optimum temperature is 25 degrees Celsius.;
CC -!- SUBUNIT: Homotetramer. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the threonine aldolase family. {ECO:0000305}.
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DR EMBL; AB001577; BAA24794.1; -; Genomic_DNA.
DR AlphaFoldDB; O50584; -.
DR SMR; O50584; -.
DR PRIDE; O50584; -.
DR BRENDA; 4.1.2.48; 5085.
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 1: Evidence at protein level;
KW Direct protein sequencing; Lyase; Pyridoxal phosphate.
FT CHAIN 1..346
FT /note="Low specificity L-threonine aldolase"
FT /id="PRO_0000121578"
FT MOD_RES 207
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000305"
FT MUTAGEN 207
FT /note="K->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:9464392"
FT MUTAGEN 207
FT /note="K->R: 1000-fold decrease in activity."
FT /evidence="ECO:0000269|PubMed:9464392"
SQ SEQUENCE 346 AA; 37948 MW; 9B2D6FDE002DB68D CRC64;
MTDQSQQFAS DNYSGICPEA WAAMEKANHG HERAYGDDQW TARAADHFRK LFETDCEVFF
AFNGTAANSL ALSSLCQSYH SVICSETAHV ETDECGAPEF FSNGSKLLTA RSEGGKLTPA
SIREVALKRQ DIHYPKPRVV TITQATEVGS VYRPDELKAI SATCKELGLN LHMDGARFSN
ACAFLGCTPA ELTWKAGIDV LCFGGTKNGM AVGEAILFFN RKLAEDFDYR CKQAGQLASK
MRFLSAPWVG LLEDGAWLRH AAHANHCAQL LSSLVADIPG VELMFPVEAN GVFLQMSEPA
LEALRNKGWR FYTFIGSGGA RFMCSWDTEE ARVRELAADI RAVMSA
