LTAA_AERJA
ID LTAA_AERJA Reviewed; 338 AA.
AC O07051;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=L-allo-threonine aldolase;
DE Short=L-allo-TA;
DE EC=4.1.2.49;
DE AltName: Full=L-allo-threonine acetaldehyde-lyase;
GN Name=ltaA;
OS Aeromonas jandaei.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC Aeromonadaceae; Aeromonas.
OX NCBI_TaxID=650;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, PYRIDOXAL
RP PHOSPHATE AT LYS-199, MUTAGENESIS OF LYS-51; LYS-199 AND LYS-224, AND
RP COFACTOR.
RC STRAIN=DK-39;
RX PubMed=9171400; DOI=10.1128/jb.179.11.3555-3560.1997;
RA Liu J.-Q., Dairi T., Kataoka M., Shimizu S., Yamada H.;
RT "L-allo-threonine aldolase from Aeromonas jandaei DK-39: gene cloning,
RT nucleotide sequencing, and identification of the pyridoxal 5'-phosphate-
RT binding lysine residue by site-directed mutagenesis.";
RL J. Bacteriol. 179:3555-3560(1997).
RN [2]
RP CATALYTIC ACTIVITY, AND CHARACTERIZATION.
RC STRAIN=DK-39;
RX PubMed=9228760; DOI=10.1111/j.1574-6968.1997.tb12577.x;
RA Kataoka M., Wada M., Nishi K., Yamada H., Shimizu S.;
RT "Purification and characterization of L-allo-threonine aldolase from
RT Aeromonas jandaei DK-39.";
RL FEMS Microbiol. Lett. 151:245-248(1997).
CC -!- FUNCTION: Stereospecifically catalyzes the interconversion of L-allo-
CC threonine and glycine.
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=4.1.2.49;
CC Evidence={ECO:0000269|PubMed:9228760};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:9171400};
CC -!- SUBUNIT: Homotetramer.
CC -!- SIMILARITY: Belongs to the threonine aldolase family. {ECO:0000305}.
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DR EMBL; D87890; BAA20404.1; -; Genomic_DNA.
DR PIR; T46877; T46877.
DR PDB; 3WGB; X-ray; 2.60 A; A/B/C/D=1-338.
DR PDB; 3WGC; X-ray; 2.50 A; A/B/C/D=1-338.
DR PDBsum; 3WGB; -.
DR PDBsum; 3WGC; -.
DR AlphaFoldDB; O07051; -.
DR SMR; O07051; -.
DR KEGG; ag:BAA20404; -.
DR BioCyc; MetaCyc:MON-12836; -.
DR BRENDA; 4.1.2.49; 10667.
DR GO; GO:0008732; F:L-allo-threonine aldolase activity; IEA:UniProtKB-EC.
DR GO; GO:0006520; P:cellular amino acid metabolic 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; 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; PTHR48097:SF9; 1.
DR Pfam; PF01212; Beta_elim_lyase; 1.
DR PIRSF; PIRSF017617; Thr_aldolase; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Lyase; Pyridoxal phosphate.
FT CHAIN 1..338
FT /note="L-allo-threonine aldolase"
FT /id="PRO_0000121574"
FT MOD_RES 199
FT /note="N6-(pyridoxal phosphate)lysine"
FT MUTAGEN 51
FT /note="K->A: No loss of activity."
FT /evidence="ECO:0000269|PubMed:9171400"
FT MUTAGEN 199
FT /note="K->A,C: Loss of activity."
FT /evidence="ECO:0000269|PubMed:9171400"
FT MUTAGEN 224
FT /note="K->A: No loss of activity."
FT /evidence="ECO:0000269|PubMed:9171400"
FT HELIX 9..11
FT /evidence="ECO:0007829|PDB:3WGC"
FT HELIX 16..23
FT /evidence="ECO:0007829|PDB:3WGC"
FT HELIX 30..32
FT /evidence="ECO:0007829|PDB:3WGC"
FT HELIX 36..48
FT /evidence="ECO:0007829|PDB:3WGC"
FT STRAND 52..58
FT /evidence="ECO:0007829|PDB:3WGC"
FT HELIX 60..71
FT /evidence="ECO:0007829|PDB:3WGC"
FT STRAND 77..81
FT /evidence="ECO:0007829|PDB:3WGC"
FT HELIX 85..88
FT /evidence="ECO:0007829|PDB:3WGC"
FT HELIX 93..96
FT /evidence="ECO:0007829|PDB:3WGC"
FT STRAND 101..105
FT /evidence="ECO:0007829|PDB:3WGC"
FT HELIX 115..121
FT /evidence="ECO:0007829|PDB:3WGC"
FT STRAND 132..141
FT /evidence="ECO:0007829|PDB:3WGC"
FT HELIX 148..160
FT /evidence="ECO:0007829|PDB:3WGC"
FT STRAND 164..169
FT /evidence="ECO:0007829|PDB:3WGC"
FT HELIX 172..179
FT /evidence="ECO:0007829|PDB:3WGC"
FT HELIX 183..187
FT /evidence="ECO:0007829|PDB:3WGC"
FT STRAND 191..199
FT /evidence="ECO:0007829|PDB:3WGC"
FT STRAND 207..211
FT /evidence="ECO:0007829|PDB:3WGC"
FT HELIX 213..226
FT /evidence="ECO:0007829|PDB:3WGC"
FT HELIX 234..246
FT /evidence="ECO:0007829|PDB:3WGC"
FT HELIX 251..264
FT /evidence="ECO:0007829|PDB:3WGC"
FT STRAND 271..273
FT /evidence="ECO:0007829|PDB:3WGC"
FT STRAND 279..285
FT /evidence="ECO:0007829|PDB:3WGC"
FT STRAND 287..290
FT /evidence="ECO:0007829|PDB:3WGC"
FT HELIX 294..301
FT /evidence="ECO:0007829|PDB:3WGC"
FT STRAND 312..315
FT /evidence="ECO:0007829|PDB:3WGC"
FT HELIX 322..335
FT /evidence="ECO:0007829|PDB:3WGC"
SQ SEQUENCE 338 AA; 36290 MW; 332E6006A1882214 CRC64;
MRYIDLRSDT VTQPTDAMRQ CMLHAEVGDD VYGEDPGVNA LEAYGADLLG KEAALFVPSG
TMSNLLAVMS HCQRGEGAVL GSAAHIYRYE AQGSAVLGSV ALQPVPMQAD GSLALADVRA
AIAPDDVHFT PTRLVCLENT HNGKVLPLPY LREMRELVDE HGLQLHLDGA RLFNAVVASG
HTVRELVAPF DSVSICLSKG LGAPVGSLLV GSHAFIARAR RLRKMVGGGM RQAGILAQAG
LFALQQHVVR LADDHRRARQ LAEGLAALPG IRLDLAQVQT NMVFLQLTSG ESAPLLAFMK
ARGILFSGYG ELRLVTHLQI HDDDIEEVID AFTEYLGA
