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Protein

L-allo-threonine aldolase

Gene

ltaA

Organism
Aeromonas jandaei
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Stereospecifically catalyzes the interconversion of L-allo-threonine and glycine.

Catalytic activityi

L-allo-threonine = glycine + acetaldehyde.1 Publication

Cofactori

pyridoxal 5'-phosphate1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-12836.
BRENDAi4.1.2.49. 10667.

Names & Taxonomyi

Protein namesi
Recommended name:
L-allo-threonine aldolase (EC:4.1.2.49)
Short name:
L-allo-TA
Alternative name(s):
L-allo-threonine acetaldehyde-lyase
Gene namesi
Name:ltaA
OrganismiAeromonas jandaei
Taxonomic identifieri650 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAeromonadalesAeromonadaceaeAeromonas

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi51 – 511K → A: No loss of activity. 1 Publication
Mutagenesisi199 – 1991K → A or C: Loss of activity. 1 Publication
Mutagenesisi224 – 2241K → A: No loss of activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 338338L-allo-threonine aldolasePRO_0000121574Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei199 – 1991N6-(pyridoxal phosphate)lysine

Interactioni

Subunit structurei

Homotetramer.

Structurei

Secondary structure

1
338
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi9 – 113Combined sources
Helixi16 – 238Combined sources
Helixi30 – 323Combined sources
Helixi36 – 4813Combined sources
Beta strandi52 – 587Combined sources
Helixi60 – 7112Combined sources
Beta strandi77 – 815Combined sources
Helixi85 – 884Combined sources
Helixi93 – 964Combined sources
Beta strandi101 – 1055Combined sources
Helixi115 – 1217Combined sources
Beta strandi132 – 14110Combined sources
Helixi148 – 16013Combined sources
Beta strandi164 – 1696Combined sources
Helixi172 – 1798Combined sources
Helixi183 – 1875Combined sources
Beta strandi191 – 1999Combined sources
Beta strandi207 – 2115Combined sources
Helixi213 – 22614Combined sources
Helixi234 – 24613Combined sources
Helixi251 – 26414Combined sources
Beta strandi271 – 2733Combined sources
Beta strandi279 – 2857Combined sources
Beta strandi287 – 2904Combined sources
Helixi294 – 3018Combined sources
Beta strandi312 – 3154Combined sources
Helixi322 – 33514Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3WGBX-ray2.60A/B/C/D1-338[»]
3WGCX-ray2.50A/B/C/D1-338[»]
ProteinModelPortaliO07051.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the threonine aldolase family.Curated

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProiIPR001597. ArAA_b-elim_lyase/Thr_aldolase.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
IPR023603. Threonine_aldolase.
[Graphical view]
PfamiPF01212. Beta_elim_lyase. 1 hit.
[Graphical view]
PIRSFiPIRSF017617. Thr_aldolase. 1 hit.
SUPFAMiSSF53383. SSF53383. 1 hit.

Sequencei

Sequence statusi: Complete.

O07051-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRYIDLRSDT VTQPTDAMRQ CMLHAEVGDD VYGEDPGVNA LEAYGADLLG
60 70 80 90 100
KEAALFVPSG TMSNLLAVMS HCQRGEGAVL GSAAHIYRYE AQGSAVLGSV
110 120 130 140 150
ALQPVPMQAD GSLALADVRA AIAPDDVHFT PTRLVCLENT HNGKVLPLPY
160 170 180 190 200
LREMRELVDE HGLQLHLDGA RLFNAVVASG HTVRELVAPF DSVSICLSKG
210 220 230 240 250
LGAPVGSLLV GSHAFIARAR RLRKMVGGGM RQAGILAQAG LFALQQHVVR
260 270 280 290 300
LADDHRRARQ LAEGLAALPG IRLDLAQVQT NMVFLQLTSG ESAPLLAFMK
310 320 330
ARGILFSGYG ELRLVTHLQI HDDDIEEVID AFTEYLGA
Length:338
Mass (Da):36,290
Last modified:July 1, 1997 - v1
Checksum:i332E6006A1882214
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D87890 Genomic DNA. Translation: BAA20404.1.
PIRiT46877.

Genome annotation databases

KEGGiag:BAA20404.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D87890 Genomic DNA. Translation: BAA20404.1.
PIRiT46877.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3WGBX-ray2.60A/B/C/D1-338[»]
3WGCX-ray2.50A/B/C/D1-338[»]
ProteinModelPortaliO07051.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGiag:BAA20404.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-12836.
BRENDAi4.1.2.49. 10667.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProiIPR001597. ArAA_b-elim_lyase/Thr_aldolase.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
IPR023603. Threonine_aldolase.
[Graphical view]
PfamiPF01212. Beta_elim_lyase. 1 hit.
[Graphical view]
PIRSFiPIRSF017617. Thr_aldolase. 1 hit.
SUPFAMiSSF53383. SSF53383. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "L-allo-threonine aldolase from Aeromonas jandaei DK-39: gene cloning, nucleotide sequencing, and identification of the pyridoxal 5'-phosphate-binding lysine residue by site-directed mutagenesis."
    Liu J.-Q., Dairi T., Kataoka M., Shimizu S., Yamada H.
    J. Bacteriol. 179:3555-3560(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, PYRIDOXAL PHOSPHATE AT LYS-199, MUTAGENESIS OF LYS-51; LYS-199 AND LYS-224, COFACTOR.
    Strain: DK-39.
  2. "Purification and characterization of L-allo-threonine aldolase from Aeromonas jandaei DK-39."
    Kataoka M., Wada M., Nishi K., Yamada H., Shimizu S.
    FEMS Microbiol. Lett. 151:245-248(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, CHARACTERIZATION.
    Strain: DK-39.

Entry informationi

Entry nameiLTAA_AERJA
AccessioniPrimary (citable) accession number: O07051
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 1, 1997
Last modified: July 6, 2016
This is version 65 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.