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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)DescriptionActionsGraphical viewLength
Mutagenesisi51K → A: No loss of activity. 1 Publication1
Mutagenesisi199K → A or C: Loss of activity. 1 Publication1
Mutagenesisi224K → A: No loss of activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001215741 – 338L-allo-threonine aldolaseAdd BLAST338

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei199N6-(pyridoxal phosphate)lysine1

Interactioni

Subunit structurei

Homotetramer.

Structurei

Secondary structure

1338
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi9 – 11Combined sources3
Helixi16 – 23Combined sources8
Helixi30 – 32Combined sources3
Helixi36 – 48Combined sources13
Beta strandi52 – 58Combined sources7
Helixi60 – 71Combined sources12
Beta strandi77 – 81Combined sources5
Helixi85 – 88Combined sources4
Helixi93 – 96Combined sources4
Beta strandi101 – 105Combined sources5
Helixi115 – 121Combined sources7
Beta strandi132 – 141Combined sources10
Helixi148 – 160Combined sources13
Beta strandi164 – 169Combined sources6
Helixi172 – 179Combined sources8
Helixi183 – 187Combined sources5
Beta strandi191 – 199Combined sources9
Beta strandi207 – 211Combined sources5
Helixi213 – 226Combined sources14
Helixi234 – 246Combined sources13
Helixi251 – 264Combined sources14
Beta strandi271 – 273Combined sources3
Beta strandi279 – 285Combined sources7
Beta strandi287 – 290Combined sources4
Helixi294 – 301Combined sources8
Beta strandi312 – 315Combined sources4
Helixi322 – 335Combined sources14

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3WGBX-ray2.60A/B/C/D1-338[»]
3WGCX-ray2.50A/B/C/D1-338[»]
ProteinModelPortaliO07051.
SMRiO07051.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the threonine aldolase family.Curated

Phylogenomic databases

KOiK20801.

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3WGBX-ray2.60A/B/C/D1-338[»]
3WGCX-ray2.50A/B/C/D1-338[»]
ProteinModelPortaliO07051.
SMRiO07051.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGiag:BAA20404.

Phylogenomic databases

KOiK20801.

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...

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: November 30, 2016
This is version 67 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.