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Protein

Alanine racemase, catabolic

Gene

dadX

Organism
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Isomerizes L-alanine to D-alanine which is then oxidized to pyruvate by DadA.1 Publication

Catalytic activityi

L-alanine = D-alanine.1 Publication

Cofactori

pyridoxal 5'-phosphate1 Publication

Kineticsi

  1. KM=1.40 mM for D-alanine1 Publication
  2. KM=1.40 mM for L-alanine1 Publication
  1. Vmax=134 µmol/min/mg enzyme toward D-alanine1 Publication
  2. Vmax=155 µmol/min/mg enzyme toward L-alanine1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei33 – 331Proton acceptor; specific for D-alanineUniRule annotation
Binding sitei129 – 1291Substrate1 Publication
Active sitei253 – 2531Proton acceptor; specific for L-alanineUniRule annotation
Binding sitei301 – 3011Substrate; via amide nitrogenUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BRENDAi5.1.1.1. 5087.

Names & Taxonomyi

Protein namesi
Recommended name:
Alanine racemase, catabolic1 Publication (EC:5.1.1.11 Publication)
Gene namesi
Name:dadX1 PublicationImported
Ordered Locus Names:PA5302
OrganismiPseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Taxonomic identifieri208964 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
Proteomesi
  • UP000002438 Componenti: Chromosome

Organism-specific databases

PseudoCAPiPA5302.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 357357Alanine racemase, catabolicPRO_0000114547Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei33 – 331N6-(pyridoxal phosphate)lysine1 Publication
Modified residuei122 – 1221N6-carboxylysine1 Publication

Proteomic databases

PaxDbiQ9HTQ2.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

STRINGi208964.PA5302.

Structurei

Secondary structure

1
357
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 95Combined sources
Helixi10 – 2415Combined sources
Beta strandi26 – 316Combined sources
Helixi33 – 375Combined sources
Helixi41 – 488Combined sources
Turni49 – 513Combined sources
Beta strandi53 – 597Combined sources
Helixi60 – 689Combined sources
Beta strandi75 – 773Combined sources
Helixi84 – 863Combined sources
Helixi87 – 926Combined sources
Beta strandi95 – 995Combined sources
Helixi102 – 1109Combined sources
Beta strandi117 – 1237Combined sources
Beta strandi125 – 1273Combined sources
Beta strandi129 – 1324Combined sources
Helixi134 – 14613Combined sources
Beta strandi150 – 1567Combined sources
Helixi169 – 18113Combined sources
Helixi193 – 1986Combined sources
Beta strandi205 – 2073Combined sources
Helixi211 – 2144Combined sources
Beta strandi218 – 2214Combined sources
Helixi226 – 2283Combined sources
Beta strandi233 – 24513Combined sources
Beta strandi250 – 2523Combined sources
Helixi253 – 2553Combined sources
Beta strandi260 – 26910Combined sources
Helixi272 – 2743Combined sources
Beta strandi285 – 2884Combined sources
Beta strandi291 – 2955Combined sources
Beta strandi304 – 3074Combined sources
Beta strandi319 – 3279Combined sources
Helixi329 – 3357Combined sources
Helixi340 – 3456Combined sources
Beta strandi352 – 3554Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1RCQX-ray1.45A1-357[»]
ProteinModelPortaliQ9HTQ2.
SMRiQ9HTQ2. Positions 1-357.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9HTQ2.

Family & Domainsi

Sequence similaritiesi

Belongs to the alanine racemase family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CJ4. Bacteria.
COG0787. LUCA.
HOGENOMiHOG000031446.
InParanoidiQ9HTQ2.
KOiK01775.
OMAiPSDWVRP.
OrthoDBiEOG6PP9NJ.
PhylomeDBiQ9HTQ2.

Family and domain databases

Gene3Di2.40.37.10. 1 hit.
3.20.20.10. 1 hit.
HAMAPiMF_01201. Ala_racemase.
InterProiIPR000821. Ala_racemase.
IPR009006. Ala_racemase/Decarboxylase_C.
IPR011079. Ala_racemase_C.
IPR001608. Ala_racemase_N.
IPR020622. Ala_racemase_pyridoxalP-BS.
IPR029066. PLP-binding_barrel.
[Graphical view]
PfamiPF00842. Ala_racemase_C. 1 hit.
PF01168. Ala_racemase_N. 1 hit.
[Graphical view]
PRINTSiPR00992. ALARACEMASE.
SMARTiSM01005. Ala_racemase_C. 1 hit.
[Graphical view]
SUPFAMiSSF50621. SSF50621. 1 hit.
SSF51419. SSF51419. 1 hit.
TIGRFAMsiTIGR00492. alr. 1 hit.
PROSITEiPS00395. ALANINE_RACEMASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9HTQ2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRPARALIDL QALRHNYRLA REATGARALA VIKADAYGHG AVRCAEALAA
60 70 80 90 100
EADGFAVACI EEGLELREAG IRQPILLLEG FFEASELELI VAHDFWCVVH
110 120 130 140 150
CAWQLEAIER ASLARPLNVW LKMDSGMHRV GFFPEDFSAA HERLRASGKV
160 170 180 190 200
AKIVMMSHFS RADELDCPRT EEQLAAFAAA SQGLEGEISL RNSPAVLGWP
210 220 230 240 250
KVPSDWVRPG ILLYGATPFE RAHPLADRLR PVMTLESKVI SVRDLPAGEP
260 270 280 290 300
VGYGARYSTE RSQRIGVVAM GYADGYPRHA ADGTLVFIDG KPGRLVGRVS
310 320 330 340 350
MDMLTVDLTD HPQAGLGSRV ELWGPNVPVG ALAAQFGSIP YQLLCNLKRV

PRVYSGA
Length:357
Mass (Da):38,915
Last modified:March 1, 2001 - v1
Checksum:i199F4021D02FFF48
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti138 – 1381S → R in AAD47081 (PubMed:10977898).Curated
Sequence conflicti178 – 1781A → S in AAD47081 (PubMed:10977898).Curated
Sequence conflicti262 – 2621S → R in AAD47081 (PubMed:10977898).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF165881 Genomic DNA. Translation: AAD47081.1.
AE004091 Genomic DNA. Translation: AAG08687.1.
PIRiF82982.
RefSeqiNP_253989.1. NC_002516.2.
WP_003114351.1. NZ_ASJY01000820.1.

Genome annotation databases

EnsemblBacteriaiAAG08687; AAG08687; PA5302.
GeneIDi878055.
KEGGipae:PA5302.
PATRICi19845459. VBIPseAer58763_5556.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF165881 Genomic DNA. Translation: AAD47081.1.
AE004091 Genomic DNA. Translation: AAG08687.1.
PIRiF82982.
RefSeqiNP_253989.1. NC_002516.2.
WP_003114351.1. NZ_ASJY01000820.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1RCQX-ray1.45A1-357[»]
ProteinModelPortaliQ9HTQ2.
SMRiQ9HTQ2. Positions 1-357.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi208964.PA5302.

Proteomic databases

PaxDbiQ9HTQ2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAG08687; AAG08687; PA5302.
GeneIDi878055.
KEGGipae:PA5302.
PATRICi19845459. VBIPseAer58763_5556.

Organism-specific databases

PseudoCAPiPA5302.

Phylogenomic databases

eggNOGiENOG4105CJ4. Bacteria.
COG0787. LUCA.
HOGENOMiHOG000031446.
InParanoidiQ9HTQ2.
KOiK01775.
OMAiPSDWVRP.
OrthoDBiEOG6PP9NJ.
PhylomeDBiQ9HTQ2.

Enzyme and pathway databases

BRENDAi5.1.1.1. 5087.

Miscellaneous databases

EvolutionaryTraceiQ9HTQ2.

Family and domain databases

Gene3Di2.40.37.10. 1 hit.
3.20.20.10. 1 hit.
HAMAPiMF_01201. Ala_racemase.
InterProiIPR000821. Ala_racemase.
IPR009006. Ala_racemase/Decarboxylase_C.
IPR011079. Ala_racemase_C.
IPR001608. Ala_racemase_N.
IPR020622. Ala_racemase_pyridoxalP-BS.
IPR029066. PLP-binding_barrel.
[Graphical view]
PfamiPF00842. Ala_racemase_C. 1 hit.
PF01168. Ala_racemase_N. 1 hit.
[Graphical view]
PRINTSiPR00992. ALARACEMASE.
SMARTiSM01005. Ala_racemase_C. 1 hit.
[Graphical view]
SUPFAMiSSF50621. SSF50621. 1 hit.
SSF51419. SSF51419. 1 hit.
TIGRFAMsiTIGR00492. alr. 1 hit.
PROSITEiPS00395. ALANINE_RACEMASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization of the alanine racemases from Pseudomonas aeruginosa PAO1."
    Strych U., Huang H.-C., Krause K.L., Benedik M.J.
    Curr. Microbiol. 41:290-294(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
    Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.
  3. "Crystal structure at 1.45 A resolution of alanine racemase from a pathogenic bacterium, Pseudomonas aeruginosa, contains both internal and external aldimine forms."
    LeMagueres P., Im H., Dvorak A., Strych U., Benedik M.J., Krause K.L.
    Biochemistry 42:14752-14761(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL PHOSPHATE AND LYSINE, COFACTOR, SUBUNIT, PYRIDOXAL PHOSPHATE AT LYS-33, CARBAMYLATION AT LYS-122.

Entry informationi

Entry nameiALR2_PSEAE
AccessioniPrimary (citable) accession number: Q9HTQ2
Secondary accession number(s): Q9S419
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 5, 2002
Last sequence update: March 1, 2001
Last modified: January 20, 2016
This is version 109 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, Complete proteome, Reference proteome

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.