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Reviewed, UniProtKB/Swiss-Prot P10724 (ALR_BACST)

Last modified June 16, 2009. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Alanine racemase
    EC=5.1.1.1
Gene names
Name: alr
Synonyms: dal
OrganismBacillus stearothermophilus (Geobacillus stearothermophilus)
Taxonomic identifier1422 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeGeobacillus

Protein attributes

Sequence length388 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Provides the D-alanine required for cell wall biosynthesis. HAMAP MF_01201

Catalytic activity

L-alanine = D-alanine. HAMAP MF_01201

Cofactor

Pyridoxal phosphate. HAMAP MF_01201

Pathway

Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine from L-alanine: step 1/1. HAMAP MF_01201

Cell wall biogenesis; peptidoglycan biosynthesis. HAMAP MF_01201

Subunit structure

Homodimer. HAMAP MF_01201

Sequence similarities

Belongs to the alanine racemase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 388388Alanine racemase HAMAP MF_01201
PRO_0000114499

Sites

Active site391Proton acceptor; specific for D-alanine Ref.8
Active site2651Proton acceptor; specific for L-alanine Ref.8

Amino acid modifications

Modified residue391N6-(pyridoxal phosphate)lysine

Experimental info

Mutagenesis391K → A: Loss of activity. HAMAP MF_01201
Mutagenesis1661H → A: 6.5-fold decrease in activity. HAMAP MF_01201
Mutagenesis2191R → A: 100-fold decrease in activity. Ref.7
Mutagenesis2191R → E: 1000-fold decrease in activity. Ref.7
Mutagenesis2191R → K: 4-fold decrease in activity. Ref.7
Mutagenesis2651Y → A: 5000-fold decrease in activity. HAMAP MF_01201
Mutagenesis2651Y → F: Loss of activity. HAMAP MF_01201
Mutagenesis2651Y → S: 2000-fold decrease in activity. HAMAP MF_01201
Sequence conflict37 – 382VV → PP AA sequence Ref.3
Sequence conflict57 – 626AGASRL → RGPPP in AAA22220. Ref.1
Sequence conflict288 – 2892WL → V in AAA22220. Ref.1

Secondary structure

........................................................................... 388
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P10724-1 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: F54AA581F135EA7A

FASTA38843,593
        10         20         30         40         50         60 
MNDFHRDTWA EVDLDAIYDN VENLRRLLPD DTHIMAVVKA NAYGHGDVQV ARTALEAGAS 

        70         80         90        100        110        120 
RLAVAFLDEA LALREKGIEA PILVLGASRP ADAALAAQQR IALTVFRSDW LEEASALYSG 

       130        140        150        160        170        180 
PFPIHFHLKM DTGMGRLGVK DEEETKRIVA LIERHPHFVL EGLYTHFATA DEVNTDYFSY 

       190        200        210        220        230        240 
QYTRFLHMLE WLPSRPPLVH CANSAASLRF PDRTFNMVRF GIAMYGLAPS PGIKPLLPYP 

       250        260        270        280        290        300 
LKEAFSLHSR LVHVKKLQPG EKVSYGATYT AQTEEWIGTI PIGYADGWLR RLQHFHVLVD 

       310        320        330        340        350        360 
GQKAPIVGRI CMDQCMIRLP GPLPVGTKVT LIGRQGDEVI SIDDVARHLE TINYEVPCTI 

       370        380 
SYRVPRIFFR HKRIMEVRNA IGRGESSA 

« Hide

References

[1]"Thermostable alanine racemase from Bacillus stearothermophilus: DNA and protein sequence determination and secondary structure prediction."
Tanizawa K., Ohshima A., Scheidegger A., Inagaki K., Tanaka H., Soda K.
Biochemistry 27:1311-1316(1988) [PubMed: 2835089] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Mechanism of inactivation of alanine racemase by beta, beta, beta-trifluoroalanine."
Faraci W.S., Walsh C.T.
Biochemistry 28:431-437(1989) [PubMed: 2496744] [Abstract]
Cited for: PROTEIN SEQUENCE OF 31-43.
[3]"Time-dependent inhibition of Bacillus stearothermophilus alanine racemase by (1-aminoethyl)phosphonate isomers by isomerization to noncovalent slowly dissociating enzyme-(1-aminoethyl)phosphonate complexes."
Badet B., Inagaki K., Soda K., Walsh C.T.
Biochemistry 25:3275-3282(1986) [PubMed: 3730360] [Abstract]
Cited for: PROTEIN SEQUENCE OF 36-43.
[4]"Determination of the structure of alanine racemase from Bacillus stearothermophilus at 1.9-A resolution."
Shaw J.P., Petsko G.A., Ringe D.
Biochemistry 36:1329-1342(1997) [PubMed: 9063881] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), SEQUENCE REVISION.
[5]"Reaction of alanine racemase with 1-aminoethylphosphonic acid forms a stable external aldimine."
Stamper C.G., Morollo A.A., Ringe D.
Biochemistry 37:10438-10445(1998) [PubMed: 9671513] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
[6]"Structure of a Michaelis complex analogue: propionate binds in the substrate carboxylate site of alanine racemase."
Morollo A.A., Petsko G.A., Ringe D.
Biochemistry 38:3293-3301(1999) [PubMed: 10079072] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
Strain: ATCC 12980 / DSM 22 / IFO 12550 / NCIB 8923 / NCTC 10339.
[7]"Evidence for a two-base mechanism involving tyrosine-265 from arginine-219 mutants of alanine racemase."
Sun S., Toney M.D.
Biochemistry 38:4058-4065(1999) [PubMed: 10194319] [Abstract]
Cited for: MUTAGENESIS OF ARG-219.
[8]"Tyrosine 265 of alanine racemase serves as a base abstracting alpha-hydrogen from L-alanine: the counterpart residue to lysine 39 specific to D-alanine."
Watanabe A., Yoshimura T., Mikami B., Esaki N.
J. Biochem. 126:781-786(1999) [PubMed: 10502689] [Abstract]
Cited for: ACTIVE SITES, MUTAGENESIS.
+Additional computationally mapped references.

Cross-references

Sequence databases

M19142 Genomic DNA. Translation: AAA22220.1.
PIRA29984.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1BD0X-ray1.60A/B1-388[»]
1EPVX-ray2.20A/B2-388[»]
1FTXX-ray2.20A/B2-388[»]
1L6FX-ray2.00A/B1-388[»]
1L6GX-ray2.00A/B1-388[»]
1NIUX-ray2.20A/B1-388[»]
1SFTX-ray1.90A/B1-388[»]
1XQKX-ray1.95A/B1-382[»]
1XQLX-ray1.80A/B1-382[»]
2SFPX-ray1.90A/B1-388[»]
ModBaseSearch...

Enzyme and pathway databases

BRENDA5.1.1.1. 266715.

Family and domain databases

HAMAPMF_01201.
[Tree]
InterProIPR011079. Ala_racemase_C.
IPR001608. Ala_racemase_N.
IPR000821. Ala_racemase_reg.
[Graphical view]
PfamPF00842. Ala_racemase_C. 1 hit.
PF01168. Ala_racemase_N. 1 hit.
[Graphical view]
PRINTSPR00992. ALARACEMASE.
TIGRFAMsTIGR00492. alr. 1 hit.
PROSITEPS00395. ALANINE_RACEMASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameALR_BACST
AccessionPrimary (citable) accession number: P10724
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: November 1, 1997
Last modified: June 16, 2009
This is version 88 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents