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Q8RSU9 (ALR_CORGL) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 80. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Alanine racemase
EC=5.1.1.1
Gene names
Name:alr
Ordered Locus Names:Cgl0588, cg0681
OrganismCorynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025) [Reference proteome] [HAMAP]
Taxonomic identifier196627 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Corynebacteriaceae › Corynebacterium ›

Protein attributes

Sequence length361 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids By similarity.

Catalytic activity

L-alanine = D-alanine. HAMAP-Rule MF_01201

Cofactor

Pyridoxal phosphate.

Pathway

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

Subunit structure

Homodimer Probable.

Sequence similarities

Belongs to the alanine racemase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 361361Alanine racemase HAMAP-Rule MF_01201
PRO_0000114512

Sites

Active site341Proton acceptor; specific for D-alanine By similarity
Active site2561Proton acceptor; specific for L-alanine By similarity
Binding site1291Substrate By similarity
Binding site3041Substrate; via amide nitrogen By similarity

Amino acid modifications

Modified residue341N6-(pyridoxal phosphate)lysine

Secondary structure

1 .............................................................. 361
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q8RSU9 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: 6E95CAF6456B6037

FASTA36139,174
        10         20         30         40         50         60 
MNLLTTKIDL DAIAHNTRVL KQMAGPAKLM AVVKANAYNH GVEKVAPVIA AHGADAFGVA 

        70         80         90        100        110        120 
TLAEAMQLRD IGISQEVLCW IWTPEQDFRA AIDRNIDLAV ISPAHAKALI ETDAEHIRVS 

       130        140        150        160        170        180 
IKIDSGLHRS GVDEQEWEGV FSALAAAPHI EVTGMFTHLA CADEPENPET DRQIIAFRRA 

       190        200        210        220        230        240 
LALARKHGLE CPVNHVCNSP AFLTRSDLHM EMVRPGLAFY GLEPVAGLEH GLKPAMTWEA 

       250        260        270        280        290        300 
KVSVVKQIEA GQGTSYGLTW RAEDRGFVAV VPAGYADGMP RHAQGKFSVT IDGLDYPQVG 

       310        320        330        340        350        360 
RVCMDQFVIS LGDNPHGVEA GAKAVIFGEN GHDATDFAER LDTINYEVVC RPTGRTVRAY 


V

« Hide

References

« Hide 'large scale' references
[1]"The alanine racemase gene alr is an alternative to antibiotic resistance genes in cloning systems for industrial Corynebacterium glutamicum strains."
Tauch A., Goetker S., Puehler A., Kalinowski J., Thierbach G.
J. Biotechnol. 99:79-91(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
[2]"The Corynebacterium glutamicum genome: features and impacts on biotechnological processes."
Ikeda M., Nakagawa S.
Appl. Microbiol. Biotechnol. 62:99-109(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
[3]"The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its impact on the production of L-aspartate-derived amino acids and vitamins."
Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A., Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A., Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F., Moeckel B. expand/collapse author list , Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O., Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.
J. Biotechnol. 104:5-25(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
[4]"Crystal structure of alanine racemase from Corynebacterium glutamicum at 2.1 A resolution."
Miyaguchi I., Sasaki C., Kato R., Oikawa T., Sugio S.
Submitted (SEP-2006) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL PHOSPHATE, COFACTOR, SUBUNIT, PYRIDOXAL PHOSPHATE AT LYS-34.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AY077456 Genomic DNA. Translation: AAL77207.1.
BA000036 Genomic DNA. Translation: BAB97981.1.
BX927149 Genomic DNA. Translation: CAF19293.1.
RefSeqNP_599824.1. NC_003450.3.
YP_224879.1. NC_006958.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2DY3X-ray2.10A/B/C/D1-361[»]
ProteinModelPortalQ8RSU9.
SMRQ8RSU9. Positions 1-361.
ModBaseSearch...

Protein-protein interaction databases

STRING196627.cg0681.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAB97981; BAB97981; BAB97981.
CAF19293; CAF19293; cg0681.
GeneID1018592.
3343955.
KEGGcgb:cg0681.
cgl:NCgl0563.
PATRIC21493226. VBICorGlu203724_0579.

Phylogenomic databases

eggNOGCOG0787.
HOGENOMHOG000031444.
KOK01775.
OMANFKSIEI.
ProtClustDBPRK00053.

Enzyme and pathway databases

BioCycCGLU196627:GJDM-586-MONOMER.
UniPathwayUPA00042; UER00497.

Family and domain databases

Gene3D2.40.37.10. 1 hit.
HAMAPMF_01201. Ala_racemase.
InterProIPR000821. Ala_racemase.
IPR009006. Ala_racemase/Decarboxylase_C.
IPR011079. Ala_racemase_C.
IPR001608. Ala_racemase_N.
[Graphical view]
PfamPF00842. Ala_racemase_C. 1 hit.
PF01168. Ala_racemase_N. 1 hit.
[Graphical view]
PRINTSPR00992. ALARACEMASE.
SMARTSM01005. Ala_racemase_C. 1 hit.
[Graphical view]
SUPFAMSSF50621. Racem_decarbox_C. 1 hit.
TIGRFAMsTIGR00492. alr. 1 hit.
PROSITEPS00395. ALANINE_RACEMASE. False negative.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ8RSU9.

Entry information

Entry nameALR_CORGL
AccessionPrimary (citable) accession number: Q8RSU9
Entry history
Integrated into UniProtKB/Swiss-Prot: October 10, 2002
Last sequence update: June 1, 2002
Last modified: May 1, 2013
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

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

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