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A3PIR7 (ALR_RHOS1) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 61. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Alanine racemase

EC=5.1.1.1
Gene names
Name:alr
Ordered Locus Names:Rsph17029_1123
OrganismRhodobacter sphaeroides (strain ATCC 17029 / ATH 2.4.9) [Complete proteome] [HAMAP]
Taxonomic identifier349101 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeRhodobacter

Protein attributes

Sequence length349 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids By similarity. HAMAP-Rule MF_01201

Catalytic activity

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

Cofactor

Pyridoxal phosphate By similarity. HAMAP-Rule MF_01201

Pathway

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

Sequence similarities

Belongs to the alanine racemase family.

Ontologies

Keywords
   LigandPyridoxal phosphate
   Molecular functionIsomerase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processD-alanine biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Molecular_functionalanine racemase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

pyridoxal phosphate binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 349349Alanine racemase HAMAP-Rule MF_01201
PRO_1000138617

Sites

Active site351Proton acceptor; specific for D-alanine By similarity
Active site2441Proton acceptor; specific for L-alanine By similarity
Binding site1301Substrate By similarity
Binding site2921Substrate; via amide nitrogen By similarity

Amino acid modifications

Modified residue351N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
A3PIR7 [UniParc].

Last modified April 3, 2007. Version 1.
Checksum: 1C8D83E8C5A21DB9

FASTA34937,052
        10         20         30         40         50         60 
MATATLTIDL DAIAANWRAL DQMTASDCQT GAVVKADSYG LGAAKVAHAL ARAGARRFFV 

        70         80         90        100        110        120 
ATCEEGADVR RALGSGPQIC VFSGHMEGDT ALIRDFDLTP MLNSIDQLTR HFEALGGQPF 

       130        140        150        160        170        180 
GLQLDSGMNR LGLEPGEWEA VAGFALEAGP ELLMSHLACS DDPDHPMNAE QLGAFRAMTD 

       190        200        210        220        230        240 
GTGVPRSLSA TGGILLGPAW HFELTRPGIG LYGGRPFEEA RPVVRLSLPV IQVREVEIGE 

       250        260        270        280        290        300 
PVGYSNTWTA EHTSTIATVA AGYADGLPRT LSSRATLYAG RVPCPLVGRV SMDLITVDVS 

       310        320        330        340 
HLPEVPETLD ILGPHQTPDD LADTAGTIGY EILTSLGRRY QRRYGALAA 

« Hide

References

[1]"Complete sequence of chromosome 1 of Rhodobacter sphaeroides ATCC 17029."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Richardson P., Mackenzie C., Choudhary M., Donohue T.J., Kaplan S.
Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 17029 / ATH 2.4.9.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000577 Genomic DNA. Translation: ABN76233.1.
RefSeqYP_001043005.1. NC_009049.1.

3D structure databases

ProteinModelPortalA3PIR7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING349101.Rsph17029_1123.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABN76233; ABN76233; Rsph17029_1123.
GeneID4895179.
KEGGrsh:Rsph17029_1123.
PATRIC23169976. VBIRhoSph114483_1299.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0787.
HOGENOMHOG000031445.
KOK01775.
OMARIGISIY.
OrthoDBEOG6PP9NJ.

Enzyme and pathway databases

BioCycRSPH349101:GHC8-1143-MONOMER.
UniPathwayUPA00042; UER00497.

Family and domain databases

Gene3D2.40.37.10. 1 hit.
3.20.20.10. 1 hit.
HAMAPMF_01201. Ala_racemase.
InterProIPR000821. Ala_racemase.
IPR009006. Ala_racemase/Decarboxylase_C.
IPR011079. Ala_racemase_C.
IPR001608. Ala_racemase_N.
IPR029066. PLP-binding_barrel.
[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. SSF50621. 1 hit.
SSF51419. SSF51419. 1 hit.
TIGRFAMsTIGR00492. alr. 1 hit.
ProtoNetSearch...

Entry information

Entry nameALR_RHOS1
AccessionPrimary (citable) accession number: A3PIR7
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: April 3, 2007
Last modified: June 11, 2014
This is version 61 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways