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Q0SP05 (Q0SP05_BORAP) Unreviewed, UniProtKB/TrEMBL

Last modified April 16, 2014. Version 77. Feed History...

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

Names and origin

Protein attributes

Sequence length366 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. SAAS SAAS009006 RuleBase RU004247 HAMAP-Rule MF_01201

Cofactor

Pyridoxal phosphate By similarity. SAAS SAAS009006 HAMAP-Rule MF_01201

Pathway

Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine from L-alanine: step 1/1. RuleBase RU004247 HAMAP-Rule MF_01201

Sequence similarities

Belongs to the alanine racemase family. RuleBase RU004188 HAMAP-Rule MF_01201

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Sites

Active site351Proton acceptor; specific for D-alanine By similarity HAMAP-Rule MF_01201
Active site2621Proton acceptor; specific for L-alanine By similarity HAMAP-Rule MF_01201
Binding site1331Substrate By similarity HAMAP-Rule MF_01201
Binding site3101Substrate; via amide nitrogen By similarity HAMAP-Rule MF_01201

Amino acid modifications

Modified residue351N6-(pyridoxal phosphate)lysine By similarity HAMAP-Rule MF_01201

Experimental info

Non-terminal residue11 EMBL ABQ43059.1
Non-terminal residue3661 EMBL ABQ43059.1

Sequences

Sequence LengthMass (Da)Tools
Q0SP05 [UniParc].

Last modified September 5, 2006. Version 1.
Checksum: DCD3E95D73B80FC3

FASTA36642,300
        10         20         30         40         50         60 
MSSNKTIIIN LNNLEHNLNL IKNKIGEKEI VATLKGDAYG HGLINIFKFF KAKKINYFGL 

        70         80         90        100        110        120 
SNIEDAKTLK KIDKSTKILM YIKVDKKEIK NLIKLELLPF VADFEYLFLI EKECALQKKK 

       130        140        150        160        170        180 
IKVHLKIDVG MNRYGIKIDS ALEIATYIQN SKFLELEGVC SHLPTTENFK ITQKQIEQFL 

       190        200        210        220        230        240 
FFLETLKQKN INPKFVHISN SGHIINYKLN PQFNMVRPGL ILYGYCPTLK NKKTTLNFKP 

       250        260        270        280        290        300 
VLNLFSKVVF IKNVKKGEKI SYSGTFQAKE DMKIGIIPIG YFDGIPQNIN NNFYFLINNK 

       310        320        330        340        350        360 
KCKIRGKVCM NLTIVEIPKD LKVETGSKVE IVSEKLSINE MSKFSKRSHY ELLCNIGKYE 


NRKYLD 

« Hide

References

« Hide 'large scale' references
[1]"Comparative genome analysis: selection pressure on the Borrelia vls cassettes is essential for infectivity."
Glockner G., Schulte-Spechtel U., Schilhabel M., Felder M., Suhnel J., Wilske B., Platzer M.
BMC Genomics 7:211-211(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PKo.
[2]"Comparative genome analysis: Selection pressure on the Borrelia vls cassettes is essential for infectivity."
Gloeckner G., Schulte-Spechtel U., Schilhabel M.B., Felder M., Suehnel J., Wilske B., Platzer M.
Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: PKo EMBL ABH01423.1.
[3]"Wide distribution of a high-virulence Borrelia burgdorferi clone in Europe and North America."
Qiu W.G., Bruno J.F., McCaig W.D., Xu Y., Livey I., Schriefer M.M., Luft B.J.
Emerg. Infect. Dis. 14:1097-1104(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Strain: PKo EMBL ABQ43059.1.
[4]"Whole-genome sequences of two Borrelia afzelii and two Borrelia garinii Lyme disease agent isolates."
Casjens S.R., Mongodin E.F., Qiu W.G., Dunn J.J., Luft B.J., Fraser-Liggett C.M., Schutzer S.E.
J. Bacteriol. 193:6995-6996(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PKo EMBL AEL69390.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000395 Genomic DNA. Translation: ABH01423.1.
EF537505 Genomic DNA. Translation: ABQ43059.1.
CP002933 Genomic DNA. Translation: AEL69390.1.
RefSeqYP_005592380.1. NC_017238.1.
YP_709599.1. NC_008277.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING390236.BAPKO_0161.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABH01423; ABH01423; BAPKO_0161.
AEL69390; AEL69390; BafPKo_0157.
GeneID12159112.
4227442.
KEGGbaf:BAPKO_0161.
bafz:BafPKo_0157.
PATRIC37188613. VBIBorAfz3878_0224.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0787.
HOGENOMHOG000031444.
KOK01775.
OMAADLYTVW.
OrthoDBEOG6PP9NJ.
ProtClustDBCLSK507396.

Enzyme and pathway databases

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.
IPR020622. Ala_racemase_pyridoxalP-BS.
[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.
TIGRFAMsTIGR00492. alr. 1 hit.
PROSITEPS00395. ALANINE_RACEMASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameQ0SP05_BORAP
AccessionPrimary (citable) accession number: Q0SP05
Entry history
Integrated into UniProtKB/TrEMBL: September 5, 2006
Last sequence update: September 5, 2006
Last modified: April 16, 2014
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)