Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

B9J0N7 (B9J0N7_BACCQ) Unreviewed, UniProtKB/TrEMBL

Last modified July 9, 2014. Version 45. 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 namesRecommended name:
Alanine racemase HAMAP-Rule MF_01201 RuleBase RU004247

EC=5.1.1.1 HAMAP-Rule MF_01201 RuleBase RU004247
Gene names
Name:alr EMBL ACM10771.1
Ordered Locus Names:BCQ_0268 EMBL ACM10771.1
OrganismBacillus cereus (strain Q1) [Complete proteome] [HAMAP] EMBL ACM10771.1
Taxonomic identifier361100 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group

Protein attributes

Sequence length389 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. HAMAP-Rule MF_01201

Catalytic activity

L-alanine = D-alanine. HAMAP-Rule MF_01201 RuleBase RU004247 SAAS SAAS020622

Cofactor

Pyridoxal phosphate By similarity. HAMAP-Rule MF_01201 SAAS SAAS020622

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. HAMAP-Rule MF_01201 RuleBase RU004188

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Sites

Active site411Proton acceptor; specific for D-alanine By similarity HAMAP-Rule MF_01201
Active site2701Proton acceptor; specific for L-alanine By similarity HAMAP-Rule MF_01201
Binding site1381Substrate By similarity HAMAP-Rule MF_01201
Binding site3171Substrate; via amide nitrogen By similarity HAMAP-Rule MF_01201

Amino acid modifications

Modified residue411N6-(pyridoxal phosphate)lysine By similarity HAMAP-Rule MF_01201

Sequences

Sequence LengthMass (Da)Tools
B9J0N7 [UniParc].

Last modified March 24, 2009. Version 1.
Checksum: E26652ECAA0961A3

FASTA38943,649
        10         20         30         40         50         60 
MEEAPFYRDT WVEVDLDAIY NNVTHIKEFI PSDVEIFAVV KGNAYGHDYV PVAKTALEAG 

        70         80         90        100        110        120 
ATRLAVAFLD EALVLRRAGI TAPILVLGPS PPRDINVAAE NDVALTVFQK EWVDEAIKLW 

       130        140        150        160        170        180 
DGSSTMKYHI NFDSGMGRIG IRERKELKGF LKSLEGAPFL ELEGVYTHFA TADEVETSYF 

       190        200        210        220        230        240 
DKQYNTFLEQ LSWLKEFGVD PKFVHTANSA ATLRFQGITF NAVRIGIAMY GLSPSVEIRP 

       250        260        270        280        290        300 
FLPFKLEPAL SLHTKVAHIK QVIKGDGISY NVTYRTKTEE WIATVAIGYA DGWLRRLQGF 

       310        320        330        340        350        360 
EVLVNGKRVP IVGRVTMDQF MIHLPCKVPL GTKVTLIGRQ GDEYISATEV AEYSGTINYE 

       370        380 
IITTISFRVP RIFIRNGKVV EVINYLNDI 

« Hide

References

[1]"Complete genome sequence of the extremophilic Bacillus cereus strain Q1 with industrial applications."
Xiong Z., Jiang Y., Qi D., Lu H., Yang F., Yang J., Chen L., Sun L., Xu X., Xue Y., Zhu Y., Jin Q.
J. Bacteriol. 191:1120-1121(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Q1 EMBL ACM10771.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000227 Genomic DNA. Translation: ACM10771.1.
RefSeqYP_002528063.1. NC_011969.1.

3D structure databases

ProteinModelPortalB9J0N7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING361100.BCQ_0268.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACM10771; ACM10771; BCQ_0268.
GeneID7374484.
KEGGbcq:BCQ_0268.
PATRIC18907995. VBIBacCer120424_0243.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0787.
HOGENOMHOG000031444.
KOK01775.
OMAPSECAGV.
OrthoDBEOG6PP9NJ.

Enzyme and pathway databases

BioCycBCER361100:GJ7M-264-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.
IPR020622. Ala_racemase_pyridoxalP-BS.
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.
PROSITEPS00395. ALANINE_RACEMASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameB9J0N7_BACCQ
AccessionPrimary (citable) accession number: B9J0N7
Entry history
Integrated into UniProtKB/TrEMBL: March 24, 2009
Last sequence update: March 24, 2009
Last modified: July 9, 2014
This is version 45 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)