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Q73ET6 (Q73ET6_BACC1) Unreviewed, UniProtKB/TrEMBL

Last modified May 29, 2013. Version 76. Feed History...

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

Protein namesRecommended name:
Alanine racemase HAMAP-Rule MF_01201
EC=5.1.1.1 HAMAP-Rule MF_01201
Gene names
Name:dal EMBL AAS39208.1
Ordered Locus Names:BCE_0272 EMBL AAS39208.1
OrganismBacillus cereus (strain ATCC 10987) [Complete proteome] [HAMAP] EMBL AAS39208.1
Taxonomic identifier222523 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group ›

Protein attributes

Sequence length389 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 RuleBase RU000608 SAAS SAAS020622

Cofactor

Pyridoxal phosphate By similarity. HAMAP-Rule MF_01201 RuleBase RU000608 SAAS SAAS020622

Pathway

Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine from L-alanine: step 1/1. HAMAP-Rule MF_01201 RuleBase RU004247 SAAS SAAS020622

Sequence similarities

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

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
Q73ET6 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 4FEB93DB0B35B290

FASTA38943,592
        10         20         30         40         50         60 
MEEAPFYRDT WVEVDLDAIY NNVTHIKEFI PSGVEIFAVV 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 MIHLPCEVPL GTKVTLIGRQ GDEYISATEV AEYSGTINYE 

       370        380 
IITTISFRVP RIFIRNGKVV EVINYLNDI

« Hide

References

[1]"The genome sequence of Bacillus cereus ATCC 10987 reveals metabolic adaptations and a large plasmid related to Bacillus anthracis pXO1."
Rasko D.A., Ravel J., Okstad O.A., Helgason E., Cer R.Z., Jiang L., Shores K.A., Fouts D.E., Tourasse N.J., Angiuoli S.V., Kolonay J., Nelson W.C., Kolsto A.-B., Fraser C.M., Read T.D.
Nucleic Acids Res. 32:977-988(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 10987 EMBL AAS39208.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE017194 Genomic DNA. Translation: AAS39208.1.
RefSeqNP_976600.1. NC_003909.8.

3D structure databases

ProteinModelPortalQ73ET6.
SMRQ73ET6. Positions 4-389.
ModBaseSearch...

Protein-protein interaction databases

STRING222523.BCE_0272.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAS39208; AAS39208; BCE_0272.
GeneID2747492.
KEGGbca:BCE_0272.
PATRIC18849382. VBIBacCer118379_0267.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0787.
HOGENOMHOG000031444.
KOK01775.
OMADELGHHF.
ProtClustDBCLSK915752.

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. Racem_decarbox_C. 1 hit.
TIGRFAMsTIGR00492. alr. 1 hit.
PROSITEPS00395. ALANINE_RACEMASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameQ73ET6_BACC1
AccessionPrimary (citable) accession number: Q73ET6
Entry history
Integrated into UniProtKB/TrEMBL: July 5, 2004
Last sequence update: July 5, 2004
Last modified: May 29, 2013
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
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