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E0SEJ8 (E0SEJ8_DICD3) Unreviewed, UniProtKB/TrEMBL

Last modified April 16, 2014. Version 29. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Protein attributes

Sequence length358 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 SAAS SAAS009006

Cofactor

Pyridoxal phosphate By similarity. HAMAP-Rule MF_01201 SAAS SAAS009006

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Sites

Active site341Proton acceptor; specific for D-alanine By similarity HAMAP-Rule MF_01201
Active site2541Proton acceptor; specific for L-alanine By similarity HAMAP-Rule MF_01201
Binding site1291Substrate By similarity HAMAP-Rule MF_01201
Binding site3021Substrate; via amide nitrogen By similarity HAMAP-Rule MF_01201

Amino acid modifications

Modified residue341N6-(pyridoxal phosphate)lysine By similarity HAMAP-Rule MF_01201

Sequences

Sequence LengthMass (Da)Tools
E0SEJ8 [UniParc].

Last modified November 2, 2010. Version 1.
Checksum: F5A96642E0B86506

FASTA35838,924
        10         20         30         40         50         60 
MKTATAVIDR QALRHNLQRI RQMAPQSRLI AIVKANAYGH GAVEAARAFS DADGYGVSRL 

        70         80         90        100        110        120 
SEALALRAAG ITKPILLLEG FFAADELPLL AEHQLETAVH CEEQLAALEQ ARLPHPLTVW 

       130        140        150        160        170        180 
MKLDTGMHRL GVLPEKAEAF YARLSACANV VQPVNIMSHF CRADEPQAGT TQHQLDCFDA 

       190        200        210        220        230        240 
FVQDKPGRQS IAASGGILLW PQTHRDQIRP GIIQYGVSPL AQGDASQWQL KPAMTLTSHL 

       250        260        270        280        290        300 
IAVREHHADE PVGYGGTWTS PRATRMGVIA IGYGDGYPRD AKSGTPVWIN GREVPLSGRV 

       310        320        330        340        350 
SMDMITVDLG PNAQDKVGDE VILWGGPLPV EKVAAHSGIS AYELITRLTS RTRLEYIG 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP002038 Genomic DNA. Translation: ADM99932.1.
RefSeqYP_003884489.1. NC_014500.1.

3D structure databases

ProteinModelPortalE0SEJ8.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADM99932; ADM99932; Dda3937_03446.
GeneID9735211.
KEGGddd:Dda3937_03446.
PATRIC42319777. VBIDicDad25310_3677.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000031446.
KOK01775.
OMAINNQLAP.

Enzyme and pathway databases

BioCycDDAD198628:GHFQ-3826-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.
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 nameE0SEJ8_DICD3
AccessionPrimary (citable) accession number: E0SEJ8
Entry history
Integrated into UniProtKB/TrEMBL: November 2, 2010
Last sequence update: November 2, 2010
Last modified: April 16, 2014
This is version 29 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)