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E6SH16 (E6SH16_THEM7) Unreviewed, UniProtKB/TrEMBL

Last modified July 9, 2014. Version 23. Feed History...

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

Sequence length514 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 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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Sites

Active site451Proton acceptor; specific for D-alanine By similarity HAMAP-Rule MF_01201
Binding site1541Substrate By similarity HAMAP-Rule MF_01201
Binding site3581Substrate; via amide nitrogen By similarity HAMAP-Rule MF_01201

Amino acid modifications

Modified residue451N6-(pyridoxal phosphate)lysine By similarity HAMAP-Rule MF_01201

Sequences

Sequence LengthMass (Da)Tools
E6SH16 [UniParc].

Last modified March 8, 2011. Version 1.
Checksum: 1FCCC8D127210BA6

FASTA51453,114
        10         20         30         40         50         60 
MTWPAELAAA LARARIEVDL DVLAANLAAV RRFVRPGTRI LAVVKGDGYG LGAEMAARTL 

        70         80         90        100        110        120 
VAAGADGLGT DTLEAALRLR RAGITAPILV FQPVDPALAH HWVREGLTAT VHDETTLRRL 

       130        140        150        160        170        180 
AQAAESARAG QAARTGSPPG PCAVHLEVDM GFGRGGFHPD RVAAALAEAQ SLPGIRVEGL 

       190        200        210        220        230        240 
YAHFPTAARP GLALRLLDRF LRLVQRLEQQ GLRPPLVHCA ESHLLVLASH AQLDMVRVGN 

       250        260        270        280        290        300 
LLYGYAPRAA RRAGLAVRPP SRLVVRVGAV RRAASLDPGY RGGWARPGAP VAVLPVGLAD 

       310        320        330        340        350        360 
GLRPVREARF WSDRLVILAR RLLGALGASR VLGAAGLPPG PRLRVGGREV PLRGEFMMNH 

       370        380        390        400        410        420 
CLLDATGLDL EPGQEVELVV GRLTAAAHLP VVYLRGGRPV AVAWPQRQVV ELVAAPLAFP 

       430        440        450        460        470        480 
AGPASGTDGT APDSLAHAGL PAGHPAEVPL PAAEVPGGAG GDAGAGPVPA AVPGPVACAV 

       490        500        510 
QGPVAGPVPA PVRAPAGPVA ARRGPVRPDE ETVE 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP002344 Genomic DNA. Translation: ADU50647.1.
RefSeqYP_004101374.1. NC_014831.1.

3D structure databases

ProteinModelPortalE6SH16.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADU50647; ADU50647; Tmar_0526.
GeneID10080900.
KEGGtmr:Tmar_0526.
PATRIC45378226. VBITheMar50867_0529.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK01775.

Enzyme and pathway databases

BioCycTMAR644966:GHKT-556-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.
IPR001608. Ala_racemase_N.
IPR020622. Ala_racemase_pyridoxalP-BS.
IPR029066. PLP-binding_barrel.
[Graphical view]
PfamPF01168. Ala_racemase_N. 1 hit.
[Graphical view]
PRINTSPR00992. ALARACEMASE.
SUPFAMSSF50621. SSF50621. 2 hits.
SSF51419. SSF51419. 1 hit.
PROSITEPS00395. ALANINE_RACEMASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameE6SH16_THEM7
AccessionPrimary (citable) accession number: E6SH16
Entry history
Integrated into UniProtKB/TrEMBL: March 8, 2011
Last sequence update: March 8, 2011
Last modified: July 9, 2014
This is version 23 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)