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D5ECS6 (D5ECS6_AMICL) Unreviewed, UniProtKB/TrEMBL

Last modified July 9, 2014. Version 35. 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 attributes

Sequence length374 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

Cofactor

Pyridoxal phosphate By similarity. HAMAP-Rule MF_01201 SAAS SAAS001608

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 site371Proton acceptor; specific for D-alanine By similarity HAMAP-Rule MF_01201
Active site2641Proton acceptor; specific for L-alanine By similarity HAMAP-Rule MF_01201
Binding site1351Substrate By similarity HAMAP-Rule MF_01201
Binding site3131Substrate; via amide nitrogen By similarity HAMAP-Rule MF_01201

Amino acid modifications

Modified residue371N6-(pyridoxal phosphate)lysine By similarity HAMAP-Rule MF_01201

Sequences

Sequence LengthMass (Da)Tools
D5ECS6 [UniParc].

Last modified June 15, 2010. Version 1.
Checksum: EBADE8BFCFA1E59F

FASTA37440,802
        10         20         30         40         50         60 
MSWRPTRLEV DLEKVRNNYR AIRKHVGESV RIFGVVKGDA YNLGADKIGR VLADMGVDFF 

        70         80         90        100        110        120 
AVATGDEAIS LRESGIESPI LVLGPSPYGI AEEYVRLGIR AAINDKGIAK ALSDASVRLQ 

       130        140        150        160        170        180 
KPAYGHVKID SGMGRIGFFP HEAADAVEEI SHLPGLNLEG IFTHFAISDA RDLTYTYEQH 

       190        200        210        220        230        240 
STFVKVIGEL EKRGITFSIK HCCNSGATLA LPQFVMDGVR PGQLVVGMYP SKEVVRSIAI 

       250        260        270        280        290        300 
EPVFEFKTAI SAIRTVPAGK KLSYGLTYET TADERIAVIP VGYHDGYSRE LSGKGTEVLI 

       310        320        330        340        350        360 
HGKRCPIVGR ICMDQALVDV SVLQNPQIGD EVVLLGKQGE ETITGDEIAD KIGTIFTTLP 

       370 
NMIGKRVPRV YLNE 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001997 Genomic DNA. Translation: ADE56358.1.
RefSeqYP_003553082.1. NC_014011.1.

3D structure databases

ProteinModelPortalD5ECS6.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADE56358; ADE56358; Amico_0212.
GeneID8963110.
KEGGaco:Amico_0212.
PATRIC35452560. VBIAmiCol31354_0222.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000031444.
KOK01775.
OMAHVANSYI.

Enzyme and pathway databases

BioCycACOL572547:GHQ0-212-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.
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.
ProtoNetSearch...

Entry information

Entry nameD5ECS6_AMICL
AccessionPrimary (citable) accession number: D5ECS6
Entry history
Integrated into UniProtKB/TrEMBL: June 15, 2010
Last sequence update: June 15, 2010
Last modified: July 9, 2014
This is version 35 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)