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E1QY34 (E1QY34_OLSUV) Unreviewed, UniProtKB/TrEMBL

Last modified July 9, 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 length386 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. RuleBase RU004247 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. RuleBase RU004247 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 site431Proton 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 site1411Substrate By similarity HAMAP-Rule MF_01201
Binding site3191Substrate; via amide nitrogen By similarity HAMAP-Rule MF_01201

Amino acid modifications

Modified residue431N6-(pyridoxal phosphate)lysine By similarity HAMAP-Rule MF_01201

Sequences

Sequence LengthMass (Da)Tools
E1QY34 [UniParc].

Last modified November 30, 2010. Version 1.
Checksum: 895098B851FD21B6

FASTA38642,248
        10         20         30         40         50         60 
MPNVSYPKNR WAWVEVDLNA IRKNTRAFKA LLEPRTQMMC AVKADAYGHG AVECAKAMAS 

        70         80         90        100        110        120 
SGASQFAVAT VDEGVELRRG GVAQPILMLN ECPLEGIDDL LAFDVMPSVY TSGFALAYGE 

       130        140        150        160        170        180 
RAVSLGKVGR YHLAIDTGMS RIGVLPEDVV EFRRMIDFHR GLECAGSFTH FATADAIGDW 

       190        200        210        220        230        240 
DFRQQSLRFS DAVSALEGAG LEVGLVHCDN TPGTVLHPEN HFDMCRVGIG LYGLQPSETT 

       250        260        270        280        290        300 
APRIALEPAM SVRARVTRVV NPAVGEGVGY GFTYRVPKPN IQIATVPVGY ADGLSRSLSN 

       310        320        330        340        350        360 
NMDVLVRGMR ARQVGRICMD QFMFAVDVND IRAYHPATAV ERGDVVTLIG RDGDDEISAD 

       370        380 
EMADRRDTIN YEVVCNFSQR LDRIFT 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP002106 Genomic DNA. Translation: ADK67298.1.
RefSeqYP_003800178.1. NC_014363.1.

3D structure databases

ProteinModelPortalE1QY34.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADK67298; ADK67298; Olsu_0166.
GeneID9500826.
KEGGols:Olsu_0166.
PATRIC42402227. VBIOlsUli28891_0164.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000031444.
KOK01775.

Enzyme and pathway databases

BioCycOULI633147:GHMD-174-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 nameE1QY34_OLSUV
AccessionPrimary (citable) accession number: E1QY34
Entry history
Integrated into UniProtKB/TrEMBL: November 30, 2010
Last sequence update: November 30, 2010
Last modified: July 9, 2014
This is version 29 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)