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F8VEX5 (F8VEX5_SALBC) 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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Names and origin

Protein attributes

Sequence length356 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 RuleBase RU004188

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Sites

Active site351Proton acceptor; specific for D-alanine By similarity HAMAP-Rule MF_01201
Active site2531Proton acceptor; specific for L-alanine By similarity HAMAP-Rule MF_01201
Binding site1301Substrate By similarity HAMAP-Rule MF_01201
Binding site3011Substrate; via amide nitrogen By similarity HAMAP-Rule MF_01201

Amino acid modifications

Modified residue351N6-(pyridoxal phosphate)lysine By similarity HAMAP-Rule MF_01201

Sequences

Sequence LengthMass (Da)Tools
F8VEX5 [UniParc].

Last modified September 21, 2011. Version 1.
Checksum: 617A9BA2A5E9EEBF

FASTA35638,600
        10         20         30         40         50         60 
MTRPIQASLD LQAMKQNLAI VRRAAPEARV WSVVKANAYG HGIERVWGAL GATDGFAMLN 

        70         80         90        100        110        120 
LEEAITLRER GWKGPILMLE GFFHAQELEQ YDTYRLTTCI HSNWQLKALQ NARLNAPLDI 

       130        140        150        160        170        180 
YVKVNSGMNR LGFQPERAQT VWQQLRAIRN VGTMTLMSHF AQADHPEGIG EAMARIALAT 

       190        200        210        220        230        240 
EGLECPYSLS NSAATLWHPE AHYDWVRPGI ILYGASPSGL WRDIANTGLK PVMTLSSEII 

       250        260        270        280        290        300 
GVQTLKAGEK VGYGGCYTAG QEQRIGIVAA GYADGYPRHA PTGTPVLVDG IRTGTIGTVS 

       310        320        330        340        350 
MDMLAVDLTP CPQAGIGTPV ELWGKDIKVD DVASAAGTLG YELLCAVAPR VPFVTT 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
FR877557 Genomic DNA. Translation: CCC30737.1.
RefSeqYP_004730515.1. NC_015761.1.

3D structure databases

ProteinModelPortalF8VEX5.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCCC30737; CCC30737; SBG_1661.
GeneID10967583.
KEGGsbg:SBG_1661.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK01775.
OMAYGHGLER.

Enzyme and pathway databases

BioCycSBON218493:GJAH-1671-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 nameF8VEX5_SALBC
AccessionPrimary (citable) accession number: F8VEX5
Entry history
Integrated into UniProtKB/TrEMBL: September 21, 2011
Last sequence update: September 21, 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)