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E1V7Q5 (E1V7Q5_HALED) Unreviewed, UniProtKB/TrEMBL

Last modified February 19, 2014. Version 27. Feed History...

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

Sequence length366 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. RuleBase RU004188 HAMAP-Rule MF_01201

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Sites

Active site351Proton acceptor; specific for D-alanine By similarity HAMAP-Rule MF_01201
Active site2561Proton acceptor; specific for L-alanine By similarity HAMAP-Rule MF_01201
Binding site1311Substrate By similarity HAMAP-Rule MF_01201
Binding site3041Substrate; 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
E1V7Q5 [UniParc].

Last modified November 30, 2010. Version 1.
Checksum: 65C9103CEFFC0470

FASTA36639,342
        10         20         30         40         50         60 
MARPLRADID LDALCHNYRL ARDLAPTSRS LAVLKADAYG HGLVPCARAL EGLAPAFAVA 

        70         80         90        100        110        120 
CLEEAEALRE GGITAPIVLL EGIFSADELA RVEALKLGTV VHSDWQVEAL LSHRPAEPIP 

       130        140        150        160        170        180 
TWVKVDSGMH RLGFAPERAA SVWARLSAAP AQACDLHLMS HFATADHADT AYFEHQMRTL 

       190        200        210        220        230        240 
NALAETLNAP TCLANSPATL ARPESHGAWN RPGVMLYGSD PLEASNSASR ELEPVMTLRS 

       250        260        270        280        290        300 
QLIAVRDLDE GEPVGYGGRW RAPRPSRIGV VACGYGDGYD RHAIDGTPAL VAGRRTTLVG 

       310        320        330        340        350        360 
KVSMDMLTVD LTDIPEADIG SEVVLWGRAA NGEVLSVDEV ARHCDTISYT LLTGVLPRVP 


RRYHSG 

« Hide

References

[1]"A blueprint of ectoine metabolism from the genome of the industrial producer Halomonas elongata DSM 2581(T)."
Schwibbert K., Marin-Sanguino A., Bagyan I., Heidrich G., Lentzen G., Seitz H., Rampp M., Schuster S.C., Klenk H.P., Pfeiffer F., Oesterhelt D., Kunte H.J.
Environ. Microbiol. 13:1973-1994(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 33173 / DSM 2581 / NBRC 15536 / NCIMB 2198 / 1H9.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
FN869568 Genomic DNA. Translation: CBV43493.1.
RefSeqYP_003898678.1. NC_014532.1.

3D structure databases

ProteinModelPortalE1V7Q5.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCBV43493; CBV43493; HELO_3609.
GeneID9747860.
KEGGhel:HELO_3609.
PATRIC42356781. VBIHalElo161731_2804.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000031446.
KOK01775.
OMAINNQLAP.

Enzyme and pathway databases

BioCycHELO768066:GJEE-2677-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 nameE1V7Q5_HALED
AccessionPrimary (citable) accession number: E1V7Q5
Entry history
Integrated into UniProtKB/TrEMBL: November 30, 2010
Last sequence update: November 30, 2010
Last modified: February 19, 2014
This is version 27 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)