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E8VAB8 (E8VAB8_BACST) Unreviewed, UniProtKB/TrEMBL

Last modified July 9, 2014. Version 28. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

Names and origin

Protein attributes

Sequence length389 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 RuleBase RU004247 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 site411Proton acceptor; specific for D-alanine By similarity HAMAP-Rule MF_01201
Active site2661Proton acceptor; specific for L-alanine By similarity HAMAP-Rule MF_01201
Binding site1371Substrate By similarity HAMAP-Rule MF_01201
Binding site3131Substrate; via amide nitrogen By similarity HAMAP-Rule MF_01201

Amino acid modifications

Modified residue411N6-(pyridoxal phosphate)lysine By similarity HAMAP-Rule MF_01201

Sequences

Sequence LengthMass (Da)Tools
E8VAB8 [UniParc].

Last modified April 5, 2011. Version 1.
Checksum: 4802B7C182ACCD58

FASTA38943,265
        10         20         30         40         50         60 
MSTKPFYRDT WAEIDLSAIK ENVSNMKKHI GEHVHLMAVV KANAYGHGDA ETAKAALDAG 

        70         80         90        100        110        120 
ASCLAVAILD EAISLRKKGL KAPILVLGAV PPEYVAIAAE YDVTLTGYSV EWLQEAARHT 

       130        140        150        160        170        180 
KKGSLHFHLK VDTGMNRLGV KTEEEVQNVM AILDRNPRLK CKGVFTHFAT ADEKERGYFL 

       190        200        210        220        230        240 
MQFERFKELI APLPLKNLMV HCANSAAGLR LKKGFFNAVR FGIGMYGLRP SADMSDEIPF 

       250        260        270        280        290        300 
QLRPAFTLHS TLSHVKLIRK GESVSYGAEY TAEKDTWIGT VPVGYADGWL RKLKGTDILV 

       310        320        330        340        350        360 
KGKRLKIAGR ICMDQFMVEL DQEYPPGTKV TLIGRQGDEY ISMDEIAGRL ETINYEVACT 

       370        380 
ISSRVPRMFL ENGSIMEVRN PLLQVNISN 

« Hide

References

« Hide 'large scale' references
[1]"Complete genome sequence of Bacillus subtilis BSn5, an endophytic bacterium of Amorphophallus konjac with antimicrobial activity for the plant pathogen Erwinia carotovora subsp. carotovora."
Deng Y., Zhu Y., Wang P., Zhu L., Zheng J., Li R., Ruan L., Peng D., Sun M.
J. Bacteriol. 193:2070-2071(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: BSn5 EMBL ADV95398.1.
[2]"Complete Genome Sequence of Bacillus Subtilis BSn5, a Strain of Plant-associated Bacterium with Antimicrobial Activity to Soil-borne Plant Pathogens."
Deng Y., Sun M.
Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: BSn5.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP002468 Genomic DNA. Translation: ADV95398.1.
RefSeqYP_004206425.1. NC_014976.1.

3D structure databases

ProteinModelPortalE8VAB8.
SMRE8VAB8. Positions 4-382.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADV95398; ADV95398; BSn5_13950.
GeneID10183488.
KEGGbsn:BSn5_13950.
PATRIC46872934. VBIBacSub180317_2847.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000031444.
KOK01775.

Enzyme and pathway databases

BioCycBSUB936156:GHCY-2840-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 nameE8VAB8_BACST
AccessionPrimary (citable) accession number: E8VAB8
Entry history
Integrated into UniProtKB/TrEMBL: April 5, 2011
Last sequence update: April 5, 2011
Last modified: July 9, 2014
This is version 28 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)