Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

E8MS79 (E8MS79_BIFL1) Unreviewed, UniProtKB/TrEMBL

Last modified July 9, 2014. Version 25. 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

Protein attributes

Sequence length452 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 RuleBase RU004247

Sequence similarities

Belongs to the alanine racemase family. HAMAP-Rule MF_01201

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Sites

Active site631Proton acceptor; specific for D-alanine By similarity HAMAP-Rule MF_01201
Active site3031Proton acceptor; specific for L-alanine By similarity HAMAP-Rule MF_01201
Binding site1651Substrate By similarity HAMAP-Rule MF_01201
Binding site3671Substrate; via amide nitrogen By similarity HAMAP-Rule MF_01201

Amino acid modifications

Modified residue631N6-(pyridoxal phosphate)lysine By similarity HAMAP-Rule MF_01201

Sequences

Sequence LengthMass (Da)Tools
E8MS79 [UniParc].

Last modified April 5, 2011. Version 1.
Checksum: 75C28E8031FDD596

FASTA45248,328
        10         20         30         40         50         60 
MSMNAAPEIA FSSEQGKANY AAARRQYPAQ AIVNLKTMRD NMAHLVSVVG GPNSGTAVMG 

        70         80         90        100        110        120 
VVKADAYGHG LLPAALAALA GGATWLGTAQ SHEALLLRKL GIGPDRCRIL TWVYNGTEVP 

       130        140        150        160        170        180 
FDELIAADID VSVGSLPGID AVAAAARKLG KPARVHVKVD SGFGRNGFTP AGFDAALAKL 

       190        200        210        220        230        240 
VPLAKEGVLH IVGQWSHLAV ADSPDVPEFV SSTDRQIETF KDFTRRMEQA GIPPEIRHLA 

       250        260        270        280        290        300 
NTAATLDRPE IHFELTRPGI GLYGYEPDPA MGTPRDWHLT PAMRLQAQLG TVKDVEAGHG 

       310        320        330        340        350        360 
ISYGRTYLTP DNTSTAIVPL GYADGIHRSA SGFDMEGAKH VEKPGGPVRI MTTEGPKLYR 

       370        380        390        400        410        420 
VCGRVCMDQF IVDLHGSAAE LGVHEGDTVE LFGPGRGEDY VEPTADDWAR AADTISYEIF 

       430        440        450 
TCLRNRIPRL YEHAAEVLPA ADLAKLDPAT LL 

« Hide

References

[1]"Bifidobacteria can protect from enteropathogenic infection through production of acetate."
Fukuda S., Toh H., Hase K., Oshima K., Nakanishi Y., Yoshimura K., Tobe T., Clarke J.M., Topping D.L., Suzuki T., Taylor T.D., Itoh K., Kikuchi J., Morita H., Hattori M., Ohno H.
Nature 469:543-547(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 157F EMBL BAJ70623.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP010890 Genomic DNA. Translation: BAJ70623.1.
RefSeqYP_004208401.1. NC_015052.1.

3D structure databases

ProteinModelPortalE8MS79.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAJ70623; BAJ70623; BLIF_0479.
GeneID10207170.
KEGGblf:BLIF_0479.
PATRIC46884924. VBIBifLon182273_0492.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000031444.
KOK01775.
OMALWQLEAI.

Enzyme and pathway databases

BioCycBLON565040:GHFW-494-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 nameE8MS79_BIFL1
AccessionPrimary (citable) accession number: E8MS79
Entry history
Integrated into UniProtKB/TrEMBL: April 5, 2011
Last sequence update: April 5, 2011
Last modified: July 9, 2014
This is version 25 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)