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

B2SHB9 (ALR_FRATM) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 47. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Alanine racemase

EC=5.1.1.1
Gene names
Name:alr
Ordered Locus Names:FTM_1271
OrganismFrancisella tularensis subsp. mediasiatica (strain FSC147) [Complete proteome] [HAMAP]
Taxonomic identifier441952 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaThiotrichalesFrancisellaceaeFrancisella

Protein attributes

Sequence length365 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

Cofactor

Pyridoxal phosphate By similarity. HAMAP-Rule MF_01201

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.

Ontologies

Keywords
   LigandPyridoxal phosphate
   Molecular functionIsomerase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processD-alanine biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Molecular_functionalanine racemase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

pyridoxal phosphate binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 365365Alanine racemase HAMAP-Rule MF_01201
PRO_1000138599

Sites

Active site321Proton acceptor; specific for D-alanine By similarity
Active site2571Proton acceptor; specific for L-alanine By similarity
Binding site1281Substrate By similarity
Binding site3051Substrate; via amide nitrogen By similarity

Amino acid modifications

Modified residue321N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
B2SHB9 [UniParc].

Last modified July 1, 2008. Version 1.
Checksum: 90F5F4FE7B8BA060

FASTA36541,432
        10         20         30         40         50         60 
MNILKISKQT LRNNIKIIRE YIGNAKMCFP VKANAYGHGI EDIVENTHDL VDFFAVANSL 

        70         80         90        100        110        120 
EAFRVTAVAK NPVLVFGVIY YEYIEKMISE NIRVSIQDYE DIEKLEQIAK ELDKKVYAHI 

       130        140        150        160        170        180 
NINTGMNRMG VNYNDACRTI QRAYESDWLI LEGVYSHLAC ADNRDHPTNI KQKNRFDSIV 

       190        200        210        220        230        240 
KFTKGLSQDI ICHLSNSYGF LGQKGICYDM VRPGILSYGF LPEFYVDRVI REIKPIARLL 

       250        260        270        280        290        300 
SKVVKIITLQ EGEGVGYSLI YRGFEGEQLA VIPIGYGDGF PRELGDRGFV NINDVMYPMA 

       310        320        330        340        350        360 
GRMSMDGLTV SLGINEYDVK VGDTVELISA IPRNRNSAFS IAKQTNTIEY DIMSTLNDRI 


IRKII 

« Hide

References

[1]"Molecular evolutionary consequences of niche restriction in Francisella tularensis, a facultative intracellular pathogen."
Larsson P., Elfsmark D., Svensson K., Wikstroem P., Forsman M., Brettin T., Keim P., Johansson A.
PLoS Pathog. 5:E1000472-E1000472(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: FSC147.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000915 Genomic DNA. Translation: ACD31127.1.
RefSeqYP_001891906.1. NC_010677.1.

3D structure databases

ProteinModelPortalB2SHB9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING441952.FTM_1271.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACD31127; ACD31127; FTM_1271.
GeneID6291127.
KEGGftm:FTM_1271.
PATRIC17957405. VBIFraTul67519_1587.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0787.
HOGENOMHOG000263445.
KOK01775.
OMALWQLEAI.
OrthoDBEOG6PP9NJ.

Enzyme and pathway databases

BioCycFTUL441952:GIY0-1265-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.
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.
ProtoNetSearch...

Entry information

Entry nameALR_FRATM
AccessionPrimary (citable) accession number: B2SHB9
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: July 1, 2008
Last modified: June 11, 2014
This is version 47 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways