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Q8X4I9 (ALR2_ECO57) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 90. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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, catabolic

EC=5.1.1.1
Gene names
Name:dadX
Synonyms:dadB
Ordered Locus Names:Z1953, ECs1685
OrganismEscherichia coli O157:H7 [Complete proteome] [HAMAP]
Taxonomic identifier83334 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length356 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Isomerizes L-alanine to D-alanine which is then oxidized to pyruvate by DadA 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

Sequence similarities

Belongs to the alanine racemase family.

Sequence caution

The sequence BAB35108.1 differs from that shown. Reason: Frameshift at position 321.

Ontologies

Keywords
   LigandPyridoxal phosphate
   Molecular functionIsomerase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processalanine metabolic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   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 – 356356Alanine racemase, catabolic HAMAP-Rule MF_01201
PRO_0000114519

Sites

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

Amino acid modifications

Modified residue351N6-(pyridoxal phosphate)lysine By similarity

Experimental info

Sequence conflict314 – 3152AG → RD in BAB35108. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q8X4I9 [UniParc].

Last modified March 5, 2002. Version 1.
Checksum: 28B67F19517A3B09

FASTA35638,859
        10         20         30         40         50         60 
MTRPIQASLD LQALKQNLSI VRQAAPHARV WSVVKANAYG HGIERIWSAL GATDGFALLN 

        70         80         90        100        110        120 
LEEAITLRER GWKGPILMLE GFFHAQDLEM YDQHRLTTCV HSNWQLKALQ NARLKAPLDI 

       130        140        150        160        170        180 
YLKVNSGMNR LGFQPDRVLT VWQQLRAMAN VGEMTLMSHF AEAEHPDGIS GAMARIEQAA 

       190        200        210        220        230        240 
EGLECRRSLS NSAATLWHPE AHFDWVRPGI ILYGASPSGQ WRDIANTGLR PVMTLSSEII 

       250        260        270        280        290        300 
GVQTLKAGER VGYGGRYTAR DEQRIGIVAA GYADGYPRHA PTGTPVLVDG VRTMTVGTVS 

       310        320        330        340        350 
MDMLAVDLTP CPQAGIGTPV ELWGKEIKID DVAAAAGTVG YELMCALALR VPVVTV 

« Hide

References

[1]"Genome sequence of enterohaemorrhagic Escherichia coli O157:H7."
Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., Davis N.W. expand/collapse author list , Lim A., Dimalanta E.T., Potamousis K., Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A., Blattner F.R.
Nature 409:529-533(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.
[2]"Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12."
Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T. expand/collapse author list , Kuhara S., Shiba T., Hattori M., Shinagawa H.
DNA Res. 8:11-22(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE005174 Genomic DNA. Translation: AAG56041.1.
BA000007 Genomic DNA. Translation: BAB35108.1. Frameshift.
PIRE85697.
E90839.
RefSeqNP_287429.1. NC_002655.2.

3D structure databases

ProteinModelPortalQ8X4I9.
SMRQ8X4I9. Positions 3-356.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING155864.Z1953.

Proteomic databases

PRIDEQ8X4I9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAG56041; AAG56041; Z1953.
BAB35108; BAB35108; BAB35108.
GeneID960219.
KEGGece:Z1953.
ecs:ECs1685.
PATRIC18352622. VBIEscCol44059_1536.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0787.
HOGENOMHOG000031446.
KOK01775.
OMAMAHFADA.
OrthoDBEOG6PP9NJ.
ProtClustDBPRK03646.

Enzyme and pathway databases

BioCycECOL386585:GJFA-1667-MONOMER.
ECOO157:DADX-MONOMER.

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 nameALR2_ECO57
AccessionPrimary (citable) accession number: Q8X4I9
Secondary accession number(s): Q8X2W4
Entry history
Integrated into UniProtKB/Swiss-Prot: March 5, 2002
Last sequence update: March 5, 2002
Last modified: March 19, 2014
This is version 90 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