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A7ZKW1 (A7ZKW1_ECO24) Unreviewed, UniProtKB/TrEMBL

Last modified February 19, 2014. Version 51. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Alanine racemase HAMAP-Rule MF_01201

EC=5.1.1.1 HAMAP-Rule MF_01201
Gene names
Name:alr1 EMBL ABV19018.1
Ordered Locus Names:EcE24377A_1335 EMBL ABV19018.1
OrganismEscherichia coli O139:H28 (strain E24377A / ETEC) [Complete proteome] [HAMAP] EMBL ABV19018.1
Taxonomic identifier331111 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length356 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. HAMAP-Rule MF_01201 RuleBase RU004188

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Sites

Active site351Proton acceptor; specific for D-alanine By similarity HAMAP-Rule MF_01201
Active site2531Proton acceptor; specific for L-alanine By similarity HAMAP-Rule MF_01201
Binding site1301Substrate By similarity HAMAP-Rule MF_01201
Binding site3011Substrate; 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
A7ZKW1 [UniParc].

Last modified October 23, 2007. Version 1.
Checksum: 817FAA44C8B3ED70

FASTA35638,871
        10         20         30         40         50         60 
MTRPIQASLD LQALKQNLSI VRQAAPHARV WSVVKANAYG HGIERIWSAL GATDGFALLN 

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

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

       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]"The pangenome structure of Escherichia coli: comparative genomic analysis of E. coli commensal and pathogenic isolates."
Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F., Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R., Henderson I.R., Sperandio V., Ravel J.
J. Bacteriol. 190:6881-6893(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: E24377A / ETEC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000800 Genomic DNA. Translation: ABV19018.1.
RefSeqYP_001462440.1. NC_009801.1.

3D structure databases

ProteinModelPortalA7ZKW1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING331111.EcE24377A_1335.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABV19018; ABV19018; EcE24377A_1335.
GeneID5590763.
KEGGecw:EcE24377A_1335.
PATRIC18291926. VBIEscCol31211_1624.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycECOL331111:GH7P-1325-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 nameA7ZKW1_ECO24
AccessionPrimary (citable) accession number: A7ZKW1
Entry history
Integrated into UniProtKB/TrEMBL: October 23, 2007
Last sequence update: October 23, 2007
Last modified: February 19, 2014
This is version 51 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)