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E8Y5H0 (E8Y5H0_ECOKO) Unreviewed, UniProtKB/TrEMBL

Last modified July 9, 2014. Version 32. 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:alr EMBL AFH15409.1
Ordered Locus Names:EKO11_4268 EMBL ADX52827.1
ORF Names:KO11_02100 EMBL AFH15409.1
OrganismEscherichia coli (strain ATCC 55124 / KO11) [Complete proteome] [HAMAP] EMBL ADX52827.1
Taxonomic identifier595495 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length359 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. SAAS SAAS020622 HAMAP-Rule MF_01201

Cofactor

Pyridoxal phosphate By similarity. SAAS SAAS020622 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. RuleBase RU004188 HAMAP-Rule MF_01201

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Sites

Active site341Proton acceptor; specific for D-alanine By similarity HAMAP-Rule MF_01201
Active site2551Proton acceptor; specific for L-alanine By similarity HAMAP-Rule MF_01201
Binding site1291Substrate By similarity HAMAP-Rule MF_01201
Binding site3031Substrate; via amide nitrogen By similarity HAMAP-Rule MF_01201

Amino acid modifications

Modified residue341N6-(pyridoxal phosphate)lysine By similarity HAMAP-Rule MF_01201

Sequences

Sequence LengthMass (Da)Tools
E8Y5H0 [UniParc].

Last modified April 5, 2011. Version 1.
Checksum: FDE9B438115342C2

FASTA35939,153
        10         20         30         40         50         60 
MQAATVVINR RALRHNLQRL RELAPASKMV AVVKANAYGH GLLETARTLP DADAFGVARL 

        70         80         90        100        110        120 
EEALRLRAGG ITKPVLLLEG FFDARDLPTI SAQHFHTAVH NEEQLAALEE ASLDEPVTVW 

       130        140        150        160        170        180 
MKLDTGMHRL GVRPEQAEAF YHRLTQCKNV RQPVNIVSHF ARADEPKCGA TEKQLAIFNT 

       190        200        210        220        230        240 
FCEGKPGQRS IAASGGILLW PQSHFDWVRP GIILYGVSPL EDRSTGADFG CQPVMSLTSS 

       250        260        270        280        290        300 
LIAVREHKAG EPVGYGGTWV SERDTRLGVV AMGYGDGYPR AAPSGTPVLV NGREVPIVGR 

       310        320        330        340        350 
VAMDMICVDL GPQAQDKAGD PVILWGEGLP VERIAEMTKV SAYELITRLT SRVAMKYVD 

« Hide

References

[1]"Complete sequence of chromosome of Escherichia coli KO11."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., Munk A.C., Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N., Ivanova N., Ovchinnikova G., Pagani I., Keating D., Landick R., Woyke T.
Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 55124 / KO11 and KO11 EMBL ADX52827.1.
[2]"Optical mapping and sequencing of the Escherichia coli KO11 genome reveal extensive chromosomal rearrangements, and multiple tandem copies of the Zymomonas mobilis pdc and adhB genes."
Turner P.C., Yomano L.P., Jarboe L.R., York S.W., Baggett C.L., Moritz B.E., Zentz E.B., Shanmugam K.T., Ingram L.O.
J. Ind. Microbiol. Biotechnol. 39:629-639(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: KO11FL EMBL AFH15409.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP002516 Genomic DNA. Translation: ADX52827.1.
CP002970 Genomic DNA. Translation: AFH15409.1.
RefSeqYP_005279891.1. NC_016902.1.
YP_006162761.1. NC_017660.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADX52827; ADX52827; EKO11_4268.
AFH15409; AFH15409; KO11_02100.
GeneID11778879.
12759929.
KEGGekf:KO11_02100.
eko:EKO11_4268.
PATRIC48648710. VBIEscCol13896_4337.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK01775.
OMALWQLEAI.

Enzyme and pathway databases

BioCycECOL595495:GI1Q-4351-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 nameE8Y5H0_ECOKO
AccessionPrimary (citable) accession number: E8Y5H0
Entry history
Integrated into UniProtKB/TrEMBL: April 5, 2011
Last sequence update: April 5, 2011
Last modified: July 9, 2014
This is version 32 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)