NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-21, AND CHARACTERIZATION.
DOI=10.1006/bbrc.2001.5817; PubMed=11676496 [NCBI, ExPASy, EBI, Israel, Japan]
Yokoigawa K., Hirasawa R., Ueno H., Okubo Y., Umesako S., Soda K.;
"Gene cloning and characterization of alanine racemases from Shigella dysenteriae, Shigella boydii, Shigella flexneri, and Shigella sonnei.";
Biochem. Biophys. Res. Commun. 288:676-684(2001).

Comments

FUNCTION: Provides the D-alanine required for cell wall biosynthesis.
CATALYTIC ACTIVITY: L-alanine = D-alanine.
COFACTOR: Pyridoxal phosphate.
BIOPHYSICOCHEMICAL PROPERTIES:

pH dependence: Optimum pH is 8-10;
Temperature dependence: Optimum temperature is 50 degrees Celsius;
PATHWAY: Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine from L-alanine: step 1/1 .
PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis .
SUBUNIT: Monomer but homodimer in the presence of the substrate.
SIMILARITY: Belongs to the alanine racemase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AB070926; BAB71771.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

P10724; 1BD0. [HSSP ENTRY / PDB]

ModBase

P0A6B6.

Ontologies

GO:0008784;	Molecular function: alanine racemase activity (inferred from electronic annotation from HAMAP).
GO:0030170;	Molecular function: pyridoxal phosphate binding (inferred from electronic annotation from HAMAP).
GO:0006522;	Biological process: alanine metabolic process (inferred from electronic annotation from HAMAP).
GO:0009252;	Biological process: peptidoglycan biosynthetic process (inferred from electronic annotation from HAMAP).
GO:0008360;	Biological process: regulation of cell shape (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

HAMAP

MF_01201; -; 1.
PBIL [Tree]

InterPro

IPR011079; Ala_racemase_C.
IPR001608; Ala_racemase_N.
IPR000821; Ala_racemase_reg.
Graphical view of domain structure.

Pfam

PF00842; Ala_racemase_C; 1.
PF01168; Ala_racemase_N; 1.
Pfam graphical view of domain structure.

PRINTS

PR00992; ALARACEMASE.

TIGRFAMs

TIGR00492; alr; 1.

PROSITE

PS00395; ALANINE_RACEMASE; 1.

Other

ProtoNet

P0A6B6.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Cell shape; Cell wall biogenesis/degradation; Direct protein sequencing; Isomerase; Peptidoglycan synthesis; Pyridoxal phosphate.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 359`	`359`	`Alanine racemase, biosynthetic.`	`PRO_0000114563`
`ACT_SITE`	`34 34`		`Proton acceptor; specific for D-alanine (By similarity).`
`ACT_SITE`	`255 255`		`Proton acceptor; specific for L-alanine (By similarity).`
`BINDING`	`34 34`		`Pyridoxal phosphate (covalent) (By similarity).`

Sequence information

Length: 359 AA [This is the length of the unprocessed precursor]

Molecular weight: 39153 Da [This is the MW of the unprocessed precursor]

CRC64: FDE9B438115342C2 [This is a checksum on the sequence]

        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

P0A6B6 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools