P0A6B5 (ALR1_SHIFL) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Alanine racemase, biosynthetic
EC=5.1.1.1

Gene names

Name:	alr
Ordered Locus Names:	SF4152, S3578

Organism

Shigella flexneri [Complete proteome] [HAMAP]

Taxonomic identifier

623 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Shigella

Protein attributes

Sequence length	359 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the interconversion of L-alanine and D-alanine. Provides the D-alanine required for cell wall biosynthesis.
Catalytic activity	L-alanine = D-alanine. HAMAP-Rule MF_01201
Cofactor	Pyridoxal phosphate.
Pathway	Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine from L-alanine: step 1/1. HAMAP-Rule MF_01201 Cell wall biogenesis; peptidoglycan biosynthesis. HAMAP-Rule MF_01201
Subunit structure	Monomer but homodimer in the presence of the substrate.
Sequence similarities	Belongs to the alanine racemase family.
Biophysicochemical properties	pH dependence: Optimum pH is 8-10. HAMAP-Rule MF_01201 Temperature dependence: Optimum temperature is 50 degrees Celsius.

Ontologies

Keywords
Biological process	Cell shape Cell wall biogenesis/degradation Peptidoglycan synthesis
Ligand	Pyridoxal phosphate
Molecular function	Isomerase
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological_process	D-alanine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway peptidoglycan biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway regulation of cell shape Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	alanine racemase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 359	359	Alanine racemase, biosynthetic HAMAP-Rule MF_01201		PRO_0000114565
Sites
	Active site	34	1	Proton acceptor; specific for D-alanine By similarity
	Active site	255	1	Proton acceptor; specific for L-alanine By similarity
	Binding site	129	1	Substrate By similarity
	Binding site	303	1	Substrate; via amide nitrogen By similarity
Amino acid modifications
	Modified residue	34	1	N6-(pyridoxal phosphate)lysine By similarity
Experimental info
	Sequence conflict	138	1	E → G in BAB71772. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P0A6B5 [UniParc]. Last modified June 7, 2005. Version 1. Checksum: FDE9B438115342C2	FASTA	359	39,153
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Gene cloning and characterization of alanine racemases from Shigella dysenteriae, Shigella boydii, Shigella flexneri, and Shigella sonnei." Yokoigawa K., Hirasawa R., Ueno H., Okubo Y., Umesako S., Soda K. Biochem. Biophys. Res. Commun. 288:676-684(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-21, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
[2]	"Genome sequence of Shigella flexneri 2a: insights into pathogenicity through comparison with genomes of Escherichia coli K12 and O157." Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J., Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L., Xue Y. , Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H., Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J. Nucleic Acids Res. 30:4432-4441(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 301 / Serotype 2a.
[3]	"Complete genome sequence and comparative genomics of Shigella flexneri serotype 2a strain 2457T." Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G., Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T., Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R. Infect. Immun. 71:2775-2786(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700930 / 2457T / Serotype 2a.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB070927 Genomic DNA. Translation: BAB71772.1. AE005674 Genomic DNA. Translation: AAN45574.1. AE014073 Genomic DNA. Translation: AAP18624.1.
RefSeq	NP_709867.1. NC_004337.2. NP_838813.1. NC_004741.1.
3D structure databases
ProteinModelPortal	P0A6B5.
SMR	P0A6B5. Positions 1-359.
ModBase	Search...
Protein-protein interaction databases
STRING	198214.SF4152.
Proteomic databases
PaxDb	P0A6B5.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAN45574; AAN45574; SF4152. AAP18624; AAP18624; S3578.
GeneID	1025471. 1079800.
KEGG	sfl:SF4152. sfx:S3578.
PATRIC	18708936. VBIShiFle31049_3906.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0787.
HOGENOM	HOG000031446.
KO	K01775.
OMA	HQLETAV.
ProtClustDB	PRK00053.
Enzyme and pathway databases
BRENDA	5.1.1.1. 5712.
UniPathway	UPA00042; UER00497. UPA00219.
Family and domain databases
Gene3D	2.40.37.10. 1 hit.
HAMAP	MF_01201. Ala_racemase.
InterPro	IPR000821. Ala_racemase. IPR009006. Ala_racemase/Decarboxylase_C. IPR011079. Ala_racemase_C. IPR001608. Ala_racemase_N. IPR020622. Ala_racemase_pyridoxalP-BS. [Graphical view]
Pfam	PF00842. Ala_racemase_C. 1 hit. PF01168. Ala_racemase_N. 1 hit. [Graphical view]
PRINTS	PR00992. ALARACEMASE.
SMART	SM01005. Ala_racemase_C. 1 hit. [Graphical view]
SUPFAM	SSF50621. Racem_decarbox_C. 1 hit.
TIGRFAMs	TIGR00492. alr. 1 hit.
PROSITE	PS00395. ALANINE_RACEMASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	P0A6B5.

Entry information

Entry name

ALR1_SHIFL

Accession

Primary (citable) accession number: P0A6B5
Secondary accession number(s): P29743, P78136

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 7, 2005
Last sequence update:	June 7, 2005
Last modified:	May 1, 2013
This is version 65 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program