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Protein

Alanine racemase, biosynthetic

Gene

alr

Organism
Shigella flexneri
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the interconversion of L-alanine and D-alanine. Provides the D-alanine required for cell wall biosynthesis.1 Publication

Catalytic activityi

L-alanine = D-alanine.1 Publication

Cofactori

pyridoxal 5'-phosphate1 Publication

pH dependencei

Optimum pH is 8-10.1 Publication

Temperature dependencei

Optimum temperature is 50 degrees Celsius.1 Publication

Pathwayi: D-alanine biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes D-alanine from L-alanine.
Proteins known to be involved in this subpathway in this organism are:
  1. Alanine racemase (dadX), Alanine racemase (AJR26_013130), Alanine racemase (AJR27_018310), Alanine racemase (AJR25_000400), Alanine racemase, biosynthetic (alr), Alanine racemase (AJR26_020090)
This subpathway is part of the pathway D-alanine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes D-alanine from L-alanine, the pathway D-alanine biosynthesis and in Amino-acid biosynthesis.

Pathwayi: peptidoglycan biosynthesis

This protein is involved in the pathway peptidoglycan biosynthesis, which is part of Cell wall biogenesis.
View all proteins of this organism that are known to be involved in the pathway peptidoglycan biosynthesis and in Cell wall biogenesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei34Proton acceptor; specific for D-alanineBy similarity1
Binding sitei129SubstrateBy similarity1
Active sitei255Proton acceptor; specific for L-alanineBy similarity1
Binding sitei303Substrate; via amide nitrogenBy similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionIsomerase
Biological processCell shape, Cell wall biogenesis/degradation, Peptidoglycan synthesis
LigandPyridoxal phosphate

Enzyme and pathway databases

BRENDAi5.1.1.1. 5712.
UniPathwayiUPA00042; UER00497.
UPA00219.

Names & Taxonomyi

Protein namesi
Recommended name:
Alanine racemase, biosynthetic (EC:5.1.1.1)
Gene namesi
Name:alr
Ordered Locus Names:SF4152, S3578
OrganismiShigella flexneri
Taxonomic identifieri623 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeShigella
Proteomesi
  • UP000002673 Componenti: Chromosome
  • UP000001006 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001145651 – 359Alanine racemase, biosyntheticAdd BLAST359

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei34N6-(pyridoxal phosphate)lysineBy similarity1

Proteomic databases

PaxDbiP0A6B5.
PRIDEiP0A6B5.

Interactioni

Subunit structurei

Monomer but homodimer in the presence of the substrate.1 Publication

Structurei

3D structure databases

ProteinModelPortaliP0A6B5.
SMRiP0A6B5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the alanine racemase family.Curated

Phylogenomic databases

eggNOGiENOG4105CJ4. Bacteria.
COG0787. LUCA.
HOGENOMiHOG000031446.
KOiK01775.
OMAiWEILCGF.

Family and domain databases

Gene3Di2.40.37.10. 1 hit.
3.20.20.10. 1 hit.
HAMAPiMF_01201. Ala_racemase. 1 hit.
InterProiView protein in InterPro
IPR000821. Ala_racemase.
IPR009006. Ala_racemase/Decarboxylase_C.
IPR011079. Ala_racemase_C.
IPR001608. Ala_racemase_N.
IPR020622. Ala_racemase_pyridoxalP-BS.
IPR029066. PLP-binding_barrel.
PfamiView protein in Pfam
PF00842. Ala_racemase_C. 1 hit.
PF01168. Ala_racemase_N. 1 hit.
PRINTSiPR00992. ALARACEMASE.
SMARTiView protein in SMART
SM01005. Ala_racemase_C. 1 hit.
SUPFAMiSSF50621. SSF50621. 1 hit.
SSF51419. SSF51419. 1 hit.
TIGRFAMsiTIGR00492. alr. 1 hit.
PROSITEiView protein in PROSITE
PS00395. ALANINE_RACEMASE. 1 hit.

Sequencei

Sequence statusi: Complete.

P0A6B5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQAATVVINR RALRHNLQRL RELAPASKMV AVVKANAYGH GLLETARTLP
60 70 80 90 100
DADAFGVARL EEALRLRAGG ITKPVLLLEG FFDARDLPTI SAQHFHTAVH
110 120 130 140 150
NEEQLAALEE ASLDEPVTVW MKLDTGMHRL GVRPEQAEAF YHRLTQCKNV
160 170 180 190 200
RQPVNIVSHF ARADEPKCGA TEKQLAIFNT FCEGKPGQRS IAASGGILLW
210 220 230 240 250
PQSHFDWVRP GIILYGVSPL EDRSTGADFG CQPVMSLTSS LIAVREHKAG
260 270 280 290 300
EPVGYGGTWV SERDTRLGVV AMGYGDGYPR AAPSGTPVLV NGREVPIVGR
310 320 330 340 350
VAMDMICVDL GPQAQDKAGD PVILWGEGLP VERIAEMTKV SAYELITRLT

SRVAMKYVD
Length:359
Mass (Da):39,153
Last modified:June 7, 2005 - v1
Checksum:iFDE9B438115342C2
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti138E → G in BAB71772 (PubMed:11676496).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB070927 Genomic DNA. Translation: BAB71772.1.
AE005674 Genomic DNA. Translation: AAN45574.1.
AE014073 Genomic DNA. Translation: AAP18624.1.
RefSeqiNP_709867.1. NC_004337.2.
WP_001147328.1. NZ_MSKF02000025.1.

Genome annotation databases

EnsemblBacteriaiAAN45574; AAN45574; SF4152.
AAP18624; AAP18624; S3578.
GeneIDi1025471.
KEGGisfl:SF4152.
sfx:S3578.
PATRICifig|198214.7.peg.4899.

Similar proteinsi

Entry informationi

Entry nameiALR1_SHIFL
AccessioniPrimary (citable) accession number: P0A6B5
Secondary accession number(s): P29743, P78136
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: June 7, 2005
Last modified: September 27, 2017
This is version 91 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families