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Protein

Alanine racemase, catabolic

Gene

dadX

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Isomerizes L-alanine to D-alanine which is then oxidized to pyruvate by DadA.By similarity

Catalytic activityi

L-alanine = D-alanine.

Cofactori

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei35 – 351Proton acceptor; specific for D-alanineBy similarity
Binding sitei130 – 1301SubstrateBy similarity
Active sitei253 – 2531Proton acceptor; specific for L-alanineBy similarity
Binding sitei301 – 3011Substrate; via amide nitrogenBy similarity

GO - Molecular functioni

  • alanine racemase activity Source: EcoCyc
  • pyridoxal phosphate binding Source: UniProtKB-HAMAP

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BioCyciEcoCyc:ALARACECAT-MONOMER.
ECOL316407:JW1179-MONOMER.
MetaCyc:ALARACECAT-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Alanine racemase, catabolic (EC:5.1.1.1)
Gene namesi
Name:dadX
Synonyms:alnB, dadB
Ordered Locus Names:b1190, JW1179
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11408. dadX.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 356356Alanine racemase, catabolicPRO_0000114517Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei35 – 351N6-(pyridoxal phosphate)lysineBy similarity

Proteomic databases

EPDiP29012.
PaxDbiP29012.
PRIDEiP29012.

Expressioni

Inductioni

By alanine.1 Publication

Interactioni

Protein-protein interaction databases

BioGridi4260105. 645 interactions.
DIPiDIP-9395N.
IntActiP29012. 2 interactions.
STRINGi511145.b1190.

Structurei

3D structure databases

ProteinModelPortaliP29012.
SMRiP29012. Positions 3-354.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the alanine racemase family.Curated

Phylogenomic databases

eggNOGiENOG4105CJ4. Bacteria.
COG0787. LUCA.
HOGENOMiHOG000031446.
InParanoidiP29012.
KOiK01775.
OMAiHMTHFSD.
PhylomeDBiP29012.

Family and domain databases

Gene3Di2.40.37.10. 1 hit.
3.20.20.10. 1 hit.
HAMAPiMF_01201. Ala_racemase. 1 hit.
InterProiIPR000821. 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]
PfamiPF00842. Ala_racemase_C. 1 hit.
PF01168. Ala_racemase_N. 1 hit.
[Graphical view]
PRINTSiPR00992. ALARACEMASE.
SMARTiSM01005. Ala_racemase_C. 1 hit.
[Graphical view]
SUPFAMiSSF50621. SSF50621. 1 hit.
SSF51419. SSF51419. 1 hit.
TIGRFAMsiTIGR00492. alr. 1 hit.
PROSITEiPS00395. ALANINE_RACEMASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P29012-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTRPIQASLD LQALKQNLSI VRQAATHARV WSVVKANAYG HGIERIWSAI
60 70 80 90 100
GATDGFALLN LEEAITLRER GWKGPILMLE GFFHAQDLEI YDQHRLTTCV
110 120 130 140 150
HSNWQLKALQ NARLKAPLDI YLKVNSGMNR LGFQPDRVLT VWQQLRAMAN
160 170 180 190 200
VGEMTLMSHF AEAEHPDGIS GAMARIEQAA EGLECRRSLS NSAATLWHPE
210 220 230 240 250
AHFDWVRPGI ILYGASPSGQ WRDIANTGLR PVMTLSSEII GVQTLKAGER
260 270 280 290 300
VGYGGRYTAR DEQRIGIVAA GYADGYPRHA PTGTPVLVDG VRTMTVGTVS
310 320 330 340 350
MDMLAVDLTP CPQAGIGTPV ELWGKEIKID DVAAAAGTVG YELMCALALR

VPVVTV
Length:356
Mass (Da):38,845
Last modified:November 1, 1997 - v2
Checksum:iFFF3226B47E5AAB3
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti172 – 1721A → R in AAC36881 (PubMed:7906689).Curated
Sequence conflicti215 – 2151A → R in AAC36881 (PubMed:7906689).Curated
Sequence conflicti281 – 2811P → L in AAC36881 (PubMed:7906689).Curated
Sequence conflicti349 – 3491L → V in AAC36881 (PubMed:7906689).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L02948 Unassigned DNA. Translation: AAC36881.1.
U00096 Genomic DNA. Translation: AAC74274.1.
AP009048 Genomic DNA. Translation: BAA36045.1.
PIRiC64865. C53383.
RefSeqiNP_415708.1. NC_000913.3.
WP_000197881.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC74274; AAC74274; b1190.
BAA36045; BAA36045; BAA36045.
GeneIDi945754.
KEGGiecj:JW1179.
eco:b1190.
PATRICi32117626. VBIEscCol129921_1235.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L02948 Unassigned DNA. Translation: AAC36881.1.
U00096 Genomic DNA. Translation: AAC74274.1.
AP009048 Genomic DNA. Translation: BAA36045.1.
PIRiC64865. C53383.
RefSeqiNP_415708.1. NC_000913.3.
WP_000197881.1. NZ_LN832404.1.

3D structure databases

ProteinModelPortaliP29012.
SMRiP29012. Positions 3-354.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260105. 645 interactions.
DIPiDIP-9395N.
IntActiP29012. 2 interactions.
STRINGi511145.b1190.

Proteomic databases

EPDiP29012.
PaxDbiP29012.
PRIDEiP29012.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74274; AAC74274; b1190.
BAA36045; BAA36045; BAA36045.
GeneIDi945754.
KEGGiecj:JW1179.
eco:b1190.
PATRICi32117626. VBIEscCol129921_1235.

Organism-specific databases

EchoBASEiEB1380.
EcoGeneiEG11408. dadX.

Phylogenomic databases

eggNOGiENOG4105CJ4. Bacteria.
COG0787. LUCA.
HOGENOMiHOG000031446.
InParanoidiP29012.
KOiK01775.
OMAiHMTHFSD.
PhylomeDBiP29012.

Enzyme and pathway databases

BioCyciEcoCyc:ALARACECAT-MONOMER.
ECOL316407:JW1179-MONOMER.
MetaCyc:ALARACECAT-MONOMER.

Miscellaneous databases

PROiP29012.

Family and domain databases

Gene3Di2.40.37.10. 1 hit.
3.20.20.10. 1 hit.
HAMAPiMF_01201. Ala_racemase. 1 hit.
InterProiIPR000821. 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]
PfamiPF00842. Ala_racemase_C. 1 hit.
PF01168. Ala_racemase_N. 1 hit.
[Graphical view]
PRINTSiPR00992. ALARACEMASE.
SMARTiSM01005. Ala_racemase_C. 1 hit.
[Graphical view]
SUPFAMiSSF50621. SSF50621. 1 hit.
SSF51419. SSF51419. 1 hit.
TIGRFAMsiTIGR00492. alr. 1 hit.
PROSITEiPS00395. ALANINE_RACEMASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiALR2_ECOLI
AccessioniPrimary (citable) accession number: P29012
Secondary accession number(s): O87498, P78246
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: November 1, 1997
Last modified: September 7, 2016
This is version 140 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.