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Protein

Alanine racemase

Gene

alr

Organism
Streptomyces lavendulae subsp. lavendulae
Status
Unreviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids.UniRule annotation

Catalytic activityi

L-alanine = D-alanine.UniRule annotationSAAS annotation

Cofactori

pyridoxal 5'-phosphateUniRule annotation

Pathwayi: D-alanine biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes D-alanine from L-alanine.UniRule annotation
Proteins known to be involved in this subpathway in this organism are:
  1. Alanine racemase (alr)
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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei38 – 381Proton acceptor; specific for D-alanineUniRule annotation
Binding sitei136 – 1361SubstrateUniRule annotation
Active sitei270 – 2701Proton acceptor; specific for L-alanineUniRule annotation
Binding sitei318 – 3181Substrate; via amide nitrogenUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

IsomeraseUniRule annotationSAAS annotation

Keywords - Ligandi

Pyridoxal phosphateUniRule annotationSAAS annotation

Enzyme and pathway databases

BRENDAi5.1.1.1. 133.
UniPathwayiUPA00042; UER00497.

Names & Taxonomyi

Protein namesi
Recommended name:
Alanine racemaseUniRule annotation (EC:5.1.1.1UniRule annotation)
Gene namesi
Name:alrImported
OrganismiStreptomyces lavendulae subsp. lavendulaeImported
Taxonomic identifieri58340 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaStreptomycetalesStreptomycetaceaeStreptomyces

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei38 – 381N6-(pyridoxal phosphate)lysineUniRule annotationCombined sources

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1VFHX-ray2.00A1-378[»]
1VFSX-ray1.90A/B1-378[»]
1VFTX-ray2.30A/B1-378[»]
ProteinModelPortaliQ65YW7.
SMRiQ65YW7. Positions 3-378.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ65YW7.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini249 – 376128Ala_racemase_CInterPro annotationAdd
BLAST

Sequence similaritiesi

Belongs to the alanine racemase family.UniRule annotationSAAS annotation

Family and domain databases

Gene3Di2.40.37.10. 1 hit.
3.20.20.10. 1 hit.
HAMAPiMF_01201. Ala_racemase.
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.

Q65YW7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNETPTRVYA EIDLDAVRAN VRALRARAPR SALMAVVKSN AYGHGAVPCA
60 70 80 90 100
RAAQEAGAAW LGTATPEEAL ELRAAGIQGR IMCWLWTPGG PWREAIETDI
110 120 130 140 150
DVSVSGMWAL DEVRAAARAA GRTARIQLKA DTGLGRNGCQ PADWAELVGA
160 170 180 190 200
AVAAQAEGTV QVTGVWSHFA CADEPGHPSI RLQLDAFRDM LAYAEKEGVD
210 220 230 240 250
PEVRHIANSP ATLTLPETHF DLVRTGLAVY GVSPSPELGT PAQLGLRPAM
260 270 280 290 300
TLRASLALVK TVPAGHGVSY GHHYVTESET HLALVPAGYA DGIPRNASGR
310 320 330 340 350
GPVLVAGKIR RAAGRIAMDQ FVVDLGEDLA EAGDEAVILG DAERGEPTAE
360 370
DWAQAAHTIA YEIVTRIGGR VPRVYLGG
Length:378
Mass (Da):39,890
Last modified:October 25, 2004 - v1
Checksum:i292ADA9BFF81D75D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB176676 Genomic DNA. Translation: BAD44772.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB176676 Genomic DNA. Translation: BAD44772.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1VFHX-ray2.00A1-378[»]
1VFSX-ray1.90A/B1-378[»]
1VFTX-ray2.30A/B1-378[»]
ProteinModelPortaliQ65YW7.
SMRiQ65YW7. Positions 3-378.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00042; UER00497.
BRENDAi5.1.1.1. 133.

Miscellaneous databases

EvolutionaryTraceiQ65YW7.

Family and domain databases

Gene3Di2.40.37.10. 1 hit.
3.20.20.10. 1 hit.
HAMAPiMF_01201. Ala_racemase.
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...

Publicationsi

  1. "Self-protection mechanism in D-cycloserine-producing Streptomyces lavendulae. Gene cloning, characterization, and kinetics of its alanine racemase and D-alanyl-D-alanine ligase, which are target enzymes of D-cycloserine."
    Noda M., Kawahara Y., Ichikawa A., Matoba Y., Matsuo H., Lee D.G., Kumagai T., Sugiyama M.
    J. Biol. Chem. 279:46143-46152(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
  2. "Structural evidence that alanine racemase from a D-cycloserine-producing microorganism exhibits resistance to its own product."
    Noda M., Matoba Y., Kumagai T., Sugiyama M.
    J. Biol. Chem. 279:46153-46161(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS), PYRIDOXAL PHOSPHATE AT LYS-38.

Entry informationi

Entry nameiQ65YW7_STRLA
AccessioniPrimary (citable) accession number: Q65YW7
Entry historyi
Integrated into UniProtKB/TrEMBL: October 25, 2004
Last sequence update: October 25, 2004
Last modified: June 8, 2016
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources

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.