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Protein

Alanine racemase

Gene

alr

Organism
Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
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. May also act on other amino acids.UniRule annotation

Catalytic activityi

L-alanine = D-alanine.UniRule annotation

Cofactori

pyridoxal 5'-phosphateUniRule annotation1 Publication

Pathway:iD-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 sitei40 – 401Proton acceptor; specific for D-alanineUniRule annotation
Binding sitei136 – 1361SubstrateUniRule annotation
Active sitei263 – 2631Proton acceptor; specific for L-alanineUniRule annotation
Binding sitei310 – 3101Substrate; via amide nitrogenUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BioCyciSPNE170187:GHGN-1705-MONOMER.
BRENDAi5.1.1.1. 1960.
UniPathwayiUPA00042; UER00497.

Names & Taxonomyi

Protein namesi
Recommended name:
Alanine racemaseUniRule annotation (EC:5.1.1.1UniRule annotation)
Gene namesi
Name:alr
Synonyms:alaR
Ordered Locus Names:SP_1698
OrganismiStreptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Taxonomic identifieri170187 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus
ProteomesiUP000000585 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 367367Alanine racemasePRO_0000114581Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei40 – 401N6-(pyridoxal phosphate)lysine
Modified residuei129 – 1291N6-carboxylysine1 Publication

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

STRINGi170187.SpneT_02001280.

Structurei

Secondary structure

1
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi10 – 145Combined sources
Helixi15 – 2713Combined sources
Beta strandi34 – 385Combined sources
Helixi40 – 445Combined sources
Helixi48 – 558Combined sources
Helixi56 – 583Combined sources
Beta strandi60 – 667Combined sources
Helixi67 – 759Combined sources
Beta strandi82 – 876Combined sources
Helixi90 – 923Combined sources
Helixi93 – 986Combined sources
Beta strandi102 – 1054Combined sources
Helixi108 – 1169Combined sources
Beta strandi125 – 1306Combined sources
Beta strandi136 – 1394Combined sources
Helixi142 – 15413Combined sources
Beta strandi158 – 1647Combined sources
Helixi175 – 18915Combined sources
Beta strandi196 – 2016Combined sources
Helixi203 – 2086Combined sources
Helixi210 – 2123Combined sources
Beta strandi215 – 2195Combined sources
Helixi221 – 2244Combined sources
Turni228 – 2314Combined sources
Beta strandi243 – 2486Combined sources
Beta strandi250 – 2556Combined sources
Beta strandi260 – 2623Combined sources
Helixi263 – 2653Combined sources
Beta strandi273 – 2797Combined sources
Helixi282 – 2843Combined sources
Helixi288 – 2903Combined sources
Beta strandi294 – 2974Combined sources
Beta strandi300 – 3045Combined sources
Beta strandi313 – 3197Combined sources
Beta strandi326 – 3338Combined sources
Beta strandi336 – 3383Combined sources
Helixi340 – 3478Combined sources
Helixi351 – 3566Combined sources
Beta strandi364 – 3674Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3S46X-ray2.00A/B1-367[»]
ProteinModelPortaliP0A2W8.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A2W8.

Family & Domainsi

Sequence similaritiesi

Belongs to the alanine racemase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0787.
HOGENOMiHOG000031444.
KOiK01775.
OMAiITMDQLM.
OrthoDBiEOG6PP9NJ.

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.

P0A2W8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKASPHRPTK ALIHLGAIRQ NIQQMGAHIP QGTLKLAVVK ANAYGHGAVA
60 70 80 90 100
VAKAIQDDVD GFCVSNIDEA IELRQAGLSK PILILGVSEI EAVALAKEYD
110 120 130 140 150
FTLTVAGLEW IQALLDKEVD LTGLTVHLKI DSGMGRIGFR EASEVEQAQD
160 170 180 190 200
LLQQHGVCVE GIFTHFATAD EESDDYFNAQ LERFKTILAS MKEVPELVHA
210 220 230 240 250
SNSATTLWHV ETIFNAVRMG DAMYGLNPSG AVLDLPYDLI PALTLESALV
260 270 280 290 300
HVKTVPAGAC MGYGATYQAD SEQVIATVPI GYADGWTRDM QNFSVLVDGQ
310 320 330 340 350
ACPIVGRVSM DQITIRLPKL YPLGTKVTLI GSNGDKEITA TQVATYRVTI
360
NYEVVCLLSD RIPREYY
Length:367
Mass (Da):39,858
Last modified:March 15, 2005 - v1
Checksum:iA79E2F1B439B18B7
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti354 – 3541V → E in CAA90279 (PubMed:8830261).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF171873 Genomic DNA. Translation: AAD51027.1.
AE005672 Genomic DNA. Translation: AAK75776.1.
Z49988 Genomic DNA. Translation: CAA90279.1.
PIRiG95197.
S71015.
RefSeqiWP_000648075.1. NZ_AKVY01000001.1.

Genome annotation databases

EnsemblBacteriaiAAK75776; AAK75776; SP_1698.
KEGGispn:SP_1698.
PATRICi19707839. VBIStrPne105772_1762.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF171873 Genomic DNA. Translation: AAD51027.1.
AE005672 Genomic DNA. Translation: AAK75776.1.
Z49988 Genomic DNA. Translation: CAA90279.1.
PIRiG95197.
S71015.
RefSeqiWP_000648075.1. NZ_AKVY01000001.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3S46X-ray2.00A/B1-367[»]
ProteinModelPortaliP0A2W8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi170187.SpneT_02001280.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAK75776; AAK75776; SP_1698.
KEGGispn:SP_1698.
PATRICi19707839. VBIStrPne105772_1762.

Phylogenomic databases

eggNOGiCOG0787.
HOGENOMiHOG000031444.
KOiK01775.
OMAiITMDQLM.
OrthoDBiEOG6PP9NJ.

Enzyme and pathway databases

UniPathwayiUPA00042; UER00497.
BioCyciSPNE170187:GHGN-1705-MONOMER.
BRENDAi5.1.1.1. 1960.

Miscellaneous databases

EvolutionaryTraceiP0A2W8.

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

« Hide 'large scale' publications
  1. Guynn L.J., Strych U., Benedik M.J.
    Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC BAA-334 / TIGR4.
  3. "The mmsA locus of Streptococcus pneumoniae encodes a RecG-like protein involved in DNA repair and in three-strand recombination."
    Martin B., Sharples G.J., Humbert O., Lloyd R.G., Claverys J.-P.
    Mol. Microbiol. 19:1035-1045(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 257-367.
  4. "The crystal structure of alanine racemase from Streptococcus pneumoniae, a target for structure-based drug design."
    Im H., Sharpe M.L., Strych U., Davlieva M., Krause K.L.
    BMC Microbiol. 11:116-116(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL PHOSPHATE, COFACTOR, SUBUNIT, PYRIDOXAL PHOSPHATE AT LYS-40, CARBAMYLATION AT LYS-129.

Entry informationi

Entry nameiALR_STRPN
AccessioniPrimary (citable) accession number: P0A2W8
Secondary accession number(s): Q54899, Q9S3V7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: March 15, 2005
Last modified: July 22, 2015
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.