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P0A2W8

- ALR_STRPN

UniProt

P0A2W8 - ALR_STRPN

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Protein
Alanine racemase
Gene
alr, alaR, SP_1698
Organism
Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Status
Reviewed - 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 By similarity.UniRule annotation

Catalytic activityi

L-alanine = D-alanine.UniRule annotation

Cofactori

Pyridoxal phosphate.1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei40 – 401Proton acceptor; specific for D-alanine By similarity
Binding sitei136 – 1361Substrate By similarity
Active sitei263 – 2631Proton acceptor; specific for L-alanine By similarity
Binding sitei310 – 3101Substrate; via amide nitrogen By similarity

GO - Molecular functioni

  1. alanine racemase activity Source: UniProtKB-HAMAP
  2. pyridoxal phosphate binding Source: UniProtKB-HAMAP
Complete GO annotation...

GO - Biological processi

  1. D-alanine biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BioCyciSPNE170187:GHGN-1705-MONOMER.
BRENDAi5.1.1.1. 5946.
UniPathwayiUPA00042; UER00497.

Names & Taxonomyi

Protein namesi
Recommended name:
Alanine racemase (EC:5.1.1.1)
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: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 367367Alanine racemaseUniRule annotation
PRO_0000114581Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei40 – 401N6-(pyridoxal phosphate)lysineUniRule annotation
Modified residuei129 – 1291N6-carboxylysine

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

STRINGi170187.SP_1698.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3S46X-ray2.00A/B1-367[»]
ProteinModelPortaliP0A2W8.

Miscellaneous databases

EvolutionaryTraceiP0A2W8.

Family & Domainsi

Sequence similaritiesi

Belongs to the alanine racemase family.

Phylogenomic databases

eggNOGiCOG0787.
HOGENOMiHOG000031444.
KOiK01775.
OMAiIYSHLAL.
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

MKASPHRPTK ALIHLGAIRQ NIQQMGAHIP QGTLKLAVVK ANAYGHGAVA    50
VAKAIQDDVD GFCVSNIDEA IELRQAGLSK PILILGVSEI EAVALAKEYD 100
FTLTVAGLEW IQALLDKEVD LTGLTVHLKI DSGMGRIGFR EASEVEQAQD 150
LLQQHGVCVE GIFTHFATAD EESDDYFNAQ LERFKTILAS MKEVPELVHA 200
SNSATTLWHV ETIFNAVRMG DAMYGLNPSG AVLDLPYDLI PALTLESALV 250
HVKTVPAGAC MGYGATYQAD SEQVIATVPI GYADGWTRDM QNFSVLVDGQ 300
ACPIVGRVSM DQITIRLPKL YPLGTKVTLI GSNGDKEITA TQVATYRVTI 350
NYEVVCLLSD RIPREYY 367
Length:367
Mass (Da):39,858
Last modified:March 15, 2005 - v1
Checksum:iA79E2F1B439B18B7
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti354 – 3541V → E in CAA90279. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF171873 Genomic DNA. Translation: AAD51027.1.
AE005672 Genomic DNA. Translation: AAK75776.1.
Z49988 Genomic DNA. Translation: CAA90279.1.
PIRiG95197.
S71015.
RefSeqiNP_346136.1. NC_003028.3.
WP_000648075.1. NZ_AKVY01000001.1.

Genome annotation databases

EnsemblBacteriaiAAK75776; AAK75776; SP_1698.
GeneIDi931137.
KEGGispn:SP_1698.
PATRICi19707839. VBIStrPne105772_1762.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF171873 Genomic DNA. Translation: AAD51027.1 .
AE005672 Genomic DNA. Translation: AAK75776.1 .
Z49988 Genomic DNA. Translation: CAA90279.1 .
PIRi G95197.
S71015.
RefSeqi NP_346136.1. NC_003028.3.
WP_000648075.1. NZ_AKVY01000001.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3S46 X-ray 2.00 A/B 1-367 [» ]
ProteinModelPortali P0A2W8.
ModBasei Search...

Protein-protein interaction databases

STRINGi 170187.SP_1698.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAK75776 ; AAK75776 ; SP_1698 .
GeneIDi 931137.
KEGGi spn:SP_1698.
PATRICi 19707839. VBIStrPne105772_1762.

Phylogenomic databases

eggNOGi COG0787.
HOGENOMi HOG000031444.
KOi K01775.
OMAi IYSHLAL.
OrthoDBi EOG6PP9NJ.

Enzyme and pathway databases

UniPathwayi UPA00042 ; UER00497 .
BioCyci SPNE170187:GHGN-1705-MONOMER.
BRENDAi 5.1.1.1. 5946.

Miscellaneous databases

EvolutionaryTracei P0A2W8.

Family and domain databases

Gene3Di 2.40.37.10. 1 hit.
3.20.20.10. 1 hit.
HAMAPi MF_01201. Ala_racemase.
InterProi 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.
[Graphical view ]
Pfami PF00842. Ala_racemase_C. 1 hit.
PF01168. Ala_racemase_N. 1 hit.
[Graphical view ]
PRINTSi PR00992. ALARACEMASE.
SMARTi SM01005. Ala_racemase_C. 1 hit.
[Graphical view ]
SUPFAMi SSF50621. SSF50621. 1 hit.
SSF51419. SSF51419. 1 hit.
TIGRFAMsi TIGR00492. alr. 1 hit.
PROSITEi PS00395. ALANINE_RACEMASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: September 3, 2014
This is version 71 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

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